|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
14-322 |
0e+00 |
|
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2).
Pssm-ID: 381377 [Multi-domain] Cd Length: 309 Bit Score: 681.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 14 EYRRCGRSGIKLPAISLGLWHNFGDATRVENSRALLQRAFDLGITHFDLANNYGPPPGSAECNFGRILQEDFLPWRDELV 93
Cdd:cd19151 1 KYNRCGRSGLKLPAISLGLWHNFGDVDRYENSRAMLRRAFDLGITHFDLANNYGPPPGSAEENFGRILKEDLKPYRDELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 94 ISTKAGYTMWDGPYGDWGSRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGISNYPAD 173
Cdd:cd19151 81 ISTKAGYTMWPGPYGDWGSKKYLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGISNYPPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 174 RARQAIDILEDLGTPCLIHQPKYSLFERWVEDGLLALLQEKGVGSIAFSPLAGGQLTDRYLNGIPEDSRAASGSRFLKPE 253
Cdd:cd19151 161 EAREAAAILKDLGTPCLIHQPKYSMFNRWVEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYLNGIPEDSRAAKGSSFLKPE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 379053588 254 QITADKLEKVRQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVGMLANRRFSATECA 322
Cdd:cd19151 241 QITEEKLAKVRRLNEIAQARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALDNREFSEEELA 309
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
15-322 |
0e+00 |
|
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo. Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2). It catalyzes the conversion of 3-hydroxybutanal (3-HB) to 1,3-butanediol (1,3-BDO) by using NADPH as a cofactor.
Pssm-ID: 381315 [Multi-domain] Cd Length: 308 Bit Score: 585.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 15 YRRCGRSGIKLPAISLGLWHNFGDATRVENSRALLQRAFDLGITHFDLANNYGPPPGSAECNFGRILQEDFLPWRDELVI 94
Cdd:cd19089 1 YRRCGRSGLHLPAISLGLWHNFGDYTSPEEARELLRTAFDLGITHFDLANNYGPPPGSAEENFGRILKRDLRPYRDELVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 95 STKAGYTMWDGPYGDWGSRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGISNYPADR 174
Cdd:cd19089 81 STKAGYGMWPGPYGDGGSRKYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPGAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 175 ARQAIDILEDLGTPCLIHQPKYSLFERWVEDGLLALLQEKGVGSIAFSPLAGGQLTDRYLNGIPEDSRAASGSRFLKPEQ 254
Cdd:cd19089 161 ARRAIALLRELGVPLIIHQPRYSLLDRWAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKYLNGIPPDSRRAAESKFLTEEA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 379053588 255 ITADKLEKVRQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVGMLANRRFSATECA 322
Cdd:cd19089 241 LTPEKLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAALKNLDFSEEELA 308
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
15-322 |
0e+00 |
|
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
Pssm-ID: 381376 [Multi-domain] Cd Length: 309 Bit Score: 535.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 15 YRRCGRSGIKLPAISLGLWHNFGDATRVENSRALLQRAFDLGITHFDLANNYGPPPGSAECNFGRILQEDFLPWRDELVI 94
Cdd:cd19150 2 YRRCGKSGLKLPALSLGLWHNFGDDTPLETQRAILRTAFDLGITHFDLANNYGPPPGSAEENFGRILREDFAGYRDELII 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 95 STKAGYTMWDGPYGDWGSRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGISNYPADR 174
Cdd:cd19150 82 STKAGYDMWPGPYGEWGSRKYLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYSPER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 175 ARQAIDILEDLGTPCLIHQPKYSLFERWVE-DGLLALLQEKGVGSIAFSPLAGGQLTDRYLNGIPEDSRAASGsRFLKPE 253
Cdd:cd19150 162 TREAAAILRELGTPLLIHQPSYNMLNRWVEeSGLLDTLQELGVGCIAFTPLAQGLLTDKYLNGIPEGSRASKE-RSLSPK 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 379053588 254 QITADKLEKVRQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVGMLANRRFSATECA 322
Cdd:cd19150 241 MLTEANLNSIRALNEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGALDNLTFSADELA 309
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
1-330 |
1.03e-172 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 482.95 E-value: 1.03e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 1 MVYQPDENRYHTMEYRRCGRSGIKLPAISLGLWHNFGDATRVENSRALLQRAFDLGITHFDLANNYGPPPGSAECNFGRI 80
Cdd:PRK09912 1 MVWLANPERYGQMQYRYCGKSGLRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGPPPGSAEENFGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 81 LQEDFLPWRDELVISTKAGYTMWDGPYGDWGSRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQG 160
Cdd:PRK09912 81 LREDFAAYRDELIISTKAGYDMWPGPYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 161 KALYVGISNYPADRARQAIDILEDLGTPCLIHQPKYSLFERWVE-DGLLALLQEKGVGSIAFSPLAGGQLTDRYLNGIPE 239
Cdd:PRK09912 161 KALYVGISSYSPERTQKMVELLREWKIPLLIHQPSYNLLNRWVDkSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 240 DSR---AASGSRFLKPEQITADKLEKVRQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVGMLANRRF 316
Cdd:PRK09912 241 DSRmhrEGNKVRGLTPKMLTEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQALNNLTF 320
|
330
....*....|....*
gi 379053588 317 SATECAEIDA-ILDG 330
Cdd:PRK09912 321 STEELAQIDQhIADG 335
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
13-331 |
1.23e-135 |
|
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme transport and metabolism, General function prediction only];
Pssm-ID: 440431 [Multi-domain] Cd Length: 316 Bit Score: 387.61 E-value: 1.23e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 13 MEYRRCGRSGIKLPAISLGLWhNFGDATR---VENSRALLQRAFDLGITHFDLANNYGPppGSAECNFGRILQEDflpWR 89
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTM-TFGGPWGgvdEAEAIAILDAALDAGINFFDTADVYGP--GRSEELLGEALKGR---PR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 90 DELVISTKAGYTMWDGPYGDWGSRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGISN 169
Cdd:COG0667 75 DDVVIATKVGRRMGPGPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 170 YPADRARQAIDILEDLgTPCLIHQPKYSLFERWVEDGLLALLQEKGVGSIAFSPLAGGQLTDRYLNG--IPEDSRAAsgs 247
Cdd:COG0667 155 YSAEQLRRALAIAEGL-PPIVAVQNEYSLLDRSAEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGatFPEGDRAA--- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 248 RFLKPEQITADKLEKVRQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVGMLANrRFSATECAEIDAI 327
Cdd:COG0667 231 TNFVQGYLTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADL-ELSAEDLAALDAA 309
|
....
gi 379053588 328 LDGW 331
Cdd:COG0667 310 LAAV 313
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
22-309 |
6.97e-103 |
|
Shaker potassium channel beta subunit family and similar proteins; This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. The family also includes Drosophila melanogaster Hk protein, a founding member of aldo-keto reductase family 6 member B1 (AKR6B1), as well as voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa, founding members of AKR6C1and AKR6C2, respectively. Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381300 [Multi-domain] Cd Length: 297 Bit Score: 303.74 E-value: 6.97e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 22 GIKLPAISLGLWHNFGDATRVENSRALLQRAFDLGITHFDLANNYGPppGSAECNFGRILQedflPW-RDELVISTKAGY 100
Cdd:cd19074 1 GLKVSELSLGTWLTFGGQVDDEDAKACVRKAYDLGINFFDTADVYAA--GQAEEVLGKALK----GWpRESYVISTKVFW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 101 TMWDGPYgDWG-SRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGISNYPADRARQAI 179
Cdd:cd19074 75 PTGPGPN-DRGlSRKHIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 180 DILEDLG-TPCLIHQPKYSLFERWVEDGLLALLQEKGVGSIAFSPLAGGQLTDRYLNGIPEDSRAA---SGSRFLKPEQI 255
Cdd:cd19074 154 DLARQFGlIPPVVEQPQYNMLWREIEEEVIPLCEKNGIGLVVWSPLAQGLLTGKYRDGIPPPSRSRatdEDNRDKKRRLL 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 379053588 256 TADKLEKVRQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVG 309
Cdd:cd19074 234 TDENLEKVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVK 287
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
13-311 |
4.56e-98 |
|
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381369 [Multi-domain] Cd Length: 319 Bit Score: 292.58 E-value: 4.56e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 13 MEYRRCGRSGIKLPAISLGLWHNFGDATRVENSRALLQRAFDLGITHFDLANNYGPppGSAECNFGRILQEdfLPW-RDE 91
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSWVTFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYAN--GQSEEIMGQAIKE--LGWpRSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 92 LVISTKAGYTMWDGPYGDWG-SRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGISNY 170
Cdd:cd19143 77 YVVSTKIFWGGGGPPPNDRGlSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGTSEW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 171 PADRARQAIDILEDLG-TPCLIHQPKYSLFERW-VEDGLLALLQEKGVGSIAFSPLAGGQLTDRYLNGIPEDSRAA-SGS 247
Cdd:cd19143 157 SAQQIEEAHEIADRLGlIPPVMEQPQYNLFHRErVEVEYAPLYEKYGLGTTTWSPLASGLLTGKYNNGIPEGSRLAlPGY 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 379053588 248 RFLKPEQIT--ADKLEKVRQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVGML 311
Cdd:cd19143 237 EWLKDRKEElgQEKIEKVRKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEENLKAL 302
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
28-328 |
1.62e-84 |
|
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain regulatory domains - these are reported to have oxidoreductase activity.
Pssm-ID: 425554 [Multi-domain] Cd Length: 290 Bit Score: 256.85 E-value: 1.62e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 28 ISLGLWHNFGDATRV--ENSRALLQRAFDLGITHFDLANNYGPppGSAECNFGRILQEDfLPWRDELVISTKagYTMWDG 105
Cdd:pfam00248 1 IGLGTWQLGGGWGPIskEEALEALRAALEAGINFIDTAEVYGD--GKSEELLGEALKDY-PVKRDKVVIATK--VPDGDG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 106 PYGDWGSRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGISNYPADRARQAidiLEDL 185
Cdd:pfam00248 76 PWPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKA---LTKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 186 GTPCLIHQPKYSLFERWVEDGLLALLQEKGVGSIAFSPLAGGQLTDRYLngipEDSRAASGSRFLKPEQITADKLEKVRQ 265
Cdd:pfam00248 153 KIPIVAVQVEYNLLRRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYT----RDPDKGPGERRRLLKKGTPLNLEALEA 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 379053588 266 LNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVGmLANRRFSATECAEIDAIL 328
Cdd:pfam00248 229 LEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLG-ALEFPLSDEEVARIDELL 290
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
14-325 |
2.23e-80 |
|
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381305 [Multi-domain] Cd Length: 312 Bit Score: 247.11 E-value: 2.23e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 14 EYRRCGRSGIKLPAISLGLWHnFGDATR------VENSRALLQRAFDLGITHFDLANNYGPppGSAECNFGRILqEDFLP 87
Cdd:cd19079 1 EYVRLGNSGLKVSRLCLGCMS-FGDPKWrpwvldEEESRPIIKRALDLGINFFDTANVYSG--GASEEILGRAL-KEFAP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 88 wRDELVISTKAGYTMWDGPYGDWGSRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGI 167
Cdd:cd19079 77 -RDEVVIATKVYFPMGDGPNGRGLSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 168 SNYPADRARQAIDILEDLG-TPCLIHQPKYSLFERWVEDGLLALLQEKGVGSIAFSPLAGGQLTDRYLNGIPEDSRAASG 246
Cdd:cd19079 156 SSMYAWQFAKALHLAEKNGwTKFVSMQNHYNLLYREEEREMIPLCEEEGIGVIPWSPLARGRLARPWGDTTERRRSTTDT 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 379053588 247 SRFLKPEQITADKlEKVRQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVGMLaNRRFSATECAEID 325
Cdd:cd19079 236 AKLKYDYFTEADK-EIVDRVEEVAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAAL-DIKLSEEEIKYLE 312
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
13-327 |
3.59e-78 |
|
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, Saccharopolyspora erythraea EryBII, and Streptomyces avermitilis aveBVIII are founding members of aldo-keto reductase family 12 member A1 (AKR12A1), B1 (AKR12B1), and C1(AKR12C1), respectively. TylCII acts as a NDP-hexose 2,3-enoyl reductase. EryBII is a mycarose/desosamine reductase involved in L-mycarose and D-desosamine production. aveBVIII functions as a dTDP-4-keto-6-deoxy-L-hexose-2,3-reductase.
Pssm-ID: 381313 [Multi-domain] Cd Length: 310 Bit Score: 241.32 E-value: 3.59e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 13 MEYRRCGRSGIKLPAISLGLWhNFGDATRVENSRALLQRAFDLGITHFDLANNYGPppGSAECNFGRILQEDflpwRDEL 92
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGTM-NFGGRTDEETSFAIMDRALDAGINFFDTADVYGG--GRSEEIIGRWIAGR----RDDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 93 VISTKAGYTMWDGPYGDWGSRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGISNYPA 172
Cdd:cd19087 74 VLATKVFGPMGDDPNDRGLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 173 DRARQAIDILEDLGTPCLI-HQPKYSLFERWVEDGLLALLQEKGVGSIAFSPLAGGQLTDRYLNGIPEDSRAASGSRFLK 251
Cdd:cd19087 154 WQIAKAQGIAARRGLLRFVsEQPMYNLLKRQAELEILPAARAYGLGVIPYSPLAGGLLTGKYGKGKRPESGRLVERARYQ 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 379053588 252 PEQITADKLEKVRQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVGMLAnRRFSATECAEIDAI 327
Cdd:cd19087 234 ARYGLEEYRDIAERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALE-ITLTPELLAEIDEL 308
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
22-325 |
1.77e-74 |
|
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381310 [Multi-domain] Cd Length: 296 Bit Score: 231.26 E-value: 1.77e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 22 GIKLPAISLGLW----HNFGDATRvENSRALLQRAFDLGITHFDLANNYGPppGSAECNFGRILQEDflpwRDELVISTK 97
Cdd:cd19084 1 DLKVSRIGLGTWaiggTWWGEVDD-QESIEAIKAAIDLGINFFDTAPVYGF--GHSEEILGKALKGR----RDDVVIATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 98 AGyTMWDGPYGDW--GSRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGISNYPADRA 175
Cdd:cd19084 74 CG-LRWDGGKGVTkdLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 176 RQAIDIledlgTPCLIHQPKYSLFERWVEDGLLALLQEKGVGSIAFSPLAGGQLTDRYLNGI---PEDSRAAsgSRFLKP 252
Cdd:cd19084 153 EEARKY-----GPIVSLQPPYSMLEREIEEELLPYCRENGIGVLPYGPLAQGLLTGKYKKEPtfpPDDRRSR--FPFFRG 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 379053588 253 EQItADKLEKVRQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVGMLaNRRFSATECAEID 325
Cdd:cd19084 226 ENF-EKNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGAL-DWELTEEELKEID 296
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
26-309 |
4.64e-74 |
|
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications. Members have very distinct functions and include the prokaryotic 2,5-diketo-D-gluconic acid reductases and beta-keto ester reductases, the eukaryotic aldose reductases, aldehyde reductases, hydroxysteroid dehydrogenases, steroid 5beta-reductases, potassium channel beta-subunits, and aflatoxin aldehyde reductases, among others.
Pssm-ID: 381296 [Multi-domain] Cd Length: 232 Bit Score: 228.17 E-value: 4.64e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 26 PAISLGLWHnFGDATRVENSRALLQRAFDLGITHFDLANNYGPppGSAECNFGRILQEDflPWRDELVISTKAGYTMWDG 105
Cdd:cd06660 1 SRLGLGTMT-FGGDGDEEEAFALLDAALEAGGNFFDTADVYGD--GRSERLLGRWLKGR--GNRDDVVIATKGGHPPGGD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 106 PYGDWGSRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGISNYPADRARQAIDILEDL 185
Cdd:cd06660 76 PSRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKAH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 186 G-TPCLIHQPKYSLFERWV-EDGLLALLQEKGVGSIAFSPLAGGqltdrylngipedsraasgsrflkpeqitadklekv 263
Cdd:cd06660 156 GlPGFAAVQPQYSLLDRSPmEEELLDWAEENGLPLLAYSPLARG------------------------------------ 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 379053588 264 rqlnelaarrgqkLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVG 309
Cdd:cd06660 200 -------------PAQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
13-327 |
5.76e-73 |
|
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an uncharacterized aldo-keto reductase from Polaromonas sp.
Pssm-ID: 381317 [Multi-domain] Cd Length: 319 Bit Score: 228.27 E-value: 5.76e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 13 MEYRRCGRSGIKLPAISLG---------LWHNFGdATRVENSRALLQRAFDLGITHFDLANNYGPppGSAECNFGRILQE 83
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGtmtfgggggFFGAWG-GVDQEEADRLVDIALDAGINFFDTADVYSE--GESEEILGKALKG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 84 DflpwRDELVISTKAGYTMWDGPYGDWGSRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKAL 163
Cdd:cd19091 78 R----RDDVLIATKVRGRMGEGPNDVGLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 164 YVGISNYPADRARQAIDILEDLG-TPCLIHQPKYSLFERWVEDGLLALLQEKGVGSIAFSPLAGGQLTDRYLNG--IPED 240
Cdd:cd19091 154 YIGVSNFSAWQIMKALGISERRGlARFVALQAYYSLLGRDLEHELMPLALDQGVGLLVWSPLAGGLLSGKYRRGqpAPEG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 241 SRAASGSRFLKPeqITADKLEKV-RQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVGMlANRRFSAT 319
Cdd:cd19091 234 SRLRRTGFDFPP--VDRERGYDVvDALREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGA-AGLSLTPE 310
|
....*...
gi 379053588 320 ECAEIDAI 327
Cdd:cd19091 311 EIARLDKV 318
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
19-309 |
7.11e-68 |
|
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a founding member of aldo-keto reductase family 9 member C1 (AKR9C1).
Pssm-ID: 381307 [Multi-domain] Cd Length: 308 Bit Score: 214.77 E-value: 7.11e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 19 GRSGIKLPAISLGLWhNFGDATRVENSRALLQRAFDLGITHFDLANNY-----GPPPGSAECNFGRILQEdfLPWRDELV 93
Cdd:cd19081 3 GRTGLSVSPLCLGTM-VFGWTADEETSFALLDAFVDAGGNFIDTADVYsawvpGNAGGESETIIGRWLKS--RGKRDRVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 94 ISTKAGYTMWDGPYGdwGSRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGISNYPAD 173
Cdd:cd19081 80 IATKVGFPMGPNGPG--LSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYSAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 174 RARQAIDILEDLGTP---CLihQPKYSLFER-WVEDGLLALLQEKGVGSIAFSPLAGGQLTDRYLNGIPEDSRAASGS-- 247
Cdd:cd19081 158 RLQEALELSRQHGLPryvSL--QPEYNLVDReSFEGELLPLCREEGIGVIPYSPLAGGFLTGKYRSEADLPGSTRRGEaa 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 379053588 248 -RFLKPEQitadkLEKVRQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVG 309
Cdd:cd19081 236 kRYLNERG-----LRILDALDEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLA 293
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
25-329 |
1.03e-66 |
|
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is a founding member of aldo-keto reductase family 11 member B3(AKR11B3). It is responsible for methylglyoxal detoxification.
Pssm-ID: 381311 [Multi-domain] Cd Length: 292 Bit Score: 211.29 E-value: 1.03e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 25 LPAISLGLW-----HNFGDATRvENSRALLQRAFDLGITHFDLANNYGPppGSAECNFGRILQEDflpwRDELVISTKAG 99
Cdd:cd19085 1 VSRLGLGCWqfgggYWWGDQDD-EESIATIHAALDAGINFFDTAEAYGD--GHSEEVLGKALKGR----RDDVVIATKVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 100 YtmwdgpygDWGSRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGISNYPadraRQAI 179
Cdd:cd19085 74 P--------DNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFG----PAQL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 180 DILEDLGtPCLIHQPKYSLFERWVEDGLLALLQEKGVGSIAFSPLAGGQLTDRYLNGI---PEDSRaasgSRFLKP--EQ 254
Cdd:cd19085 142 EEALDAG-RIDSNQLPYNLLWRAIEYEILPFCREHGIGVLAYSPLAQGLLTGKFSSAEdfpPGDAR----TRLFRHfePG 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 379053588 255 ITADKLEKVRQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVGmLANRRFSATECAEIDAILD 329
Cdd:cd19085 217 AEEETFEALEKLKEIADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAA-AVDLELSPSVLERLDEISD 290
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
14-324 |
1.92e-62 |
|
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor. Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381302 [Multi-domain] Cd Length: 303 Bit Score: 200.90 E-value: 1.92e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 14 EYRRCGRSGIKLPAISLGLW--HNFGDATRVENSRALLQRAFDLGITHFDLANNYGPppGSAECNFGRILQEdflpWRDE 91
Cdd:cd19076 1 PTRKLGTQGLEVSALGLGCMgmSAFYGPADEEESIATLHRALELGVTFLDTADMYGP--GTNEELLGKALKD----RRDE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 92 LVISTKAGYTMWDGPY--GDWGSRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGISN 169
Cdd:cd19076 75 VVIATKFGIVRDPGSGfrGVDGRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLSE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 170 YPADRARQA-----IDILedlgtpclihQPKYSLFERWVEDGLLALLQEKGVGSIAFSPLAGGQLTDRY--LNGIPEDSR 242
Cdd:cd19076 155 ASADTIRRAhavhpITAV----------QSEYSLWTRDIEDEVLPTCRELGIGFVAYSPLGRGFLTGAIksPEDLPEDDF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 243 AASGSRFlKPEQITADkLEKVRQLNELAARRGQKLSQMALAWVL-RNDNVtsVLI-GASKPSQIEDAVGMLaNRRFSATE 320
Cdd:cd19076 225 RRNNPRF-QGENFDKN-LKLVEKLEAIAAEKGCTPAQLALAWVLaQGDDI--VPIpGTKRIKYLEENVGAL-DVVLTPEE 299
|
....
gi 379053588 321 CAEI 324
Cdd:cd19076 300 LAEI 303
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
15-312 |
7.85e-62 |
|
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381367 [Multi-domain] Cd Length: 310 Bit Score: 199.60 E-value: 7.85e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 15 YRRCGRSGIKLPAISLGLWHNFGDATRVENSRALLQRAFDLGITHFDLANNYGPppGSAECNFGRILQEDflPW-RDELV 93
Cdd:cd19141 2 YRNLGKSGLRVSCLGLGTWVTFGSQISDEVAEELVTLAYENGINLFDTAEVYAA--GKAEIVLGKILKKK--GWrRSSYV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 94 ISTKagyTMWDG-PYGDWG-SRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGISNYP 171
Cdd:cd19141 78 ITTK---IFWGGkAETERGlSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 172 ADRARQAIDILEDLG-TPCLIHQPKYSLFER-WVEDGLLALLQEKGVGSIAFSPLAGGQLTDRYLNGIPEDSRAA-SGSR 248
Cdd:cd19141 155 AMEIMEAYSVARQFNlIPPIVEQAEYHLFQReKVEMQLPELFHKIGVGAMTWSPLACGILSGKYDDGVPEYSRASlKGYQ 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 379053588 249 FLKpEQITADK----LEKVRQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVGMLA 312
Cdd:cd19141 235 WLK-EKILSEEgrrqQAKLKELQIIADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQAIQ 301
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
13-328 |
1.47e-60 |
|
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo sapiens, Mus musculus, Mustela putorius, Rattus norvegicus, and Kvb1.1, Kvb1.2 from Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A3 (AKR6A3), A8 (AKR6A8), A10a (AKR6A10a), A13 (AKR6A13), A7 (AKR6A7) and A10b (AKR6A10b), respectively. KCAB1B, also called Shaker channel b-subunit 1(Kvb1), K(+) channel subunit beta-1, or Kv-beta-1, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It modulates action potentials via its effect on the pore-forming alpha subunits.
Pssm-ID: 381385 [Multi-domain] Cd Length: 323 Bit Score: 196.80 E-value: 1.47e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 13 MEYRRCGRSGIKLPAISLGLWHNFGDATRVENSRALLQRAFDLGITHFDLANNYGPppGSAECNFGRILQEDflPWR-DE 91
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAA--GKAEVILGSIIKKK--GWRrSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 92 LVISTKagyTMWDGPY-GDWG-SRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGISN 169
Cdd:cd19159 77 LVITTK---LYWGGKAeTERGlSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 170 YPADRARQAIDILEDLG-TPCLIHQPKYSLFERW-VEDGLLALLQEKGVGSIAFSPLAGGQLTDRYLNGIPEDSRAASGS 247
Cdd:cd19159 154 WSAMEIMEAYSVARQFNmIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKC 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 248 -RFLKPEQITAD---KLEKVRQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVGML-ANRRFSATECA 322
Cdd:cd19159 234 yQWLKERIVSEEgrkQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIqVLPKMTSHVVN 313
|
....*.
gi 379053588 323 EIDAIL 328
Cdd:cd19159 314 EIDNIL 319
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
19-311 |
3.13e-60 |
|
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD), are founding members of aldo-keto reductase family 9 member A1-3 (AKR9A1-3), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis. AAD (EC1.1.1.91) is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). The AKR9B family includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381306 [Multi-domain] Cd Length: 307 Bit Score: 195.13 E-value: 3.13e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 19 GRSGIKLPAISLG---LWHNFGDATRVENSRALLQRAFDLGITHFDLANNYgpPPGSAECNFGRILQEDflpwRDELVIS 95
Cdd:cd19080 4 GRSGLRVSPLALGtmtFGTEWGWGADREEARAMFDAYVEAGGNFIDTANNY--TNGTSERLLGEFIAGN----RDRIVLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 96 TKagYTMWDGP----YGdwG-SRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGISNY 170
Cdd:cd19080 78 TK--YTMNRRPgdpnAG--GnHRKNLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 171 PADRARQAIDILEDLG-TPCLIHQPKYSLFERWVEDGLLALLQEKGVGSIAFSPLAGGQLTDRYLNGIPEDSRAASGSRF 249
Cdd:cd19080 154 PAWVVARANTLAELRGwSPFVALQIEYSLLERTPERELLPMARALGLGVTPWSPLGGGLLTGKYQRGEEGRAGEAKGVTV 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 379053588 250 LKPEQITADkLEKVRQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVGML 311
Cdd:cd19080 234 GFGKLTERN-WAIVDVVAAVAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGAL 294
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
13-328 |
2.10e-59 |
|
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.
Pssm-ID: 381384 [Multi-domain] Cd Length: 324 Bit Score: 193.76 E-value: 2.10e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 13 MEYRRCGRSGIKLPAISLGLWHNFGDATRVENSRALLQRAFDLGITHFDLANNYGPppGSAECNFGRILQEDflPWR-DE 91
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAA--GKAEVVLGNIIKKK--GWRrSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 92 LVISTKagyTMWDGPY-GDWG-SRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGISN 169
Cdd:cd19158 77 LVITTK---IFWGGKAeTERGlSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 170 YPADRARQAIDILEDLG-TPCLIHQPKYSLFERW-VEDGLLALLQEKGVGSIAFSPLAGGQLTDRYLNGIPEDSRAA-SG 246
Cdd:cd19158 154 WSSMEIMEAYSVARQFNlIPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASlKG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 247 SRFLKPEQITAD---KLEKVRQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVGML-ANRRFSATECA 322
Cdd:cd19158 234 YQWLKDKILSEEgrrQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIqVLPKLSSSIVH 313
|
....*.
gi 379053588 323 EIDAIL 328
Cdd:cd19158 314 EIDSIL 319
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
13-328 |
4.02e-57 |
|
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo sapiens, Rattus norvegicus, and Mus musculus, are founding members of aldo-keto reductase family 6 member A9 (AKR6A9), A12 (AKR6A12), A14 (AKR6A14), respectively. KCAB3B, also called Shaker channel b-subunit 3 (Kvb3), K(+) channel subunit beta-3, or Kv-beta-3, is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. It alters the functional properties of Kv1.5.
Pssm-ID: 381386 [Multi-domain] Cd Length: 325 Bit Score: 187.89 E-value: 4.02e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 13 MEYRRCGRSGIKLPAISLGLWHNFGDATRVENSRALLQRAFDLGITHFDLANNYGPppGSAECNFGRILQEDflPWR-DE 91
Cdd:cd19160 3 MKYRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDLLTVAYEHGVNLFDTAEVYAA--GKAERTLGNILKSK--GWRrSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 92 LVISTKagyTMWDG-PYGDWG-SRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGISN 169
Cdd:cd19160 79 YVVTTK---IYWGGqAETERGlSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 170 YPADRARQAIDILEDLG-TPCLIHQPKYSLFER-WVEDGLLALLQEKGVGSIAFSPLAGGQLTDRYLNGIPEDSRAA-SG 246
Cdd:cd19160 156 WSAMEIMEAYSVARQFNlIPPVCEQAEYHLFQReKVEMQLPELYHKIGVGSVTWSPLACGLITGKYDGRVPDTCRAAvKG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 247 SRFLKPEQITAD---KLEKVRQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVGML-ANRRFSATECA 322
Cdd:cd19160 236 YQWLKEKVQSEEgkkQQAKVKELHPIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGSIqVLSQLTPQTVM 315
|
....*.
gi 379053588 323 EIDAIL 328
Cdd:cd19160 316 EIDALL 321
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
25-328 |
1.03e-56 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 185.95 E-value: 1.03e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 25 LPAISLGLW-----HNFG-----DATRvenSRALLQRAFDLGITHFDLANNYGPppGSAECNFGRILQEdflpWRDELVI 94
Cdd:cd19102 1 LTTIGLGTWaigggGWGGgwgpqDDRD---SIAAIRAALDLGINWIDTAAVYGL--GHSEEVVGRALKG----LRDRPIV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 95 STKAGyTMWD--GPYGDWGSRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGISNYPA 172
Cdd:cd19102 72 ATKCG-LLWDeeGRIRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 173 DRARQAIDIledlgTPCLIHQPKYSLFERWVEDGLLALLQEKGVGSIAFSPLAGGQLTDR----YLNGIPEDSRAAsGSR 248
Cdd:cd19102 151 DQMKRCQAI-----HPIASLQPPYSLLRRGIEAEILPFCAEHGIGVIVYSPMQSGLLTGKmtpeRVASLPADDWRR-RSP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 249 FLKPEQITADkLEKVRQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVGMlANRRFSATECAEIDAIL 328
Cdd:cd19102 225 FFQEPNLARN-LALVDALRPIAERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGA-ADLRLTPEELAEIEALL 302
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
23-309 |
7.65e-52 |
|
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase YqkF is a founding member of aldo-keto reductase family 11 member C1 (AKR11C1). It may function as oxidoreductase. This family also includes Bacillus halodurans AKR11C1, an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase.
Pssm-ID: 381312 [Multi-domain] Cd Length: 238 Bit Score: 171.12 E-value: 7.65e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 23 IKLPAISLGLW----HNFGDATRvENSRALLQRAFDLGITHFDLANNYGPppGSAECNFGRILQEDflpwRDELVISTKA 98
Cdd:cd19086 1 LEVSEIGFGTWglggDWWGDVDD-AEAIRALRAALDLGINFFDTADVYGD--GHSERLLGKALKGR----RDKVVIATKF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 99 GYTMWDGPYGDWG-SRKYLIASLDQSLKRMGLEYVDIFYHHRPDPE-TPLKETMKALDHLVRQGKALYVGISnypADRAR 176
Cdd:cd19086 74 GNRFDGGPERPQDfSPEYIREAVEASLKRLGTDYIDLYQLHNPPDEvLDNDELFEALEKLKQEGKIRAYGVS---VGDPE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 177 QAIDILEDLGTPCLIHQpkYSLFERWVEDGLLALLQEKGVGSIAFSPLAGGQLTDrylngipedsraasgsrflkpeqit 256
Cdd:cd19086 151 EALAALRRGGIDVVQVI--YNLLDQRPEEELFPLAEEHGVGVIARVPLASGLLTG------------------------- 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 379053588 257 adklekvrqlnelaarrgqKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVG 309
Cdd:cd19086 204 -------------------KLAQAALRFILSHPAVSTVIPGARSPEQVEENAA 237
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
15-326 |
7.92e-52 |
|
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381375 [Multi-domain] Cd Length: 315 Bit Score: 173.61 E-value: 7.92e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 15 YRRCGRSGIKLPAISLGLW-----HNFGDATrVENSRALLQRAFDLGITHFDLANNYGpppgsaecnFG---RILQEDFL 86
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTWaigggPWWGGSD-DNESIRTIHAALDLGINLIDTAPAYG---------FGhseEIVGKAIK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 87 PWRDELVISTKAGyTMWDGPYGDWGS-------RKYLIAS-----LDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALD 154
Cdd:cd19149 71 GRRDKVVLATKCG-LRWDREGGSFFFvrdgvtvYKNLSPEsireeVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 155 HLVRQGKALYVGISNYPADrarqAIDILEDLGTPCLIhQPKYSLFERWVEDGLLALLQEKGVGSIAFSPLAGGQLTDRYl 234
Cdd:cd19149 150 ELKRQGKIRAIGASNVSVE----QIKEYVKAGQLDII-QEKYSMLDRGIEKELLPYCKKNNIAFQAYSPLEQGLLTGKI- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 235 ngIPEDSRAASGSRFLKPeQITADKLEKVRQLNE----LAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVGM 310
Cdd:cd19149 224 --TPDREFDAGDARSGIP-WFSPENREKVLALLEkwkpLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPEQAEENAKA 300
|
330
....*....|....*.
gi 379053588 311 LaNRRFSATECAEIDA 326
Cdd:cd19149 301 G-DIRLSAEDIATMRS 315
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
13-329 |
6.41e-51 |
|
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.
Pssm-ID: 381368 [Multi-domain] Cd Length: 325 Bit Score: 171.49 E-value: 6.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 13 MEYRRCGRSGIKLPAISLGLWHNFGDATRVENSRALLQRAFDLGITHFDLANnyGPPPGSAECNFGRILQEDflPW-RDE 91
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGTWSTFSTAISEEQAEEIVTLAYENGINYFDTSD--AFTSGQAETELGRILKKK--GWkRSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 92 LVISTKagyTMWD-GPYGDWGSRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGISNY 170
Cdd:cd19142 77 YIVSTK---IYWSyGSEERGLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 171 PADRARQAIDILEDLGTPCLI-HQPKYSLFER-WVEDGLLALLQEKGVGSIAFSPLA-------GGQLTDRYLNGIPEDS 241
Cdd:cd19142 154 SPVEIMEAFSIARQFNCPTPIcEQSEYHMFCReKMELYMPELYNKVGVGLITWSPLSlgldpgiSEETRRLVTKLSFKSS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 242 RAASGSRFLKPEQITADKLEKVRQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVGMLA-NRRFSATE 320
Cdd:cd19142 234 KYKVGSDGNGIHEETRRASHKLRELSLIAERLGCDLTQLLIAWSLKNENVQCVLIGASSLEQLYSQLNSLQlLPKLNSAV 313
|
....*....
gi 379053588 321 CAEIDAILD 329
Cdd:cd19142 314 MEELERILD 322
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
22-328 |
1.66e-50 |
|
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli aldehyde reductase (AKR13C1) and Thermotoga maritima aldo-keto reductase (AKR13C2). Aldehyde reductase (EC 1.1.1.21), also called aldose reductase, is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides.
Pssm-ID: 381304 [Multi-domain] Cd Length: 301 Bit Score: 169.72 E-value: 1.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 22 GIKLPAISLG---LWHNFGDATRVENSRALLQRAFDLGITHFDLANNYGPPPGSaecnfgRILQEDFLPWRDELVISTKA 98
Cdd:cd19078 1 GLEVSAIGLGcmgMSHGYGPPPDKEEMIELIRKAVELGITFFDTAEVYGPYTNE------ELVGEALKPFRDQVVIATKF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 99 GYTMWDGPYGDWG--SRKYLI-ASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGISNYPADRA 175
Cdd:cd19078 75 GFKIDGGKPGPLGldSRPEHIrKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 176 RQAIDIledlgTPCLIHQPKYSLFERWVEDGLLALLQEKGVGSIAFSPLAGGQLTDRYLNGI---PEDSRAASgSRFlKP 252
Cdd:cd19078 155 RRAHAV-----CPVTAVQSEYSMMWREPEKEVLPTLEELGIGFVPFSPLGKGFLTGKIDENTkfdEGDDRASL-PRF-TP 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 379053588 253 EQITADkLEKVRQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVGMlANRRFSATECAEIDAIL 328
Cdd:cd19078 228 EALEAN-QALVDLLKEFAEEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGA-ADIELTPEELREIEDAL 301
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
16-327 |
4.70e-50 |
|
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1).
Pssm-ID: 381309 [Multi-domain] Cd Length: 307 Bit Score: 168.75 E-value: 4.70e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 16 RRCGRSGIKLPAISLGL----WHNFGDATRVENSRALLQRAFDLGITHFDLANNYGPppGSAECNFGRILQEDFlpwRDE 91
Cdd:cd19083 2 VKLGKSDIDVNPIGLGTnavgGHNLYPNLDEEEGKDLVREALDNGVNLLDTAFIYGL--GRSEELVGEVLKEYN---RNE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 92 LVISTKAGYTMWDGPYGDWGSRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGISNYP 171
Cdd:cd19083 77 VVIATKGAHKFGGDGSVLNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 172 ADRARQA-----IDILEDlgtpclihqpKYSLFERWVEDGLLALLQEKGVGSIAFSPLAGGQLTDRYLNGI---PEDSRA 243
Cdd:cd19083 157 LEQLKEAnkdgyVDVLQG----------EYNLLQREAEEDILPYCVENNISFIPYFPLASGLLAGKYTKDTkfpDNDLRN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 244 ASGSrfLKPEQITADkLEKVRQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVGMLaNRRFSATECAE 323
Cdd:cd19083 227 DKPL--FKGERFSEN-LDKVDKLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKAL-DVTLTEEEIAF 302
|
....
gi 379053588 324 IDAI 327
Cdd:cd19083 303 IDAL 306
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
22-309 |
1.31e-49 |
|
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase. Escherichia coli YeaE may act as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381298 [Multi-domain] Cd Length: 263 Bit Score: 166.25 E-value: 1.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 22 GIKLPAISLGLW----HNFGDATRVENSRALLQRAFDLGITHFDLANNYGPppGSAECNFGRILqEDFLpwRDELVISTK 97
Cdd:cd19072 1 GEEVPVLGLGTWgiggGMSKDYSDDKKAIEALRYAIELGINLIDTAEMYGG--GHAEELVGKAI-KGFD--REDLFITTK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 98 AgytmwdgpYGDWGSRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGISNYPADRARQ 177
Cdd:cd19072 76 V--------SPDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 178 AIDILEDlgTPCLIHQPKYSLFERWVEDGLLALLQEKGVGSIAFSPLAGGQLTDRYLNGIpedsraasgsrflkpeqita 257
Cdd:cd19072 148 AQSYLKK--GPIVANQVEYNLFDREEESGLLPYCQKNGIAIIAYSPLEKGKLSNAKGSPL-------------------- 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 379053588 258 dklekvrqLNELAARRGQKLSQMALAWVLRNDNVTsVLIGASKPSQIEDAVG 309
Cdd:cd19072 206 --------LDEIAKKYGKTPAQIALNWLISKPNVI-AIPKASNIEHLEENAG 248
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
24-325 |
2.44e-49 |
|
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR (EC 1.1.1.65) is the prototype of this family. It catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+), and is involved in the PLP salvage pathway.
Pssm-ID: 381319 [Multi-domain] Cd Length: 293 Bit Score: 166.63 E-value: 2.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 24 KLPAISLGLWhNFGDAT---RVENSRALLQRAFDL----GITHFDLANNYGPppGSAECNFGRILQEdfLPWRDELVIST 96
Cdd:cd19093 1 EVSPLGLGTW-QWGDRLwwgYGEYGDEDLQAAFDAaleaGVNLFDTAEVYGT--GRSERLLGRFLKE--LGDRDEVVIAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 97 K-AGYTmWDGPYGDwgsrkyLIASLDQSLKRMGLEYVDIFYHHRPDP-ETPLKETMKALDHLVRQGKALYVGISNYPADR 174
Cdd:cd19093 76 KfAPLP-WRLTRRS------VVKALKASLERLGLDSIDLYQLHWPGPwYSQIEALMDGLADAVEEGLVRAVGVSNYSADQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 175 ARQAIDILEDLGTPCLIHQPKYSLFERWVE-DGLLALLQEKGVGSIAFSPLAGGQLTDRYlngipEDSRAASGSRFLKPE 253
Cdd:cd19093 149 LRRAHKALKERGVPLASNQVEYSLLYRDPEqNGLLPACDELGITLIAYSPLAQGLLTGKY-----SPENPPPGGRRRLFG 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 379053588 254 QITADKLEKVRQ-LNELAARRGQKLSQMALAWVLRNDNVtsVLIGASKPSQIEDAVGMLAnRRFSATECAEID 325
Cdd:cd19093 224 RKNLEKVQPLLDaLEEIAEKYGKTPAQVALNWLIAKGVV--PIPGAKNAEQAEENAGALG-WRLSEEEVAELD 293
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
26-309 |
8.70e-49 |
|
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1/AKR7A3/AFAR) from Rattus norvegicus, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR1/AFAR) and aflatoxin B1 aldehyde reductase member 3 (AKR7A3/AFAR2) from Homo sapiens, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR2) from Rattus norvegicus, and aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AKR7A5/AFAR) from Mus musculus, are founding members of aldo-keto reductase family 7 member A1-5 (AKR7A1-5), respectively. AKR7A2 (EC 1.1.1.n11), also called AFB1 aldehyde reductase 1, or AFB1-AR 1, or aldoketoreductase 7, or succinic semialdehyde reductase, or SSA reductase, catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate (GHB). It has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). AKR7A2, AKR7A3 (also called AFB1 aldehyde reductase 2 or AFB1-AR 2), and AKR7A4 (also called AFB1 aldehyde reductase 3, or AFB1-AR 3, or aldoketoreductase 7-like), may be involved in protection of liver against the toxic and carcinogenic effects of aflatoxin B1 (AFB1), a potent hepatocarcinogen. They can reduce the dialdehyde protein-binding form of AFB1 to the non-binding AFB1 dialcohol.
Pssm-ID: 381301 [Multi-domain] Cd Length: 304 Bit Score: 165.42 E-value: 8.70e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 26 PAISLGLwHNFGDATR---VENSRALLQRAFDLGITHFDLANNYgpPPGSAEcnfgRILQEdFLPWRDELVISTKAgytm 102
Cdd:cd19075 1 PKIILGT-MTFGSQGRfttAEAAAELLDAFLERGHTEIDTARVY--PDGTSE----ELLGE-LGLGERGFKIDTKA---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 103 wDGPYGDWGSRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGISNYPADRARQAIDIL 182
Cdd:cd19075 69 -NPGVGGGLSPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEIC 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 183 EDLG--TPClIHQPKYSLFERWVEDGLLALLQEKGVGSIAFSPLAGGQLTDRY--LNGIPEDSRAASGS--------RFL 250
Cdd:cd19075 148 KENGwvLPT-VYQGMYNAITRQVETELFPCLRKLGIRFYAYSPLAGGFLTGKYkySEDKAGGGRFDPNNalgklyrdRYW 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 379053588 251 KPEQITAdklekVRQLNELAARRGQKLSQMALAWVL--------RNDnvtSVLIGASKPSQIEDAVG 309
Cdd:cd19075 227 KPSYFEA-----LEKVEEAAEKEGISLAEAALRWLYhhsaldgeKGD---GVILGASSLEQLEENLA 285
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
21-308 |
1.10e-47 |
|
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and Escherichia coli YdhF are prototypes of this family. They are uncharacterized aldo/keto reductase family oxidoreductases.
Pssm-ID: 381318 [Multi-domain] Cd Length: 287 Bit Score: 161.95 E-value: 1.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 21 SGIKLPAISLGLWHNFGDATRVENSRALLQRAFDLGITHFDLANNYGPppGSAECNFGRILQEDfLPWRDELVISTKAGY 100
Cdd:cd19092 2 EGLEVSRLVLGCMRLADWGESAEELLSLIEAALELGITTFDHADIYGG--GKCEELFGEALALN-PGLREKIEIQTKCGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 101 TMWDGPYGDWG-----SRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGISNY-PADr 174
Cdd:cd19092 79 RLGDDPRPGRIkhydtSKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFtPSQ- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 175 arqaIDILED-LGTPCLIHQPKYSLFER-WVEDGLLALLQEKGVGSIAFSPLAGGQLTDRYLngipedsraasgsrflkp 252
Cdd:cd19092 158 ----IELLQSyLDQPLVTNQIELSLLHTeAIDDGTLDYCQLLDITPMAWSPLGGGRLFGGFD------------------ 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 379053588 253 eqitaDKLEKVRQ-LNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAV 308
Cdd:cd19092 216 -----ERFQRLRAaLEELAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSAV 267
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
43-308 |
4.29e-47 |
|
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde dehydrogenase is a founding member of aldo-keto reductase family 13 member B1 (AKR13B1). phenylacetaldehyde dehydrogenase (EC 1.2.1.39) catalyzes the NAD+-dependent oxidation of phenylactealdehyde to phenylacetic acid.
Pssm-ID: 381314 [Multi-domain] Cd Length: 256 Bit Score: 159.69 E-value: 4.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 43 ENSRALLQRAFDLGITHFDLANNYGPppGSAEcnfgRILQEDFLPWRDELVISTKAGYTMwDGPyGDW---GSRKYLIAS 119
Cdd:cd19088 24 EEAIAVLRRALELGVNFIDTADSYGP--DVNE----RLIAEALHPYPDDVVIATKGGLVR-TGP-GWWgpdGSPEYLRQA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 120 LDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGISNYPADRARQAIDIledlgTPCLIHQPKYSLF 199
Cdd:cd19088 96 VEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAI-----VRIVSVQNRYNLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 200 ERwVEDGLLALLQEKGVGSIAFSPLAGGQLtdrylngipedsrAASGSRflkpeqitadklekvrqLNELAARRGQKLSQ 279
Cdd:cd19088 171 NR-DDEGVLDYCEAAGIAFIPWFPLGGGDL-------------AQPGGL-----------------LAEVAARLGATPAQ 219
|
250 260
....*....|....*....|....*....
gi 379053588 280 MALAWVLRNDNVTSVLIGASKPSQIEDAV 308
Cdd:cd19088 220 VALAWLLARSPVMLPIPGTSSVEHLEENL 248
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
35-311 |
2.17e-46 |
|
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) and Streptomyces glaucescens aldo-keto reductase (StrT) are founding members of aldo-keto reductase family 10 member A1 (AKR10A1) and A2 (AKR10A2). BlmT is bluensomycin aldo-keto reductase (AKR) and StrT is streptomycin AKR.
Pssm-ID: 381308 [Multi-domain] Cd Length: 291 Bit Score: 158.87 E-value: 2.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 35 NFGDATRVENSRALLQRAFDLGITHFDLANNYG--PPPGSAECNFGRILQEDFLpwRDELVISTKAGYTMWDGPYGDWGS 112
Cdd:cd19082 9 DFGTRIDEEEAFALLDAFVELGGNFIDTARVYGdwVERGASERVIGEWLKSRGN--RDKVVIATKGGHPDLEDMSRSRLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 113 RKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGISNYPADRARQAIDILEDLGTPCL-I 191
Cdd:cd19082 87 PEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNWSTERIAEANAYAKAHGLPGFaA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 192 HQPKYSLF----ERWVEDGL-------LALLQEKGVGSIAFSPLAGGQLTDRYLNGIPEDSRAAsgSRFLkpeqiTADKL 260
Cdd:cd19082 167 SSPQWSLArpnePPWPGPTLvamdeemRAWHEENQLPVFAYSSQARGFFSKRAAGGAEDDSELR--RVYY-----SEENF 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 379053588 261 EKVRQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVGML 311
Cdd:cd19082 240 ERLERAKELAEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAAA 290
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
26-310 |
5.46e-46 |
|
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381321 [Multi-domain] Cd Length: 253 Bit Score: 156.63 E-value: 5.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 26 PAISLGLWHNFGDATRV--ENSRALLQRAFDLGITHFDLANNYGpppgSAECNFGRILQEDFlpwRDELVISTKAGYTmW 103
Cdd:cd19095 1 SVLGLGTSGIGRVWGVPseAEAARLLNTALDLGINLIDTAPAYG----RSEERLGRALAGLR---RDDLFIATKVGTH-G 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 104 DG--PYGDWgSRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGISNYP--ADRARQA- 178
Cdd:cd19095 73 EGgrDRKDF-SPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVSGDGeeLEAAIASg 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 179 -IDILedlgtpclihQPKYSLFERWvEDGLLALLQEKGVGSIAFSPLAGGQLTDRylngipedsraasgsrflkpEQITA 257
Cdd:cd19095 152 vFDVV----------QLPYNVLDRE-EEELLPLAAEAGLGVIVNRPLANGRLRRR--------------------VRRRP 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 379053588 258 DKLEKVRQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVGM 310
Cdd:cd19095 201 LYADYARRPEFAAEIGGATWAQAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
35-327 |
5.66e-46 |
|
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the prototype of this family. It is an NADP(H)-dependent aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NADP(H) as a hydride donor.
Pssm-ID: 381320 [Multi-domain] Cd Length: 328 Bit Score: 158.88 E-value: 5.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 35 NFGDATRVENSRALLQRAFDLGITHFDLANNYGPPP-----GSAECNFGRILQEDflPWRDELVISTK-AGYT--MWDGP 106
Cdd:cd19094 10 TWGEQNTEAEAHEQLDYAFDEGVNFIDTAEMYPVPPspetqGRTEEIIGSWLKKK--GNRDKVVLATKvAGPGegITWPR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 107 YGDWG-SRKYLIASLDQSLKRMGLEYVDIFYHHRPD------------------PETPLKETMKALDHLVRQGKALYVGI 167
Cdd:cd19094 88 GGGTRlDRENIREAVEGSLKRLGTDYIDLYQLHWPDrytplfgggyytepseeeDSVSFEEQLEALGELVKAGKIRHIGL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 168 SNYPADRARQAIDILEDLGTP--CLIHQPkYSLFERWVEDGLLALLQEKGVGSIAFSPLAGGQLTDRYLNG--IPEDSRA 243
Cdd:cd19094 168 SNETPWGVMKFLELAEQLGLPriVSIQNP-YSLLNRNFEEGLAEACHRENVGLLAYSPLAGGVLTGKYLDGaaRPEGGRL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 244 ASGSRFLkPEQITADKLEKVRQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVGMLaNRRFSATECAE 323
Cdd:cd19094 247 NLFPGYM-ARYRSPQALEAVAEYVKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLKENIDAF-DVPLSDELLAE 324
|
....
gi 379053588 324 IDAI 327
Cdd:cd19094 325 IDAV 328
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
26-308 |
1.01e-45 |
|
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH) and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. The family also includes L-galactose dehydrogenase (L-galDH) and D-arabinose 1-dehydrogenase (ARA2). L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381316 [Multi-domain] Cd Length: 278 Bit Score: 156.56 E-value: 1.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 26 PAISLG---LWHNFGDaTRVENSRALLQRAFDLGITHFDLANNYGPppgsAECNFGRILQEdflPWRDELVISTKAGYTM 102
Cdd:cd19090 1 SALGLGtagLGGVFGG-VDDDEAVATIRAALDLGINYIDTAPAYGD----SEERLGLALAE---LPREPLVLSTKVGRLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 103 wdGPYGDWgSRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMK-----ALDHLVRQGKALYVGISNYPADRARQ 177
Cdd:cd19090 73 --EDTADY-SADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILAPggaleALLELKEEGLIKHIGLGGGPPDLLRR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 178 AIDilEDLGTPCLIHQpKYSLFERWVEDGLLALLQEKGVGSIAFSPLAGGQLTDRYlngipeDSRAASGsrflkPEQITA 257
Cdd:cd19090 150 AIE--TGDFDVVLTAN-RYTLLDQSAADELLPAAARHGVGVINASPLGMGLLAGRP------PERVRYT-----YRWLSP 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 379053588 258 DKLEKVRQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAV 308
Cdd:cd19090 216 ELLDRAKRLYELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNV 266
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
13-308 |
4.22e-44 |
|
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+).
Pssm-ID: 381389 [Multi-domain] Cd Length: 293 Bit Score: 152.71 E-value: 4.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 13 MEYRRCGRSGIKLPAISLG---LWHNFGDaTRVENSRALLQRAFDLGITHFDLANNYGPppGSAECNFGRILQEdfLPwR 89
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGaspLGGVFGP-VDEEEAIRTVHEALDSGINYIDTAPWYGQ--GRSETVLGKALKG--IP-R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 90 DELVISTKAG-YT-----MWDGpygdwgSRKYLIASLDQSLKRMGLEYVDIFYHH----RPDPETPLKETMKALDHLVRQ 159
Cdd:cd19163 75 DSYYLATKVGrYGldpdkMFDF------SAERITKSVEESLKRLGLDYIDIIQVHdiefAPSLDQILNETLPALQKLKEE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 160 GKALYVGISNYP-------ADRARQAID-ILedlgTPClihqpKYSLFERWVEDgLLALLQEKGVGSIAFSPLAGGQLTD 231
Cdd:cd19163 149 GKVRFIGITGYPldvlkevLERSPVKIDtVL----SYC-----HYTLNDTSLLE-LLPFFKEKGVGVINASPLSMGLLTE 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 379053588 232 RylnGIPEDSRAasgsrflkPEQItadkLEKVRQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAV 308
Cdd:cd19163 219 R---GPPDWHPA--------SPEI----KEACAKAAAYCKSRGVDISKLALQFALSNPDIATTLVGTASPENLRKNL 280
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-327 |
1.59e-43 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 152.03 E-value: 1.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 14 EYRRCGRSGIKLPAISLG------LWhnfGDATRvENSRALLQRAFDLGITHFDLANNYGPppGSAECNFGRILQEDflp 87
Cdd:cd19104 1 KYRRFGRTGLKVSELTFGgggiggLM---GRTTR-EEQIAAVRRALDLGINFFDTAPSYGD--GKSEENLGRALKGL--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 88 wRDELVISTKAGYTmwDGPYGDWGSRkyLIASLDQSLKRMGLEYVDIFY-HHRPDPETP--------------LKETMKA 152
Cdd:cd19104 72 -PAGPYITTKVRLD--PDDLGDIGGQ--IERSVEKSLKRLKRDSVDLLQlHNRIGDERDkpvggtlsttdvlgLGGVADA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 153 LDHLVRQGKALYVGIS---NYPAdrARQAID--------ILEDLGTPCLIHQPkYSLFERWVEDGLLALLQEKGVGSIAF 221
Cdd:cd19104 147 FERLRSEGKIRFIGITglgNPPA--IRELLDsgkfdavqVYYNLLNPSAAEAR-PRGWSAQDYGGIIDAAAEHGVGVMGI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 222 SPLAGGQLTDRYLNGIPEDSRAASgsrflkPEQITADKLEKVRqlnELAARRGQKLSQMALAWVLRNDNVTSVLIGASKP 301
Cdd:cd19104 224 RVLAAGALTTSLDRGREAPPTSDS------DVAIDFRRAAAFR---ALAREWGETLAQLAHRFALSNPGVSTVLVGVKNR 294
|
330 340
....*....|....*....|....*.
gi 379053588 302 SQIEDAVGMLANRRFSATECAEIDAI 327
Cdd:cd19104 295 EELEEAVAAEAAGPLPAENLARLEAL 320
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
13-329 |
1.22e-42 |
|
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor.
Pssm-ID: 381370 [Multi-domain] Cd Length: 323 Bit Score: 149.90 E-value: 1.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 13 MEYRRCGRSGIKLPAI---SLGLWHNFGDATRVENSRALLQRAFDLGITHFDLANNYGPppgSAEC-------NFGRilq 82
Cdd:cd19144 1 IPTRTLGRNGPSVPALgfgAMGLSAFYGPPKPDEERFAVLDAAFELGCTFWDTADIYGD---SEELigrwfkqNPGK--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 83 edflpwRDELVISTKAGYTM--WDGPYGDWGSRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQG 160
Cdd:cd19144 75 ------REKIFLATKFGIEKnvETGEYSVDGSPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 161 KALYVGISNYPADRARQAidiledlgtpCLIH-----QPKYSLFERWVEDGLLALLQ---EKGVGSIAFSPLAGGQLTDR 232
Cdd:cd19144 149 KIKHIGLSECSAETLRRA----------HAVHpiaavQIEYSPFSLDIERPEIGVLDtcrELGVAIVAYSPLGRGFLTGA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 233 YLNgiPEDSRAASGSRFL---KPEQITADkLEKVRQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVG 309
Cdd:cd19144 219 IRS--PDDFEEGDFRRMAprfQAENFPKN-LELVDKIKAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLG 295
|
330 340
....*....|....*....|
gi 379053588 310 MLaNRRFSATECAEIDAILD 329
Cdd:cd19144 296 AL-KVKLTEEEEKEIREIAE 314
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-306 |
1.41e-42 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 147.73 E-value: 1.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 13 MEYRRCGRSGIKLPAISLGlwhnfGDATRVENSrALLQRAFDLGITHFDLANNYGPppGSAECNFGRILQEdfLPwRDEL 92
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFG-----GGGLPRESP-ELLRRALDLGINYFDTAEGYGN--GNSEEIIGEALKG--LR-RDKV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 93 VISTKAGytmwdgPYGDWGSRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLK---ETMKALDHLVRQGKALYVGIS- 168
Cdd:cd19105 70 FLATKAS------PRLDKKDKAELLKSVEESLKRLQTDYIDIYQLHGVDTPEERLlneELLEALEKLKKEGKVRFIGFSt 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 169 -NYPADRARQAIDiledlgTPCL-IHQPKYS-LFERWVEDGLLALLQEKGVGSIAFSPLAGGQLtdrylngipedsRAAS 245
Cdd:cd19105 144 hDNMAEVLQAAIE------SGWFdVIMVAYNfLNQPAELEEALAAAAEKGIGVVAMKTLAGGYL------------QPAL 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 379053588 246 GSRFLKPeqitadklekvrqlnelaarrGQKLSQMALAWVLRNDNVTSVLIGASKPSQIED 306
Cdd:cd19105 206 LSVLKAK---------------------GFSLPQAALKWVLSNPRVDTVVPGMRNFAELEE 245
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
21-325 |
9.96e-42 |
|
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this family. It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381364 [Multi-domain] Cd Length: 266 Bit Score: 145.85 E-value: 9.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 21 SGIKLPAISLGLWHNFGDATRVENSRALLQRAFDLGITHFDLANNYGppPGSAEcnfgRILQEDFLPWRDELVISTKAgy 100
Cdd:cd19138 7 DGTKVPALGQGTWYMGEDPAKRAQEIEALRAGIDLGMTLIDTAEMYG--DGGSE----ELVGEAIRGRRDKVFLVSKV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 101 tmwdgpYGDWGSRKYLIASLDQSLKRMGLEYVDIFYHHRPDpETPLKETMKALDHLVRQGKALYVGISNYPADRARQAID 180
Cdd:cd19138 79 ------LPSNASRQGTVRACERSLRRLGTDYLDLYLLHWRG-GVPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 181 ILEdlGTPCLIHQPKYSLFERWVEDGLLALLQEKGVGSIAFSPLAGGQLTDRYLNGIPEdsraasgsrflkpeqitadkl 260
Cdd:cd19138 152 VPG--GGNCAANQVLYNLGSRGIEYDLLPWCREHGVPVMAYSPLAQGGLLRRGLLENPT--------------------- 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 261 ekvrqLNELAARRGQKLSQMALAWVLRNDNVtsvlIGASKPSQIEDAVgmlANRR-----FSATECAEID 325
Cdd:cd19138 209 -----LKEIAARHGATPAQVALAWVLRDGNV----IAIPKSGSPEHAR---ENAAaadleLTEEDLAELD 266
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
22-328 |
2.37e-41 |
|
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381374 [Multi-domain] Cd Length: 302 Bit Score: 145.91 E-value: 2.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 22 GIKLPAISLGLWHNFGD---ATRVENSRALLQRAFDLGITHFDLANNYGPppGSAECNFGRILQEdfLPWRDELVISTKA 98
Cdd:cd19148 1 DLPVSRIALGTWAIGGWmwgGTDEKEAIETIHKALDLGINLIDTAPVYGF--GLSEEIVGKALKE--YGKRDRVVIATKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 99 GYTmWD--GPYGDWGSRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGISNY-PA--D 173
Cdd:cd19148 77 GLE-WDegGEVVRNSSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFsPEqmE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 174 RARQAidiledlgTPCLIHQPKYSLFERWVEDGLLALLQEKGVGSIAFSPLAGGQLTDRYL--NGIPEDSRAASGSRFLK 251
Cdd:cd19148 156 TFRKV--------APLHTVQPPYNLFEREIEKDVLPYARKHNIVTLAYGALCRGLLSGKMTkdTKFEGDDLRRTDPKFQE 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 379053588 252 PEqiTADKLEKVRQLNELAARRGQK-LSQMALAWVLRNDNVTSVLIGASKPSQIEDAVGMLAnRRFSATECAEIDAIL 328
Cdd:cd19148 228 PR--FSQYLAAVEELDKLAQERYGKsVIHLAVRWLLDQPGVSIALWGARKPEQLDAVDEVFG-WSLNDEDMKEIDAIL 302
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
26-311 |
8.49e-41 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 144.40 E-value: 8.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 26 PAISLGLWhNFGDATRVENSRALLQRAFDLGITHFDLANNY-----GPPPGSAECNFGRILQEDFLpwRDELVISTKAGy 100
Cdd:cd19752 1 SELCLGTM-YFGTRTDEETSFAILDRYVAAGGNFLDTANNYafwteGGVGGESERLIGRWLKDRGN--RDDVVIATKVG- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 101 tmwdGPYGDWG---------SRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGISNYP 171
Cdd:cd19752 77 ----AGPRDPDggpespeglSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 172 ADRARQAIDILEDLGTP---CLihQPKYSLF----------ERWVEDGLLALLQEKGVGSI-AFSPLAGGQLTDrylNGI 237
Cdd:cd19752 153 AWRLERARQIARQQGWAefsAI--QQRHSYLrprpgadfgvQRIVTDELLDYASSRPDLTLlAYSPLLSGAYTR---PDR 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 379053588 238 PEdsraasgsrflkPEQI-TADKLEKVRQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVGML 311
Cdd:cd19752 228 PL------------PEQYdGPDSDARLAVLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAAL 290
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
13-327 |
2.80e-40 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 144.58 E-value: 2.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 13 MEYRRCGRSGIKLPAISLGLWH-NFGDAtrvENSRALLQRAFDLGITHFDLANNYGpppGSaECNFGRILQEdflpWRDE 91
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGMRlPRKDE---EEAEALIRRAIDNGINYIDTARGYG---DS-EEFLGKALKG----PRDK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 92 LVISTKAGYTMWDgpygdwgsRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMK------ALDHLVRQGKALYV 165
Cdd:COG1453 70 VILATKLPPWVRD--------PEDMRKDLEESLKRLQTDYIDLYLIHGLNTEEDLEKVLKpggaleALEKAKAEGKIRHI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 166 GISNY-PADRARQAIDilEDLGTPCLIHqpkYSLFERWVEDG--LLALLQEKGVGSIAFSPLAGGQLTDrylngIPEdsr 242
Cdd:COG1453 142 GFSTHgSLEVIKEAID--TGDFDFVQLQ---YNYLDQDNQAGeeALEAAAEKGIGVIIMKPLKGGRLAN-----PPE--- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 243 aasgsrflkpeqitadklekvrqlnELAARRGQKLS--QMALAWVLRNDNVTSVLIGASKPSQIEDAVgMLANRRFSATE 320
Cdd:COG1453 209 -------------------------KLVELLCPPLSpaEWALRFLLSHPEVTTVLSGMSTPEQLDENL-KTADNLEPLTE 262
|
....*..
gi 379053588 321 cAEIDAI 327
Cdd:COG1453 263 -EELAIL 268
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
21-330 |
5.28e-40 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 140.96 E-value: 5.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 21 SGIKLPAISLGLWHNFGDATRvensrALLQRAFDLGITHFDLANNYGpppgsAECNFGRILQEDFLPwRDELVISTKAgy 100
Cdd:COG0656 1 NGVEIPALGLGTWQLPGEEAA-----AAVRTALEAGYRHIDTAAMYG-----NEEGVGEAIAASGVP-REELFVTTKV-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 101 tmwdgpYGDWGSRKYLIASLDQSLKRMGLEYVDIFYHHRPDPEtPLKETMKALDHLVRQGKALYVGISNYPADRARqaiD 180
Cdd:COG0656 68 ------WNDNHGYDDTLAAFEESLERLGLDYLDLYLIHWPGPG-PYVETWRALEELYEEGLIRAIGVSNFDPEHLE---E 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 181 ILEDLGTPCLIHQPKYSLFERwvEDGLLALLQEKGVGSIAFSPLAGGQLTDrylngipedsraasgsrflkpeqitadkl 260
Cdd:COG0656 138 LLAETGVKPAVNQVELHPYLQ--QRELLAFCREHGIVVEAYSPLGRGKLLD----------------------------- 186
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 379053588 261 EKVrqLNELAARRGQKLSQMALAWVLRNDNVtsVLIGASKPSQIE---DAVGMlanrRFSATECAEIDAILDG 330
Cdd:COG0656 187 DPV--LAEIAEKHGKTPAQVVLRWHLQRGVV--VIPKSVTPERIRenlDAFDF----ELSDEDMAAIDALDRG 251
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
21-325 |
1.11e-38 |
|
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding members of aldo-keto reductase family 8 member A1-2 (AKR8A1-2), respectively. PLR (EC 1.1.1.65), also called PL reductase (PL-red), catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+).
Pssm-ID: 381303 [Multi-domain] Cd Length: 302 Bit Score: 138.91 E-value: 1.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 21 SGIKLPAISLGL----WHnfGDATRVENSRALLQRAFDLGITHFDLANNYGPPPGSAecNFGriLQEDFL----PWRDEL 92
Cdd:cd19077 1 NGKLVGPIGLGLmgltWR--PNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHA--NLK--LLARFFrkypEYADKV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 93 VISTKAGYTM-WDGPYGdwgSRKYLIASLDQSLKRMG-LEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGISNY 170
Cdd:cd19077 75 VLSVKGGLDPdTLRPDG---SPEAVRKSIENILRALGgTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 171 PADRARQAIDIledlgTPCLIHQPKYSLFERWVED-GLLALLQEKGVGSIAFSPLAGGQLTDRY--LNGIPEDSRAASGS 247
Cdd:cd19077 152 SAETIRRAHAV-----HPIAAVEVEYSLFSREIEEnGVLETCAELGIPIIAYSPLGRGLLTGRIksLADIPEGDFRRHLD 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 379053588 248 RFlkPEQITADKLEKVRQLNELAARRGQKLSQMALAWVLRNDNVTSVLI-GASKPSQIEDAVGmLANRRFSATECAEID 325
Cdd:cd19077 227 RF--NGENFEKNLKLVDALQELAEKKGCTPAQLALAWILAQSGPKIIPIpGSTTLERVEENLK-AANVELTDEELKEIN 302
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
16-324 |
1.79e-38 |
|
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381371 [Multi-domain] Cd Length: 304 Bit Score: 138.33 E-value: 1.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 16 RRCGRSGIKLPAISLG---LWHNFGDATRVENSRALLQRAFDLGITHFDLANNYGPppGSAECNFGRILQEdflPWRDEL 92
Cdd:cd19145 3 VKLGSQGLEVSAQGLGcmgLSGDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYGP--NTNEVLLGKALKD---GPREKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 93 VISTKAGYTMWDGPYGDW-GSRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGISNYP 171
Cdd:cd19145 78 QLATKFGIHEIGGSGVEVrGDPAYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSEAS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 172 ADRARQAIDIledlgTPCLIHQPKYSLFERWVEDGLLALLQEKGVGSIAFSPLAGGqltdrYLNGIPEDSRAASGSRFLK 251
Cdd:cd19145 158 ADTIRRAHAV-----HPITAVQLEWSLWTRDIEEEIIPTCRELGIGIVPYSPLGRG-----FFAGKAKLEELLENSDVRK 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 379053588 252 P-EQITADKLEKVRQLNE----LAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVGMLAnRRFSATECAEI 324
Cdd:cd19145 228 ShPRFQGENLEKNKVLYErveaLAKKKGCTPAQLALAWVLHQGEDVVPIPGTTKIKNLNQNIGALS-VKLTKEDLKEI 304
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
25-312 |
5.74e-38 |
|
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381388 [Multi-domain] Cd Length: 290 Bit Score: 136.72 E-value: 5.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 25 LPAISLGLWHNFGDAtrveNSRALLQRAFDLGITHFDLANNYGPppGSAECNFGRILQEdfLPwRDELVISTKAGYTMWD 104
Cdd:cd19162 5 LGAASLGNLARAGED----EAAATLDAAWDAGIRYFDTAPLYGL--GLSERRLGAALAR--HP-RAEYVVSTKVGRLLEP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 105 GPYG-------DWG-SRKYLIASLDQSLKRMGLEYVDIFYHHRPDP--ETPLKETMKALDHLVRQGKALYVGISnypADR 174
Cdd:cd19162 76 GAAGrpagadrRFDfSADGIRRSIEASLERLGLDRLDLVFLHDPDRhlLQALTDAFPALEELRAEGVVGAIGVG---VTD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 175 ARQAIDILEDLGTPCLIHQPKYSLFERWVEDGLLALLQEKGVGSIAFSPLAGGQLtdryLNGIPEDSRAASGsrflkpeQ 254
Cdd:cd19162 153 WAALLRAARRADVDVVMVAGRYTLLDRRAATELLPLCAAKGVAVVAAGVFNSGIL----ATDDPAGDRYDYR-------P 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 379053588 255 ITADKLEKVRQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVGMLA 312
Cdd:cd19162 222 ATPEVLARARRLAAVCRRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLALLR 279
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
15-328 |
1.72e-37 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 136.06 E-value: 1.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 15 YRRCGRSGIKLPAISLG---LWHNFGDATRvENSRALLQRAFDLGITHFDLANNYGPPpgSAECNFGRILQEDFLPwRDE 91
Cdd:PLN02587 1 LRELGSTGLKVSSVGFGaspLGSVFGPVSE-EDAIASVREAFRLGINFFDTSPYYGGT--LSEKVLGKALKALGIP-REK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 92 LVISTKAGYtmwdgpYGDwG---SRKYLIASLDQSLKRMGLEYVDIFYHHrpDPE-----TPLKETMKALDHLVRQGKAL 163
Cdd:PLN02587 77 YVVSTKCGR------YGE-GfdfSAERVTKSVDESLARLQLDYVDILHCH--DIEfgsldQIVNETIPALQKLKESGKVR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 164 YVGISNYPADRARQAIDILEDLGTPCLIHQPKYSLFERWVEDgLLALLQEKGVGSIAFSPLAGGQLTDrylNGIPEDSRA 243
Cdd:PLN02587 148 FIGITGLPLAIFTYVLDRVPPGTVDVILSYCHYSLNDSSLED-LLPYLKSKGVGVISASPLAMGLLTE---NGPPEWHPA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 244 asgsrflkPEQITadklEKVRQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAV-GMLANRRFSATE-- 320
Cdd:PLN02587 224 --------PPELK----SACAAAATHCKEKGKNISKLALQYSLSNKDISTTLVGMNSVQQVEENVaAATELETSGIDEel 291
|
....*...
gi 379053588 321 CAEIDAIL 328
Cdd:PLN02587 292 LSEVEAIL 299
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-308 |
3.96e-36 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 130.29 E-value: 3.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 15 YRRCGRSGIKLPAISLGLWHnFGDATRvENSRALLQRAFDLGITHFDLANNYgpppGSAECNFGRILQedflPWRDELVI 94
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGP-LGRLSQ-EEAAAIIRRALDLGINYFDTAPSY----GDSEEKIGKALK----GRRDKVFL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 95 STKAGYTMWDGPYgdwgsrkyliASLDQSLKRMGLEYVDIFYHH----RPDPETPL--KETMKALDHLVRQGKALYVGIS 168
Cdd:cd19100 71 ATKTGARDYEGAK----------RDLERSLKRLGTDYIDLYQLHavdtEEDLDQVFgpGGALEALLEAKEEGKIRFIGIS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 169 NYPADRARQAIDILE-DlgtpclIHQPKYSLFERWV---EDGLLALLQEKGVGSIAFSPLAGGQLTDrylngipedsraa 244
Cdd:cd19100 141 GHSPEVLLRALETGEfD------VVLFPINPAGDHIdsfREELLPLAREKGVGVIAMKVLAGGRLLS------------- 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 379053588 245 sgSRFLKPEQitadklekvrqlnelaarrgqklsqmALAWVLRNDNVTSVLIGASKPSQIEDAV 308
Cdd:cd19100 202 --GDPLDPEQ--------------------------ALRYALSLPPVDVVIVGMDSPEELDENL 237
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
22-294 |
3.86e-35 |
|
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381363 [Multi-domain] Cd Length: 260 Bit Score: 128.46 E-value: 3.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 22 GIKLPAISLGLWHNFG----DATRVENSRALLQRAFDLGITHFDLANNYGPppGSAECNFGRILQeDFLpwRDELVISTK 97
Cdd:cd19137 1 GEKIPALGLGTWGIGGfltpDYSRDEEMVELLKTAIELGYTHIDTAEMYGG--GHTEELVGKAIK-DFP--REDLFIVTK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 98 AGYTMWdgpygdwgSRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGISNYPADRARQ 177
Cdd:cd19137 76 VWPTNL--------RYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 178 AIDILEdlgTPCLIHQPKYSLFER-WVEDGLLALLQEKGVGSIAFSPLAGGQltdrylngipedsraasgsrflkpeqit 256
Cdd:cd19137 148 AISKSQ---TPIVCNQVKYNLEDRdPERDGLLEYCQKNGITVVAYSPLRRGL---------------------------- 196
|
250 260 270
....*....|....*....|....*....|....*...
gi 379053588 257 adkLEKVRQLNELAARRGQKLSQMALAWVLRNDNVTSV 294
Cdd:cd19137 197 ---EKTNRTLEEIAKNYGKTIAQIALAWLIQKPNVVAI 231
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
23-329 |
1.14e-34 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 128.22 E-value: 1.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 23 IKLPAISLGLW----------HNFGDATRVENSRALLQRAFDLGITHFDLANNYGPppGSAEcnfgRILQEdFLPW--RD 90
Cdd:cd19103 2 KKLPKIALGTWswgsggaggdQVFGNHLDEDTLKAVFDKAMAAGLNLWDTAAVYGM--GASE----KILGE-FLKRypRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 91 ELVISTKagYTmwdgPYGDWGSRKYLIASLDQSLKRMGLEYVDIFYHHRP-DPEtplKETMKALDhLVRQGKALYVGISN 169
Cdd:cd19103 75 DYIISTK--FT----PQIAGQSADPVADMLEGSLARLGTDYIDIYWIHNPaDVE---RWTPELIP-LLKSGKVKHVGVSN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 170 YPADRARQAIDILEDLGTPCLIHQPKYSLFER-WVEDGLLALLQEKGVGSIAFSPLAGGQLTDRYL--NGIPEDS-RAAS 245
Cdd:cd19103 145 HNLAEIKRANEILAKAGVSLSAVQNHYSLLYRsSEEAGILDYCKENGITFFAYMVLEQGALSGKYDtkHPLPEGSgRAET 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 246 GSRFLkpeqitaDKLEKVRQ-LNELAARRGQKLSQMALAWVLRNDnvTSVLIGASKPSQIEDAVGMlANRRFSATECAEI 324
Cdd:cd19103 225 YNPLL-------PQLEELTAvMAEIGAKHGASIAQVAIAWAIAKG--TTPIIGVTKPHHVEDAARA-ASITLTDDEIKEL 294
|
....*
gi 379053588 325 DAILD 329
Cdd:cd19103 295 EQLAD 299
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
13-327 |
1.31e-33 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 126.51 E-value: 1.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 13 MEYRRCGRSGIKLPAISLGLWhNFGDATRVENSRALLQRAFDLGITHFDLANNYGPPP-----GSAECNFGRILQEDflP 87
Cdd:PRK10625 1 MQYHRIPHSSLEVSTLGLGTM-TFGEQNSEADAHAQLDYAVAQGINLIDVAEMYPVPPrpetqGLTETYIGNWLAKR--G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 88 WRDELVISTKAGytmwdGPY--GDWG-------SRKYLIASLDQSLKRMGLEYVDIFYHHRPDPET-------------- 144
Cdd:PRK10625 78 SREKLIIASKVS-----GPSrnNDKGirpnqalDRKNIREALHDSLKRLQTDYLDLYQVHWPQRPTncfgklgyswtdsa 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 145 ---PLKETMKALDHLVRQGKALYVGISNYPADRARQAIDILE--DLGTPCLIHQPkYSLFERWVEDGLLALLQEKGVGSI 219
Cdd:PRK10625 153 pavSLLETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEkhDLPRIVTIQNP-YSLLNRSFEVGLAEVSQYEGVELL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 220 AFSPLAGGQLTDRYLNGI-PEDSRAASGSRFLKpeqITADKLEK-VRQLNELAARRGQKLSQMALAWVLRNDNVTSVLIG 297
Cdd:PRK10625 232 AYSCLAFGTLTGKYLNGAkPAGARNTLFSRFTR---YSGEQTQKaVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLLG 308
|
330 340 350
....*....|....*....|....*....|
gi 379053588 298 ASKPSQIEDAVGMLaNRRFSATECAEIDAI 327
Cdd:PRK10625 309 ATTMEQLKTNIESL-HLTLSEEVLAEIEAV 337
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
31-328 |
4.36e-32 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 121.55 E-value: 4.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 31 GLWH-NFGDATRVENSRAL--LQRAFDLGITHFDLANNYGPppgsAECNFGRILQEdfLPWRDELVISTKaGYTMWDGPY 107
Cdd:cd19101 8 GMWQlSGGHGGIRDEDAAVraMAAYVDAGLTTFDCADIYGP----AEELIGEFRKR--LRRERDAADDVQ-IHTKWVPDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 108 GDWG-SRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETP-LKETMKALDHLVRQGKALYVGISNYPADRARQAIDiledL 185
Cdd:cd19101 81 GELTmTRAYVEAAIDRSLKRLGVDRLDLVQFHWWDYSDPgYLDAAKHLAELQEEGKIRHLGLTNFDTERLREILD----A 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 186 GTPCLIHQPKYSLFERWVEDGLLALLQEKGVGSIAFSPLAGGQLTDRYLnGIPEDSRAASGSRFLKPEQITADK------ 259
Cdd:cd19101 157 GVPIVSNQVQYSLLDRRPENGMAALCEDHGIKLLAYGTLAGGLLSEKYL-GVPEPTGPALETRSLQKYKLMIDEwggwdl 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 260 -LEKVRQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVgMLANRRFSATECAEIDAIL 328
Cdd:cd19101 236 fQELLRTLKAIADKHGVSIANVAVRWVLDQPGVAGVIVGARNSEHIDDNV-RAFSFRLDDEDRAAIDAVL 304
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
20-327 |
4.15e-31 |
|
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381366 [Multi-domain] Cd Length: 253 Bit Score: 117.74 E-value: 4.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 20 RSGIKLPAISLGLWHNFGDAtrvenSRALLQRAFDLGITHFDLANNYGpppgsAECNFGRILQEDFLPwRDELVISTKag 99
Cdd:cd19140 3 VNGVRIPALGLGTYPLTGEE-----CTRAVEHALELGYRHIDTAQMYG-----NEAQVGEAIAASGVP-RDELFLTTK-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 100 ytMWDGPYgdwgSRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGISNYPADRARQAI 179
Cdd:cd19140 70 --VWPDNY----SPDDFLASVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 180 DILEdlgTPCLIHQPKYSLFERwvEDGLLALLQEKGVGSIAFSPLAGGQLTDRYLngipedsraasgsrflkpeqitadk 259
Cdd:cd19140 144 ELSE---APLFTNQVEYHPYLD--QRKLLDAAREHGIALTAYSPLARGEVLKDPV------------------------- 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 379053588 260 lekvrqLNELAARRGQKLSQMALAWVLRNDNVtSVLIGASKPSQIEDAVGMLaNRRFSATECAEIDAI 327
Cdd:cd19140 194 ------LQEIGRKHGKTPAQVALRWLLQQEGV-AAIPKATNPERLEENLDIF-DFTLSDEEMARIAAL 253
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
21-329 |
3.36e-28 |
|
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins; Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis.
Pssm-ID: 381372 [Multi-domain] Cd Length: 326 Bit Score: 111.36 E-value: 3.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 21 SGIKLPAISLG-LWHNFGDATRVENSRALLQRAFDLGITHFDLANNYgpPPGSAEcnfgRILQEdflpW------RDELV 93
Cdd:cd19146 12 SPLCLGAMSFGeAWKSMMGECDKETAFKLLDAFYEQGGNFIDTANNY--QGEESE----RWVGE----WmasrgnRDEMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 94 ISTK--AGYTMWDGP-----YGDwGSRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVG 166
Cdd:cd19146 82 LATKytTGYRRGGPIkiksnYQG-NHAKSLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 167 ISNYPADRARQAIDILEDLG-TPCLIHQPKYSLFERWVEDGLLALLQEKGVGSIAFSPLAGGQL-TDRylngipEDSRAA 244
Cdd:cd19146 161 VSDTPAWVVSKANAYARAHGlTQFVVYQGHWSAAFRDFERDILPMCEAEGMALAPWGVLGQGQFrTEE------EFKRRG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 245 SGSRFLKPEQITADKLEKVrqLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVGMLAnrrFSATEcAEI 324
Cdd:cd19146 235 RSGRKGGPQTEKERKVSEK--LEKVAEEKGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIEALG---ISLSD-EEI 308
|
....*
gi 379053588 325 DAILD 329
Cdd:cd19146 309 QEIED 313
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
26-305 |
9.29e-28 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 110.11 E-value: 9.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 26 PAISLG------LWHNFGDATrvenSRALLQRAFDLGITHFDLANNYGPppGSAECNFGRILQEdfLPwRDELVISTKAG 99
Cdd:cd19161 1 SELGLGtaglgnLYTAVSNAD----ADATLDAAWDSGIRYFDTAPMYGH--GLAEHRLGDFLRE--KP-RDEFVLSTKVG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 100 YTMW---DG---PYGDWG-----------SRKYLIASLDQSLKRMGLEYVDIFYHHRPDPET--------PLKETM---- 150
Cdd:cd19161 72 RLLKparEGsvpDPNGFVdplpfeivydySYDGIMRSFEDSLQRLGLNRIDILYVHDIGVYThgdrkerhHFAQLMsggf 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 151 KALDHLVRQG--KALYVGISNYPA-DRARQAIDIledlgtPCLIHQPKYSLFERWVEDGLLALLQEKGVGSIAFSPLAGG 227
Cdd:cd19161 152 KALEELKKAGviKAFGLGVNEVQIcLEALDEADL------DCFLLAGRYSLLDQSAEEEFLPRCEQRGTSLVIGGVFNSG 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 379053588 228 QLtdrylngipedSRAASGSRFLKPEQITADKLEKVRQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIE 305
Cdd:cd19161 226 IL-----------ATGTKSGAKFNYGDAPAEIISRVMEIEKICDAYNVPLAAAALQFPLRHPAVASVLTGARNPAQLR 292
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
43-314 |
6.83e-27 |
|
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381378 [Multi-domain] Cd Length: 308 Bit Score: 107.70 E-value: 6.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 43 ENSRALLQRAFDLGITHFDLANNYGPppGSAECNFGRILQEdfLPwRDELVISTKAGYTMW----DGPYGD---WGSRKY 115
Cdd:cd19152 20 EEAKATLVAAWDLGIRYFDTAPWYGA--GLSEERLGAALRE--LG-REDYVISTKVGRLLVplqeVEPTFEpgfWNPLPF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 116 LI----------ASLDQSLKRMGLEYVDIFYHHRPDPETP-----------LKETMKALDHLVRQGKALYVGI-SNypad 173
Cdd:cd19152 95 DAvfdysydgilRSIEDSLQRLGLSRIDLLSIHDPDEDLAgaesdehfaqaIKGAFRALEELREEGVIKAIGLgVN---- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 174 RARQAIDILEDLGTPCLIHQPKYSLFERWVEDGLLALLQEKGVGSIAFSPLAGGQLtdrylngipedsraASGSRFLKPE 253
Cdd:cd19152 171 DWEVILRILEEADLDWVMLAGRYTLLDHSAARELLPECEKRGVKVVNAGPFNSGFL--------------AGGDNFDYYE 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 379053588 254 --QITADKLEKVRQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVGMLANR 314
Cdd:cd19152 237 ygPAPPELIARRDRIEALCEQHGVSLAAAALQFALAPPAVASVAPGASSPERVEENVALLATE 299
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
25-325 |
4.27e-26 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti isatin reductase and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381299 [Multi-domain] Cd Length: 243 Bit Score: 103.89 E-value: 4.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 25 LPAISLGLWHNFGDatrveNSRALLQRAFDLGITHFDLANNYGPPPGSAEcnfgrILQEDFLPwRDELVISTKAGYTMWD 104
Cdd:cd19073 1 IPALGLGTWQLRGD-----DCANAVKEALELGYRHIDTAEIYNNEAEVGE-----AIAESGVP-REDLFITTKVWRDHLR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 105 gpYGDwgsrkyLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGISNYpadRARQAIDILED 184
Cdd:cd19073 70 --PED------LKKSVDRSLEKLGTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNF---TIELLEEALDI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 185 LGTPCLIHQPKYSLFerWVEDGLLALLQEKGVGSIAFSPLAGGqltdrylngipedsraasgsrflkpeqitadKLEKVR 264
Cdd:cd19073 139 SPLPIAVNQVEFHPF--LYQAELLEYCRENDIVITAYSPLARG-------------------------------EVLRDP 185
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 379053588 265 QLNELAARRGQKLSQMALAWVLRNDnvTSVLIGASKPSQIEDAVGmLANRRFSATECAEID 325
Cdd:cd19073 186 VIQEIAEKYDKTPAQVALRWLVQKG--IVVIPKASSEDHLKENLA-IFDWELTSEDVAKID 243
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
46-308 |
3.15e-25 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 103.17 E-value: 3.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 46 RALLQRAFDLGITHFDLANNYGPppGSAECNFGRILQE---DFLPWRDELVISTKAGY--TMWDGPYGDWGSR------- 113
Cdd:cd19099 24 REALKAALDSGINVIDTAINYRG--GRSERLIGKALRElieKGGIKRDEVVIVTKAGYipGDGDEPLRPLKYLeeklgrg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 114 ----------------KYLIASLDQSLKRMGLEYVDIFYHHRPDPETP----------LKETMKALDHLVRQGKALYVGI 167
Cdd:cd19099 102 lidvadsaglrhcispAYLEDQIERSLKRLGLDTIDLYLLHNPEEQLLelgeeefydrLEEAFEALEEAVAEGKIRYYGI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 168 S------NYPADRARQAIDILEDLG--------------TPCLIHQPkYSLFERWVEDG----LLALLQEKGVGSIAFSP 223
Cdd:cd19099 182 StwdgfrAPPALPGHLSLEKLVAAAeevggdnhhfkviqLPLNLLEP-EALTEKNTVKGealsLLEAAKELGLGVIASRP 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 224 LAGGQLtdrylngipedsraasgsrflkpeqitadkLEKVRQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQ 303
Cdd:cd19099 261 LNQGQL------------------------------LGELRLADLLALPGGATLAQRALQFARSTPGVDSALVGMRRPEH 310
|
....*
gi 379053588 304 IEDAV 308
Cdd:cd19099 311 VDENL 315
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
46-308 |
2.88e-24 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 99.52 E-value: 2.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 46 RALLQRAFDLGITHFDLANNYGpppgSAECNFGRILQEDflpwrDELVISTKAGYTMWDGPYgdwgSRKYLIASLDQSLK 125
Cdd:cd19097 29 KKILEYALKAGINTLDTAPAYG----DSEKVLGKFLKRL-----DKFKIITKLPPLKEDKKE----DEAAIEASVEASLK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 126 RMGLEYVDIFYHHRPDPET-PLKETMKALDHLVRQGKALYVGISNYPADRARQAIDILEdlgtpCLIHQPKYSLFE-RWV 203
Cdd:cd19097 96 RLKVDSLDGLLLHNPDDLLkHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKALESFK-----IDIIQLPFNILDqRFL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 204 EDGLLALLQEKGVG----SIafsplaggqltdrYLNGI--PEDSRAASGSRFLKPeqitadkleKVRQLNELAARRGQKL 277
Cdd:cd19097 171 KSGLLAKLKKKGIEiharSV-------------FLQGLllMEPDKLPAKFAPAKP---------LLKKLHELAKKLGLSP 228
|
250 260 270
....*....|....*....|....*....|.
gi 379053588 278 SQMALAWVLRNDNVTSVLIGASKPSQIEDAV 308
Cdd:cd19097 229 LELALGFVLSLPEIDKIVVGVDSLEQLKEII 259
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
26-308 |
5.97e-24 |
|
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381322 [Multi-domain] Cd Length: 255 Bit Score: 98.40 E-value: 5.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 26 PAISLG---LWHNFGDATRVENSRALLQRAFDLGITHFDLANNYGppPGSAECNFGRILQEDflpWRDELVISTKagytm 102
Cdd:cd19096 1 SVLGFGtmrLPESDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYG--GGKSEEILGEALKEG---PREKFYLATK----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 103 wdGPYGDWGSRKYLIASLDQSLKRMGLEYVDIF-YHHRPDPETPLK----ETMKALDHLVRQGKALYVGISNYpaDRARQ 177
Cdd:cd19096 71 --LPPWSVKSAEDFRRILEESLKRLGVDYIDFYlLHGLNSPEWLEKarkgGLLEFLEKAKKEGLIRHIGFSFH--DSPEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 178 AIDILE----DLgtpCLIHqpkYSLFERWVEDG--LLALLQEKGVGSIAFSPLAGGQLTDRylngiPEdsraasgsrflk 251
Cdd:cd19096 147 LKEILDsydfDF---VQLQ---YNYLDQENQAGrpGIEYAAKKGMGVIIMEPLKGGGLANN-----PP------------ 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 379053588 252 peqitadklekvrQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAV 308
Cdd:cd19096 204 -------------EALAILCGAPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENI 247
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
12-308 |
7.78e-23 |
|
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381379 [Multi-domain] Cd Length: 294 Bit Score: 96.07 E-value: 7.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 12 TMEYRRCGRSGIKLPAISLGlwHNFGDATRVENSRALLQRAFDLGITHFDLANNYGPPpgSAECNFGRILQEDFLPwRDE 91
Cdd:cd19153 4 TLEIALGNVSPVGLGTAALG--GVYGDGLEQDEAVAIVAEAFAAGINHFDTSPYYGAE--SSEAVLGKALAALQVP-RSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 92 LVISTKAGYtmwdgpYGDWG---SRKYLIASLDQSLKRMGLEYVDIFYHHR---PDPETPLKETMKALDHLVRQGKALYV 165
Cdd:cd19153 79 YTVATKVGR------YRDSEfdySAERVRASVATSLERLHTTYLDVVYLHDiefVDYDTLVDEALPALRTLKDEGVIKRI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 166 GISNYPadrarqaIDILEDLGTPCLIHQPK-------YSLFERWVEDGLLALLQEKGVGSIAFSPLAGGQLTDRylnGIP 238
Cdd:cd19153 153 GIAGYP-------LDTLTRATRRCSPGSLDavlsychLTLQDARLESDAPGLVRGAGPHVINASPLSMGLLTSQ---GPP 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 379053588 239 EDSRAASGSRflkpeqitadklEKVRQLNELAARRGQKLSQMALAWVLRNDN-VTSVLIGASKPSQIEDAV 308
Cdd:cd19153 223 PWHPASGELR------------HYAAAADAVCASVEASLPDLALQYSLAAHAgVGTVLLGPSSLAQLRSML 281
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
25-306 |
1.14e-21 |
|
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. The family includes AKR1A/B/C/D/E/G/I, AKR2A/B/C/D/E, AKR3A/B/C/D/E/G, AKR4A/B/C, AKR5A/B/C/D/E/F/G/H, and similar proteins.
Pssm-ID: 381297 [Multi-domain] Cd Length: 251 Bit Score: 92.16 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 25 LPAISLGLWHNFGDATRvensrALLQRAFDLGITHFDLANNYGpppgsaecN---FGRILQEDFLPwRDELVISTKagyt 101
Cdd:cd19071 1 MPLIGLGTYKLKPEETA-----EAVLAALEAGYRHIDTAAAYG--------NeaeVGEAIRESGVP-REELFITTK---- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 102 MWDGPYGdwgsRKYLIASLDQSLKRMGLEYVDIFYHHRP------DPETPLKETMKALDHLVRQGKALYVGISNYPadrA 175
Cdd:cd19071 63 LWPTDHG----YERVREALEESLKDLGLDYLDLYLIHWPvpgkegGSKEARLETWRALEELVDEGLVRSIGVSNFN---V 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 176 RQAIDILEDLGTPCLIHQPKYSLFerWVEDGLLALLQEKGVGSIAFSPLAGGQLtdrylngipedsraasgsrflkpeqi 255
Cdd:cd19071 136 EHLEELLAAARIKPAVNQIELHPY--LQQKELVEFCKEHGIVVQAYSPLGRGRR-------------------------- 187
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 379053588 256 tadKLEKVRQLNELAARRGQKLSQMALAWVLRNDNVtsVLIGASKPSQIED 306
Cdd:cd19071 188 ---PLLDDPVLKEIAKKYGKTPAQVLLRWALQRGVV--VIPKSSNPERIKE 233
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
22-327 |
2.08e-21 |
|
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis NADPH-dependent conjugated polyketone reductase C2 (CPR), and similar proteins; Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase (EC 1.1.1.190/EC 1.1.1.191) and Candida parapsilosis NADPH-dependent CPR (EC 1.1.1.358/EC 1.1.1.168) are founding members of aldo-keto reductase family 3 member C2 (AKR3C2) and C3 (AKR3C3), respectively. Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase catalyzes the conversion from (Indol-3-yl)ethanol to (indol-3-yl)acetaldehyde in a NAD/NADP-dependent manner. CPR, also called 2-dehydropantolactone reductase, or 2-dehydropantolactone reductase (A-specific), or ketopantoyl-lactone reductase, acts as a NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. It reduces ketopantoyl lactone and isatin.
Pssm-ID: 381346 [Multi-domain] Cd Length: 269 Bit Score: 91.91 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 22 GIKLPAISLGL---WHNFGDATRVENSRALLQRAFDLGITHFDLANNYGpppgsAECNFGRILQEDFLPwRDELVISTKA 98
Cdd:cd19120 1 GSKIPAIAFGTgtaWYKSGDDDIQRDLVDSVKLALKAGFRHIDTAEMYG-----NEKEVGEALKESGVP-REDLFITTKV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 99 GYTMWDGPygdwgsrkyliASLDQSLKRMGLEYVDIFYHHRP----DPETPLKETMKALDHLVRQGKALYVGISNYpadR 174
Cdd:cd19120 75 SPGIKDPR-----------EALRKSLAKLGVDYVDLYLIHSPffakEGGPTLAEAWAELEALKDAGLVRSIGVSNF---R 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 175 ARQAIDILEDLGTPCLIHQPKYSLFERWVEDGLLALLQEKGVGSIAFSPLAggQLTdrylngipedsraasgsrflkpeQ 254
Cdd:cd19120 141 IEDLEELLDTAKIKPAVNQIEFHPYLYPQQPALLEYCREHGIVVSAYSPLS--PLT-----------------------R 195
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 379053588 255 ITADKLEKVrqLNELAARRGQKLSQMALAWVLRNDNVtsVLIGASKPSQIEDAVGMlANRRFSATECAEIDAI 327
Cdd:cd19120 196 DAGGPLDPV--LEKIAEKYGVTPAQVLLRWALQKGIV--VVTTSSKEERMKEYLEA-FDFELTEEEVEEIDKA 263
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
21-311 |
2.64e-21 |
|
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; Phanerochaete chrysosporium ADD (EC1.1.1.91) is a founding member of aldo-keto reductase family 9 member A3. It is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). This family also includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381373 [Multi-domain] Cd Length: 319 Bit Score: 92.58 E-value: 2.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 21 SGIKLPAISLG-LWHNFGDATRVENSRALLQRAFDLGITHFDLANNYGPPpgSAECNFGRILQEDFLpwRDELVISTKAG 99
Cdd:cd19147 11 SPLILGAMSIGdAWSGFMGSMDKEQAFELLDAFYEAGGNFIDTANNYQDE--QSETWIGEWMKSRKN--RDQIVIATKFT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 100 --YTMWDGPYGD----WG-SRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMKALDHLVRQGKALYVGISNYPA 172
Cdd:cd19147 87 tdYKAYEVGKGKavnyCGnHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDTPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 173 DRARQAIDILEDLG-TPCLIHQPKYSLFERWVEDGLLALLQEKGVGSIAFSPLAGGQLTDRYLngipEDSRAASGS---R 248
Cdd:cd19147 167 WVVSAANYYATAHGkTPFSVYQGRWNVLNRDFERDIIPMARHFGMALAPWDVLGGGKFQSKKA----VEERKKNGEglrS 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 379053588 249 FLKPEQITADKLEKVRQLNELAARRG-QKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVGML 311
Cdd:cd19147 243 FVGGTEQTPEEVKISEALEKVAEEHGtESVTAIALAYVRSKAPNVFPLVGGRKIEHLKDNIEAL 306
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
20-292 |
6.79e-20 |
|
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381361 [Multi-domain] Cd Length: 265 Bit Score: 87.38 E-value: 6.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 20 RSGIKLPAISLGLWHNFGdatrvENSRALLQRAFDLGITHFDLANNYGpppgsAECNFGRILQEDFLPwRDELVISTKag 99
Cdd:cd19135 8 SNGVEMPILGLGTSHSGG-----YSHEAVVYALKECGYRHIDTAKRYG-----CEELLGKAIKESGVP-REDLFLTTK-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 100 ytMWDGPYGDwgsrKYLIASLDQSLKRMGLEYVDIFYHHRPDPETP-------LKETMKALDHLVRQGKALYVGISNYpa 172
Cdd:cd19135 75 --LWPSDYGY----ESTKQAFEASLKRLGVDYLDLYLLHWPDCPSSgknvketRAETWRALEELYDEGLCRAIGVSNF-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 173 drarqAIDILEDLGTPCLI----HQPKYSLFERWVEdgLLALLQEKGVGSIAFSPLAGGQLtdrylngipedsraasgsr 248
Cdd:cd19135 147 -----LIEHLEQLLEDCSVvphvNQVEFHPFQNPVE--LIEYCRDNNIVFEGYCPLAKGKA------------------- 200
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 379053588 249 fLKPEQITadklekvrqlnELAARRGQKLSQMALAWVLRNDNVT 292
Cdd:cd19135 201 -LEEPTVT-----------ELAKKYQKTPAQILIRWSIQNGVVT 232
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
25-327 |
3.38e-19 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 85.10 E-value: 3.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 25 LPAISLGLWHNFGDATRvensrALLQRAFDLGITHFDLANNYGpppgsAECNFGRILQEDFLPwRDELVISTKagytMWD 104
Cdd:cd19139 1 IPAFGLGTFRLKDDVVI-----DSVRTALELGYRHIDTAQIYD-----NEAAVGQAIAESGVP-RDELFITTK----IWI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 105 GPYgdwgSRKYLIASLDQSLKRMGLEYVDIFYHHRPDP--ETPLKETMKALDHLVRQGKALYVGISNYPADRARQAIDIL 182
Cdd:cd19139 66 DNL----SKDKLLPSLEESLEKLRTDYVDLTLIHWPSPndEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 183 --EDLGTpcliHQPKYSLFERwvEDGLLALLQEKGVGSIAFSPLAGGQLTDrylngIPedsraasgsrflkpeqitadkl 260
Cdd:cd19139 142 gaGAIAT----NQIELSPYLQ--NRKLVAHCKQHGIHVTSYMTLAYGKVLD-----DP---------------------- 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 379053588 261 ekvrQLNELAARRGQKLSQMALAWVLRNDnvTSVLIGASKPSQIEDAVGMLaNRRFSATECAEIDAI 327
Cdd:cd19139 189 ----VLAAIAERHGATPAQIALAWAMARG--YAVIPSSTKREHLRSNLLAL-DLTLDADDMAAIAAL 248
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
25-308 |
6.05e-19 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 85.41 E-value: 6.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 25 LPAISLG---LWHNFGDATRVENSRALLQRAFDLGITHFDLANNYGPppgsAECNFGRILQEDFLPW-RDELVISTKAG- 99
Cdd:cd19164 13 LPPLIFGaatFSYQYTTDPESIPPVDIVRRALELGIRAFDTSPYYGP----SEIILGRALKALRDEFpRDTYFIITKVGr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 100 YTMWDGPYgdwgSRKYLIASLDQSLKRMGLEYVDIFYHHrpDPE-TPLKETMKALDHLVR---QGKALYVGISNYPADR- 174
Cdd:cd19164 89 YGPDDFDY----SPEWIRASVERSLRRLHTDYLDLVYLH--DVEfVADEEVLEALKELFKlkdEGKIRNVGISGYPLPVl 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 175 ARQAIDILEDLGTP--CLIHQPKYSLferwVEDGLLA----LLQEKGVGSI--AfSPLAGGQLTDRylnGIPEDSRAasg 246
Cdd:cd19164 163 LRLAELARTTAGRPldAVLSYCHYTL----QNTTLLAyipkFLAAAGVKVVlnA-SPLSMGLLRSQ---GPPEWHPA--- 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 379053588 247 SRFLKpeqitadklEKVRQLNELAARRGQKLSQMALAWVLRNDN-VTSVLIGASKPSQIEDAV 308
Cdd:cd19164 232 SPELR---------AAAAKAAEYCQAKGTDLADVALRYALREWGgEGPTVVGCSNVDELEEAV 285
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
22-292 |
1.64e-18 |
|
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 83.59 E-value: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 22 GIKLPAISLGLWhnfgdatRVENSRALLQR---AFDLGITHFDLANNYGPPPGsaecnFGRILQEDFLPwRDELVISTKa 98
Cdd:cd19157 7 GVKMPWLGLGVF-------KVEEGSEVVNAvktALKNGYRSIDTAAIYGNEEG-----VGKGIKESGIP-REELFITSK- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 99 gytMWDGpygDWGSRKYLiASLDQSLKRMGLEYVDIFYHHRPDpETPLKETMKALDHLVRQGKALYVGISNYpadrarqA 178
Cdd:cd19157 73 ---VWNA---DQGYDSTL-KAFEASLERLGLDYLDLYLIHWPV-KGKYKETWKALEKLYKDGRVRAIGVSNF-------Q 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 179 IDILEDLGTPC----LIHQPKYSlfERWVEDGLLALLQEKGVGSIAFSPLAGGQLTDRYLngipedsraasgsrflkpeq 254
Cdd:cd19157 138 VHHLEDLLADAeivpMVNQVEFH--PRLTQKELRDYCKKQGIQLEAWSPLMQGQLLDNPV-------------------- 195
|
250 260 270
....*....|....*....|....*....|....*...
gi 379053588 255 itadklekvrqLNELAARRGQKLSQMALAWVLRNDNVT 292
Cdd:cd19157 196 -----------LKEIAEKYNKSVAQVILRWDLQNGVVT 222
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
22-291 |
5.02e-18 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; Escherichia coli DkgA/YqhE is a founding member of aldo-keto reductase family 5 member C2 (AKR5C2). DkgA/YqhE (EC 1.1.1.274), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives.
Pssm-ID: 381357 [Multi-domain] Cd Length: 256 Bit Score: 82.03 E-value: 5.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 22 GIKLPAISLGLWHNFGDATRvensrALLQRAFDLGITHFDLANNYGpppgsAECNFGRILQEDFLPwRDELVISTKagyt 101
Cdd:cd19131 7 GNTIPQLGLGVWQVSNDEAA-----SAVREALEVGYRSIDTAAIYG-----NEEGVGKAIRASGVP-REELFITTK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 102 MWDGPYGDWGSRKyliaSLDQSLKRMGLEYVDIFYHHRPDP-ETPLKETMKALDHLVRQGKALYVGISNYPADRARQAID 180
Cdd:cd19131 72 LWNSDQGYDSTLR----AFDESLRKLGLDYVDLYLIHWPVPaQDKYVETWKALIELKKEGRVKSIGVSNFTIEHLQRLID 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 181 ileDLGTPCLIHQpkYSLFERWVEDGLLALLQEKGVGSIAFSPLAGGQLTDrylngipedsraasgsrflkpeqitaDKL 260
Cdd:cd19131 148 ---ETGVVPVVNQ--IELHPRFQQRELRAFHAKHGIQTESWSPLGQGGLLS--------------------------DPV 196
|
250 260 270
....*....|....*....|....*....|.
gi 379053588 261 ekvrqLNELAARRGQKLSQMALAWVLRNDNV 291
Cdd:cd19131 197 -----IGEIAEKHGKTPAQVVIRWHLQNGLV 222
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
24-286 |
1.63e-17 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 80.84 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 24 KLPAISLGLWHNFGDAtrVENSralLQRAFDLGITHFDLANNYGpppgsAECNFGRILQEDFLPwRDELVISTKagytMW 103
Cdd:PRK11172 2 SIPAFGLGTFRLKDQV--VIDS---VKTALELGYRAIDTAQIYD-----NEAAVGQAIAESGVP-RDELFITTK----IW 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 104 DGPYgdwgSRKYLIASLDQSLKRMGLEYVDIFYHHRPDP--ETPLKETMKALDHLVRQGKALYVGISNYPADRARQAIDI 181
Cdd:PRK11172 67 IDNL----AKDKLIPSLKESLQKLRTDYVDLTLIHWPSPndEVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQAIAA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 182 L--EDLGTpcliHQPKYS--LFERwvedGLLALLQEKGVGSIAFSPLAGGQ-LTDRYLNGIpedsraasgsrflkpeqit 256
Cdd:PRK11172 143 VgaENIAT----NQIELSpyLQNR----KVVAFAKEHGIHVTSYMTLAYGKvLKDPVIARI------------------- 195
|
250 260 270
....*....|....*....|....*....|
gi 379053588 257 adklekvrqlnelAARRGQKLSQMALAWVL 286
Cdd:PRK11172 196 -------------AAKHNATPAQVILAWAM 212
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
34-327 |
1.72e-17 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 81.17 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 34 HNFGDATRVENSRALLQRAFDLGITHFDLANNYGPPPGSaecnfgRILQEDFLPWRDELVISTKAGYTMwdGPYGDWG-- 111
Cdd:PRK10376 31 GVFGPPKDRDAAIAVLREAVALGVNHIDTSDFYGPHVTN------QLIREALHPYPDDLTIVTKVGARR--GEDGSWLpa 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 112 -SRKYLIASLDQSLKRMGLEYVDI------FYHHRPDPEtPLKETMKALDHLVRQGKALYVGISNYPADRARQAIDIled 184
Cdd:PRK10376 103 fSPAELRRAVHDNLRNLGLDVLDVvnlrlmGDGHGPAEG-SIEEPLTVLAELQRQGLVRHIGLSNVTPTQVAEARKI--- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 185 lgTPCLIHQPKYSLFERwVEDGLLALLQEKGVGSIAFSPLAGgqltdrylngipedsraasgsrfLKPEQITAdklekvr 264
Cdd:PRK10376 179 --AEIVCVQNHYNLAHR-ADDALIDALARDGIAYVPFFPLGG-----------------------FTPLQSST------- 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 379053588 265 qLNELAARRGQKLSQMALAWVL-RNDNVtsVLI-GASKPSQIEDAVGMlANRRFSATECAEIDAI 327
Cdd:PRK10376 226 -LSDVAASLGATPMQVALAWLLqRSPNI--LLIpGTSSVAHLRENLAA-AELVLSEEVLAELDGI 286
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
21-306 |
5.09e-17 |
|
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 (NADP-dependent D-sorbitol-6-phosphate dehydrogenase or NADP-S6PDH) from Malus domestica, and AKR2A2 (NADPH-dependent mannose-6-phosphate reductase or NADPH-M6PR) from Apium graveolens. NADP-S6PDH (EC 1.1.1.200), also called aldose-6-phosphate reductase [NADPH], synthesizes sorbitol-6-phosphate, a key intermediate in the synthesis of sorbitol which is a major photosynthetic product in many members of the Rosaceae family. NADPH-M6PR (EC 1.1.1.224), also called NADPH-dependent M6P reductase, is a key enzyme involved in mannitol biosynthesis.
Pssm-ID: 381338 [Multi-domain] Cd Length: 308 Bit Score: 80.22 E-value: 5.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 21 SGIKLPAISLGLWhnfgdatRVENS--RALLQRAFDLGITHFDLANNYGpppgsAECNFGRILQEDF---LPWRDELVIS 95
Cdd:cd19112 7 SGHKMPVIGLGVW-------RMEPGeiKELILNAIKIGYRHFDCAADYK-----NEKEVGEALAEAFktgLVKREDLFIT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 96 TKagytMWDGPYGdwgsrkYLIASLDQSLKRMGLEYVDIFYHHRP-----------------------DPETPLKETMKA 152
Cdd:cd19112 75 TK----LWNSDHG------HVIEACKDSLKKLQLDYLDLYLVHFPvatkhtgvgttgsalgedgvldiDVTISLETTWHA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 153 LDHLVRQGKALYVGISNYPadrarqaIDILEDLGTPCLIhQPKYSLFER---WVEDGLLALLQEKGVGSIAFSPLAGGql 229
Cdd:cd19112 145 MEKLVSAGLVRSIGISNYD-------IFLTRDCLAYSKI-KPAVNQIEThpyFQRDSLVKFCQKHGISVTAHTPLGGA-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 230 tdrylngipedsrAASGSRF--LKPEQitaDKLekvrqLNELAARRGQKLSQMALAWVL-RNdnvTSVLIGASKPSQIED 306
Cdd:cd19112 215 -------------AANAEWFgsVSPLD---DPV-----LKDLAKKYGKSAAQIVLRWGIqRN---TAVIPKSSKPERLKE 270
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
22-239 |
5.90e-16 |
|
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes prostaglandin F2-alpha synthase (PGFS) from Leishmania major (AKR5A1) and Trypanosoma brucei (AKR5A2). PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity for synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde. The AKR5G family of AKR includes Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase, which corresponds to aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381352 [Multi-domain] Cd Length: 254 Bit Score: 76.32 E-value: 5.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 22 GIKLPAISLGLWH-NFGDATRvensRALlQRAFDLGITHFDLANNYgpppgSAECNFGRILQEDFLPwRDELVISTKagy 100
Cdd:cd19126 6 GTRMPWLGLGVFQtPDGDETE----RAV-QTALENGYRSIDTAAIY-----KNEEGVGEAIRESGVP-REELFVTTK--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 101 tMWDGpygDWGSRKYLIAsLDQSLKRMGLEYVDIFYHHRPDPETpLKETMKALDHLVRQGKALYVGISNYpadrarqAID 180
Cdd:cd19126 72 -LWND---DQRARRTEDA-FQESLDRLGLDYVDLYLIHWPGKDK-FIDTWKALEKLYASGKVKAIGVSNF-------QEH 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 379053588 181 ILEDLGTPCLIhQPKYSLFE---RWVEDGLLALLQEKGVGSIAFSPLAGGQ-LTDRYLNGIPE 239
Cdd:cd19126 139 HLEELLAHADV-VPAVNQVEfhpYLTQKELRGYCKSKGIVVEAWSPLGQGGlLSNPVLAAIGE 200
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
21-286 |
1.05e-14 |
|
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a founding member of aldo-keto reductase family 2 member E4 (AKR2E4). It is a NADP-dependent oxidoreductase with high 3-dehydroecdysone reductase activity. It may play a role in the regulation of molting and has lower activity with phenylglyoxal and isatin (in vitro). This family also includes 3-dehydroecdysone 3b-reductase from Spodoptera littoralis and Trichoplusia ni, DL-glyceraldehyde reductase from Drosophila melanogaster, aldo-keto reductase from Bombyx mori, which correspond to aldo-keto reductase family 2 member E1, E2, E3 and E5 (AKR2E1/2/3/5), respectively.
Pssm-ID: 381342 [Multi-domain] Cd Length: 292 Bit Score: 73.09 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 21 SGIKLPAISLGLWhNFGDATRVENSralLQRAFDLGITHFDLANNYGpppgsAECNFGRILQEDF---LPWRDELVISTK 97
Cdd:cd19116 7 DGNEIPAIALGTW-KLKDDEGVRQA---VKHAIEAGYRHIDTAYLYG-----NEAEVGEAIREKIaegVVKREDLFITTK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 98 agytMWdgpyGDWGSRKYLIASLDQSLKRMGLEYVDIFYHHRP-------DPETPLK---------ETMKALDHLVRQGK 161
Cdd:cd19116 78 ----LW----NSYHEREQVEPALRESLKRLGLDYVDLYLIHWPvafkennDSESNGDgslsdidylETWRGMEDLVKLGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 162 ALYVGISNYpadRARQAIDILEDLGTPCLIHQPKYSLfeRWVEDGLLALLQEKGVGSIAFSPLaggqltdrylnGIPEds 241
Cdd:cd19116 150 TRSIGVSNF---NSEQINRLLSNCNIKPAVNQIEVHP--TLTQEKLVAYCQSNGIVVMAYSPF-----------GRLV-- 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 379053588 242 raasGSRFLKPEQITADklekvRQLNELAARRGQKLSQMALAWVL 286
Cdd:cd19116 212 ----PRGQTNPPPRLDD-----PTLVAIAKKYGKTTAQIVLRYLI 247
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
21-305 |
2.54e-14 |
|
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis.
Pssm-ID: 381348 [Multi-domain] Cd Length: 291 Bit Score: 72.27 E-value: 2.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 21 SGIKLPAISLGLWHNfgDATRVENSRALLqRAFDLGITHFDLANNYgpppgSAECNFGRILQeDFLPW-----RDELVIS 95
Cdd:cd19122 5 NGVKIPAVGFGTFAN--EGAKGETYAAVT-KALDVGYRHLDCAWFY-----LNEDEVGDAVR-DFLKEnpsvkREDLFIC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 96 TKagytMWDG--PYGDwgsrkyLIASLDQSLKRMGLEYVDIFYHHRP------DPETP----------LKE-------TM 150
Cdd:cd19122 76 TK----VWNHlhEPED------VKWSIDNSLKNLKLDYIDLFLVHWPiaaeknDQRSPklgpdgkyviLKDltenpepTW 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 151 KALDHLVRQGKALYVGISNYPADRARQAIDILEDLGTpclIHQPKYSLFERWVEdgLLALLQEKGVGSIAFSPLaGGQlt 230
Cdd:cd19122 146 RAMEEIYESGKAKAIGVSNWTIPGLKKLLSFAKVKPH---VNQIEIHPFLPNEE--LVDYCFSNDILPEAYSPL-GSQ-- 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 379053588 231 drylNGIPEdsraasgsrflkpeqiTADKLEKVRQLNELAARRGQKLSQMALAWVLRNDNVtsVLIGASKPSQIE 305
Cdd:cd19122 218 ----NQVPS----------------TGERVSENPTLNEVAEKGGYSLAQVLIAWGLRRGYV--VLPKSSTPSRIE 270
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
22-292 |
2.65e-14 |
|
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from Leishmania major and Trypanosoma brucei are founding members of aldo-keto reductase family 5 member A1 (AKR5A1) and A2 (AKR5A2), respectively. PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity toward the synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde.
Pssm-ID: 381382 [Multi-domain] Cd Length: 266 Bit Score: 71.78 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 22 GIKLPAISLGLWHnFGDATRVENSralLQRAFDLGITHFDLANNYgpppgSAECNFGRILQEDFLPwRDELVISTKagyt 101
Cdd:cd19156 6 GVEMPRLGLGVWR-VQDGAEAENA---VKWAIEAGYRHIDTAAIY-----KNEEGVGQGIRESGVP-REEVFVTTK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 102 MWDGpygDWGSRKYLiASLDQSLKRMGLEYVDIFYHHRPDpETPLKETMKALDHLVRQGKALYVGISNYPADRarqaidi 181
Cdd:cd19156 72 LWNS---DQGYESTL-AAFEESLEKLGLDYVDLYLIHWPV-KGKFKDTWKAFEKLYKEKKVRAIGVSNFHEHH------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 182 LEDLGTPCLIhQP---KYSLFERWVEDGLLALLQEKGVGSIAFSPLAGGQLtdrylngipedsraasgsrflkpeqitad 258
Cdd:cd19156 140 LEELLKSCKV-APmvnQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGKL----------------------------- 189
|
250 260 270
....*....|....*....|....*....|....
gi 379053588 259 kLEKVRqLNELAARRGQKLSQMALAWVLRNDNVT 292
Cdd:cd19156 190 -LSNPV-LKAIGKKYGKSAAQVIIRWDIQHGIIT 221
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
22-327 |
5.85e-14 |
|
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) is a founding member of the aldo-keto reductase family 5 member B1 (AKR5B1). M6DH (EC 1.1.1.218), also called naloxone reductase, oxidizes the C-6 hydroxy group of morphine and codeine.
Pssm-ID: 381353 [Multi-domain] Cd Length: 268 Bit Score: 70.90 E-value: 5.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 22 GIKLPAISLGLWhnfgdATRVENSRALLQRAFDLGITHFDLANNYGpppgsAECNFGRILQEDFLPwRDELVISTKagyt 101
Cdd:cd19127 6 GVEMPALGLGVF-----QTPPEETADAVATALADGYRLIDTAAAYG-----NEREVGEGIRRSGVD-RSDIFVTTK---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 102 MWDGPYGDWGSRKyliaSLDQSLKRMGLEYVDIFYHHRPDPeTPLKETM---KALDHLVRQGKALYVGISNYPADRARQA 178
Cdd:cd19127 71 LWISDYGYDKALR----GFDASLRRLGLDYVDLYLLHWPVP-NDFDRTIqayKALEKLLAEGRVRAIGVSNFTPEHLERL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 179 IDiledlGTPCLIHQPKYSLFERWVEDGLLALLQEKGVGSIAFSPLaGGQLTDRylngipeDSRAASGSRFLKPEQITad 258
Cdd:cd19127 146 ID-----ATTVVPAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPI-GGVMRYG-------ASGPTGPGDVLQDPTIT-- 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 379053588 259 klekvrqlnELAARRGQKLSQMALAWVLRNDnvTSVLIGASKPSQIEDAVGMLaNRRFSATECAEIDAI 327
Cdd:cd19127 211 ---------GLAEKYGKTPAQIVLRWHLQNG--VSAIPKSVHPERIAENIDIF-DFALSAEDMAAIDAL 267
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
21-327 |
6.02e-14 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381380 [Multi-domain] Cd Length: 303 Bit Score: 71.29 E-value: 6.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 21 SGIKLPAISLGLWHNFGDATRvensrALLQRAFDLGITHFDLANNYgpppgSAECNFGRILQEDF---LPWRDELVISTK 97
Cdd:cd19154 8 NGVKMPLIGLGTWQSKGAEGI-----TAVRTALKAGYRLIDTAFLY-----QNEEAIGEALAELLeegVVKREDLFITTK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 98 AGYTMwdgpygdwGSRKYLIASLDQSLKRMGLEYVDIFYHHRP-------------------DPETPLKETMKALDHLVR 158
Cdd:cd19154 78 LWTHE--------HAPEDVEEALRESLKKLQLEYVDLYLIHAPaafkddegesgtmengmsiHDAVDVEDVWRGMEKVYD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 159 QGKALYVGISNYPADRARQAIDILEdlgTPCLIHQPKYSLFerWVEDGLLALLQEKGVGSIAFSPLaggqltdrylnGIP 238
Cdd:cd19154 150 EGLTKAIGVSNFNNDQIQRILDNAR---VKPHNNQVECHLY--FPQKELVEFCKKHNISVTSYATL-----------GSP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 239 EDSRAASGSRFLKPEQITADKLEKvrqlnELAARRGQKLSQMALAWVLrnDNVTSVLIGASKPSQIEDAvGMLANRRFSA 318
Cdd:cd19154 214 GRANFTKSTGVSPAPNLLQDPIVK-----AIAEKHGKTPAQVLLRYLL--QRGIAVIPKSATPSRIKEN-FNIFDFSLSE 285
|
....*....
gi 379053588 319 TECAEIDAI 327
Cdd:cd19154 286 EDMATLEEI 294
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
21-304 |
1.18e-13 |
|
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase (ALR) from Hordeum vulgare (AKR4C1), Bromus inermis (AKR4C2), Avena fatua (AKR4C3), and Xerophyta viscosa (AKR4C4), two aldose reductases, DpAR1 (AKR4C5) and DpAR2(AKR4C6), from Digitalis purpurea, aldehyde reductase from Zea mays (AKR4C7), four aldo-keto reductases from Arabidopsis thaliana (AKR4C8-11), and another three aldo-keto reductases from Aloe arborescens (AKR4C12) and Oryza sativa (AKR4C14/15). ALR (EC 1.1.1.21), also called AR, aldehyde reductase, or polyol dehydrogenase (NADP(+)), is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. Both DpAR1 and DpAR2 reduce the ketone group of steroid structures. They may be involved in plant steroid metabolism in general and in cardenolide biosynthesis in particular. Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops.
Pssm-ID: 381351 [Multi-domain] Cd Length: 287 Bit Score: 70.07 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 21 SGIKLPAISLGLWHnfGDATRVENSralLQRAFDLGITHFDLANNYGpppgsAECNFGRILQEDF---LPWRDELVISTK 97
Cdd:cd19125 7 TGAKIPAVGLGTWQ--ADPGVVGNA---VKTAIKEGYRHIDCAAIYG-----NEKEIGKALKKLFedgVVKREDLFITSK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 98 agytMW-------DGPygdwgsrkyliASLDQSLKRMGLEYVDIFYHHRP--------------DPETPLKETMKALDHL 156
Cdd:cd19125 77 ----LWctdhapeDVP-----------PALEKTLKDLQLDYLDLYLIHWPvrlkkgahmpepeeVLPPDIPSTWKAMEKL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 157 VRQGKALYVGISNYpadRARQAIDILEDLGTPCLIHQPKYSLFerWVEDGLLALLQEKGVGSIAFSPLaggqltdrylng 236
Cdd:cd19125 142 VDSGKVRAIGVSNF---SVKKLEDLLAVARVPPAVNQVECHPG--WQQDKLHEFCKSKGIHLSAYSPL------------ 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 379053588 237 ipedsrAASGSRFLKPEQITADKLEKVrqlnelAARRGQKLSQMALAWVLRNDnvTSVLIGASKPSQI 304
Cdd:cd19125 205 ------GSPGTTWVKKNVLKDPIVTKV------AEKLGKTPAQVALRWGLQRG--TSVLPKSTNEERI 258
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
25-230 |
1.20e-13 |
|
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like protein is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase similar to Bacillus subtilis glyoxal reductase (YvgN) that reduces glyoxal and methylglyoxal (2-oxopropanal).
Pssm-ID: 381362 [Multi-domain] Cd Length: 262 Bit Score: 69.58 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 25 LPAISLGLWHNFGDatrvENSRALLQRAFDLGITHFDLANNYGpppgsAECNFGRILQeDFLPW----RDELVISTKAGy 100
Cdd:cd19136 1 MPILGLGTFRLRGE----EEVRQAVDAALKAGYRLIDTASVYR-----NEADIGKALR-DLLPKyglsREDIFITSKLA- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 101 tmwdgPYGDWGSRKYliASLDQSLKRMGLEYVDIFYHHRP-----DPETPL-----KETMKALDHLVRQGKALYVGISNY 170
Cdd:cd19136 70 -----PKDQGYEKAR--AACLGSLERLGTDYLDLYLIHWPgvqglKPSDPRnaelrRESWRALEDLYKEGKLRAIGVSNY 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 379053588 171 padRARQAIDILEDLGTPCLIHQpkyslFE---RWVEDGLLALLQEKGVGSIAFSPLAGGQLT 230
Cdd:cd19136 143 ---TVRHLEELLKYCEVPPAVNQ-----VEfhpHLVQKELLKFCKDHGIHLQAYSSLGSGDLR 197
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
21-305 |
1.35e-13 |
|
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde reductase 1 (ARI, EC 1.1.1.2), Trichosporonoides megachilieni NADPH-dependent erthyrose reductase (ER) 1/2 and 3, are founding members of aldo-keto reductase family 3 member B1 (AKR3B1), B2 (AKR3B2), and B3 (AKR3B3), respectively. Sporidiobolus salmonicolor NADPH-ARI, also called alcohol dehydrogenase [NADP(+)], or aldehyde reductase I, or ALR 1, catalyzes the asymmetric reduction of aliphatic and aromatic aldehydes and ketones to an R-enantiomer. It reduces ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Trichosporonoides megachilieni NADPH-ERs catalyze the reduction of D-erythrose.
Pssm-ID: 381344 [Multi-domain] Cd Length: 283 Bit Score: 70.13 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 21 SGIKLPAISLGLWHNFGDATRvensrALLQRAFDLGITHFDLANNYGPPP--GSAecnFGRILQEDFLPWRDELVISTKA 98
Cdd:cd19118 3 TGNKIPAIGLGTWQAEPGEVG-----AAVKIALKAGYRHLDLAKVYQNQHevGQA---LKELLKEEPGVKREDLFITSKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 99 gytmwdgpygdWGSR---KYLIASLDQSLKRMGLEYVDIFYHHRP------------------------DPETPLKETMK 151
Cdd:cd19118 75 -----------WNNShrpEYVEPALDDTLKELGLDYLDLYLIHWPvafkptgdlnpltavptnggevdlDLSVSLVDTWK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 152 ALDHLVRQGKALYVGISNYPADRARqaiDILEDLGTPCLIHQPKYSlfERWVEDGLLALLQEKGVGSIAFSPLAGGQLTD 231
Cdd:cd19118 144 AMVELKKTGKVKSIGVSNFSIDHLQ---AIIEETGVVPAVNQIEAH--PLLLQDELVDYCKSKNIHITAYSPLGNNLAGL 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 379053588 232 RYLNGIPEdsraasgsrflkpeqitadklekvrqLNELAARRGQKLSQMALAWVLRNDNvtSVLIGASKPSQIE 305
Cdd:cd19118 219 PLLVQHPE--------------------------VKAIAAKLGKTPAQVLIAWGIQRGH--SVIPKSVTPSRIR 264
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
21-224 |
2.16e-13 |
|
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol dehydrogenase [NADP(+)] (ALR, EC 1.1.1.2) from Homo sapiens (AKR1A1), Sus scrofa (AKR1A2), Rattus norvegicus (liver, AKR1A3), and Mus musculus (AKR1A4). ALR, also known as aldehyde reductase, or ALDR1, catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid.
Pssm-ID: 381332 [Multi-domain] Cd Length: 305 Bit Score: 69.72 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 21 SGIKLPAISLGLWHNfgDATRVENSralLQRAFDLGITHFDLANNYGpppgsAECNFGRILQEDFLPW----RDELVIST 96
Cdd:cd19106 3 TGQKMPLIGLGTWKS--KPGQVKAA---VKYALDAGYRHIDCAAVYG-----NEQEVGEALKEKVGPGkavpREDLFVTS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 97 KAgytmwdgpygdWGSRKY---LIASLDQSLKRMGLEYVDIFYHHRP------------DP-------ETPLKETMKALD 154
Cdd:cd19106 73 KL-----------WNTKHHpedVEPALRKTLKDLQLDYLDLYLIHWPyafergdnpfpkNPdgtirydSTHYKETWKAME 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 379053588 155 HLVRQGKALYVGISNYpadRARQAIDILEdLGTpcliHQPKYSLFE---RWVEDGLLALLQEKGVGSIAFSPL 224
Cdd:cd19106 142 KLVDKGLVKAIGLSNF---NSRQIDDILS-VAR----IKPAVLQVEchpYLAQNELIAHCKARGLVVTAYSPL 206
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
21-305 |
2.44e-13 |
|
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are founding members of aldo-keto reductase family 3 member A1 (AKR3A1) and A2 (AKR3A2), respectively. Gcy1p, also called galactose-inducible crystallin-like protein 1, is a glycerol dehydrogenase involved in glycerol catabolism under microaerobic conditions. It has mRNA binding activity. Ypr1p acts as a 2-methylbutyraldehyde reductase that displays high specific activity towards 2-methylbutyraldehyde, as well as other aldehydes such as hexanal.
Pssm-ID: 381343 [Multi-domain] Cd Length: 284 Bit Score: 69.06 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 21 SGIKLPAISLGLWHNFGDatrveNSRALLQRAFDLGITHFDLANNYGpppgsAECNFGRILQEDFLPwRDELVISTKagy 100
Cdd:cd19117 10 TGAEIPAVGLGTWQSKPN-----EVAKAVEAALKAGYRHIDTAAIYG-----NEEEVGQGIKDSGVP-REEIFITTK--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 101 tMWdgpyGDWGSRkyLIASLDQSLKRMGLEYVDIFYHHRPDP-------ETPLKE--------------TMKALDHLVRQ 159
Cdd:cd19117 76 -LW----CTWHRR--VEEALDQSLKKLGLDYVDLYLMHWPVPldpdgndFLFKKDdgtkdhepdwdfikTWELMQKLPAT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 160 GKALYVGISNYPADRARqaiDILEDLGTPCLIHQPKYSLFERWVEDGLLALLQEKGVGSIAFSPLaggqltdrylngipe 239
Cdd:cd19117 149 GKVKAIGVSNFSIKNLE---KLLASPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPL--------------- 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 379053588 240 dsrAASGSRFLKPEQITadklekvrqlnELAARRGQKLSQMALAWVLRNDnvTSVLIGASKPSQIE 305
Cdd:cd19117 211 ---GSTNAPLLKEPVII-----------KIAKKHGKTPAQVIISWGLQRG--YSVLPKSVTPSRIE 260
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
22-228 |
4.16e-13 |
|
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B (DkgB) from Corynebacterium sp. and 2,5-diketo-D-gluconic acid reductase Zymomonas mobilis are founding members of aldo-keto reductase family 5 member D1 (AKR5D1) and E1 (AKR5E1), respectively. DkgB (EC 1.1.1.274), also called 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381358 [Multi-domain] Cd Length: 255 Bit Score: 68.07 E-value: 4.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 22 GIKLPAISLGLWHNFGDATrVENSRALLQRAFDLgithFDLANNYGpppgsAECNFGRILQEDFLPwRDELVISTKAgyt 101
Cdd:cd19132 4 GTQIPAIGFGTYPLKGDEG-VEAVVAALQAGYRL----LDTAFNYE-----NEGAVGEAVRRSGVP-REELFVTTKL--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 102 mwdgPYGDWGSRKYLiASLDQSLKRMGLEYVDIFYHHRPDPETPLK-ETMKALDHLVRQGKALYVGISNYPADRARQAID 180
Cdd:cd19132 70 ----PGRHHGYEEAL-RTIEESLYRLGLDYVDLYLIHWPNPSRDLYvEAWQALIEAREEGLVRSIGVSNFLPEHLDRLID 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 379053588 181 ileDLGTPCLIHQpkYSLFERWVEDGLLALLQEKGVGSIAFSPLAGGQ 228
Cdd:cd19132 145 ---ETGVTPAVNQ--IELHPYFPQAEQRAYHREHGIVTQSWSPLGRGS 187
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
21-286 |
1.37e-12 |
|
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes Glycine max NAD(P)H-dependent 6'-deoxychalcone synthase (6DCS, EC 3.1.170), chalcone reductase (CHR, EC 2.3.1.74) from Medicago sativa, Glycyrrhiza echinate, and Glycyrrhiza glabra, which are founding members of aldo-keto reductase family 4 member A1 (AKR4A1), A2 (AKR4A2), A3 (AKR4A3), and A4 (AKR4A4), respectively. NAD(P)H-6DCS co-acts with chalcone synthase in formation of 4,2',4'-trihydroxychalcone, involved in the biosynthesis of glyceollin type phytoalexins. CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. The AKR4B family of AKR includes Sesbania rostrate chalcone reductase (CHR, AKR4B1), Papaver somniferum codeinone reductase (COR, AKR4B2/ AKR4B3), Fragaria x ananassa D-galacturonate reductase (GalUR, AKR4B4), deoxymugineic acid synthase 1 (DMAS1) from Zea mays (AKR4B5), Oryza sativa (AKR4B6), Hordeum vulgare (AKR4B7), Triticum aestivum (AKR4B8), and Erythroxylum coca methylecgonone reductase (MecgoR, AKR4B10). CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. NADPH-dependent COR and non-functional NADPH-dependent COR from Papaver somniferum are founding members of aldo-keto reductase family 4 member B2 (AKR4B2) and B3 (AKR4B3), respectively. NADPH-dependent COR (EC 1.1.1.247) reduces codeinone to codeine in the penultimate step in morphine biosynthesis. It can use morphinone, hydrocodone, and hydromorphone as substrates during reductive reaction with NADPH as cofactor, and morphine and dihydrocodeine as substrates during oxidative reaction with NADP as cofactor. GalUR (EC 1.1.1.365), also called aldo-keto reductase 2 (AKR2), is involved in ascorbic acid (vitamin C) biosynthesis by catalyzing the conversion from L-galactonate and NADP(+) to D-galacturonate and NADPH. DMAS1 (EC 1.1.1.285) catalyzes the reduction of a 3''-keto intermediate during the biosynthesis of 2'-deoxymugineic acid (DMA) from L-Met. It is involved in the formation of phytosiderophores (MAs) belonging to the mugineic acid family and required to acquire iron. MecgoR catalyzes the stereospecific reduction of methylecgonone to methylecgonine, the penultimate step in cocaine biosynthesis.
Pssm-ID: 381350 [Multi-domain] Cd Length: 281 Bit Score: 66.91 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 21 SGIKLPAISLGlwhNFGDATRVENSRALLQRAFDLGITHFDLANNYGpppgsAECNFGRILQEDF----LPWRDELVIST 96
Cdd:cd19124 1 SGQTMPVIGMG---TASDPPSPEDIKAAVLEAIEVGYRHFDTAAAYG-----TEEALGEALAEALrlglVKSRDELFVTS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 97 KagytMW--DGPYGDwgsrkyLIASLDQSLKRMGLEYVDIFYHHRP------------DPETPL----KETMKALDHLVR 158
Cdd:cd19124 73 K----LWcsDAHPDL------VLPALKKSLRNLQLEYVDLYLIHWPvslkpgkfsfpiEEEDFLpfdiKGVWEAMEECQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 159 QGKALYVGISNYPADRARqaiDILEDLGTPCLIHQPKYSLfeRWVEDGLLALLQEKGVGSIAFSPLAGGqltdrylnGIP 238
Cdd:cd19124 143 LGLTKAIGVSNFSCKKLQ---ELLSFATIPPAVNQVEMNP--AWQQKKLREFCKANGIHVTAYSPLGAP--------GTK 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 379053588 239 EDSRAASGSRFLKpeqitadklekvrqlnELAARRGQKLSQMALAWVL 286
Cdd:cd19124 210 WGSNAVMESDVLK----------------EIAAAKGKTVAQVSLRWVY 241
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
20-327 |
1.45e-12 |
|
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a founding member of aldo-keto reductase family 3 member G1 (AKR3G1). It is an aldo/keto reductase that catalyzes the NADPH-dependent reduction of aldehyde- and ketone-groups of different classes of carbonyl compounds to the corresponding alcohols.
Pssm-ID: 381349 [Multi-domain] Cd Length: 297 Bit Score: 67.05 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 20 RSGIKLPAISLGLWhnfgDATRVENSRALlQRAFDLGITHFDLANNYGpppgsAECNFGRILQEDF---LPWRDELVIST 96
Cdd:cd19123 7 SNGDLIPALGLGTW----KSKPGEVGQAV-KQALEAGYRHIDCAAIYG-----NEAEIGAALAEVFkegKVKREDLWITS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 97 KagytMWDgpygDWGSRKYLIASLDQSLKRMGLEYVDIFYHHRP------------------DPETPLKETMKALDHLVR 158
Cdd:cd19123 77 K----LWN----NSHAPEDVLPALEKTLADLQLDYLDLYLMHWPvalkkgvgfpesgedllsLSPIPLEDTWRAMEELVD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 159 QGKALYVGISNYPADRARqaiDILEDLGTPCLIHQPKYSLFERWVEdgLLALLQEKGVGSIAFSPLAGGqltDRylngiP 238
Cdd:cd19123 149 KGLCRHIGVSNFSVKKLE---DLLATARIKPAVNQVELHPYLQQPE--LLAFCRDNGIHLTAYSPLGSG---DR-----P 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 239 EDSRAASGSRFLKPEQItadklekvrqlNELAARRGQKLSQMALAWVLRNDnvTSVLIGASKPSQIEdavgmlANrrFSA 318
Cdd:cd19123 216 AAMKAEGEPVLLEDPVI-----------NKIAEKHGASPAQVLIAWAIQRG--TVVIPKSVNPERIQ------QN--LEA 274
|
330
....*....|...
gi 379053588 319 TEC----AEIDAI 327
Cdd:cd19123 275 AEVeldaSDMATI 287
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
22-228 |
1.65e-12 |
|
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid reductase (2,5-DKG reductase) is a founding member of aldo-keto reductase family 5 member F1 (AKR5F1). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381359 [Multi-domain] Cd Length: 255 Bit Score: 66.44 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 22 GIKLPAISLGLWHNFGDAtrvENSRALLQrAFDLGITHFDLANNYGpppgsAECNFGRILQEDFLPwRDELVISTKagyt 101
Cdd:cd19133 6 GVEMPILGFGVFQIPDPE---ECERAVLE-AIKAGYRLIDTAAAYG-----NEEAVGRAIKKSGIP-REELFITTK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 102 MWDGPYGDWGSRKyliaSLDQSLKRMGLEYVDIFYHHRP--DpetpLKETMKALDHLVRQGKALYVGISNYPADRarqAI 179
Cdd:cd19133 72 LWIQDAGYEKAKK----AFERSLKRLGLDYLDLYLIHQPfgD----VYGAWRAMEELYKEGKIRAIGVSNFYPDR---LV 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 379053588 180 DILEDLGTPCLIHQPKYSLFerWVEDGLLALLQEKGVGSIAFSPLAGGQ 228
Cdd:cd19133 141 DLILHNEVKPAVNQIETHPF--NQQIEAVEFLKKYGVQIEAWGPFAEGR 187
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
26-305 |
2.02e-12 |
|
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), also called aldehyde reductase, is the prototype of this family. It catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
Pssm-ID: 381354 [Multi-domain] Cd Length: 277 Bit Score: 66.39 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 26 PAISLGLWHnfgdATRVENSRALlQRAFDLGITHFDLANNYGPPPGSAECnFGRILQEDFLPwRDELVISTKAGYTMwdg 105
Cdd:cd19128 2 PRLGFGTYK----ITESESKEAV-KNAIKAGYRHIDCAYYYGNEAFIGIA-FSEIFKDGGVK-REDLFITSKLWPTM--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 106 pygdwgSRKYLIA-SLDQSLKRMGLEYVDIFYHHRP-------------------DPETPLKETMKALDHLVRQGKALYV 165
Cdd:cd19128 72 ------HQPENVKeQLLITLQDLQLEYLDLFLIHWPlafdmdtdgdprddnqiqsLSKKPLEDTWRAMEQCVDEKLTKNI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 166 GISNYpadrarqAIDILEDLGTPCLIhQPKYSLFERWVE---DGLLALLQEKGVGSIAFSPLAGGQLTDRylNGIPEDSr 242
Cdd:cd19128 146 GVSNY-------STKLLTDLLNYCKI-KPFMNQIECHPYfqnDKLIKFCIENNIHVTAYRPLGGSYGDGN--LTFLNDS- 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 379053588 243 aasgsrflkpeqitadklekvrQLNELAARRGQKLSQMALAW-VLRNDNVTSVLIGASKPSQIE 305
Cdd:cd19128 215 ----------------------ELKALATKYNTTPPQVIIAWhLQKWPKNYSVIPKSANKSRCQ 256
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
25-330 |
4.40e-12 |
|
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding member of aldo-keto reductase family 5 member H1 (AKR5H1). It is a NADPH-dependent aldo-keto reductase that reduces methylglyoxal and phenylglyoxal.
Pssm-ID: 381360 [Multi-domain] Cd Length: 263 Bit Score: 65.26 E-value: 4.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 25 LPAISLGLWhnfgDATRVENSRALLQrAFDLGITHFDLANNYGpppgsAECNFGRILQEDFLPwRDELVISTKagytMWD 104
Cdd:cd19134 11 MPVIGLGVG----ELSDDEAERSVSA-ALEAGYRLIDTAAAYG-----NEAAVGRAIAASGIP-RGELFVTTK----LAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 105 GPYGDWGSRKYLIASLDqslkRMGLEYVDIFYHHRPDP-ETPLKETMKALDHLVRQGKALYVGISNYPADRARQAIDIle 183
Cdd:cd19134 76 PDQGFTASQAACRASLE----RLGLDYVDLYLIHWPAGrEGKYVDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDL-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 184 DLGTPCLihqPKYSLFERWVEDGLLALLQEKGVGSIAFSPLAGGQLTDrylngipedsraasgsrflKPEqITAdklekv 263
Cdd:cd19134 150 TFFTPAV---NQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGRLLD-------------------NPA-VTA------ 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 379053588 264 rqlneLAARRGQKLSQMALAWVLRNDNVtsVLIGASKPSQIEDAVGMLaNRRFSATECAEIDAILDG 330
Cdd:cd19134 201 -----IAAAHGRTPAQVLLRWSLQLGNV--VISRSSNPERIASNLDVF-DFELTADHMDALDGLDDG 259
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
21-222 |
5.75e-12 |
|
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent D-xylose reductase (XR) from Pichia stipites, Kluyveromyces lactis, Pachysolen tannophilus, Candida tropicalis, and Candida tenuis, Gre3p from Saccharomyces cerevisiae, XR from Candida tropicalis, Pichia guilliermondii, Debaryomyces hansenli, and Debaryomyces nepalensis, which correspond to aldo-keto reductase family 2 member B1-B10 (AKR2B1-10), respectively. XR (EC1.1.1.307) catalyzes the NAD(P)H dependent reduction of xylose to xylitol.
Pssm-ID: 381339 [Multi-domain] Cd Length: 310 Bit Score: 65.55 E-value: 5.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 21 SGIKLPAISLGLWhnfgdatRVENSRALLQ--RAFDLGITHFDLANNYGPPPGSAEcNFGRILQEDFLPwRDELVISTKa 98
Cdd:cd19113 7 SGYKMPSVGFGCW-------KLDNATAADQiyQAIKAGYRLFDGAEDYGNEKEVGE-GVNRAIDEGLVK-REELFLTSK- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 99 gytMWDgpygDWGSRKYLIASLDQSLKRMGLEYVDIFYHHRP-------------------------DPETPLKETMKAL 153
Cdd:cd19113 77 ---LWN----NFHDPKNVETALNKTLSDLKLDYVDLFLIHFPiafkfvpieekyppgfycgdgdnfvYEDVPILDTWKAL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 379053588 154 DHLVRQGKALYVGISNYPAdrarqaiDILEDLGTPCLI--------HQPkYSLFERWVEdgllaLLQEKGVGSIAFS 222
Cdd:cd19113 150 EKLVDAGKIKSIGVSNFPG-------ALILDLLRGATIkpavlqieHHP-YLQQPKLIE-----YAQKAGITITAYS 213
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
22-170 |
1.02e-11 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381337 [Multi-domain] Cd Length: 286 Bit Score: 64.44 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 22 GIKLPAISLGLWHNFGDATRvensrALLQRAFDLGITHFDLANNYGpppgsAECNFGRILQEdflpW-------RDELVI 94
Cdd:cd19111 1 GFPMPVIGLGTYQSPPEEVR-----AAVDYALFVGYRHIDTALSYQ-----NEKAIGEALKW----WlkngklkREEVFI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 95 STKAgytmWdgPYGDwgSRKYLIASLDQSLKRMGLEYVDIFYHH-------------RPDPETPLKETMKALDHLVRQGK 161
Cdd:cd19111 67 TTKL----P--PVYL--EFKDTEKSLEKSLENLKLPYVDLYLIHhpcgfvnkkdkgeRELASSDVTSVWRAMEALVSEGK 138
|
....*....
gi 379053588 162 ALYVGISNY 170
Cdd:cd19111 139 VKSIGLSNF 147
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
21-227 |
5.47e-11 |
|
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar proteins; Saccharomyces cerevisiae Ara1p (EC 1.1.1.117), also called D-arabinose 1-dehydrogenase (NAD(P)(+)), is a founding members of aldo-keto reductase family 3 member C1 (AKR3C1). It catalyzes the oxidation of D-arabinose, L-xylose, L-fucose, and L-galactose in the presence of NADP(+).
Pssm-ID: 381345 [Multi-domain] Cd Length: 294 Bit Score: 62.51 E-value: 5.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 21 SGIKLPAISLGLWHnfgDATRVENSRALLQRAFDLGITHFDLANNYGPPPGSAECnFGRILQEDFLPwRDELVISTKAGY 100
Cdd:cd19119 8 TGASIPALGLGTAS---PHEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEA-IKRAIDDGSIK-REELFITTKVWP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 101 TMWDgpygdwgsrkYLIASLDQSLKRMGLEYVDIFYHHRPDP------ETPLK-------------------ETMKALDH 155
Cdd:cd19119 83 TFYD----------EVERSLDESLKALGLDYVDLLLVHWPVCfekdsdDSGKPftpvnddgktryaasgdhiTTYKQLEK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 379053588 156 LVRQGKALYVGISNYpadrarqAIDILEDLGTPCLIhQPKYSLFE---RWVEDGLLALLQEKGVGSIAFSPLAGG 227
Cdd:cd19119 153 IYLDGRAKAIGVSNY-------SIVYLERLIKECKV-VPAVNQVElhpHLPQMDLRDFCFKHGILVTAYSPLGSH 219
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
22-327 |
6.52e-11 |
|
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; Corynebacterium sp. DkgA is a founding member of aldo-keto reductase family 5 member C1 (AKR5C1). DkgA (EC 1.1.1.346), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates.
Pssm-ID: 381356 [Multi-domain] Cd Length: 256 Bit Score: 61.85 E-value: 6.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 22 GIKLPAISLGLWhNFGDAtrvENSRALlQRAFDLGITHFDLANNYGPPPGsaecnFGRILQEDFLPwRDELVISTKagyt 101
Cdd:cd19130 7 GNSIPQLGYGVF-KVPPA---DTQRAV-ATALEVGYRHIDTAAIYGNEEG-----VGAAIAASGIP-RDELFVTTK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 102 MWDGPYGDWGSRkyliASLDQSLKRMGLEYVDIFYHHRPDPETPLK-ETMKALDHLVRQGKALYVGISNY-PADRARqai 179
Cdd:cd19130 72 LWNDRHDGDEPA----AAFAESLAKLGLDQVDLYLVHWPTPAAGNYvHTWEAMIELRAAGRTRSIGVSNFlPPHLER--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 180 dILEDLGTPCLIHQpkYSLFERWVEDGLLALLQEKGVGSIAFSPLagGQltdrylngipedsraasGSRFLKPeqitadk 259
Cdd:cd19130 145 -IVAATGVVPAVNQ--IELHPAYQQRTIRDWAQAHDVKIEAWSPL--GQ-----------------GKLLGDP------- 195
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 379053588 260 lekvrQLNELAARRGQKLSQMALAWVLRNDNVtsVLIGASKPSQIEDAVGMLaNRRFSATECAEIDAI 327
Cdd:cd19130 196 -----PVGAIAAAHGKTPAQIVLRWHLQKGHV--VFPKSVRRERMEDNLDVF-DFDLTDTEIAAIDAL 255
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
21-277 |
1.04e-10 |
|
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, EC 1.1.1.365), also called D-galacturonic acid reductase, or GalUR, is a founding member of aldo-keto reductase family 3 member D1 (AKR3D1). It mediates the reduction of D-galacturonate to L-galactonate, the first step in D-galacturonate catabolic process. It also has activity with D-glucuronate and DL-glyceraldehyde. Its activity is seen only with NADPH and not with NADH.
Pssm-ID: 381347 [Multi-domain] Cd Length: 279 Bit Score: 61.39 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 21 SGIKLPAISLGLWHnfGDATRVensRALLQRAFDLGITHFDLANNYGpppgsAECNFGRILQEDFLPW--RDELVISTKA 98
Cdd:cd19121 8 TGASIPAVGLGTWQ--AKAGEV---KAAVAHALKIGYRHIDGALCYQ-----NEDEVGEGIKEAIAGGvkREDLFVTTKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 99 GYTMWDGPygdwgsrkylIASLDQSLKRMGLEYVDIFYHHRP--------DPETPLKE--------------TMKALDHL 156
Cdd:cd19121 78 WSTYHRRV----------ELCLDRSLKSLGLDYVDLYLVHWPvllnpngnHDLFPTLPdgsrdldwdwnhvdTWKQMEKV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 157 VRQGKALYVGISNYpadrarqAIDILEDLgTPCLIHQPKYSLFE---RWVEDGLLALLQEKGVGSIAFSPL--AGGQL-T 230
Cdd:cd19121 148 LKTGKTKAIGVSNY-------SIPYLEEL-LKHATVVPAVNQVEnhpYLPQQELVDFCKEKGILIEAYSPLgsTGSPLiS 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 379053588 231 DRYLNGIPEDSRAASGSRFLK----------PEQITADKLEKVRQLNELAARRGQKL 277
Cdd:cd19121 220 DEPVVEIAKKHNVGPGTVLISyqvargavvlPKSVTPDRIKSNLEIIDLDDEDMNKL 276
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-305 |
2.26e-10 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 60.82 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 19 GRSGIklpaISLGLWHNFGDATRVENSRA----LLQRAFDLGITHFDLANNYGpppgsaecnfgriLQEDFL-------- 86
Cdd:cd19098 11 GRPGY----INLGHAADLGSGRSVEAMRAhthaVLDAAWAAGVRYFDAARSYG-------------RAEEFLgswlrsrn 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 87 PWRDELVISTKAGYTmwdgpY-GDWG-----------SRKYLIASLDQSLKRMGlEYVDIFYHHRPDPETPLKETMKALD 154
Cdd:cd19098 74 IAPDAVFVGSKWGYT-----YtADWQvdaavhevkdhSLARLLKQWEETRSLLG-KHLDLYQIHSATLESGVLEDADVLA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 155 HLVRQGKA-LYVGISNYPADRA---RQAIDILEDLGTPCLIHQPKYSLFERWVEDgLLALLQEKGVGSIAFSPLAGGQLT 230
Cdd:cd19098 148 ALAELKAEgVKIGLSLSGPQQAetlRRALEIEIDGARLFDSVQATWNLLEQSAGE-ALEEAHEAGMGVIVKEALANGRLT 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 379053588 231 DRylNGIPEDsraasgsrflkpeqitadkLEKVRQLNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIE 305
Cdd:cd19098 227 DR--NPSPEL-------------------APLMAVLKAVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLR 280
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
22-306 |
4.66e-09 |
|
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family.
Pssm-ID: 381355 [Multi-domain] Cd Length: 295 Bit Score: 56.70 E-value: 4.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 22 GIKLPAISLGLWhnFGDATRVENSralLQRAFDLGITHFDLANNYgpppgSAECNFGRILQEDFLPW---RDELVISTKa 98
Cdd:cd19129 3 SGAIPALGFGTL--IPDPSATRNA---VKAALEAGFRHFDCAERY-----RNEAEVGEAMQEVFKAGkirREDLFVTTK- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 99 gytMWDGPYgdwgsRKYLIA-SLDQSLKRMGLEYVDIFYHHRP------DPETP--------------LKETMKALDHLV 157
Cdd:cd19129 72 ---LWNTNH-----RPERVKpAFEASLKRLQLDYLDLYLIHTPfafqpgDEQDPrdangnviyddgvtLLDTWRAMERLV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 158 RQGKALYVGISNYPADRARQAIDILEDlgTPCLIHQPKYSLFERWvedGLLALLQEKGVGSIAFSPLAGGqltdrylngi 237
Cdd:cd19129 144 DEGRCKAIGLSDVSLEKLREIFEAARI--KPAVVQVESHPYLPEW---ELLDFCKNHGIVLQAFAPLGHG---------- 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 379053588 238 pedsraaSGSRFLKPEQITAdklekvrqlneLAARRGQKLSQMALAWVLRNDnvTSVLIGASKPSQIED 306
Cdd:cd19129 209 -------MEPKLLEDPVITA-----------IARRVNKTPAQVLLAWAIQRG--TALLTTSKTPSRIRE 257
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
22-170 |
2.71e-08 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 54.31 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 22 GIKLPAISLGLWhnfgdATRVENSRALLQRAFDLGITHFDLANNYGpppgsAECNFGRILQEDFLPwRDELVISTKagyt 101
Cdd:PRK11565 12 GNVMPQLGLGVW-----QASNEEVITAIHKALEVGYRSIDTAAIYK-----NEEGVGKALKEASVA-REELFITTK---- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 102 MWDGPYGDWGsrkyliASLDQSLKRMGLEYVDIFYHHRPDPETPLK-ETMKALDHLVRQGKALYVGISNY 170
Cdd:PRK11565 77 LWNDDHKRPR------EALEESLKKLQLDYVDLYLMHWPVPAIDHYvEAWKGMIELQKEGLIKSIGVCNF 140
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
22-170 |
1.39e-07 |
|
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.
Pssm-ID: 381340 [Multi-domain] Cd Length: 302 Bit Score: 52.17 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 22 GIKLPAISLGLWHnfgdaTRVENSRALLQRAFDLGITHFDLANNYGpppgsAECNFGRILQ---EDFLPWRDELVISTKa 98
Cdd:cd19114 1 GDKMPLVGFGTAK-----IKANETEEVIYNAIKVGYRLIDGALLYG-----NEAEVGRGIRkaiQEGLVKREDLFIVTK- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 99 gytMWDgpygDWGSRKYLIASLDQSLKRMGLEYVDIFYHHRP-----------------DPET--------PLKETMKAL 153
Cdd:cd19114 70 ---LWN----NFHGKDHVREAFDRQLKDYGLDYIDLYLIHFPipaayvdpaenypflwkDKELkkfpleqsPMQECWREM 142
|
170
....*....|....*..
gi 379053588 154 DHLVRQGKALYVGISNY 170
Cdd:cd19114 143 EKLVDAGLVRNIGIANF 159
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
21-172 |
6.09e-07 |
|
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose reductase xyl1 (XR, EC 1.1.1.307) is a founding member of aldo-keto reductase family 2 member D1 (AKR2D1). It catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol in a NAD(P)H dependent manner.
Pssm-ID: 381341 [Multi-domain] Cd Length: 311 Bit Score: 50.11 E-value: 6.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 21 SGIKLPAISLGLWhnfgdatRVENSRALLQ--RAFDLGITHFDLANNYGpppGSAECNFG--RILQEDFLPwRDELVIST 96
Cdd:cd19115 9 SGYDMPLVGFGLW-------KVNNDTCADQvyNAIKAGYRLFDGACDYG---NEVEAGQGvaRAIKEGIVK-REDLFIVS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 97 KAGYTMWDGPYGDWGSRKyliasldqSLKRMGLEYVDIFYHHRP------DPE------------------TPLKETMKA 152
Cdd:cd19115 78 KLWNTFHDGERVEPICRK--------QLADWGIDYFDLFLIHFPialkyvDPAvryppgwfydgkkvefsnAPIQETWTA 149
|
170 180
....*....|....*....|
gi 379053588 153 LDHLVRQGKALYVGISNYPA 172
Cdd:cd19115 150 MEKLVDKGLARSIGVSNFSA 169
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
22-304 |
1.52e-06 |
|
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381381 [Multi-domain] Cd Length: 307 Bit Score: 49.06 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 22 GIKLPAISLGLWHnfGDATRVEnsrALLQRAFDLGITHFDLANNYGpppgsAECNFGRILQEdflpW-------RDELVI 94
Cdd:cd19155 9 GEKMPVVGLGTWQ--SSPEEIE---TAVDTALEAGYRHIDTAYVYR-----NEAAIGNVLKK----WidsgkvkREELFI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 95 STKAgytmwdgPYGdwGSRKYLIAS-LDQSLKRMGLEYVDIFYHHRP---------------------DPETPLKETMKA 152
Cdd:cd19155 75 VTKL-------PPG--GNRREKVEKfLLKSLEKLQLDYVDLYLIHFPvgslskeddsgkldptgehkqDYTTDLLDIWKA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 153 LDHLVRQGKALYVGISNYpadRARQAIDILEDLGT-PCLIHQPKYSLFErwvEDGLLALLQEKGVGSIAFSPLAGgqltd 231
Cdd:cd19155 146 MEAQVDQGLTRSIGLSNF---NREQMARILKNARIkPANLQVELHVYLQ---QKDLVDFCSTHSITVTAYAPLGS----- 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 379053588 232 rylNGIPEDSRAASGSRFLKPeqitadKLEKVRQLNELAARRGQKLSQMALAWVLRNDnvTSVLIGASKPSQI 304
Cdd:cd19155 215 ---PGAAHFSPGTGSPSGSSP------DLLQDPVVKAIAERHGKSPAQVLLRWLMQRG--VVVIPKSTNAARI 276
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
24-226 |
9.78e-06 |
|
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) from Mus musculus (liver, AKR1E1) and Homo sapiens (AKR1E2). 1,5-anhydro-D-fructose reductase), also called AF reductase, or aldo-keto reductase family 1 member C-like protein 2 (AKR1CL2), catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. AKR1E2 is a testis aldo-keto reductase (tAKR), which is also known as testis-specific protein (TSP), or LoopADR.
Pssm-ID: 381336 [Multi-domain] Cd Length: 301 Bit Score: 46.49 E-value: 9.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 24 KLPAISLGLWHnfgdATRVENSRALlQRAFDLGITHFDLANNYgpppgSAECNFGRILQEDF---LPWRDELVISTKagy 100
Cdd:cd19110 3 DIPAVGLGTWK----ASPGEVTEAV-KVAIDAGYRHFDCAYLY-----HNESEVGAGIREKIkegVVRREDLFIVSK--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 101 tMWDGPYgdwgsRKYLIAS-LDQSLKRMGLEYVDIFYHHRP------DPETPLKE-------------TMKALDHLVRQG 160
Cdd:cd19110 70 -LWCTCH-----KKSLVKTaCTRSLKALKLNYLDLYLIHWPmgfkpgEPDLPLDRsgmvipsdtdfldTWEAMEDLVIEG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 379053588 161 KALYVGISNYPADRARQAIDiledlgTPCLIHQPKYSLFE---RWVEDGLLALLQEKGVGSIAFSPLAG 226
Cdd:cd19110 144 LVKNIGVSNFNHEQLERLLN------KPGLRVKPVTNQIEchpYLTQKKLISFCQSRNVSVTAYRPLGG 206
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
22-224 |
1.14e-05 |
|
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase (AR, EC 1.1.1.21) from Homo sapiens (AKR1B1), Oryctolagus cuniculus (kidney, AKR1B2), Mus musculus (AKR1B3), Rattus norvegicus (lens, AKR1B4), Bos taurus (lens/testis, AKR1B5), and Sus scrofa (lens, AKR1B6), aldose reductase-related protein 1 (ALD1, EC1.1.1.21) from Mus musculus (AKR1B7), Rattus norvegicus (AKR1B14), and Homo sapiens (AKR1B15), Mus musculus fibroblast growth factor induced protein (FR-1 or AKR1B8, EC 1.1.1.21), Cricetulus griseus aldose reductase-related protein 2 (ALD2 or AKR1B9, EC 1.1.1.21), aldose reductase-like from Homo sapiens (ARL-1 or AKR1B10) and Rattus norvegicus (AKR1B13), aldo-keto reductase from Gallus domesticus (eye, tongue, esophagus, AKR1B12), and Oryctolagus cuniculus AR-like protein (3beta-HSD, AKR1B19). AR, also called aldehyde reductase, catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. ALD1 reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. It may play a role in the metabolism of xenobiotic aromatic aldehydes. FR-1, also called aldose reductase-related protein 2, or fibroblast growth factor-regulated protein (FGFRP), is induced by fibroblast growth factor-1. It may play a role in the regulation of the cell cycle. FR-1 belongs to the NADPH-dependent aldo-keto reductase family. ALD2 is an inducible aldo-keto reductase with a preference for aliphatic substrates. It can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. ARL-1, also called aldose reductase-like, or aldose reductase-related protein (ARP), or small intestine reductase, or SI reductase, acts as all-trans-retinaldehyde reductase that can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). It may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. AKR1B15, also called estradiol 17-beta-dehydrogenase AKR1B15, is a mitochondrial aldo-keto reductase that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. It has a strong selectivity towards NADP(H). AKR1B19 is aldose reductase-like that may show 3-beta-hydroxysteroid dehydrogenase (3beta-HSD) activity.
Pssm-ID: 381333 [Multi-domain] Cd Length: 307 Bit Score: 46.26 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 22 GIKLPAISLGLWHN-FGDATRVensralLQRAFDLGITHFDLANNYgpppgSAECNFGRILQEDF---LPWRDELVISTK 97
Cdd:cd19107 1 GAKMPILGLGTWKSpPGQVTEA------VKVAIDAGYRHIDCAYVY-----QNENEVGEAIQEKIkeqVVKREDLFIVSK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 98 AGYTMWDgpygdwgsRKYLIASLDQSLKRMGLEYVDIFYHHRPD-------------------PETPLKETMKALDHLVR 158
Cdd:cd19107 70 LWCTFHE--------KGLVKGACQKTLSDLKLDYLDLYLIHWPTgfkpgkelfpldesgnvipSDTTFLDTWEAMEELVD 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 379053588 159 QGKALYVGISNYpadrARQAIDILedLGTPCLIHQPKYSLFE---RWVEDGLLALLQEKGVGSIAFSPL 224
Cdd:cd19107 142 EGLVKAIGVSNF----NHLQIERI--LNKPGLKYKPAVNQIEchpYLTQEKLIQYCQSKGIVVTAYSPL 204
|
|
| Alpha_L_fucos |
pfam01120 |
Alpha-L-fucosidase; |
93-146 |
1.65e-03 |
|
Alpha-L-fucosidase;
Pssm-ID: 460072 Cd Length: 333 Bit Score: 39.88 E-value: 1.65e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 379053588 93 VISTK--AGYTMWDGPYGDW-----GSRKYLIASLDQSLKRMGLEYvdIFYHHRPDPETPL 146
Cdd:pfam01120 102 VLTTKhhDGFTMWDSKYSDWnsvdvGPKRDLVGELAKAVRKQGLKF--GLYYSLADWFNPD 160
|
|
| PRK14863 |
PRK14863 |
bifunctional regulator KidO; Provisional |
40-308 |
5.81e-03 |
|
bifunctional regulator KidO; Provisional
Pssm-ID: 184865 [Multi-domain] Cd Length: 292 Bit Score: 37.97 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 40 TRVENSRALLQRAFDLGITHFDLANNYGpppgSAECNFGRILQEDfLPWRdeLVISTKAgytMWDGPygdwgsrKYLIAS 119
Cdd:PRK14863 29 TPEAEARDILNIAARAGLSVLDASGLFG----RAETVLGQLIPRP-VPFR--VTLSTVR---ADRGP-------DFVEAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 120 LDQSLKRMGLEYVDIFYHHRPD----PETP-LKETMKALDHlvrQGKALYVGISNYPAD-----RARQAIDILEdlgTPC 189
Cdd:PRK14863 92 ARASLRRMGVERADAILVHSPTelfgPHGAaLWERLQALKD---QGLFAKIGVSAHASDdpvgvARRFKPDILQ---APA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379053588 190 LIhqpkysLFERWVEDGLLALLQEKGVGSiafsplaggQLTDRYLNGIpedsraasgsRFLKPEQITAD------KLEKV 263
Cdd:PRK14863 166 SL------LDQRLLADGSLQRIAGMGVEV---------HLRSIFLNGL----------LFLPPDRVPAQlkgasgRLSRV 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 379053588 264 RQLneLAARRGQKLsQMALAWVLRNDNVTSVLIGASKPSQIEDAV 308
Cdd:PRK14863 221 RRM--IAEGRSDPL-QAALGFALSRPEGSAVLVGVNSAAELSAVV 262
|
|
| HAD_PPase |
cd02616 |
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ... |
122-178 |
7.25e-03 |
|
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX which hydrolyzes pyrophosphate formed during serine-46-phosphorylated HPr (P-Ser-HPr) dephosphorylation by the bifunctional enzyme HPr kinase/phosphorylase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.
Pssm-ID: 319797 [Multi-domain] Cd Length: 207 Bit Score: 37.26 E-value: 7.25e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 379053588 122 QSLKRMGL-EYVDI------FYHHRPDPEtPLKETMKALDhlVRQGKALYVGISNYPADRARQA 178
Cdd:cd02616 112 KGLKLLGLdKYFDVivggddVTHHKPDPE-PVLKALELLG--AEPEEALMVGDSPHDILAGKNA 172
|
|
| |
