|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
1-279 |
0e+00 |
|
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: 573.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 1 MGDIPAVGLSSWKASPGKVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIRCKIKEGAVRREDLFIATKLWCTCHKKSLV 80
Cdd:cd19110 1 MEDIPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 81 ETACRKSLKALKLNYLDLYLIHWPMGFKPPHPewimscselsfclshprvqDLPLDESNMVIPSDTDFLDTWEAMEDLVI 160
Cdd:cd19110 81 KTACTRSLKALKLNYLDLYLIHWPMGFKPGEP-------------------DLPLDRSGMVIPSDTDFLDTWEAMEDLVI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 161 TGLVKNIGVSNFNHEQLERLLNKPGLRFKPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLGGSCEGVDLIDNPVIKR 240
Cdd:cd19110 142 EGLVKNIGVSNFNHEQLERLLNKPGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSCEGVDLIDDPVIQR 221
|
250 260 270
....*....|....*....|....*....|....*....
gi 1370457959 241 IAKEHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENIQ 279
Cdd:cd19110 222 IAKKHGKSPAQILIRFQIQRNVIVIPKSVTPSRIKENIQ 260
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
4-279 |
5.93e-157 |
|
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: 439.16 E-value: 5.93e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSWKASPGKVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIRCKIKEGAVRREDLFIATKLWCTCHKKSLVETA 83
Cdd:cd19107 4 MPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEKGLVKGA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 84 CRKSLKALKLNYLDLYLIHWPMGFKPPhpewimscSELsfclshprvqdLPLDESNMVIPSDTDFLDTWEAMEDLVITGL 163
Cdd:cd19107 84 CQKTLSDLKLDYLDLYLIHWPTGFKPG--------KEL-----------FPLDESGNVIPSDTTFLDTWEAMEELVDEGL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 164 VKNIGVSNFNHEQLERLLNKPGLRFKPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLG------GSCEGVDLIDNPV 237
Cdd:cd19107 145 VKAIGVSNFNHLQIERILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGspdrpwAKPEDPSLLEDPK 224
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1370457959 238 IKRIAKEHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENIQ 279
Cdd:cd19107 225 IKEIAAKHNKTTAQVLIRFPIQRNLVVIPKSVTPERIAENFK 266
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
4-279 |
1.99e-123 |
|
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: 352.17 E-value: 1.99e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSWKASPGKVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIRCKIkegaVRREDLFIATKLWCTCHKKSLVETA 83
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESG----VPREELFITTKLWPTDHGYERVREA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 84 CRKSLKALKLNYLDLYLIHWPMGFKPPhpewimscselsfclshprvqdlpldesnmviPSDTDFLDTWEAMEDLVITGL 163
Cdd:cd19071 77 LEESLKDLGLDYLDLYLIHWPVPGKEG--------------------------------GSKEARLETWRALEELVDEGL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 164 VKNIGVSNFNHEQLERLLNKPglRFKPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLGGSceGVDLIDNPVIKRIAK 243
Cdd:cd19071 125 VRSIGVSNFNVEHLEELLAAA--RIKPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRG--RRPLLDDPVLKEIAK 200
|
250 260 270
....*....|....*....|....*....|....*.
gi 1370457959 244 EHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENIQ 279
Cdd:cd19071 201 KYGKTPAQVLLRWALQRGVVVIPKSSNPERIKENLD 236
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
4-279 |
3.96e-119 |
|
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: 342.72 E-value: 3.96e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSWKA-SPGKVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIRCKIKEGAVRREDLFIATKLWCTCHKKSLVET 82
Cdd:cd19116 11 IPAIALGTWKLkDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLWNSYHEREQVEP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 83 ACRKSLKALKLNYLDLYLIHWPMGFKpphpewimscselsfclshprvQDLPLDESNMVIPSDTDFLDTWEAMEDLVITG 162
Cdd:cd19116 91 ALRESLKRLGLDYVDLYLIHWPVAFK----------------------ENNDSESNGDGSLSDIDYLETWRGMEDLVKLG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 163 LVKNIGVSNFNHEQLERLLNkpGLRFKPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLG-----GSCEGVDLIDNPV 237
Cdd:cd19116 149 LTRSIGVSNFNSEQINRLLS--NCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGrlvprGQTNPPPRLDDPT 226
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1370457959 238 IKRIAKEHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENIQ 279
Cdd:cd19116 227 LVAIAKKYGKTTAQIVLRYLIDRGVVPIPKSSNKKRIKENID 268
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
3-279 |
6.21e-119 |
|
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: 342.83 E-value: 6.21e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 3 DIPAVGLSSWKASPGKVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIRCKIKEG-AVRREDLFIATKLWCTCHKKSLVE 81
Cdd:cd19106 6 KMPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPGkAVPREDLFVTSKLWNTKHHPEDVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 82 TACRKSLKALKLNYLDLYLIHWPMGFKPPHpewimscselsfclshprvQDLPLDESNMVIPSDTDFLDTWEAMEDLVIT 161
Cdd:cd19106 86 PALRKTLKDLQLDYLDLYLIHWPYAFERGD-------------------NPFPKNPDGTIRYDSTHYKETWKAMEKLVDK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 162 GLVKNIGVSNFNHEQLERLLNKPglRFKPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLGG-------SCEGVdLID 234
Cdd:cd19106 147 GLVKAIGLSNFNSRQIDDILSVA--RIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSpdrpwakPDEPV-LLE 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1370457959 235 NPVIKRIAKEHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENIQ 279
Cdd:cd19106 224 EPKVKALAKKYNKSPAQILLRWQVQRGVVVIPKSVTPSRIKQNIQ 268
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
4-279 |
5.11e-117 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 338.05 E-value: 5.11e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSWKAS---PGKVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIRCKIKEGAVRREDLFIATKLWCTCHKKSLV 80
Cdd:cd19108 11 IPVLGFGTYAPEevpKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKLWCTFHRPELV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 81 ETACRKSLKALKLNYLDLYLIHWPMGFKPPHpewimscselsfclshprvQDLPLDESNMVIPSDTDFLDTWEAMEDLVI 160
Cdd:cd19108 91 RPALEKSLKKLQLDYVDLYLIHFPVALKPGE-------------------ELFPKDENGKLIFDTVDLCATWEAMEKCKD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 161 TGLVKNIGVSNFNHEQLERLLNKPGLRFKPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLGGSCEG--VD-----LI 233
Cdd:cd19108 152 AGLAKSIGVSNFNRRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQRDKewVDqnspvLL 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1370457959 234 DNPVIKRIAKEHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENIQ 279
Cdd:cd19108 232 EDPVLCALAKKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQ 277
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
4-278 |
4.05e-110 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 318.54 E-value: 4.05e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSWKASPGKVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIRckikEGAVRREDLFIATKLWCTCHKKSLVETA 83
Cdd:COG0656 5 IPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIA----ASGVPREELFVTTKVWNDNHGYDDTLAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 84 CRKSLKALKLNYLDLYLIHWPMgfkpphpewimscselsfclshprvqdlpldesnmvipsDTDFLDTWEAMEDLVITGL 163
Cdd:COG0656 81 FEESLERLGLDYLDLYLIHWPG---------------------------------------PGPYVETWRALEELYEEGL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 164 VKNIGVSNFNHEQLERLLNKPGLrfKPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLGgscEGvDLIDNPVIKRIAK 243
Cdd:COG0656 122 IRAIGVSNFDPEHLEELLAETGV--KPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLG---RG-KLLDDPVLAEIAE 195
|
250 260 270
....*....|....*....|....*....|....*
gi 1370457959 244 EHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENI 278
Cdd:COG0656 196 KHGKTPAQVVLRWHLQRGVVVIPKSVTPERIRENL 230
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
4-279 |
3.04e-106 |
|
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes 3-oxo-5-beta-steroid 4-dehydrogenase (EC 1.3.1.3) from Homo sapiens (AKR1D1), Rattus norvegicus (liver, AKR1D2), and Oryctolagus cuniculus (AKR1D3). 3-oxo-5-beta-steroid 4-dehydrogenase, also called delta(4)-3-ketosteroid 5-beta-reductase (EC 1.3.99.6), or delta(4)-3-oxosteroid 5-beta-reductase, or 5-beta-reductase, efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites.
Pssm-ID: 381335 [Multi-domain] Cd Length: 308 Bit Score: 310.96 E-value: 3.04e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGL---SSWKASP-GKVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIRCKIKEGAVRREDLFIATKLWCTCHKKSL 79
Cdd:cd19109 4 IPIIGLgtySEPKTTPkGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHPPEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 80 VETACRKSLKALKLNYLDLYLIHWPMGFKPphpewimscSELSFclshprvqdlPLDESNMVIPSDTDFLDTWEAMEDLV 159
Cdd:cd19109 84 VRPTLERTLKVLQLDYVDLYIIEMPMAFKP---------GDEIY----------PRDENGKWLYHKTNLCATWEALEACK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 160 ITGLVKNIGVSNFNHEQLERLLNKPGLRFKPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLGGSCEG--VD-----L 232
Cdd:cd19109 145 DAGLVKSIGVSNFNRRQLELILNKPGLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDPiwVNvssppL 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1370457959 233 IDNPVIKRIAKEHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENIQ 279
Cdd:cd19109 225 LEDPLLNSIGKKYNKTAAQVVLRFNIQRGVVVIPKSFNPERIKENFQ 271
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
4-278 |
3.93e-105 |
|
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: 307.42 E-value: 3.93e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSWKASPGKVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIRCKIKEGAVRREDLFIATKLWCTCHKKSLVETA 83
Cdd:cd19123 12 IPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLWNNSHAPEDVLPA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 84 CRKSLKALKLNYLDLYLIHWPMGFKPphpewimscselsfclshprvqDLPLDESN--MVIPSDTDFLDTWEAMEDLVIT 161
Cdd:cd19123 92 LEKTLADLQLDYLDLYLMHWPVALKK----------------------GVGFPESGedLLSLSPIPLEDTWRAMEELVDK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 162 GLVKNIGVSNFNHEQLERLLNKPglRFKPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLG---------GSCEGVdL 232
Cdd:cd19123 150 GLCRHIGVSNFSVKKLEDLLATA--RIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGsgdrpaamkAEGEPV-L 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1370457959 233 IDNPVIKRIAKEHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENI 278
Cdd:cd19123 227 LEDPVINKIAEKHGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNL 272
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
4-279 |
1.11e-104 |
|
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: 306.65 E-value: 1.11e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSWKASPGKVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIRCKIKEGAVRREDLFIATKLWCTCHKKSLVETA 83
Cdd:cd19154 12 MPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLWTHEHAPEDVEEA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 84 CRKSLKALKLNYLDLYLIHWPMGFKPPHPEWIMscselsfclshprvqdlplDESNMVIPSDTDFLDTWEAMEDLVITGL 163
Cdd:cd19154 92 LRESLKKLQLEYVDLYLIHAPAAFKDDEGESGT-------------------MENGMSIHDAVDVEDVWRGMEKVYDEGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 164 VKNIGVSNFNHEQLERLLNKPglRFKPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLG-----------GSCEGVDL 232
Cdd:cd19154 153 TKAIGVSNFNNDQIQRILDNA--RVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGspgranftkstGVSPAPNL 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1370457959 233 IDNPVIKRIAKEHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENIQ 279
Cdd:cd19154 231 LQDPIVKAIAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFN 277
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
4-279 |
3.08e-101 |
|
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: 297.33 E-value: 3.08e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSWKASPGKVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIRCKIKEGAVRREDLFIATKLWCTCHKKSLVETA 83
Cdd:cd19125 11 IPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLWCTDHAPEDVPPA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 84 CRKSLKALKLNYLDLYLIHWPMGFKpphpewimscselsfclshprvQDLPLDESNMVIPsdTDFLDTWEAMEDLVITGL 163
Cdd:cd19125 91 LEKTLKDLQLDYLDLYLIHWPVRLK----------------------KGAHMPEPEEVLP--PDIPSTWKAMEKLVDSGK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 164 VKNIGVSNFNHEQLERLLNKPglRFKPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLGGS---CEGVDLIDNPVIKR 240
Cdd:cd19125 147 VRAIGVSNFSVKKLEDLLAVA--RVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPgttWVKKNVLKDPIVTK 224
|
250 260 270
....*....|....*....|....*....|....*....
gi 1370457959 241 IAKEHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENIQ 279
Cdd:cd19125 225 VAEKLGKTPAQVALRWGLQRGTSVLPKSTNEERIKENID 263
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
4-279 |
2.26e-97 |
|
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: 287.38 E-value: 2.26e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSWKASPGKVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIRCKIKE-GAVRREDLFIATKLWCTCHKKSLVET 82
Cdd:cd19118 7 IPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEePGVKREDLFITSKLWNNSHRPEYVEP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 83 ACRKSLKALKLNYLDLYLIHWPMGFKPPHPEWIMscselsfclsHPRvqdlPLDESNMVIPSDTDFLDTWEAMEDLVITG 162
Cdd:cd19118 87 ALDDTLKELGLDYLDLYLIHWPVAFKPTGDLNPL----------TAV----PTNGGEVDLDLSVSLVDTWKAMVELKKTG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 163 LVKNIGVSNFNHEQLERLLNKPGLRfkPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLGGSCEGVD-LIDNPVIKRI 241
Cdd:cd19118 153 KVKSIGVSNFSIDHLQAIIEETGVV--PAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGNNLAGLPlLVQHPEVKAI 230
|
250 260 270
....*....|....*....|....*....|....*...
gi 1370457959 242 AKEHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENIQ 279
Cdd:cd19118 231 AAKLGKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFE 268
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
4-279 |
3.93e-92 |
|
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: 273.99 E-value: 3.93e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSWKASPGKVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIrckiKEGAVRREDLFIATKLWCTCHKKslVETA 83
Cdd:cd19117 14 IPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGI----KDSGVPREEIFITTKLWCTWHRR--VEEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 84 CRKSLKALKLNYLDLYLIHWPMGFKPPhpewimscselsfclshpRVQDLPL-DESNMVIPSDTDFLDTWEAMEDLVITG 162
Cdd:cd19117 88 LDQSLKKLGLDYVDLYLMHWPVPLDPD------------------GNDFLFKkDDGTKDHEPDWDFIKTWELMQKLPATG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 163 LVKNIGVSNFNHEQLERLLNKPGLRFKPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLGGSceGVDLIDNPVIKRIA 242
Cdd:cd19117 150 KVKAIGVSNFSIKNLEKLLASPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGST--NAPLLKEPVIIKIA 227
|
250 260 270
....*....|....*....|....*....|....*..
gi 1370457959 243 KEHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENIQ 279
Cdd:cd19117 228 KKHGKTPAQVIISWGLQRGYSVLPKSVTPSRIESNFK 264
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
4-279 |
1.29e-90 |
|
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: 270.94 E-value: 1.29e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSWKASPGKVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIRCKIKEGAVRREDLFIATKLWCTCHKKSLVETA 83
Cdd:cd19155 12 MPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLPPGGNRREKVEKF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 84 CRKSLKALKLNYLDLYLIHWPMGFkpphpewiMSCSELSFCLShprvqdlplDESNMVIPSDTDFLDTWEAMEDLVITGL 163
Cdd:cd19155 92 LLKSLEKLQLDYVDLYLIHFPVGS--------LSKEDDSGKLD---------PTGEHKQDYTTDLLDIWKAMEAQVDQGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 164 VKNIGVSNFNHEQLERLLNKPglRFKPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLG-----------GSCEGV-- 230
Cdd:cd19155 155 TRSIGLSNFNREQMARILKNA--RIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGspgaahfspgtGSPSGSsp 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1370457959 231 DLIDNPVIKRIAKEHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENIQ 279
Cdd:cd19155 233 DLLQDPVVKAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQ 281
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
4-278 |
2.05e-86 |
|
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: 260.50 E-value: 2.05e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSWKASPGKVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIRCKIKEGAVRREDLFIATKLWCTCHkkSLVETA 83
Cdd:cd19112 11 MPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLWNSDH--GHVIEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 84 CRKSLKALKLNYLDLYLIHWPMGFKppH-----PEWIMScselsfclshprvqdlplDESNMVIPSDTDFLDTWEAMEDL 158
Cdd:cd19112 89 CKDSLKKLQLDYLDLYLVHFPVATK--HtgvgtTGSALG------------------EDGVLDIDVTISLETTWHAMEKL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 159 VITGLVKNIGVSNFnheqlERLLNKPGL---RFKPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLGGSCEGVDL--- 232
Cdd:cd19112 149 VSAGLVRSIGISNY-----DIFLTRDCLaysKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGGAAANAEWfgs 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1370457959 233 ---IDNPVIKRIAKEHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENI 278
Cdd:cd19112 224 vspLDDPVLKDLAKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENI 272
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
4-279 |
1.29e-85 |
|
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: 257.46 E-value: 1.29e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSWKASPGKVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIRCKIkEGAVRREDLFIATKLWCTCHKKslVETA 83
Cdd:cd19121 12 IPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAI-AGGVKREDLFVTTKLWSTYHRR--VELC 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 84 CRKSLKALKLNYLDLYLIHWPMGFKPPHpewimscselsfclSHPRVQDLPlDESNMVIPsDTDFLDTWEAMEDLVITGL 163
Cdd:cd19121 89 LDRSLKSLGLDYVDLYLVHWPVLLNPNG--------------NHDLFPTLP-DGSRDLDW-DWNHVDTWKQMEKVLKTGK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 164 VKNIGVSNFNHEQLERLLnkPGLRFKPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLGGSceGVDLIDNPVIKRIAK 243
Cdd:cd19121 153 TKAIGVSNYSIPYLEELL--KHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGST--GSPLISDEPVVEIAK 228
|
250 260 270
....*....|....*....|....*....|....*.
gi 1370457959 244 EHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENIQ 279
Cdd:cd19121 229 KHNVGPGTVLISYQVARGAVVLPKSVTPDRIKSNLE 264
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
3-278 |
2.06e-84 |
|
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: 253.45 E-value: 2.06e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 3 DIPAVGLSSWKASPGKVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIRckikEGAVRREDLFIATKLWCTCHKKSLVET 82
Cdd:cd19131 9 TIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIR----ASGVPREELFITTKLWNSDQGYDSTLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 83 ACRKSLKALKLNYLDLYLIHWPMgfkpphpewimscselsfclshprvqdlpldesnmviPSDTDFLDTWEAMEDLVITG 162
Cdd:cd19131 85 AFDESLRKLGLDYVDLYLIHWPV-------------------------------------PAQDKYVETWKALIELKKEG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 163 LVKNIGVSNFNHEQLERLLNKPGLrfKPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLGGScegvDLIDNPVIKRIA 242
Cdd:cd19131 128 RVKSIGVSNFTIEHLQRLIDETGV--VPVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQG----GLLSDPVIGEIA 201
|
250 260 270
....*....|....*....|....*....|....*.
gi 1370457959 243 KEHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENI 278
Cdd:cd19131 202 EKHGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAENF 237
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
5-279 |
7.12e-84 |
|
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: 252.83 E-value: 7.12e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 5 PAVGLSSWKASPGKVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIRCKIKEGAVRREDLFIATKLWCTCHKKSLVETAC 84
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVKEQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 85 RKSLKALKLNYLDLYLIHWPMGFKpphpewimscselsfclsHPRVQDLPLDESNMVIpSDTDFLDTWEAMEDLVITGLV 164
Cdd:cd19128 82 LITLQDLQLEYLDLFLIHWPLAFD------------------MDTDGDPRDDNQIQSL-SKKPLEDTWRAMEQCVDEKLT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 165 KNIGVSNFNHEQLERLLNKpgLRFKPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLGGSC-EGVDLIDN-PVIKRIA 242
Cdd:cd19128 143 KNIGVSNYSTKLLTDLLNY--CKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGSYgDGNLTFLNdSELKALA 220
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1370457959 243 KEHGKSPAQILIRFQIQR---NVIVIPGSITPSHIKENIQ 279
Cdd:cd19128 221 TKYNTTPPQVIIAWHLQKwpkNYSVIPKSANKSRCQQNFD 260
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
4-279 |
1.81e-83 |
|
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: 250.65 E-value: 1.81e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSWKASPGKVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIrckiKEGAVRREDLFIATKLWCTCHKKSLVETA 83
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAI----AESGVPREDLFITTKVWRDHLRPEDLKKS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 84 CRKSLKALKLNYLDLYLIHWPmgfkpphpewimscselsfclshprvqdlpldesnmviPSDTDFLDTWEAMEDLVITGL 163
Cdd:cd19073 77 VDRSLEKLGTDYVDLLLIHWP--------------------------------------NPTVPLEETLGALKELKEAGK 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 164 VKNIGVSNFNHEQLERLLNKPGLrfKPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLggsCEGvDLIDNPVIKRIAK 243
Cdd:cd19073 119 VKSIGVSNFTIELLEEALDISPL--PIAVNQVEFHPFLYQAELLEYCRENDIVITAYSPL---ARG-EVLRDPVIQEIAE 192
|
250 260 270
....*....|....*....|....*....|....*.
gi 1370457959 244 EHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENIQ 279
Cdd:cd19073 193 KYDKTPAQVALRWLVQKGIVVIPKASSEDHLKENLA 228
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
4-279 |
1.88e-83 |
|
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: 252.03 E-value: 1.88e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSWKASPGKVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIRCKIKEGAVRREDLFIATKLWCTCHKKSLVETA 83
Cdd:cd19111 4 MPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLEFKDTEKS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 84 CRKSLKALKLNYLDLYLIHWPMGFKPPhpewimscselsfclshprvqdlplDESNMVIPSDTDFLDTWEAMEDLVITGL 163
Cdd:cd19111 84 LEKSLENLKLPYVDLYLIHHPCGFVNK-------------------------KDKGERELASSDVTSVWRAMEALVSEGK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 164 VKNIGVSNFNHEQLERLLNKPglRFKPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLGG--------SCEGVDLIDN 235
Cdd:cd19111 139 VKSIGLSNFNPRQINKILAYA--KVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSpgranqslWPDQPDLLED 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1370457959 236 PVIKRIAKEHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENIQ 279
Cdd:cd19111 217 PTVLAIAKELDKTPAQVLLRFVLQRGTGVLPKSTNKERIEENFE 260
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
2-280 |
3.15e-82 |
|
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: 249.65 E-value: 3.15e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 2 GDIPAVGLSSWKASPGKVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIRCKIKEGAVRREDLFIATKLWCTCHKKSLVE 81
Cdd:cd19115 11 YDMPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLWNTFHDGERVE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 82 TACRKSLKALKLNYLDLYLIHWPMGFK--------PphPEWimscselsfclshprvqdlpLDESNMVIPSDTDFLDTWE 153
Cdd:cd19115 91 PICRKQLADWGIDYFDLFLIHFPIALKyvdpavryP--PGW--------------------FYDGKKVEFSNAPIQETWT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 154 AMEDLVITGLVKNIGVSNFNHEQLERLLNKPglRFKPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLG--------- 224
Cdd:cd19115 149 AMEKLVDKGLARSIGVSNFSAQLLMDLLRYA--RIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGpqsfleldl 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370457959 225 -GSCEGVDLIDNPVIKRIAKEHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENIQN 280
Cdd:cd19115 227 pGAKDTPPLFEHDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDV 283
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
2-277 |
2.92e-80 |
|
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: 244.29 E-value: 2.92e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 2 GDIPAVGLSSWKASPGKVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIRCKIKEGAVRREDLFIATKLWCTCHKKSLVE 81
Cdd:cd19129 4 GAIPALGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNHRPERVK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 82 TACRKSLKALKLNYLDLYLIHWPMGFKPPHPewimscselsfclshprvQDlPLDESNMVIPSD-TDFLDTWEAMEDLVI 160
Cdd:cd19129 84 PAFEASLKRLQLDYLDLYLIHTPFAFQPGDE------------------QD-PRDANGNVIYDDgVTLLDTWRAMERLVD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 161 TGLVKNIGVSNFNHEQLERLLNKPglRFKPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLGGSCEGvDLIDNPVIKR 240
Cdd:cd19129 145 EGRCKAIGLSDVSLEKLREIFEAA--RIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGMEP-KLLEDPVITA 221
|
250 260 270
....*....|....*....|....*....|....*..
gi 1370457959 241 IAKEHGKSPAQILIRFQIQRNVIVIPGSITPSHIKEN 277
Cdd:cd19129 222 IARRVNKTPAQVLLAWAIQRGTALLTTSKTPSRIREN 258
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
4-277 |
8.27e-79 |
|
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: 238.88 E-value: 8.27e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSWKASPGKVTE-AVKEAIDAGYRHFDCAYFYHNEREVGAGIRckikEGAVRREDLFIATKLWCTCHKKSLVET 82
Cdd:cd19126 9 MPWLGLGVFQTPDGDETErAVQTALENGYRSIDTAAIYKNEEGVGEAIR----ESGVPREELFVTTKLWNDDQRARRTED 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 83 ACRKSLKALKLNYLDLYLIHWPMGFKpphpewimscselsfclshprvqdlpldesnmvipsdtdFLDTWEAMEDLVITG 162
Cdd:cd19126 85 AFQESLDRLGLDYVDLYLIHWPGKDK---------------------------------------FIDTWKALEKLYASG 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 163 LVKNIGVSNFNHEQLERLLNKPglRFKPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLGGScegvDLIDNPVIKRIA 242
Cdd:cd19126 126 KVKAIGVSNFQEHHLEELLAHA--DVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQG----GLLSNPVLAAIG 199
|
250 260 270
....*....|....*....|....*....|....*
gi 1370457959 243 KEHGKSPAQILIRFQIQRNVIVIPGSITPSHIKEN 277
Cdd:cd19126 200 EKYGKSAAQVVLRWDIQHGVVTIPKSVHASRIKEN 234
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
3-279 |
9.41e-79 |
|
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: 240.81 E-value: 9.41e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 3 DIPAVGLSSWKASPGKVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIRCKIKEGAVRREDLFIATKLWCTCHKKSLVET 82
Cdd:cd19113 10 KMPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWNNFHDPKNVET 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 83 ACRKSLKALKLNYLDLYLIHWPMGFKPphpewimscselsfclshprvqdLPLDES----------NMVIPSDTDFLDTW 152
Cdd:cd19113 90 ALNKTLSDLKLDYVDLFLIHFPIAFKF-----------------------VPIEEKyppgfycgdgDNFVYEDVPILDTW 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 153 EAMEDLVITGLVKNIGVSNFNHEQLERLLNkpGLRFKPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLG-------G 225
Cdd:cd19113 147 KALEKLVDAGKIKSIGVSNFPGALILDLLR--GATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGpqsfvelN 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370457959 226 SCEGVD---LIDNPVIKRIAKEHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENIQ 279
Cdd:cd19113 225 QGRALNtptLFEHDTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLS 281
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
4-279 |
1.30e-78 |
|
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: 238.69 E-value: 1.30e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSWKASPGKVTE-AVKEAIDAGYRHFDCAYFYHNEREVGAGIRCKIKEGAVRREDLFIATKLWCTCHKKSLVET 82
Cdd:cd19136 1 MPILGLGTFRLRGEEEVRqAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 83 ACRKSLKALKLNYLDLYLIHWPmGfkpphpewimscselsfclshprVQDLPldesnmviPSDTDF----LDTWEAMEDL 158
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWP-G-----------------------VQGLK--------PSDPRNaelrRESWRALEDL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 159 VITGLVKNIGVSNFNHEQLERLLNKPglRFKPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLGGSceGVDLIDNPVI 238
Cdd:cd19136 129 YKEGKLRAIGVSNYTVRHLEELLKYC--EVPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSG--DLRLLEDPTV 204
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1370457959 239 KRIAKEHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENIQ 279
Cdd:cd19136 205 LAIAKKYGRTPAQVLLRWALQQGIGVIPKSTNPERIAENIK 245
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
4-278 |
5.62e-77 |
|
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: 234.39 E-value: 5.62e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSWKASPGKVTE-AVKEAIDAGYRHFDCAYFYHNEREVGAGIrckiKEGAVRREDLFIATKLWCTC-----HKK 77
Cdd:cd19133 9 MPILGFGVFQIPDPEECErAVLEAIKAGYRLIDTAAAYGNEEAVGRAI----KKSGIPREELFITTKLWIQDagyekAKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 78 SLvetacRKSLKALKLNYLDLYLIHWPMGfkpphpewimscselsfclshprvqdlpldesnmvipsdtDFLDTWEAMED 157
Cdd:cd19133 85 AF-----ERSLKRLGLDYLDLYLIHQPFG----------------------------------------DVYGAWRAMEE 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 158 LVITGLVKNIGVSNFNHEQLERLLnkPGLRFKPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLGgscEG-VDLIDNP 236
Cdd:cd19133 120 LYKEGKIRAIGVSNFYPDRLVDLI--LHNEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFA---EGrNNLFENP 194
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1370457959 237 VIKRIAKEHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENI 278
Cdd:cd19133 195 VLTEIAEKYGKSVAQVILRWLIQRGIVVIPKSVRPERIAENF 236
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
4-279 |
3.00e-74 |
|
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: 228.92 E-value: 3.00e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSWkaSP----GKVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIRCKIKEGAVRREDLFIATKLWCTCHKKsl 79
Cdd:cd19119 12 IPALGLGTA--SPhedrAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVWPTFYDE-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 80 VETACRKSLKALKLNYLDLYLIHWPMGFK-----PPHPEWimscselsfclshprvqdlPLDESNMVIPSDT-DFLDTWE 153
Cdd:cd19119 88 VERSLDESLKALGLDYVDLLLVHWPVCFEkdsddSGKPFT-------------------PVNDDGKTRYAASgDHITTYK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 154 AMEDLVITGLVKNIGVSNFNHEQLERLLNKpgLRFKPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLGGSceGVDLI 233
Cdd:cd19119 149 QLEKIYLDGRAKAIGVSNYSIVYLERLIKE--CKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSH--GAPNL 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1370457959 234 DNPVIKRIAKEHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENIQ 279
Cdd:cd19119 225 KNPLVKKIAEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGK 270
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
4-279 |
2.80e-73 |
|
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: 226.00 E-value: 2.80e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGL--SSWKASPGKVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIRCKIKEGAVR-REDLFIATKLWCTCHKKSLV 80
Cdd:cd19124 5 MPVIGMgtASDPPSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKLWCSDAHPDLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 81 ETACRKSLKALKLNYLDLYLIHWPMGFKPphpewimscselsfclshprvqdlpldESNMVIPSDTDFLD-----TWEAM 155
Cdd:cd19124 85 LPALKKSLRNLQLEYVDLYLIHWPVSLKP---------------------------GKFSFPIEEEDFLPfdikgVWEAM 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 156 EDLVITGLVKNIGVSNFNHEQLERLLNKPGLRfkPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLGGSCEGV---DL 232
Cdd:cd19124 138 EECQRLGLTKAIGVSNFSCKKLQELLSFATIP--PAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTKWgsnAV 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1370457959 233 IDNPVIKRIAKEHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENIQ 279
Cdd:cd19124 216 MESDVLKEIAAAKGKTVAQVSLRWVYEQGVSLVVKSFNKERMKQNLD 262
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
3-278 |
5.73e-73 |
|
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: 224.06 E-value: 5.73e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 3 DIPAVGLSSWKASPGKVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIrckiKEGAVRREDLFIATKLWCTCHKKSLVET 82
Cdd:cd19140 7 RIPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAI----AASGVPRDELFLTTKVWPDNYSPDDFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 83 ACRKSLKALKLNYLDLYLIHWPmgfkpphpewimscselsfclshprvqdlpldesnmviPSDTDFLDTWEAMEDLVITG 162
Cdd:cd19140 83 SVEESLRKLRTDYVDLLLLHWP--------------------------------------NKDVPLAETLGALNEAQEAG 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 163 LVKNIGVSNFNHEQLERLLNKPGLRFkpLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLGgscEGvDLIDNPVIKRIA 242
Cdd:cd19140 125 LARHIGVSNFTVALLREAVELSEAPL--FTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLA---RG-EVLKDPVLQEIG 198
|
250 260 270
....*....|....*....|....*....|....*..
gi 1370457959 243 KEHGKSPAQILIRFQIQR-NVIVIPGSITPSHIKENI 278
Cdd:cd19140 199 RKHGKTPAQVALRWLLQQeGVAAIPKATNPERLEENL 235
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
4-278 |
2.60e-72 |
|
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: 223.04 E-value: 2.60e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSWKASPGK-VTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIrckiKEGAVRREDLFIATKLWCTCHKKSLVET 82
Cdd:cd19157 10 MPWLGLGVFKVEEGSeVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGI----KESGIPREELFITSKVWNADQGYDSTLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 83 ACRKSLKALKLNYLDLYLIHWPMGFKpphpewimscselsfclshprvqdlpldesnmvipsdtdFLDTWEAMEDLVITG 162
Cdd:cd19157 86 AFEASLERLGLDYLDLYLIHWPVKGK---------------------------------------YKETWKALEKLYKDG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 163 LVKNIGVSNFNHEQLERLLNKPglRFKPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLggsCEGvDLIDNPVIKRIA 242
Cdd:cd19157 127 RVRAIGVSNFQVHHLEDLLADA--EIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPL---MQG-QLLDNPVLKEIA 200
|
250 260 270
....*....|....*....|....*....|....*.
gi 1370457959 243 KEHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENI 278
Cdd:cd19157 201 EKYNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENA 236
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
4-278 |
1.81e-71 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 221.10 E-value: 1.81e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSWKASPGKVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIrckiKEGAVRREDLFIATKLWCTCHKKslVETA 83
Cdd:PRK11565 15 MPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKAL----KEASVAREELFITTKLWNDDHKR--PREA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 84 CRKSLKALKLNYLDLYLIHWPMgfkpphpewimscselsfclshprvqdlpldesnmviPSDTDFLDTWEAMEDLVITGL 163
Cdd:PRK11565 89 LEESLKKLQLDYVDLYLMHWPV-------------------------------------PAIDHYVEAWKGMIELQKEGL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 164 VKNIGVSNFNHEQLERLLNKPGLrfKPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLGGSCEGVdlIDNPVIKRIAK 243
Cdd:PRK11565 132 IKSIGVCNFQIHHLQRLIDETGV--TPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGKGV--FDQKVIRDLAD 207
|
250 260 270
....*....|....*....|....*....|....*
gi 1370457959 244 EHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENI 278
Cdd:PRK11565 208 KYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAENF 242
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
2-279 |
4.33e-71 |
|
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: 220.89 E-value: 4.33e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 2 GD-IPAVGLSSWKASPGKVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIRCKIKEGAVRREDLFIATKLWCTCHKKSLV 80
Cdd:cd19114 1 GDkMPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGKDHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 81 ETACRKSLKALKLNYLDLYLIHWPMGFKPPHPEwimscSELSFCLSHPRVQDLPLDESNMvipsdtdfLDTWEAMEDLVI 160
Cdd:cd19114 81 REAFDRQLKDYGLDYIDLYLIHFPIPAAYVDPA-----ENYPFLWKDKELKKFPLEQSPM--------QECWREMEKLVD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 161 TGLVKNIGVSNFNHEQLERLLNKPglRFKPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLGGSCEGV---------D 231
Cdd:cd19114 148 AGLVRNIGIANFNVQLILDLLTYA--KIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAVYTKvtkhlkhftN 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1370457959 232 LIDNPVIKRIAKEHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENIQ 279
Cdd:cd19114 226 LLEHPVVKKLADKHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLD 273
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
2-278 |
6.92e-71 |
|
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: 218.68 E-value: 6.92e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 2 GDIPAVGLSSWKASPGKVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIRckikEGAVRREDLFIATKLWCTCHKKSLVE 81
Cdd:cd19132 5 TQIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVR----RSGVPREELFVTTKLPGRHHGYEEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 82 TACRKSLKALKLNYLDLYLIHWPmgfkpphpewimscselsfclsHPRvQDLpldesnmvipsdtdFLDTWEAMEDLVIT 161
Cdd:cd19132 81 RTIEESLYRLGLDYVDLYLIHWP----------------------NPS-RDL--------------YVEAWQALIEAREE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 162 GLVKNIGVSNFNHEQLERLLNKPGLrfKPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLGGsceGVDLIDNPVIKRI 241
Cdd:cd19132 124 GLVRSIGVSNFLPEHLDRLIDETGV--TPAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLGR---GSGLLDEPVIKAI 198
|
250 260 270
....*....|....*....|....*....|....*..
gi 1370457959 242 AKEHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENI 278
Cdd:cd19132 199 AEKHGKTPAQVVLRWHVQLGVVPIPKSANPERQRENL 235
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
4-277 |
8.39e-71 |
|
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: 218.93 E-value: 8.39e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSWKASPGKVTE-AVKEAIDAGYRHFDCAYFYHNEREVGAGIRckikEGAVRREDLFIATKLWCTCHKKSLVET 82
Cdd:cd19156 9 MPRLGLGVWRVQDGAEAEnAVKWAIEAGYRHIDTAAIYKNEEGVGQGIR----ESGVPREEVFVTTKLWNSDQGYESTLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 83 ACRKSLKALKLNYLDLYLIHWPMGFKpphpewimscselsfclshprvqdlpldesnmvipsdtdFLDTWEAMEDLVITG 162
Cdd:cd19156 85 AFEESLEKLGLDYVDLYLIHWPVKGK---------------------------------------FKDTWKAFEKLYKEK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 163 LVKNIGVSNFNHEQLERLLNKPGLRfkPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLGGScegvDLIDNPVIKRIA 242
Cdd:cd19156 126 KVRAIGVSNFHEHHLEELLKSCKVA--PMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQG----KLLSNPVLKAIG 199
|
250 260 270
....*....|....*....|....*....|....*
gi 1370457959 243 KEHGKSPAQILIRFQIQRNVIVIPGSITPSHIKEN 277
Cdd:cd19156 200 KKYGKSAAQVIIRWDIQHGIITIPKSVHEERIQEN 234
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
4-276 |
1.87e-70 |
|
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: 218.26 E-value: 1.87e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGL---SSWKASPG-----KVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIrckiKEGAVRREDLFIATKLWCtch 75
Cdd:cd19120 4 IPAIAFgtgTAWYKSGDddiqrDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEAL----KESGVPREDLFITTKVSP--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 76 KKSLVETACRKSLKALKLNYLDLYLIHWPMGFKPphpewimscselsfclshprvqdlpldesnmvipSDTDFLDTWEAM 155
Cdd:cd19120 77 GIKDPREALRKSLAKLGVDYVDLYLIHSPFFAKE----------------------------------GGPTLAEAWAEL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 156 EDLVITGLVKNIGVSNFNHEQLERLLNKPglRFKPLTNQIECHPYLT--QKNLISFCQSRDVSVTAYRPLG----GSCEG 229
Cdd:cd19120 123 EALKDAGLVRSIGVSNFRIEDLEELLDTA--KIKPAVNQIEFHPYLYpqQPALLEYCREHGIVVSAYSPLSpltrDAGGP 200
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1370457959 230 VDlidnPVIKRIAKEHGKSPAQILIRFQIQRNVIVIPGSITPSHIKE 276
Cdd:cd19120 201 LD----PVLEKIAEKYGVTPAQVLLRWALQKGIVVVTTSSKEERMKE 243
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
3-278 |
1.46e-66 |
|
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: 208.42 E-value: 1.46e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 3 DIPAVGLSSWKASPGKVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIRckikEGAVRREDLFIATKLWCTCHKKSLVET 82
Cdd:cd19127 8 EMPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIR----RSGVDRSDIFVTTKLWISDYGYDKALR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 83 ACRKSLKALKLNYLDLYLIHWPMgfkpPHpewimscselsfclshprvqdlpldesnmvipsdtDFLDT---WEAMEDLV 159
Cdd:cd19127 84 GFDASLRRLGLDYVDLYLLHWPV----PN-----------------------------------DFDRTiqaYKALEKLL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 160 ITGLVKNIGVSNFNHEQLERLLNKPGlrFKPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLGG--------SCEGVD 231
Cdd:cd19127 125 AEGRVRAIGVSNFTPEHLERLIDATT--VVPAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGGvmrygasgPTGPGD 202
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1370457959 232 LIDNPVIKRIAKEHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENI 278
Cdd:cd19127 203 VLQDPTITGLAEKYGKTPAQIVLRWHLQNGVSAIPKSVHPERIAENI 249
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
4-279 |
1.68e-65 |
|
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: 205.64 E-value: 1.68e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSWKaSPGKVTEAVKEAI-DAGYRHFDCAYFYHNEREVGAGIrckiKEGAVRREDLFIATKLWCTCHKKSLVET 82
Cdd:cd19135 13 MPILGLGTSH-SGGYSHEAVVYALkECGYRHIDTAKRYGCEELLGKAI----KESGVPREDLFLTTKLWPSDYGYESTKQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 83 ACRKSLKALKLNYLDLYLIHWPMGfkpphPEWIMSCSELSfclshprvqdlpldesnmvipsdtdfLDTWEAMEDLVITG 162
Cdd:cd19135 88 AFEASLKRLGVDYLDLYLLHWPDC-----PSSGKNVKETR--------------------------AETWRALEELYDEG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 163 LVKNIGVSNFNHEQLERLLNKPGLRfkPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLGgscEGVDLIDNPVIKrIA 242
Cdd:cd19135 137 LCRAIGVSNFLIEHLEQLLEDCSVV--PHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLA---KGKALEEPTVTE-LA 210
|
250 260 270
....*....|....*....|....*....|....*..
gi 1370457959 243 KEHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENIQ 279
Cdd:cd19135 211 KKYQKTPAQILIRWSIQNGVVTIPKSTKEERIKENCQ 247
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
4-279 |
3.06e-64 |
|
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: 203.24 E-value: 3.06e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSW--KASPGKVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIRCKIKEG-AVRREDLFIATKLWCTCHKKSLV 80
Cdd:cd19122 9 IPAVGFGTFanEGAKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKVWNHLHEPEDV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 81 ETACRKSLKALKLNYLDLYLIHWPMGFKPphpewimscselsfclSHPRVQDLPLDESNMVIPSDTDFLD-TWEAMEDLV 159
Cdd:cd19122 89 KWSIDNSLKNLKLDYIDLFLVHWPIAAEK----------------NDQRSPKLGPDGKYVILKDLTENPEpTWRAMEEIY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 160 ITGLVKNIGVSNFNHEQLERLLNKPglRFKPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLGGSCE----GVDLIDN 235
Cdd:cd19122 153 ESGKAKAIGVSNWTIPGLKKLLSFA--KVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQvpstGERVSEN 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1370457959 236 PVIKRIAKEHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENIQ 279
Cdd:cd19122 231 PTLNEVAEKGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFK 274
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
4-278 |
3.19e-63 |
|
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: 199.37 E-value: 3.19e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSWKASPGKVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIRCKikegAVRREDLFIATKLWCTCHKKSLVETA 83
Cdd:cd19130 10 IPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIAAS----GIPRDELFVTTKLWNDRHDGDEPAAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 84 CRKSLKALKLNYLDLYLIHWPMgfkpphpewimscselsfclshprvqdlpldesnmviPSDTDFLDTWEAMEDLVITGL 163
Cdd:cd19130 86 FAESLAKLGLDQVDLYLVHWPT-------------------------------------PAAGNYVHTWEAMIELRAAGR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 164 VKNIGVSNFNHEQLERLLNKPGLrfKPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLG-GScegvdLIDNPVIKRIA 242
Cdd:cd19130 129 TRSIGVSNFLPPHLERIVAATGV--VPAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGqGK-----LLGDPPVGAIA 201
|
250 260 270
....*....|....*....|....*....|....*.
gi 1370457959 243 KEHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENI 278
Cdd:cd19130 202 AAHGKTPAQIVLRWHLQKGHVVFPKSVRRERMEDNL 237
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
4-279 |
1.65e-61 |
|
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: 194.49 E-value: 1.65e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSWKASPGKVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIRckikEGAVRREDLFIATKLWCTCHKKSLVETA 83
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIA----ESGVPRDELFITTKIWIDNLSKDKLLPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 84 CRKSLKALKLNYLDLYLIHWPmgfkPPhpewimscselsfclshprvqdlpldesNMVIPSDtdflDTWEAMEDLVITGL 163
Cdd:cd19139 77 LEESLEKLRTDYVDLTLIHWP----SP----------------------------NDEVPVE----EYIGALAEAKEQGL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 164 VKNIGVSNFNHEQLERLLNKPGLRfKPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLGgscEGvDLIDNPVIKRIAK 243
Cdd:cd19139 121 TRHIGVSNFTIALLDEAIAVVGAG-AIATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLA---YG-KVLDDPVLAAIAE 195
|
250 260 270
....*....|....*....|....*....|....*.
gi 1370457959 244 EHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENIQ 279
Cdd:cd19139 196 RHGATPAQIALAWAMARGYAVIPSSTKREHLRSNLL 231
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
4-278 |
4.28e-61 |
|
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: 193.98 E-value: 4.28e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSWK---------ASPGKVTEAVKEAIDAGYRHFDCAYFY---HNEREVGAGIRckikegAVRREDLFIATKLW 71
Cdd:cd19072 4 VPVLGLGTWGigggmskdySDDKKAIEALRYAIELGINLIDTAEMYgggHAEELVGKAIK------GFDREDLFITTKVS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 72 CTCHKKSLVETACRKSLKALKLNYLDLYLIHWPmgfkpphpewimscselsfclshprvqdlpldesNMVIPsdtdFLDT 151
Cdd:cd19072 78 PDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWP----------------------------------NPSIP----IEET 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 152 WEAMEDLVITGLVKNIGVSNFNHEQLERLLNKPGlRFKPLTNQIECHPYLT--QKNLISFCQSRDVSVTAYRPLG-GSCE 228
Cdd:cd19072 120 LRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLK-KGPIVANQVEYNLFDReeESGLLPYCQKNGIAIIAYSPLEkGKLS 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1370457959 229 GVDLIdnPVIKRIAKEHGKSPAQILIRFQIQR-NVIVIPGSITPSHIKENI 278
Cdd:cd19072 199 NAKGS--PLLDEIAKKYGKTPAQIALNWLISKpNVIAIPKASNIEHLEENA 247
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
4-279 |
7.65e-59 |
|
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: 188.53 E-value: 7.65e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSWKASPGKVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIRckikEGAVRREDLFIATKLWCTCHKKSLVETA 83
Cdd:cd19134 11 MPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIA----ASGIPRGELFVTTKLATPDQGFTASQAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 84 CRKSLKALKLNYLDLYLIHWPMgfkpphpewimscselsfclshprvqdlpldesnmviPSDTDFLDTWEAMEDLVITGL 163
Cdd:cd19134 87 CRASLERLGLDYVDLYLIHWPA-------------------------------------GREGKYVDSWGGLMKLREEGL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 164 VKNIGVSNFNHEQLERLLNKPGlrFKPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLG-GScegvdLIDNPVIKRIA 242
Cdd:cd19134 130 ARSIGVSNFTAEHLENLIDLTF--FTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGvGR-----LLDNPAVTAIA 202
|
250 260 270
....*....|....*....|....*....|....*..
gi 1370457959 243 KEHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENIQ 279
Cdd:cd19134 203 AAHGRTPAQVLLRWSLQLGNVVISRSSNPERIASNLD 239
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
6-279 |
5.99e-56 |
|
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: 181.74 E-value: 5.99e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 6 AVGLSSWKASPGKVTEAVKEAIDAGYRHFDCAYFYH---NEREVGAGIrckiKEGAVRREDLFIATKL------WCTCHK 76
Cdd:pfam00248 7 QLGGGWGPISKEEALEALRAALEAGINFIDTAEVYGdgkSEELLGEAL----KDYPVKRDKVVIATKVpdgdgpWPSGGS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 77 KSLVETACRKSLKALKLNYLDLYLIHWPmgfkpphpewimscselsfclshprvqdlpldesnmviPSDTDFLDTWEAME 156
Cdd:pfam00248 83 KENIRKSLEESLKRLGTDYIDLYYLHWP--------------------------------------DPDTPIEETWDALE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 157 DLVITGLVKNIGVSNFNHEQLERLLNKPGLrfKPLTNQIECHPY--LTQKNLISFCQSRDVSVTAYRPLGGS-------- 226
Cdd:pfam00248 125 ELKKEGKIRAIGVSNFDAEQIEKALTKGKI--PIVAVQVEYNLLrrRQEEELLEYCKKNGIPLIAYSPLGGGlltgkytr 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 227 ----CEGVDLIDN-----------PVIKRIAKEHGKSPAQILIRF--QIQRNVIVIPGSITPSHIKENIQ 279
Cdd:pfam00248 203 dpdkGPGERRRLLkkgtplnlealEALEEIAKEHGVSPAQVALRWalSKPGVTIPIPGASNPEQLEDNLG 272
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
4-277 |
3.14e-49 |
|
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: 163.57 E-value: 3.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSW-----KASPGKVTEAVKEAIDAGYRHFDCAYFYHN---EREVGAGIRCkikegavRREDLFIATKLWCTCH 75
Cdd:cd19138 11 VPALGQGTWymgedPAKRAQEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRG-------RRDKVFLVSKVLPSNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 76 KKSLVETACRKSLKALKLNYLDLYLIHWPMGfkpphpewimscselsfclshprvqdLPLDEsnmvipsdtdfldTWEAM 155
Cdd:cd19138 84 SRQGTVRACERSLRRLGTDYLDLYLLHWRGG--------------------------VPLAE-------------TVAAM 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 156 EDLVITGLVKNIGVSNFNHEQLERLLNKPGLRfKPLTNQIECHpyLTQKN----LISFCQSRDVSVTAYRPLG-GSCEGV 230
Cdd:cd19138 125 EELKKEGKIRAWGVSNFDTDDMEELWAVPGGG-NCAANQVLYN--LGSRGieydLLPWCREHGVPVMAYSPLAqGGLLRR 201
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1370457959 231 DLIDNPVIKRIAKEHGKSPAQILIRFQI-QRNVIVIPGSITPSHIKEN 277
Cdd:cd19138 202 GLLENPTLKEIAARHGATPAQVALAWVLrDGNVIAIPKSGSPEHAREN 249
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
4-279 |
1.68e-48 |
|
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: 161.58 E-value: 1.68e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSWK---------ASPGKVTEAVKEAIDAGYRHFDCAYFY---HNEREVGAGIRckikegAVRREDLFIATKLW 71
Cdd:cd19137 4 IPALGLGTWGiggfltpdySRDEEMVELLKTAIELGYTHIDTAEMYgggHTEELVGKAIK------DFPREDLFIVTKVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 72 CTCHKKSLVETACRKSLKALKLNYLDLYLIHWPmgfkppHPEwimscselsfclshprvqdLPLDEsnmvipsdtdfldT 151
Cdd:cd19137 78 PTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWP------NPN-------------------IPLEE-------------T 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 152 WEAMEDLVITGLVKNIGVSNFNHEQLERLLNKpgLRFKPLTNQIECHPY---LTQKNLISFCQSRDVSVTAYRPLGgscE 228
Cdd:cd19137 120 LSAMAEGVRQGLIRYIGVSNFNRRLLEEAISK--SQTPIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPLR---R 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1370457959 229 GVDLIdNPVIKRIAKEHGKSPAQILIRFQIQR-NVIVIPGSITPSHIKENIQ 279
Cdd:cd19137 195 GLEKT-NRTLEEIAKNYGKTIAQIALAWLIQKpNVVAIPKAGRVEHLKENLK 245
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
4-278 |
2.37e-46 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 156.34 E-value: 2.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSWKASPGKVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIRckikEGAVRREDLFIATKLWCTCHKKSLVETA 83
Cdd:PRK11172 3 IPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIA----ESGVPRDELFITTKIWIDNLAKDKLIPS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 84 CRKSLKALKLNYLDLYLIHWPmgfkPPHPEwimscselsfclshprvqdLPLDEsnmvipsdtdFLdtwEAMEDLVITGL 163
Cdd:PRK11172 79 LKESLQKLRTDYVDLTLIHWP----SPNDE-------------------VSVEE----------FM---QALLEAKKQGL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 164 VKNIGVSNFNHEQLERLLNKPGLRfKPLTNQIECHPYLTQKNLISFCQSRDVSVTAYRPLGgscEGVDLIDnPVIKRIAK 243
Cdd:PRK11172 123 TREIGISNFTIALMKQAIAAVGAE-NIATNQIELSPYLQNRKVVAFAKEHGIHVTSYMTLA---YGKVLKD-PVIARIAA 197
|
250 260 270
....*....|....*....|....*....|....*
gi 1370457959 244 EHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENI 278
Cdd:PRK11172 198 KHNATPAQVILAWAMQLGYSVIPSSTKRENLASNL 232
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
8-278 |
6.20e-40 |
|
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: 141.08 E-value: 6.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 8 GLSSWKASPGKVTEAVKEAIDAGYRHFDCAYFY---HNEREVGAGIRckikegAVRREDLFIATKL--------WCTCHK 76
Cdd:COG0667 24 GGPWGGVDEAEAIAILDAALDAGINFFDTADVYgpgRSEELLGEALK------GRPRDDVVIATKVgrrmgpgpNGRGLS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 77 KSLVETACRKSLKALKLNYLDLYLIHWPmgfkpphpewimscselsfclshprvqdlpldesnmviPSDTDFLDTWEAME 156
Cdd:COG0667 98 REHIRRAVEASLRRLGTDYIDLYQLHRP--------------------------------------DPDTPIEETLGALD 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 157 DLVITGLVKNIGVSNFNHEQLERLLNKPGLRFKPLTNQIEchpY--LTQ---KNLISFCQSRDVSVTAYRPLGG------ 225
Cdd:COG0667 140 ELVREGKIRYIGVSNYSAEQLRRALAIAEGLPPIVAVQNE---YslLDRsaeEELLPAARELGVGVLAYSPLAGglltgk 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370457959 226 ----------------------SCEGVDLIDnpVIKRIAKEHGKSPAQILIRFQIQR--NVIVIPGSITPSHIKENI 278
Cdd:COG0667 217 yrrgatfpegdraatnfvqgylTERNLALVD--ALRAIAAEHGVTPAQLALAWLLAQpgVTSVIPGARSPEQLEENL 291
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
4-279 |
8.33e-40 |
|
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: 140.06 E-value: 8.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSWKA-----------SPGKVTEAVKEAIDAGYRHFDCAYFY---HNEREVGAGIrckiKEGAVRrEDLFIATK 69
Cdd:cd19093 2 VSPLGLGTWQWgdrlwwgygeyGDEDLQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFL----KELGDR-DEVVIATK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 70 LWCTCHKKSL--VETACRKSLKALKLNYLDLYLIHWPMGFKPPHPEWimscselsfclshprvqdlpldesnmvipsdtd 147
Cdd:cd19093 77 FAPLPWRLTRrsVVKALKASLERLGLDSIDLYQLHWPGPWYSQIEAL--------------------------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 148 fldtWEAMEDLVITGLVKNIGVSNFNHEQLERLLNKPGLRFKPL-TNQIE---CHPYLTQKNLISFCQSRDVSVTAYRPL 223
Cdd:cd19093 124 ----MDGLADAVEEGLVRAVGVSNYSADQLRRAHKALKERGVPLaSNQVEyslLYRDPEQNGLLPACDELGITLIAYSPL 199
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370457959 224 G-GSCEGVDLIDNP----------------------VIKRIAKEHGKSPAQILIRFQIQRNVIVIPGSITPSHIKENIQ 279
Cdd:cd19093 200 AqGLLTGKYSPENPppggrrrlfgrknlekvqplldALEEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAG 278
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
4-279 |
7.95e-37 |
|
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: 132.33 E-value: 7.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSWKASPGKVTE---------AVKEAIDAGYRHFDCAYFY---HNEREVGAGIrckikEGavRREDLFIATKLW 71
Cdd:cd19085 1 VSRLGLGCWQFGGGYWWGdqddeesiaTIHAALDAGINFFDTAEAYgdgHSEEVLGKAL-----KG--RRDDVVIATKVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 72 cTCH-KKSLVETACRKSLKALKLNYLDLYLIHWPMGFKPPHPewimscselsfclshprvqdlpldesnmvipsdtdfld 150
Cdd:cd19085 74 -PDNlTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEE-------------------------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 151 TWEAMEDLVITGLVKNIGVSNFNHEQLERLLNkpglRFKPLTNQIECHPYLTQ--KNLISFCQSRDVSVTAYRP-----L 223
Cdd:cd19085 115 TMEALEKLKEEGKIRAIGVSNFGPAQLEEALD----AGRIDSNQLPYNLLWRAieYEILPFCREHGIGVLAYSPlaqglL 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 224 GG----------------------------SCEGVDLidnpvIKRIAKEHGKSPAQILIRFQIQRNVI--VIPGSITPSH 273
Cdd:cd19085 191 TGkfssaedfppgdartrlfrhfepgaeeeTFEALEK-----LKEIADELGVTMAQLALAWVLQQPGVtsVIVGARNPEQ 265
|
....*.
gi 1370457959 274 IKENIQ 279
Cdd:cd19085 266 LEENAA 271
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
4-278 |
4.62e-33 |
|
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: 122.25 E-value: 4.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSWKASP---GKVTE-----AVKEAIDAGYRHFDCAYFY---HNEREVGAGIrckikegAVRREDLFIATK--- 69
Cdd:cd19084 4 VSRIGLGTWAIGGtwwGEVDDqesieAIKAAIDLGINFFDTAPVYgfgHSEEILGKAL-------KGRRDDVVIATKcgl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 70 LW------CTCHKKSLVETACRKSLKALKLNYLDLYLIHWPmgfkpphpewimscselsfclsHPRVqdlPLDEsnmvip 143
Cdd:cd19084 77 RWdggkgvTKDLSPESIRKEVEQSLRRLQTDYIDLYQIHWP----------------------DPNT---PIEE------ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 144 sdtdfldTWEAMEDLVITGLVKNIGVSNFNHEQLERLLNkpglRFKPLTNQIechPY--LTQKN---LISFCQSRDVSVT 218
Cdd:cd19084 126 -------TAEALEKLKKEGKIRYIGVSNFSVEQLEEARK----YGPIVSLQP---PYsmLEREIeeeLLPYCRENGIGVL 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 219 AYRPLGG-------------------------SCE----GVDLIDnpVIKRIAKEHGKSPAQILIRFQIQRN--VIVIPG 267
Cdd:cd19084 192 PYGPLAQglltgkykkeptfppddrrsrfpffRGEnfekNLEIVD--KLKEIAEKYGKSLAQLAIAWTLAQPgvTSAIVG 269
|
330
....*....|.
gi 1370457959 268 SITPSHIKENI 278
Cdd:cd19084 270 AKNPEQLEENA 280
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
21-279 |
1.23e-32 |
|
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: 119.55 E-value: 1.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 21 EAVKEAIDAGYRHFDCAYFY---HNEREVGAGIRckikeGAVRREDLFIATKLWCT---------CHKKSLVEtACRKSL 88
Cdd:cd06660 21 ALLDAALEAGGNFFDTADVYgdgRSERLLGRWLK-----GRGNRDDVVIATKGGHPpggdpsrsrLSPEHIRR-DLEESL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 89 KALKLNYLDLYLIHWPmgfkPPhpewimscselsfclshprvqDLPLDEsnmvipsdtdfldTWEAMEDLVITGLVKNIG 168
Cdd:cd06660 95 RRLGTDYIDLYYLHRD----DP---------------------STPVEE-------------TLEALNELVREGKIRYIG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 169 VSNFNHEQLERLLN--KPGLRFKPLTNQIE---CHPYLTQKNLISFCQSRDVSVTAYRPLGGsceGvdlidnpvikriak 243
Cdd:cd06660 137 VSNWSAERLAEALAyaKAHGLPGFAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPLAR---G-------------- 199
|
250 260 270
....*....|....*....|....*....|....*...
gi 1370457959 244 ehgksPAQILIRFQIQR--NVIVIPGSITPSHIKENIQ 279
Cdd:cd06660 200 -----PAQLALAWLLSQpfVTVPIVGARSPEQLEENLA 232
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
8-279 |
2.45e-31 |
|
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: 117.66 E-value: 2.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 8 GLSSWKASPGKVTEAVKEAIDAGYRHFDCAYFYHN---EREVGAGIrckiKEGAVRREDLFIATK----------LWCTC 74
Cdd:cd19092 15 RLADWGESAEELLSLIEAALELGITTFDHADIYGGgkcEELFGEAL----ALNPGLREKIEIQTKcgirlgddprPGRIK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 75 H---KKSLVETACRKSLKALKLNYLDLYLIHwpmgfkppHPEWIMSCSELSfclshprvqdlpldesnmvipsdtdfldt 151
Cdd:cd19092 91 HydtSKEHILASVEGSLKRLGTDYLDLLLLH--------RPDPLMDPEEVA----------------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 152 wEAMEDLVITGLVKNIGVSNFNHEQLErLLNKpGLRFKPLTNQIEC---HPYLTQKNLISFCQSRDVSVTAYRPL-GGSC 227
Cdd:cd19092 134 -EAFDELVKSGKVRYFGVSNFTPSQIE-LLQS-YLDQPLVTNQIELsllHTEAIDDGTLDYCQLLDITPMAWSPLgGGRL 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1370457959 228 EGVDLID----NPVIKRIAKEHGKSPAQILIRFqIQR---NVIVIPGSITPSHIKENIQ 279
Cdd:cd19092 211 FGGFDERfqrlRAALEELAEEYGVTIEAIALAW-LLRhpaRIQPILGTTNPERIRSAVK 268
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
6-279 |
1.31e-26 |
|
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: 105.45 E-value: 1.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 6 AVGLSSWKASPGKVTE-----AVKEAIDAGYRHFDCAYFY---HNEREVGAGIRckikegaVRREDLFIATK---LW--- 71
Cdd:cd19102 10 AIGGGGWGGGWGPQDDrdsiaAIRAALDLGINWIDTAAVYglgHSEEVVGRALK-------GLRDRPIVATKcglLWdee 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 72 ---CTCHKKSLVETACRKSLKALKLNYLDLYLIHWPMGfkpphpewimscselsfclshprvqdlpldesnmvipsDTDF 148
Cdd:cd19102 83 griRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDP--------------------------------------DEPI 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 149 LDTWEAMEDLVITGLVKNIGVSNFNHEQLERLlnkpgLRFKPLT-NQIechPYL-----TQKNLISFCQSRDVSVTAYRP 222
Cdd:cd19102 125 EEAWGALAELKEEGKVRAIGVSNFSVDQMKRC-----QAIHPIAsLQP---PYSllrrgIEAEILPFCAEHGIGVIVYSP 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 223 LG-GSCEG------------------------------VDLIDnpVIKRIAKEHGKSPAQILIRFQIQRNVI--VIPGSI 269
Cdd:cd19102 197 MQsGLLTGkmtpervaslpaddwrrrspffqepnlarnLALVD--ALRPIAERHGRTVAQLAIAWVLRRPEVtsAIVGAR 274
|
330
....*....|
gi 1370457959 270 TPSHIKENIQ 279
Cdd:cd19102 275 RPDQIDETVG 284
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
8-276 |
2.00e-26 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 104.85 E-value: 2.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 8 GLSSWKASPGKVTEAVKEAIDAGYRHFDCA--Y-FYHNEREVGAGIrckiKEGAVRREDLFIATK----LWCTCHKKSL- 79
Cdd:COG4989 22 RLGEWDLSPAEAAALIEAALELGITTFDHAdiYgGYTCEALFGEAL----KLSPSLREKIELQTKcgirLPSEARDNRVk 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 80 --------VETACRKSLKALKLNYLDLYLIHWPmgfkpphpewimscselsfclshprvqDlPLdesnmvipsdTDFLDT 151
Cdd:COG4989 98 hydtskehIIASVEGSLRRLGTDYLDLLLLHRP---------------------------D-PL----------MDPEEV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 152 WEAMEDLVITGLVKNIGVSNFNHEQLErLLNKpGLRFKPLTNQIECHpyLTQKNLIS-----FCQSRDVSVTAYRPL-GG 225
Cdd:COG4989 140 AEAFDELKASGKVRHFGVSNFTPSQFE-LLQS-ALDQPLVTNQIELS--LLHTDAFDdgtldYCQLNGITPMAWSPLaGG 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1370457959 226 SCEGVDLIDNP----VIKRIAKEHGKSPAQILIRFqIQR---NVIVIPGSITPSHIKE 276
Cdd:COG4989 216 RLFGGFDEQFPrlraALDELAEKYGVSPEAIALAW-LLRhpaGIQPVIGTTNPERIKA 272
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
12-278 |
9.79e-23 |
|
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: 94.96 E-value: 9.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 12 WKASPGKVTEAVKEAIDAGYRHFDCAYFYHN---EREVGAGIRckikeGAVRREDLFIATKLwctCHKKSL--------- 79
Cdd:cd19079 30 WVLDEEESRPIIKRALDLGINFFDTANVYSGgasEEILGRALK-----EFAPRDEVVIATKV---YFPMGDgpngrglsr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 80 --VETACRKSLKALKLNYLDLYLIHWpmgfkpphpewimscselsfclshprvqdlpLDEsnmvipsDTDFLDTWEAMED 157
Cdd:cd19079 102 khIMAEVDASLKRLGTDYIDLYQIHR-------------------------------WDY-------ETPIEETLEALHD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 158 LVITGLVKNIGVSNFNHEQLERLLN---KPGL-RFKPLTNQ-------IEchpyltqKNLISFCQSRDVSVTAYRPL--- 223
Cdd:cd19079 144 VVKSGKVRYIGASSMYAWQFAKALHlaeKNGWtKFVSMQNHynllyreEE-------REMIPLCEEEGIGVIPWSPLarg 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 224 ---GGSCEGVDLI-----------------DNPVIKR---IAKEHGKSPAQILIRFQIQRNVIVIP--GSITPSHIKENI 278
Cdd:cd19079 217 rlaRPWGDTTERRrsttdtaklkydyfteaDKEIVDRveeVAKERGVSMAQVALAWLLSKPGVTAPivGATKLEHLEDAV 296
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
4-278 |
1.28e-22 |
|
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: 93.31 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSW--------KASPGKVTEAVKEAIDAGYRHFDCAYFY---HNEREVGagircKIKEGavRREDLFIATKLWC 72
Cdd:cd19086 3 VSEIGFGTWglggdwwgDVDDAEAIRALRAALDLGINFFDTADVYgdgHSERLLG-----KALKG--RRDKVVIATKFGN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 73 TCHK---------KSLVETACRKSLKALKLNYLDLYLIH-WPMgfkpphpewimscselsfclshprvqdlpldesnmvi 142
Cdd:cd19086 76 RFDGgperpqdfsPEYIREAVEASLKRLGTDYIDLYQLHnPPD------------------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 143 pSDTDFLDTWEAMEDLVITGLVKNIGVSNFNHEQLERLLNKPG-----LRFkpltNQIECHPYLTqknLISFCQSRDVSV 217
Cdd:cd19086 119 -EVLDNDELFEALEKLKQEGKIRAYGVSVGDPEEALAALRRGGidvvqVIY----NLLDQRPEEE---LFPLAEEHGVGV 190
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370457959 218 TAYRPLggsCEGVdLIdnpvikriakehGKsPAQILIRFQIQRNVI--VIPGSITPSHIKENI 278
Cdd:cd19086 191 IARVPL---ASGL-LT------------GK-LAQAALRFILSHPAVstVIPGARSPEQVEENA 236
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
23-279 |
7.07e-21 |
|
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: 88.81 E-value: 7.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 23 VKEAIDAGYRHFDCAYFY---HNEREVGAGIRckikegaVRREDLFIATKL---------WCTCHKKSLVETACRKSLKA 90
Cdd:cd19088 30 LRRALELGVNFIDTADSYgpdVNERLIAEALH-------PYPDDVVIATKGglvrtgpgwWGPDGSPEYLRQAVEASLRR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 91 LKLNYLDLYLIHWPMgfkpphpewimscselsfclshPRVqdlPLDESnmvipsdtdfldtWEAMEDLVITGLVKNIGVS 170
Cdd:cd19088 103 LGLDRIDLYQLHRID----------------------PKV---PFEEQ-------------LGALAELQDEGLIRHIGLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 171 NFNHEQLERLLNKPGLrfkpLTNQIECHPYLTQ-KNLISFCQSRDVSVTAYRPLGGsceGVDLIDNPVIKRIAKEHGKSP 249
Cdd:cd19088 145 NVTVAQIEEARAIVRI----VSVQNRYNLANRDdEGVLDYCEAAGIAFIPWFPLGG---GDLAQPGGLLAEVAARLGATP 217
|
250 260 270
....*....|....*....|....*....|..
gi 1370457959 250 AQILIRFQIQR--NVIVIPGSITPSHIKENIQ 279
Cdd:cd19088 218 AQVALAWLLARspVMLPIPGTSSVEHLEENLA 249
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-279 |
1.15e-20 |
|
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: 88.41 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 14 ASPGKVTEAVKEAIDAGYRHFDCAYFY---HNEREVGAGIRckikegAVRREDLFIATKLWCTCHKKS---LVETAcRKS 87
Cdd:cd19105 22 GLPRESPELLRRALDLGINYFDTAEGYgngNSEEIIGEALK------GLRRDKVFLATKASPRLDKKDkaeLLKSV-EES 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 88 LKALKLNYLDLYLIHwpmgfkpphpewimscselsfclshprvqdlpldesnMVIPSDTDFLDTW--EAMEDLVITGLVK 165
Cdd:cd19105 95 LKRLQTDYIDIYQLH-------------------------------------GVDTPEERLLNEEllEALEKLKKEGKVR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 166 NIGVS--NFNHEQLERLLNKPG-----LRFKPLtnqiecHPYLTQKNLISFCQSRDVSVTAYRPLGGscegvdLIDNPVI 238
Cdd:cd19105 138 FIGFSthDNMAEVLQAAIESGWfdvimVAYNFL------NQPAELEEALAAAAEKGIGVVAMKTLAG------GYLQPAL 205
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1370457959 239 KRIAKEHGKSPAQILIRFQIQRNVI--VIPGSITPSHIKENIQ 279
Cdd:cd19105 206 LSVLKAKGFSLPQAALKWVLSNPRVdtVVPGMRNFAELEENLA 248
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
5-279 |
6.63e-20 |
|
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: 86.13 E-value: 6.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 5 PAVGLSSWK--ASPGKVTEA-----VKEAIDAGYRHFDCAYFYHN-EREVGAGIRckikegAVRREDLFIATKLWCTC-- 74
Cdd:cd19095 1 SVLGLGTSGigRVWGVPSEAeaarlLNTALDLGINLIDTAPAYGRsEERLGRALA------GLRRDDLFIATKVGTHGeg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 75 ------HKKSLVETACRKSLKALKLNYLDLYLIHwpmgfkpphpewimSCSElsfclshprvqDLPLDEsnmVIpsdtdf 148
Cdd:cd19095 75 grdrkdFSPAAIRASIERSLRRLGTDYIDLLQLH--------------GPSD-----------DELTGE---VL------ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 149 ldtwEAMEDLVITGLVKNIGVSNFNHEqLERLLNKPGLRFkpltnqIEChPY----LTQKNLISFCQSRDVSVTAYRPLG 224
Cdd:cd19095 121 ----ETLEDLKAAGKVRYIGVSGDGEE-LEAAIASGVFDV------VQL-PYnvldREEEELLPLAAEAGLGVIVNRPLA 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370457959 225 GSC-------EGVDLIDNPVIKRIAKEHGKSPAQILIRFQIQ--RNVIVIPGSITPSHIKENIQ 279
Cdd:cd19095 189 NGRlrrrvrrRPLYADYARRPEFAAEIGGATWAQAALRFVLShpGVSSAIVGTTNPEHLEENLA 252
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
18-279 |
1.10e-19 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 87.57 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 18 KVTEAVKEAIDAGYRHFDCAYFYHN-EREVGAGIRCkikegavRREDLFIATKLWCTCHKKSLVETACRKSLKALKLNYL 96
Cdd:COG1453 30 EAEALIRRAIDNGINYIDTARGYGDsEEFLGKALKG-------PRDKVILATKLPPWVRDPEDMRKDLEESLKRLQTDYI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 97 DLYLIHwpmgfkpphpewimscselsfCLSHPRVQDLPLDESNMvipsdtdfldtWEAMEDLVITGLVKNIGVSnfNH-- 174
Cdd:COG1453 103 DLYLIH---------------------GLNTEEDLEKVLKPGGA-----------LEALEKAKAEGKIRHIGFS--THgs 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 175 -EQLERLLNkpglrfkplTNQIEC----HPYLTQKN-----LISFCQSRDVSVTAYRPLGGsceGvDLIDNP-VIKRIAk 243
Cdd:COG1453 149 lEVIKEAID---------TGDFDFvqlqYNYLDQDNqageeALEAAAEKGIGVIIMKPLKG---G-RLANPPeKLVELL- 214
|
250 260 270
....*....|....*....|....*....|....*...
gi 1370457959 244 EHGKSPAQILIRF--QIQRNVIVIPGSITPSHIKENIQ 279
Cdd:COG1453 215 CPPLSPAEWALRFllSHPEVTTVLSGMSTPEQLDENLK 252
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
13-279 |
5.27e-19 |
|
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: 83.76 E-value: 5.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 13 KASPGKVTEAVKEAIDAGYRHFDCAYFYHN---EREVGAGIRckikegAVRREDLFIATKL--WctchkksLVETAC--R 85
Cdd:cd19096 17 SIDEEKAIEMIRYAIDAGINYFDTAYGYGGgksEEILGEALK------EGPREKFYLATKLppW-------SVKSAEdfR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 86 K----SLKALKLNYLDLYLIHWPMgfKPPHPEWIMScselsfclshprvqdlpldesnmvipsdtdfLDTWEAMEDLVIT 161
Cdd:cd19096 84 RileeSLKRLGVDYIDFYLLHGLN--SPEWLEKARK-------------------------------GGLLEFLEKAKKE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 162 GLVKNIGVSnFnH---EQLERLLNKPGLRFkpltNQIECHpYLTQKN-----LISFCQSRDVSVTAYRPLGGsceGVDLI 233
Cdd:cd19096 131 GLIRHIGFS-F-HdspELLKEILDSYDFDF----VQLQYN-YLDQENqagrpGIEYAAKKGMGVIIMEPLKG---GGLAN 200
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1370457959 234 DNPVIKRIAKEHGKSPAQILIRFQI-QRNV-IVIPGSITPSHIKENIQ 279
Cdd:cd19096 201 NPPEALAILCGAPLSPAEWALRFLLsHPEVtTVLSGMSTPEQLDENIA 248
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
7-279 |
7.93e-19 |
|
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: 84.18 E-value: 7.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 7 VGLSSWKASPGKVT-----EAVKEAIDAGYRHFDCAYFYHN---EREVGAGIRckikegAVRREDLFIATKL-WCT---- 73
Cdd:cd19074 7 LSLGTWLTFGGQVDdedakACVRKAYDLGINFFDTADVYAAgqaEEVLGKALK------GWPRESYVISTKVfWPTgpgp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 74 ----CHKKSLVEtACRKSLKALKLNYLDLYLIHwpmGFKPphpewimscselsfclshprvqDLPLDEsnmvipsdtdfl 149
Cdd:cd19074 81 ndrgLSRKHIFE-SIHASLKRLQLDYVDIYYCH---RYDP----------------------ETPLEE------------ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 150 dTWEAMEDLVITGLVKNIGVSNFNHEQLE---RLLNKPGLRfKPLTNQIECHpYLTQK---NLISFCQSRDVSVTAYRPL 223
Cdd:cd19074 123 -TVRAMDDLIRQGKILYWGTSEWSAEQIAeahDLARQFGLI-PPVVEQPQYN-MLWREieeEVIPLCEKNGIGLVVWSPL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 224 ggsCEGV-----------------------DLIDNPV----------IKRIAKEHGKSPAQILIRFQIQRNVI--VIPGS 268
Cdd:cd19074 200 ---AQGLltgkyrdgipppsrsratdednrDKKRRLLtdenlekvkkLKPIADELGLTLAQLALAWCLRNPAVssAIIGA 276
|
330
....*....|.
gi 1370457959 269 ITPSHIKENIQ 279
Cdd:cd19074 277 SRPEQLEENVK 287
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
8-278 |
9.77e-19 |
|
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: 82.92 E-value: 9.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 8 GLSSWKASPGKVTEAVKEAIDAGYRHFDCAYFYHN-EREVGAGIRckikeGavRREDLFIATKlwcTCHKKSlvETACR- 85
Cdd:cd19100 18 GGPLGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALK-----G--RRDKVFLATK---TGARDY--EGAKRd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 86 --KSLKALKLNYLDLYLIHwpmgfkpphpewimscselsfCLSHPRVQDLPLDESNMvipsdtdfldtWEAMEDLVITGL 163
Cdd:cd19100 86 leRSLKRLGTDYIDLYQLH---------------------AVDTEEDLDQVFGPGGA-----------LEALLEAKEEGK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 164 VKNIGVSNFNHEQLERLLNKPG---LRFkPLtNQIECHPYLTQKNLISFCQSRDVSVTAYRPLGGScegvdlidnpvikR 240
Cdd:cd19100 134 IRFIGISGHSPEVLLRALETGEfdvVLF-PI-NPAGDHIDSFREELLPLAREKGVGVIAMKVLAGG-------------R 198
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1370457959 241 IAKEHGKSPAQiLIRFQIQRNVI--VIPGSITPSHIKENI 278
Cdd:cd19100 199 LLSGDPLDPEQ-ALRYALSLPPVdvVIVGMDSPEELDENL 237
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
12-279 |
3.89e-18 |
|
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: 82.66 E-value: 3.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 12 WKASPGKVTEA-----VKEAIDAGYRHFDCAYFYHN---EREVGAGIRCkikegavRREDLFIATKLWCT---------C 74
Cdd:cd19091 29 FFGAWGGVDQEeadrlVDIALDAGINFFDTADVYSEgesEEILGKALKG-------RRDDVLIATKVRGRmgegpndvgL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 75 HKKSLVEtACRKSLKALKLNYLDLYLIHWPmgfkpphpewimscselsfclshprvqDL--PLDEsnmvipsdtdfldTW 152
Cdd:cd19091 102 SRHHIIR-AVEASLKRLGTDYIDLYQLHGF---------------------------DAltPLEE-------------TL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 153 EAMEDLVITGLVKNIGVSNFNHEQLERLL---NKPGLRfKPLTNQIechpYLT------QKNLISFCQSRDVSVTAYRPL 223
Cdd:cd19091 141 RALDDLVRQGKVRYIGVSNFSAWQIMKALgisERRGLA-RFVALQA----YYSllgrdlEHELMPLALDQGVGLLVWSPL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 224 GGSC------------------------------EGVDLIDnpVIKRIAKEHGKSPAQILIRFQIQRNVI--VIPGSITP 271
Cdd:cd19091 216 AGGLlsgkyrrgqpapegsrlrrtgfdfppvdreRGYDVVD--ALREIAKETGATPAQVALAWLLSRPTVssVIIGARNE 293
|
....*...
gi 1370457959 272 SHIKENIQ 279
Cdd:cd19091 294 EQLEDNLG 301
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
23-279 |
1.08e-17 |
|
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: 80.93 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 23 VKEAIDAGYRHFDCAYFY---HNEREVGAGIRckikegAVRREDLFIATKlwcTCHKKS-----------LVETACRKSL 88
Cdd:cd19083 39 VREALDNGVNLLDTAFIYglgRSEELVGEVLK------EYNRNEVVIATK---GAHKFGgdgsvlnnspeFLRSAVEKSL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 89 KALKLNYLDLYLIHWPMGfkpphpewimscselsfclshprvqDLPLDESnmvipsdtdfldtWEAMEDLVITGLVKNIG 168
Cdd:cd19083 110 KRLNTDYIDLYYIHFPDG-------------------------ETPKAEA-------------VGALQELKDEGKIRAIG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 169 VSNFNHEQLERlLNKPGlrfkpLTNQIEcHPY-LTQ----KNLISFCQSRDVSVTAYRPL------GGSCEGVDLIDNPV 237
Cdd:cd19083 152 VSNFSLEQLKE-ANKDG-----YVDVLQ-GEYnLLQreaeEDILPYCVENNISFIPYFPLasgllaGKYTKDTKFPDNDL 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370457959 238 ---------------------IKRIAKEHGKSPAQILIRFQIQRNVI--VIPGSITPSHIKENIQ 279
Cdd:cd19083 225 rndkplfkgerfsenldkvdkLKSIADEKGVTVAHLALAWYLTRPAIdvVIPGAKRAEQVIDNLK 289
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-277 |
6.45e-17 |
|
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: 78.79 E-value: 6.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 14 ASPGKVTEAVKEAIDAGYRHFDCAYFYHNEREVGAGIRCKIKEGAVRREDLFIATKlWCT-----CHKKSLVETACRKSL 88
Cdd:cd19101 20 RDEDAAVRAMAAYVDAGLTTFDCADIYGPAEELIGEFRKRLRRERDAADDVQIHTK-WVPdpgelTMTRAYVEAAIDRSL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 89 KALKLNYLDLYLIHWpmgfkpphpeWimscselsfclshprvqdlplDesnmviPSDTDFLDTWEAMEDLVITGLVKNIG 168
Cdd:cd19101 99 KRLGVDRLDLVQFHW----------W---------------------D------YSDPGYLDAAKHLAELQEEGKIRHLG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 169 VSNFNHEQLERLLNKPglrFKPLTNQIEC-----HPyltQKNLISFCQSRDVSVTAYRPLGG----------------SC 227
Cdd:cd19101 142 LTNFDTERLREILDAG---VPIVSNQVQYslldrRP---ENGMAALCEDHGIKLLAYGTLAGgllsekylgvpeptgpAL 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370457959 228 EGVDL------IDN-----------PVIKRIAKEHGKSPAQILIRFQIQRNVI--VIPGSITPSHIKEN 277
Cdd:cd19101 216 ETRSLqkyklmIDEwggwdlfqellRTLKAIADKHGVSIANVAVRWVLDQPGVagVIVGARNSEHIDDN 284
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
26-278 |
1.68e-16 |
|
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: 77.99 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 26 AIDAGYRHFDCAYFY----------HNEREVGAGIRCKikegaVRREDLFIATKL--------WC----TCHKKSLVETA 83
Cdd:cd19094 27 AFDEGVNFIDTAEMYpvppspetqgRTEEIIGSWLKKK-----GNRDKVVLATKVagpgegitWPrgggTRLDRENIREA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 84 CRKSLKALKLNYLDLYLIHWPmgfkpphPEWIMSCSELSFCLSHPRvqdlpldesnmviPSDTDFLDTWEAMEDLVITGL 163
Cdd:cd19094 102 VEGSLKRLGTDYIDLYQLHWP-------DRYTPLFGGGYYTEPSEE-------------EDSVSFEEQLEALGELVKAGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 164 VKNIGVSN--------FNHeqLERLLNKPglrfKPLTNQiecHPY--LTQKNLISF---CQSRDVSVTAYRPLGGsceGV 230
Cdd:cd19094 162 IRHIGLSNetpwgvmkFLE--LAEQLGLP----RIVSIQ---NPYslLNRNFEEGLaeaCHRENVGLLAYSPLAG---GV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 231 ------DLIDNPVIKR-------------------------IAKEHGKSPAQILIRFQIQRNVI--VIPGSITPSHIKEN 277
Cdd:cd19094 230 ltgkylDGAARPEGGRlnlfpgymaryrspqaleavaeyvkLARKHGLSPAQLALAWVRSRPFVtsTIIGATTLEQLKEN 309
|
.
gi 1370457959 278 I 278
Cdd:cd19094 310 I 310
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
60-278 |
1.86e-16 |
|
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: 77.64 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 60 RREDLFIATKL--WCTCHKKSL----VETACRKSLKALKLNYLDLYLIHWPmgfkpphpewimscselsfclsHPRVqdl 133
Cdd:cd19081 74 KRDRVVIATKVgfPMGPNGPGLsrkhIRRAVEASLRRLQTDYIDLYQAHWD----------------------DPAT--- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 134 PLDEsnmvipsdtdfldTWEAMEDLVITGLVKNIGVSNFNHEQLERLLN---KPGL-RF---KPLTNQIECHPYltQKNL 206
Cdd:cd19081 129 PLEE-------------TLGALNDLIRQGKVRYIGASNYSAWRLQEALElsrQHGLpRYvslQPEYNLVDRESF--EGEL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 207 ISFCQSRDVSVTAYRPLGG------------------SCEGVDLIDNP-------VIKRIAKEHGKSPAQILIRFQIQRN 261
Cdd:cd19081 194 LPLCREEGIGVIPYSPLAGgfltgkyrseadlpgstrRGEAAKRYLNErglrildALDEVAAEHGATPAQVALAWLLARP 273
|
250
....*....|....*....
gi 1370457959 262 VI--VIPGSITPSHIKENI 278
Cdd:cd19081 274 GVtaPIAGARTVEQLEDLL 292
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
21-279 |
6.01e-16 |
|
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: 76.20 E-value: 6.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 21 EAVKEAIDAGYRHFDCA--YFY-HNEREVGAGIRCKIKEGAVRREDLFIATK---------------------------- 69
Cdd:cd19099 25 EALKAALDSGINVIDTAinYRGgRSERLIGKALRELIEKGGIKRDEVVIVTKagyipgdgdeplrplkyleeklgrglid 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 70 ------LWCTCHKKSLVEtACRKSLKALKLNYLDLYLIHwpmgfkppHPEWimscselsfclshprvQDLPLDESNMvip 143
Cdd:cd19099 105 vadsagLRHCISPAYLED-QIERSLKRLGLDTIDLYLLH--------NPEE----------------QLLELGEEEF--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 144 sDTDFLDTWEAMEDLVITGLVKNIGVSNFN----------HEQLERLL--------NKPGLRFKpltnQIECHPYLTQ-- 203
Cdd:cd19099 157 -YDRLEEAFEALEEAVAEGKIRYYGISTWDgfrappalpgHLSLEKLVaaaeevggDNHHFKVI----QLPLNLLEPEal 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 204 ----------KNLISFCQSRDVSVTAYRPLGGsceGVDLIDNPVIKRIAKEHGKSPAQILIRFQIQRNVI--VIPGSITP 271
Cdd:cd19099 232 tekntvkgeaLSLLEAAKELGLGVIASRPLNQ---GQLLGELRLADLLALPGGATLAQRALQFARSTPGVdsALVGMRRP 308
|
....*...
gi 1370457959 272 SHIKENIQ 279
Cdd:cd19099 309 EHVDENLA 316
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
24-279 |
4.01e-15 |
|
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: 73.79 E-value: 4.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 24 KEAIDAGYRHFDCAYFY---HNEREVGAGIRckikegaVRREDLFIATK---LWCTCHKK-------SLVETACRKSLKA 90
Cdd:cd19076 39 HRALELGVTFLDTADMYgpgTNEELLGKALK-------DRRDEVVIATKfgiVRDPGSGFrgvdgrpEYVRAACEASLKR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 91 LKLNYLDLYLIHwpmgfkpphpewimscselsfclshpRVqdlpldesnmviPSDTDFLDTWEAMEDLVITGLVKNIGVS 170
Cdd:cd19076 112 LGTDVIDLYYQH--------------------------RV------------DPNVPIEETVGAMAELVEEGKVRYIGLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 171 NFNHEQLERllnkpGLRFKPLTN-QIECHPYLT--QKNLISFCQSRDVSVTAYRPLG-----GSCEGVDLID-------N 235
Cdd:cd19076 154 EASADTIRR-----AHAVHPITAvQSEYSLWTRdiEDEVLPTCRELGIGFVAYSPLGrgfltGAIKSPEDLPeddfrrnN 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370457959 236 P---------------VIKRIAKEHGKSPAQILIRFQIQR--NVIVIPGSITPSHIKENIQ 279
Cdd:cd19076 229 PrfqgenfdknlklveKLEAIAAEKGCTPAQLALAWVLAQgdDIVPIPGTKRIKYLEENVG 289
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
3-277 |
5.26e-15 |
|
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: 73.46 E-value: 5.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 3 DIPAVGLSSWKA----SPGKVTE-----AVKEAIDAGYRHFDCAYFY---HNEREVGAGIRCkikegavRREDLFIATKl 70
Cdd:cd19149 10 EASVIGLGTWAIgggpWWGGSDDnesirTIHAALDLGINLIDTAPAYgfgHSEEIVGKAIKG-------RRDKVVLATK- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 71 wC------------------TCHK----KSLVETaCRKSLKALKLNYLDLYLIHWPmgfkpphpewimsCSELsfclshp 128
Cdd:cd19149 82 -CglrwdreggsfffvrdgvTVYKnlspESIREE-VEQSLKRLGTDYIDLYQTHWQ-------------DVET------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 129 rvqdlPLDEsnmvipsdtdfldTWEAMEDLVITGLVKNIGVSNFNHEQLERLLNKPGL-----RFKPLTNQIEchpyltq 203
Cdd:cd19149 140 -----PIEE-------------TMEALEELKRQGKIRAIGASNVSVEQIKEYVKAGQLdiiqeKYSMLDRGIE------- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 204 KNLISFCQSRDVSVTAYRPL-----------------GGSCEG------------VDLIDNpvIKRIAKEHGKSPAQILI 254
Cdd:cd19149 195 KELLPYCKKNNIAFQAYSPLeqglltgkitpdrefdaGDARSGipwfspenrekvLALLEK--WKPLCEKYGCTLAQLVI 272
|
330 340
....*....|....*....|....*
gi 1370457959 255 RFQIQR--NVIVIPGSITPSHIKEN 277
Cdd:cd19149 273 AWTLAQpgITSALCGARKPEQAEEN 297
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
24-225 |
9.56e-15 |
|
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: 72.61 E-value: 9.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 24 KEAIDAGYRHFDCAYFY---HNEREVGAGIrckikegAVRREDLFIATKL------WCTCHKKSL--VETACRKSLKALK 92
Cdd:cd19087 37 DRALDAGINFFDTADVYgggRSEEIIGRWI-------AGRRDDIVLATKVfgpmgdDPNDRGLSRrhIRRAVEASLRRLQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 93 LNYLDLYLIHwpmgfkpphpewimscselsfclsHPRVqDLPLDEsnmvipsdtdfldTWEAMEDLVITGLVKNIGVSNF 172
Cdd:cd19087 110 TDYIDLYQMH------------------------HFDR-DTPLEE-------------TLRALDDLVRQGKIRYIGVSNF 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370457959 173 NHEQLERLLN---KPGL-RF---KPLTN----QIECHpyltqknLISFCQSRDVSVTAYRPLGG 225
Cdd:cd19087 152 AAWQIAKAQGiaaRRGLlRFvseQPMYNllkrQAELE-------ILPAARAYGLGVIPYSPLAG 208
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
60-279 |
2.59e-14 |
|
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: 71.21 E-value: 2.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 60 RREDLFIATKL---------WCTCH---KKSLVETACRKSLKALKLNYLDLYLIHwpmgfkpphpewimscselsfclsh 127
Cdd:cd19752 65 NRDDVVIATKVgagprdpdgGPESPeglSAETIEQEIDKSLRRLGTDYIDLYYAH------------------------- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 128 prVQDlpldesnmvipSDTDFLDTWEAMEDLVITGLVKNIGVSNFNHEQLER----------------------LLNKPG 185
Cdd:cd19752 120 --VDD-----------RDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERarqiarqqgwaefsaiqqrhsyLRPRPG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 186 LRFKpltNQIechpyLTQKNLISFCQSR-DVSVTAYRPLGGSCEGVDliDNP---------------VIKRIAKEHGKSP 249
Cdd:cd19752 187 ADFG---VQR-----IVTDELLDYASSRpDLTLLAYSPLLSGAYTRP--DRPlpeqydgpdsdarlaVLEEVAGELGATP 256
|
250 260 270
....*....|....*....|....*....|..
gi 1370457959 250 AQILIRFQIQRNVIVIP--GSITPSHIKENIQ 279
Cdd:cd19752 257 NQVVLAWLLHRTPAIIPllGASTVEQLEENLA 288
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
3-229 |
3.24e-14 |
|
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: 71.18 E-value: 3.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 3 DIPA--VGLSSWK--------ASPGKVTEAVKEAIDAGYRHFDCAYFY---HNEREVGAGIrckikEGAVRREDLFIATK 69
Cdd:cd19148 1 DLPVsrIALGTWAiggwmwggTDEKEAIETIHKALDLGINLIDTAPVYgfgLSEEIVGKAL-----KEYGKRDRVVIATK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 70 L---WCTCHKKSLVETACR------KSLKALKLNYLDLYLIHWPmgfkpphpewimscselsfclshprvqdlplDEsnm 140
Cdd:cd19148 76 VgleWDEGGEVVRNSSPARirkeveDSLRRLQTDYIDLYQVHWP-------------------------------DP--- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 141 vipsDTDFLDTWEAMEDLVITGLVKNIGVSNFNHEQLERLlnkpgLRFKPL-TNQIechPY-----LTQKNLISFCQSRD 214
Cdd:cd19148 122 ----LVPIEETAEALKELLDEGKIRAIGVSNFSPEQMETF-----RKVAPLhTVQP---PYnlferEIEKDVLPYARKHN 189
|
250
....*....|....*
gi 1370457959 215 VSVTAYRPLggsCEG 229
Cdd:cd19148 190 IVTLAYGAL---CRG 201
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
5-278 |
6.15e-14 |
|
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: 69.89 E-value: 6.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 5 PAVGL--SSWKASPGKVT-----EAVKEAIDAGYRHFDCAYFYHN-EREVGAGIRckikegAVRREDLFIATKLwCTCHK 76
Cdd:cd19090 1 SALGLgtAGLGGVFGGVDddeavATIRAALDLGINYIDTAPAYGDsEERLGLALA------ELPREPLVLSTKV-GRLPE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 77 KSLVETACR------KSLKALKLNYLDLYLIHwpmgfkppHPEWImscselsfclshprvqdlPLDES---NMVIpsdtd 147
Cdd:cd19090 74 DTADYSADRvrrsveESLERLGRDRIDLLMIH--------DPERV------------------PWVDIlapGGAL----- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 148 fldtwEAMEDLVITGLVKNIGVSNFNHEQLERLLNkpglrfkplTNQIEC----HPY--LTQKN---LISFCQSRDVSVT 218
Cdd:cd19090 123 -----EALLELKEEGLIKHIGLGGGPPDLLRRAIE---------TGDFDVvltaNRYtlLDQSAadeLLPAAARHGVGVI 188
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370457959 219 AYRPLGG-----------SCEGVDLIDNPV-----IKRIAKEHGKSPAQILIRF--QIQRNVIVIPGSITPSHIKENI 278
Cdd:cd19090 189 NASPLGMgllagrppervRYTYRWLSPELLdrakrLYELCDEHGVPLPALALRFllRDPRISTVLVGASSPEELEQNV 266
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-276 |
8.31e-14 |
|
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: 70.06 E-value: 8.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 15 SPGKVTEAVKEAIDAGYRHFDCAYFY---HNEREVGAGIRckikegAVRREDLFIATKLWCTCHKKSL--VETACRKSLK 89
Cdd:cd19103 30 DEDTLKAVFDKAMAAGLNLWDTAAVYgmgASEKILGEFLK------RYPREDYIISTKFTPQIAGQSAdpVADMLEGSLA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 90 ALKLNYLDLYLIHWPMGFKPPHPEWImscselsfclshprvqdlpldesnmvipsdtdfldtweameDLVITGLVKNIGV 169
Cdd:cd19103 104 RLGTDYIDIYWIHNPADVERWTPELI-----------------------------------------PLLKSGKVKHVGV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 170 SNFNHEQLER---LLNKPGLRFKPLTNqiecHPYLTQKN-----LISFCQSRDVSVTAY---------------RPL-GG 225
Cdd:cd19103 143 SNHNLAEIKRaneILAKAGVSLSAVQN----HYSLLYRSseeagILDYCKENGITFFAYmvleqgalsgkydtkHPLpEG 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1370457959 226 SCEGVDLID--------NPVIKRIAKEHGKSPAQILIRFQIQRNVIVIPGSITPSHIKE 276
Cdd:cd19103 219 SGRAETYNPllpqleelTAVMAEIGAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVED 277
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
6-278 |
1.60e-13 |
|
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: 69.39 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 6 AVGLSSWKASPGKVTEAVK---EAIDAGYRHFDCAYFY-HNEREVGAGIrckiKEGAVRREDLFIATKLWCTCHKKS--- 78
Cdd:cd19144 20 AMGLSAFYGPPKPDEERFAvldAAFELGCTFWDTADIYgDSEELIGRWF----KQNPGKREKIFLATKFGIEKNVETgey 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 79 -------LVETACRKSLKALKLNYLDLYLIHwpmgfkpphpewimscselsfclshpRVqdlplDESnmvIPSDTdfldT 151
Cdd:cd19144 96 svdgspeYVKKACETSLKRLGVDYIDLYYQH--------------------------RV-----DGK---TPIEK----T 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 152 WEAMEDLVITGLVKNIGVSNFNHEQLERllnkpGLRFKPLTN-QIECHPYLT-----QKNLISFCQSRDVSVTAYRPLG- 224
Cdd:cd19144 138 VAAMAELVQEGKIKHIGLSECSAETLRR-----AHAVHPIAAvQIEYSPFSLdierpEIGVLDTCRELGVAIVAYSPLGr 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 225 GSCEG----------------------------VDLIDNpvIKRIAKEHGKSPAQILIRFQIQR--NVIVIPGSITPSHI 274
Cdd:cd19144 213 GFLTGairspddfeegdfrrmaprfqaenfpknLELVDK--IKAIAKKKNVTAGQLTLAWLLAQgdDIIPIPGTTKLKRL 290
|
....
gi 1370457959 275 KENI 278
Cdd:cd19144 291 EENL 294
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
22-279 |
1.19e-12 |
|
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: 66.91 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 22 AVKEAIDAGYRHFDCAYFY---HNER-------EVGAGIR--CKIKEGAVRREDLfiatklwctchkKSLVETACRKSLK 89
Cdd:cd19104 37 AVRRALDLGINFFDTAPSYgdgKSEEnlgralkGLPAGPYitTKVRLDPDDLGDI------------GGQIERSVEKSLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 90 ALKLNYLDLYLIHwpmgfkpphpewimscselsfclSHPRVQDLPLDESNMVIPSDTDFLDTWEAMEDLVITGLVKNIGV 169
Cdd:cd19104 105 RLKRDSVDLLQLH-----------------------NRIGDERDKPVGGTLSTTDVLGLGGVADAFERLRSEGKIRFIGI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 170 SNFNHEQLER----------------LLNKPGLRFKPltnqiECHPYLTQKNLISFCQSRDVSVTAYRPL--GGSCEGVD 231
Cdd:cd19104 162 TGLGNPPAIRelldsgkfdavqvyynLLNPSAAEARP-----RGWSAQDYGGIIDAAAEHGVGVMGIRVLaaGALTTSLD 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370457959 232 LIDNPVI----------------KRIAKEHGKSPAQILIRFQIQRNVI--VIPGSITPSHIKENIQ 279
Cdd:cd19104 237 RGREAPPtsdsdvaidfrraaafRALAREWGETLAQLAHRFALSNPGVstVLVGVKNREELEEAVA 302
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-279 |
3.22e-12 |
|
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: 64.86 E-value: 3.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 17 GKVTEA-----VKEAIDAGYRHFDCAYFYHN-EREVGagirckikEGAVRREDLFIATKL----WCTCHKKSLVETACRK 86
Cdd:cd19097 21 GKPSEKeakkiLEYALKAGINTLDTAPAYGDsEKVLG--------KFLKRLDKFKIITKLpplkEDKKEDEAAIEASVEA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 87 SLKALKLNYLDLYLIHWPmgfkpphpewimscselsfclshprvQDLPLDESNMvipsdtdfldtWEAMEDLVITGLVKN 166
Cdd:cd19097 93 SLKRLKVDSLDGLLLHNP--------------------------DDLLKHGGKL-----------VEALLELKKEGLIRK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 167 IGVSNFNHEQLERLLNkpglRFKPLTNQIECHPY---LTQKNLISFCQSRDVSV-------------TAYRPLGGSCEGV 230
Cdd:cd19097 136 IGVSVYSPEELEKALE----SFKIDIIQLPFNILdqrFLKSGLLAKLKKKGIEIharsvflqglllmEPDKLPAKFAPAK 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1370457959 231 DLIDNpvIKRIAKEHGKSPAQILIRFQIQRNVI--VIPGSITPSHIKENIQ 279
Cdd:cd19097 212 PLLKK--LHELAKKLGLSPLELALGFVLSLPEIdkIVVGVDSLEQLKEIIA 260
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
20-278 |
1.08e-11 |
|
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: 63.79 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 20 TEAVKEAIDAGYRHFDCAYFY---HNEREVGAGIrckikegAVRREDLFIATKLWCTCHKKSLVET-----------ACR 85
Cdd:cd19078 28 IELIRKAVELGITFFDTAEVYgpyTNEELVGEAL-------KPFRDQVVIATKFGFKIDGGKPGPLgldsrpehirkAVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 86 KSLKALKLNYLDLYLIHwpmgfkpphpewimscselsfclshpRVQ-DLPLDEsnmvipsdtdfldTWEAMEDLVITGLV 164
Cdd:cd19078 101 GSLKRLQTDYIDLYYQH--------------------------RVDpNVPIEE-------------VAGTMKELIKEGKI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 165 KNIGVSNFNHEQLERllnkpGLRFKPLTN-QIECH-----PyltQKNLISFCQSRDVSVTAYRPLGG------------- 225
Cdd:cd19078 142 RHWGLSEAGVETIRR-----AHAVCPVTAvQSEYSmmwreP---EKEVLPTLEELGIGFVPFSPLGKgfltgkidentkf 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370457959 226 ------------SCEGV----DLIDnpVIKRIAKEHGKSPAQILIRFQIQR--NVIVIPGSITPSHIKENI 278
Cdd:cd19078 214 degddraslprfTPEALeanqALVD--LLKEFAEEKGATPAQIALAWLLAKkpWIVPIPGTTKLSRLEENI 282
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
27-279 |
4.65e-11 |
|
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: 62.24 E-value: 4.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 27 IDAGYRHFDCAYFYHN---EREVGAGIrckikegAVRREDLFIATKL----------WCTCHKKSLVEtACRKSLKALKL 93
Cdd:cd19080 41 VEAGGNFIDTANNYTNgtsERLLGEFI-------AGNRDRIVLATKYtmnrrpgdpnAGGNHRKNLRR-SVEASLRRLQT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 94 NYLDLYLIHWPMGFKPphPEWIMScselsfclshprvqdlpldesnmvipsdtdfldtweAMEDLVITGLVKNIGVSNFN 173
Cdd:cd19080 113 DYIDLLYVHAWDFTTP--VEEVMR------------------------------------ALDDLVRAGKVLYVGISDTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 174 HEQLERLLNKPGLR-FKPLTN-QIECHpyLTQKN----LISFCQSRDVSVTAYRPLGG-----------SCEGVDLIDNP 236
Cdd:cd19080 155 AWVVARANTLAELRgWSPFVAlQIEYS--LLERTpereLLPMARALGLGVTPWSPLGGglltgkyqrgeEGRAGEAKGVT 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 237 ---------------VIKRIAKEHGKSPAQILIRFQIQRNVIVIP--GSITPSHIKENIQ 279
Cdd:cd19080 233 vgfgklternwaivdVVAAVAEELGRSAAQVALAWVRQKPGVVIPiiGARTLEQLKDNLG 292
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
4-278 |
7.68e-09 |
|
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: 55.34 E-value: 7.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSWK-----ASPGKVTEAVKEAIDAGYRHFDCAYFY-----HNEREVGAGIRckiKEGAVRREDLFIATKLWCT 73
Cdd:cd19089 11 LPAISLGLWHnfgdyTSPEEARELLRTAFDLGITHFDLANNYgpppgSAEENFGRILK---RDLRPYRDELVISTKAGYG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 74 CH---------KKSLVETaCRKSLKALKLNYLDLYLIHWPmgfkpphpewimscselsfclsHPRVqdlPLDEsnmvips 144
Cdd:cd19089 88 MWpgpygdggsRKYLLAS-LDQSLKRMGLDYVDIFYHHRY----------------------DPDT---PLEE------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 145 dtdfldTWEAMEDLVITGLVKNIGVSNFNHEQLER---LLNKPGLRFkpLTNQIechPY--LTQ---KNLISFCQSRDVS 216
Cdd:cd19089 135 ------TMTALADAVRSGKALYVGISNYPGAKARRaiaLLRELGVPL--IIHQP---RYslLDRwaeDGLLEVLEEAGIG 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 217 VTAYRPLGG-----------------SCEGVDLID-------NPVIK---RIAKEHGKSPAQILIRFQIQRNVI--VIPG 267
Cdd:cd19089 204 FIAFSPLAQglltdkylngippdsrrAAESKFLTEealtpekLEQLRklnKIAAKRGQSLAQLALSWVLRDPRVtsVLIG 283
|
330
....*....|.
gi 1370457959 268 SITPSHIKENI 278
Cdd:cd19089 284 ASSPSQLEDNV 294
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
19-104 |
1.85e-08 |
|
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: 54.52 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 19 VTEAVKEAIDAGYRHFDCAYFYHN---EREVGAGIrckiKEGAVRREDLFIATKL-W---------CTCHKKSLVEtACR 85
Cdd:cd19143 33 AKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAI----KELGWPRSDYVVSTKIfWggggpppndRGLSRKHIVE-GTK 107
|
90
....*....|....*....
gi 1370457959 86 KSLKALKLNYLDLYLIHWP 104
Cdd:cd19143 108 ASLKRLQLDYVDLVFCHRP 126
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
11-279 |
4.64e-08 |
|
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: 53.01 E-value: 4.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 11 SWKASP---GKVTEAVKEAIDAGYRHFDCAYFY------HNEREVGAGIRcKIKEgavRREDLFIATK-------LWCTC 74
Cdd:cd19077 16 TWRPNPtpdEEAFETMKAALDAGSNLWNGGEFYgppdphANLKLLARFFR-KYPE---YADKVVLSVKggldpdtLRPDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 75 HKKSLVET--ACRKSLKALKlnYLDLYlihwpmgfkpphpewimSCSelsfclshpRV-QDLPLDEsnmvipsdtdfldT 151
Cdd:cd19077 92 SPEAVRKSieNILRALGGTK--KIDIF-----------------EPA---------RVdPNVPIEE-------------T 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 152 WEAMEDLVITGLVKNIGVSNFNHEQLERllnkpGLRFKPLT-NQIECHPYLT---QKNLISFCQSRDVSVTAYRPLG-GS 226
Cdd:cd19077 131 IKALKELVKEGKIRGIGLSEVSAETIRR-----AHAVHPIAaVEVEYSLFSReieENGVLETCAELGIPIIAYSPLGrGL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 227 CEG-----VDLIDNPV---------------------IKRIAKEHGKSPAQI---LIRFQIQRNVIVIPGSITPSHIKEN 277
Cdd:cd19077 206 LTGrikslADIPEGDFrrhldrfngenfeknlklvdaLQELAEKKGCTPAQLalaWILAQSGPKIIPIPGSTTLERVEEN 285
|
..
gi 1370457959 278 IQ 279
Cdd:cd19077 286 LK 287
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
27-279 |
5.00e-08 |
|
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: 52.94 E-value: 5.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 27 IDAGYRHFDCAYFY-------HNEREVGAGIRCKIKegavrREDLFIATK-----LWCT----CHKKSLVEtACRKSLKA 90
Cdd:cd19082 27 VELGGNFIDTARVYgdwvergASERVIGEWLKSRGN-----RDKVVIATKgghpdLEDMsrsrLSPEDIRA-DLEESLER 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 91 LKLNYLDLYLIHwpmgfkpphpewimscselsfclshpR-VQDLPLDEsnmvipsdtdFLDTweaMEDLVITGLVKNIGV 169
Cdd:cd19082 101 LGTDYIDLYFLH--------------------------RdDPSVPVGE----------IVDT---LNELVRAGKIRAFGA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 170 SNFNHEQLE---RLLNKPGLRfkPLT-NQI---------ECHPYLT----QKNLISFCQSRDVSVTAYRPLGG------- 225
Cdd:cd19082 142 SNWSTERIAeanAYAKAHGLP--GFAaSSPqwslarpnePPWPGPTlvamDEEMRAWHEENQLPVFAYSSQARgffskra 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370457959 226 ------SCEGVDLIDNPV-------IKRIAKEHGKSPAQILIRFQIQR--NVIVIPGSITPSHIKENIQ 279
Cdd:cd19082 220 aggaedDSELRRVYYSEEnferlerAKELAEEKGVSPTQIALAYVLNQpfPTVPIIGPRTPEQLRDSLA 288
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
8-278 |
2.49e-07 |
|
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: 50.89 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 8 GLSSWKASPGKVTEA---VKEAIDAGYRHFDCAYFY---HNEREVGAGIrckiKEGavRREDLFIATKLWCTCHKKSLVE 81
Cdd:cd19145 21 GLSGDYGAPKPEEEGialIHHAFNSGVTFLDTSDIYgpnTNEVLLGKAL----KDG--PREKVQLATKFGIHEIGGSGVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 82 ---------TACRKSLKALKLNYLDLYLIHwpmgfkpphpewimscselsfclshpRV-QDLPLDesnmvipsdtdflDT 151
Cdd:cd19145 95 vrgdpayvrAACEASLKRLDVDYIDLYYQH--------------------------RIdTTVPIE-------------IT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 152 WEAMEDLVITGLVKNIGVSNFNHEQLERllnkpGLRFKPLTN-QIECHPYL--TQKNLISFCQSRDVSVTAYRPLG---- 224
Cdd:cd19145 136 MGELKKLVEEGKIKYIGLSEASADTIRR-----AHAVHPITAvQLEWSLWTrdIEEEIIPTCRELGIGIVPYSPLGrgff 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370457959 225 -GSCEGVDLIDNPVIKR----------------------IAKEHGKSPAQILIRFQIQR--NVIVIPGSITPSHIKENI 278
Cdd:cd19145 211 aGKAKLEELLENSDVRKshprfqgenleknkvlyerveaLAKKKGCTPAQLALAWVLHQgeDVVPIPGTTKIKNLNQNI 289
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
8-225 |
3.73e-06 |
|
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: 47.17 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 8 GLSSWKASPGKVT-EAVKEAIDA----GYRHFDCAYFYHN---ER---EVGAGIRckikegavrreDLFIATK---LWCT 73
Cdd:cd19075 6 GTMTFGSQGRFTTaEAAAELLDAflerGHTEIDTARVYPDgtsEEllgELGLGER-----------GFKIDTKanpGVGG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 74 CHKKSLVETACRKSLKALKLNYLDLYLIHWPmgfkpphpewimscselsfclshprvqdlplDESnmvipsdTDFLDTWE 153
Cdd:cd19075 75 GLSPENVRKQLETSLKRLKVDKVDVFYLHAP-------------------------------DRS-------TPLEETLA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 154 AMEDLVITGLVKNIGVSNFNHEQLERLLN--------KP----GLrFKPLTNQIEchpyltqKNLISFCQSRDVSVTAYR 221
Cdd:cd19075 117 AIDELYKEGKFKEFGLSNYSAWEVAEIVEickengwvLPtvyqGM-YNAITRQVE-------TELFPCLRKLGIRFYAYS 188
|
....
gi 1370457959 222 PLGG 225
Cdd:cd19075 189 PLAG 192
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
4-102 |
3.81e-06 |
|
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: 47.46 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 4 IPAVGLSSWKASPGKVTEAVKEAI-----DAGYRHFDCAYFYHNER-EVGAG-IrckIKEGAVRREDLFIATKL-W---- 71
Cdd:cd19142 13 VSNVGLGTWSTFSTAISEEQAEEIvtlayENGINYFDTSDAFTSGQaETELGrI---LKKKGWKRSSYIVSTKIyWsygs 89
|
90 100 110
....*....|....*....|....*....|...
gi 1370457959 72 --CTCHKKSLVEtACRKSLKALKLNYLDLYLIH 102
Cdd:cd19142 90 eeRGLSRKHIIE-SVRASLRRLQLDYIDIVIIH 121
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
8-224 |
8.82e-06 |
|
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: 46.01 E-value: 8.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 8 GLSSWKASPGKVTE-----AVKEAIDAGYRHFDCAYFY---HNEREVGAGIRckikegAVRREDLFIATKL--WCTCHKK 77
Cdd:cd19163 19 GASPLGGVFGPVDEeeairTVHEALDSGINYIDTAPWYgqgRSETVLGKALK------GIPRDSYYLATKVgrYGLDPDK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 78 SLVETACR------KSLKALKLNYLDLYLIHwpmgfkpphpewimscsELSFCLSHPRVqdlpLDESnmvIPsdtdfldt 151
Cdd:cd19163 93 MFDFSAERitksveESLKRLGLDYIDIIQVH-----------------DIEFAPSLDQI----LNET---LP-------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 152 weAMEDLVITGLVKNIGVSNFNHEQLERLLNKPglrfkplTNQIE-----CHPYL---TQKNLISFCQSRDVSVTAYRPL 223
Cdd:cd19163 141 --ALQKLKEEGKVRFIGITGYPLDVLKEVLERS-------PVKIDtvlsyCHYTLndtSLLELLPFFKEKGVGVINASPL 211
|
.
gi 1370457959 224 G 224
Cdd:cd19163 212 S 212
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
18-102 |
1.40e-04 |
|
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: 42.65 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 18 KVTEAVKEAIDAGYRHFDCAYFYHnEREVGAGIRCKIKEGAVRREDLFIATKlwctCHKKSL---------VETACRKSL 88
Cdd:cd19164 35 PPVDIVRRALELGIRAFDTSPYYG-PSEIILGRALKALRDEFPRDTYFIITK----VGRYGPddfdyspewIRASVERSL 109
|
90
....*....|....
gi 1370457959 89 KALKLNYLDLYLIH 102
Cdd:cd19164 110 RRLHTDYLDLVYLH 123
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
7-279 |
1.68e-04 |
|
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: 42.21 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 7 VGLSSW-----KASPGKVTEAVKEAIDAGYRHFDCAYFYHN---EREVGAGIRckikegAVRREDLFIATKLWCTCHKKS 78
Cdd:cd19152 5 FGTAPLgnlyeAVSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALR------ELGREDYVISTKVGRLLVPLQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 79 LVETACRKslkalklnyldlylihwpmGFKPPHP---------EWIMSCSELSFC-LSHPRVQ-----DLpldESNMVIP 143
Cdd:cd19152 79 EVEPTFEP-------------------GFWNPLPfdavfdysyDGILRSIEDSLQrLGLSRIDllsihDP---DEDLAGA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 144 SDTDFLDTW-----EAMEDLVITGLVKNIGV-SNFnHEQLERLLNKPGL-------RFKPLTnqiecHPYLTqkNLISFC 210
Cdd:cd19152 137 ESDEHFAQAikgafRALEELREEGVIKAIGLgVND-WEVILRILEEADLdwvmlagRYTLLD-----HSAAR--ELLPEC 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 211 QSRDVSVTAYRPL------GGSCEGVDlIDNPV----------IKRIAKEHGKSPAQILIRFQIQRNVI--VIPGSITPS 272
Cdd:cd19152 209 EKRGVKVVNAGPFnsgflaGGDNFDYY-EYGPAppeliarrdrIEALCEQHGVSLAAAALQFALAPPAVasVAPGASSPE 287
|
....*..
gi 1370457959 273 HIKENIQ 279
Cdd:cd19152 288 RVEENVA 294
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
6-102 |
4.01e-04 |
|
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: 40.98 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 6 AVGLSSWKASPGKVTEA---VKEAIDAGYRHFDCAYFYHN---EREVGAGIRckikEGAVRREDLFIATKLwctCHKKS- 78
Cdd:cd19153 19 TAALGGVYGDGLEQDEAvaiVAEAFAAGINHFDTSPYYGAessEAVLGKALA----ALQVPRSSYTVATKV---GRYRDs 91
|
90 100 110
....*....|....*....|....*....|.
gi 1370457959 79 -------LVETACRKSLKALKLNYLDLYLIH 102
Cdd:cd19153 92 efdysaeRVRASVATSLERLHTTYLDVVYLH 122
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
21-102 |
5.94e-03 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 37.45 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370457959 21 EAVKEAIDAGYRHFDCAYFYHN---EREVGAGirckIKEGAVRREDLFIATKlwCTCHKKSLVETACR------KSLKAL 91
Cdd:PLN02587 35 ASVREAFRLGINFFDTSPYYGGtlsEKVLGKA----LKALGIPREKYVVSTK--CGRYGEGFDFSAERvtksvdESLARL 108
|
90
....*....|.
gi 1370457959 92 KLNYLDLYLIH 102
Cdd:PLN02587 109 QLDYVDILHCH 119
|
|
| |
