|
Name |
Accession |
Description |
Interval |
E-value |
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
1-387 |
0e+00 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 707.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 1 MDRFTYWNPTKLIFGKGEVSALSDELKHYGKNVLLVYGGGSIKRNGLYDQVVSILKESGAAITELAGVEPNPRLTTVRKG 80
Cdd:COG1979 1 MNNFTFYNPTKIIFGKGQIAKLGEEIPKYGKKVLLVYGGGSIKKNGLYDQVKAALKEAGIEVVEFGGVEPNPRLETVRKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 81 VELCKENQIDFILAVGGGSVIDATKAIAAGAKYDGDAWDIVTRKHVPMEAIPFGTVLTLAATGSEMNSGSVITNWETNEK 160
Cdd:COG1979 81 VELCKEEGIDFILAVGGGSVIDGAKAIAAGAKYDGDPWDILTGKAPVEKALPLGTVLTLPATGSEMNSGSVITNEETKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 161 YGWGSPAVFPKFSILDPVNTFTVPKNHTIYGMVDMMSHVFEQYFHHTENTPYQDRMCEGLLRTVIETAPKLINDLENYEL 240
Cdd:COG1979 161 LGFGSPLVFPKFSILDPELTYTLPKRQTANGIVDIFSHVMEQYFTYPVDAPLQDRFAEGLLRTLIEEGPKALKDPEDYDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 241 RETILFTGTIALNGMLSMGARGDWASHNIEHAVSAVYDIPHAGGLAILFPNWMKHVIQENPGRFKQLAVRVFDVDPagKT 320
Cdd:COG1979 241 RANLMWAATLALNGLIGAGVPQDWATHMIEHELSALYDIDHGAGLAIVLPAWMRYVLEEKPEKFAQYAERVWGITE--GD 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515928379 321 DEEVGLEGIEKLSAFWTSLGAPNRLADYDINDEKIDLIADRAMARGE--FGQFKKLNKEDVLAILNASL 387
Cdd:COG1979 319 DEERALEGIEATEEFFESLGLPTRLSEYGIDEEDIEEMAEKATAHGMtaLGEFKDLTPEDVREILELAL 387
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
4-384 |
0e+00 |
|
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor NAD(P)H being oxidized in the process; The butanol dehydrogenase (BDH) is involved in the final step of the butanol formation pathway in anaerobic micro-organism. Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor NAD(P)H being oxidized in the process. Activity in the reverse direction is 50-fold lower than that in the forward direction. The NADH-BDH has higher activity with longer chained aldehydes and is inhibited by metabolites containing an adenine moiety. This protein family belongs to the so-called iron-containing alcohol dehydrogenase superfamily. Since members of this superfamily use different divalent ions, preferentially iron or zinc, it has been suggested to be renamed to family III metal-dependent polyol dehydrogenases. This family also includes E. coli YqhD enzyme, an NADP-dependent dehydrogenase whose activity measurements with several alcohols demonstrate preference for alcohols longer than C3. The active site of YqhD contains a Zn metal, and a modified NADPH cofactor bearing OH groups on the saturated C5 and C6 atoms, possibly due to oxygen stress on the enzyme, which would functionally work under anaerobic conditions.
Pssm-ID: 341466 [Multi-domain] Cd Length: 382 Bit Score: 643.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 4 FTYWNPTKLIFGKGEVSALSDELKHYGKNVLLVYGGGSIKRNGLYDQVVSILKESGAAITELAGVEPNPRLTTVRKGVEL 83
Cdd:cd08187 2 FTFYNPTKIIFGKGAIEELGEEIKKYGKKVLLVYGGGSIKKNGLYDRVVASLKEAGIEVVEFGGVEPNPRLETVREGIEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 84 CKENQIDFILAVGGGSVIDATKAIAAGAKYDGDAWDIVTRKHVPMEAIPFGTVLTLAATGSEMNSGSVITNWETNEKYGW 163
Cdd:cd08187 82 AREENVDFILAVGGGSVIDAAKAIAAGAKYDGDVWDFFTGKAPPEKALPVGTVLTLAATGSEMNGGAVITNEETKEKLGF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 164 GSPAVFPKFSILDPVNTFTVPKNHTIYGMVDMMSHVFEQYFHHTENTPYQDRMCEGLLRTVIETAPKLINDLENYELRET 243
Cdd:cd08187 162 GSPLLRPKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQYFTGTEDAPLQDRLAEGLLRTVIENGPKALKDPDDYEARAN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 244 ILFTGTIALNGMLSMGARGDWASHNIEHAVSAVYDIPHAGGLAILFPNWMKHVIQENPGRFKQLAVRVFDVDPaGKTDEE 323
Cdd:cd08187 242 LMWAATLALNGLLGAGRGGDWATHAIEHELSALYDITHGAGLAIVFPAWMRYVLKKKPERFAQFARRVFGIDP-GGDDEE 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515928379 324 VGLEGIEKLSAFWTSLGAPNRLADYDINDEKIDLIADRAMARGE-FGQFKKLNKEDVLAILN 384
Cdd:cd08187 321 TALEGIEALEEFFKSIGLPTTLSELGIDEEDIEEMAEKAVRGGGlGGGFKPLTREDIEEILK 382
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
9-379 |
2.11e-122 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 358.07 E-value: 2.11e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 9 PTKLIFGKGEVSALSDELKHYGKNVLLVYGGGSIKrNGLYDQVVSILKESGAAITELAGVEPNPRLTTVRKGVELCKENQ 88
Cdd:pfam00465 1 PTRIVFGAGALAELGEELKRLGARALIVTDPGSLK-SGLLDKVLASLEEAGIEVVVFDGVEPEPTLEEVDEAAALAREAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 89 IDFILAVGGGSVIDATKAIAAGAKYDGDAWDIVTRKHVPMEAIPFGTVLTLAATGSEMNSGSVITNWETNEKYGWGSPAV 168
Cdd:pfam00465 80 ADVIIAVGGGSVIDTAKAIALLLTNPGDVWDYLGGKPLTKPALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFSPKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 169 FPKFSILDPVNTFTVPKNHTIYGMVDMMSHVFEQYFhHTENTPYQDRMCEGLLRTVIETAPKLINDLENYELRETILFTG 248
Cdd:pfam00465 160 LPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYV-SKGANPLTDALALEAIRLIAENLPRAVADGEDLEARENMLLAS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 249 TIALNGMLSMGaRGdwASHNIEHAVSAVYDIPHAGGLAILFPNWMKHVIQENPGRFKQLAVRVFdvdpaGKTDEEVGLEG 328
Cdd:pfam00465 239 TLAGLAFSNAG-LG--AAHALAHALGGRYGIPHGLANAILLPYVLRFNAPAAPEKLAQLARALG-----EDSDEEAAEEA 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 515928379 329 IEKLSAFWTSLGAPNRLADYDINDEKIDLIADRAMARGEF-GQFKKLNKEDV 379
Cdd:pfam00465 311 IEALRELLRELGLPTTLSELGVTEEDLDALAEAALRDRSLaNNPRPLTAEDI 362
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
1-366 |
5.01e-104 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 312.11 E-value: 5.01e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 1 MDRFTYWNPTKLIFGKGEVSALSDELKHyGKNVLLVYGGGSIKRNGLYDQVVSILKesGAAITELAGVEPNPRLTTVRKG 80
Cdd:PRK15138 1 MNNFNLHTPTRILFGKGAIAGLREQIPA-DARVLITYGGGSVKKTGVLDQVLDALK--GMDVLEFGGIEPNPTYETLMKA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 81 VELCKENQIDFILAVGGGSVIDATKAIAAGAKYDG--DAWDIV-TRKHVPMEAIPFGTVLTLAATGSEMNSGSVITNWET 157
Cdd:PRK15138 78 VKLVREEKITFLLAVGGGSVLDGTKFIAAAANYPEniDPWHILeTGGKEIKSAIPMGSVLTLPATGSESNAGAVISRKTT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 158 NEKYGWGSPAVFPKFSILDPVNTFTVPKNHTIYGMVDMMSHVFEQYFHHTENTPYQDRMCEGLLRTVIETAPKLINDLEN 237
Cdd:PRK15138 158 GDKQAFHSPHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTYPVDAKIQDRFAEGILLTLIEEGPKALKEPEN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 238 YELRETILFTGTIALNGMLSMGARGDWASHNIEHAVSAVYDIPHAGGLAILFPNWMKHVIQENPGRFKQLAVRVFDVDpA 317
Cdd:PRK15138 238 YDVRANVMWAATQALNGLIGAGVPQDWATHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKLLQYAERVWNIT-E 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 515928379 318 GKTDEEVGlEGIEKLSAFWTSLGAPNRLADYDINDEKIDLIADRAMARG 366
Cdd:PRK15138 317 GSDDERID-AAIAATRNFFEQMGVPTRLSDYGLDGSSIPALLKKLEEHG 364
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
6-383 |
6.43e-102 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase-like (ADH) proteins. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase fold and is a member of the iron-containing alcohol dehydrogenase-like family. They are distinct from other alcohol dehydrogenases which contain different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341464 [Multi-domain] Cd Length: 379 Bit Score: 306.35 E-value: 6.43e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 6 YWNPTKLIFGKGEVSALSDELKHYGKNVLLVYGGGSIKRNGLYDQVVSILKESGAAITELAGVEPNPRLTTVRKGVELCK 85
Cdd:cd08185 1 YYQPTRILFGAGKLNELGEEALRPGKKALIVTGKGSSKKTGLLDRVKKLLEKAGVEVVVFDKVEPNPLTTTVMEGAALAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 86 ENQIDFILAVGGGSVIDATKAIAAGAKYDGDAWDIV---------TRKHVPMEAIPfgtvlTLAATGSEMNSGSVITNWE 156
Cdd:cd08185 81 EEGCDFVIGLGGGSSMDAAKAIAFMATNPGDIWDYIfggtgkgppPEKALPIIAIP-----TTAGTGSEVDPWAVITNPE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 157 TNEKYGWGSPAVFPKFSILDPVNTFTVPKNHTIY-GMvDMMSHVFEQYFhHTENTPYQDRMCEGLLRTVIETAPKLINDL 235
Cdd:cd08185 156 TKEKKGIGHPALFPKVSIVDPELMLTVPPRVTAYtGF-DALFHAFESYI-SKNANPFSDMLALEAIRLVAKYLPRAVKDG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 236 ENYELRETILFTGTIAlnGMlSMGARGDWASHNIEHAVSAVY-DIPHAGGLAILFPNWMKHVIQENPGRFKQLAvrvfDV 314
Cdd:cd08185 234 SDLEAREKMAWASTLA--GI-VIANSGTTLPHGLEHPLSGYHpNIPHGAGLAALYPAYFEFTIEKAPEKFAFVA----RA 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515928379 315 DPAGKTDEEVGLEGIEKLSAFWTSLGAPNRLADYDINDEKIDLIADRAM--ARGEFGQF-KKLNKEDVLAIL 383
Cdd:cd08185 307 EASGLSDAKAAEDFIEALRKLLKDIGLDDLLSDLGVTEEDIPWLAENAMetMGGLFANNpVELTEEDIVEIY 378
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
4-387 |
6.49e-90 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 275.85 E-value: 6.49e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 4 FTYWNPTKLIFGKGEVSALSDELKHYG-KNVLLVyGGGSIKRNGLYDQVVSILKESGAAITELAGVEPNPRLTTVRKGVE 82
Cdd:COG1454 3 FTFRLPTRIVFGAGALAELGEELKRLGaKRALIV-TDPGLAKLGLLDRVLDALEAAGIEVVVFDDVEPNPTVETVEAGAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 83 LCKENQIDFILAVGGGSVIDATKAIAAGAKYDGDAWDIVTRKHVPMEAIPFGTVLTLAATGSEMNSGSVITNWETNEKYG 162
Cdd:COG1454 82 AAREFGADVVIALGGGSAIDAAKAIALLATNPGDLEDYLGIKKVPGPPLPLIAIPTTAGTGSEVTPFAVITDPETGVKKG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 163 WGSPAVFPKFSILDPVNTFTVPKNHTIY-GMvDMMSHVFEQYFhHTENTPYQDRMCEGLLRTVIETAPKLINDLENYELR 241
Cdd:COG1454 162 IADPELLPDVAILDPELTLTLPPSLTAAtGM-DALTHAIEAYV-SKGANPLTDALALEAIRLIARNLPRAVADGDDLEAR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 242 ETILFTGTIAlnGM----LSMGargdwASHNIEHAVSAVYDIPHAGGLAILFPNWMKHVIQENPGRFKQLAvRVFDVDpA 317
Cdd:COG1454 240 EKMALASLLA--GMafanAGLG-----AVHALAHPLGGLFHVPHGLANAILLPHVLRFNAPAAPERYAEIA-RALGLD-V 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515928379 318 GKTDEEVGLEGIEKLSAFWTSLGAPNRLADYDINDEKIDLIADRAMARGEFGQF-KKLNKEDVLAILNASL 387
Cdd:COG1454 311 GLSDEEAAEALIEAIRELLRDLGIPTRLSELGVTEEDLPELAELALADRCLANNpRPLTEEDIEAILRAAY 381
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
9-383 |
1.96e-86 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. They contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases, insect-type, or short-chain alcohol dehydrogenases, iron-containing alcohol dehydrogenases, among others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.
Pssm-ID: 341481 [Multi-domain] Cd Length: 372 Bit Score: 266.62 E-value: 1.96e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 9 PTKLIFGKGEVSALSDELKHYG-KNVLLVYGGGsIKRNGLYDQVVSILKESGAAITELAGVEPNPRLTTVRKGVELCKEN 87
Cdd:cd08551 1 PTRIVFGAGALARLGEELKALGgKKVLLVTDPG-LVKAGLLDKVLESLKAAGIEVEVFDDVEPNPTVETVEAAAELAREE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 88 QIDFILAVGGGSVIDATKAIAAGAKYDGDAWDIVTRKHVPMEAIPFGTVLTLAATGSEMNSGSVITNWETNEKYGWGSPA 167
Cdd:cd08551 80 GADLVIAVGGGSVLDTAKAIAVLATNGGSIRDYEGIGKVPKPGLPLIAIPTTAGTGSEVTPNAVITDPETGRKMGIVSPY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 168 VFPKFSILDPVNTFTVPKNHTIYGMVDMMSHVFEQYFhHTENTPYQDRMCEGLLRTVIETAPKLINDLENYELRETILFT 247
Cdd:cd08551 160 LLPDVAILDPELTLSLPPSVTAATGMDALTHAIEAYT-SKKANPISDALALEAIRLIGKNLRRAVADGSDLEAREAMLLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 248 GTIAlnGMlSMGARGDWASHNIEHAVSAVYDIPHAGGLAILFPNWMKHVIQENPGRFKQLAvRVFDVDPAGKTDEEVGLE 327
Cdd:cd08551 239 SLLA--GI-AFGNAGLGAVHALAYPLGGRYHIPHGVANAILLPYVMEFNLPACPEKYAEIA-EALGEDVEGLSDEEAAEA 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 515928379 328 GIEKLSAFWTSLGAPNRLADYDINDEKIDLIADRAMA--RGEFGQFKKLNKEDVLAIL 383
Cdd:cd08551 315 AVEAVRELLRDLGIPTSLSELGVTEEDIPELAEDAMKsgRLLSNNPRPLTEEDIREIY 372
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
5-385 |
7.63e-79 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341485 [Multi-domain] Cd Length: 380 Bit Score: 247.45 E-value: 7.63e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 5 TYWNPTKLIFGKGEVSALSDELKHYG-KNVLLVYGGGsIKRNGLYDQVVSILKESGAAITELAGVEPNPRLTTVRKGVEL 83
Cdd:cd14863 1 TYSQLTPVIFGAGAVEQIGELLKELGcKKVLLVTDKG-LKKAGIVDKIIDLLEEAGIEVVVFDDVEPDPPDEIVDEAAEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 84 CKENQIDFILAVGGGSVIDATKAIAAGAKYDGDAWD-IVTRKHVPMEAIPFGTVLTLAATGSEMNSGSVITNWETNEKYG 162
Cdd:cd14863 80 AREEGADGVIGIGGGSVLDTAKAIAVLLTNPGPIIDyALAGPPVPKPGIPLIAIPTTAGTGSEVTPIAVITDEENGVKKS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 163 WGSPAVFPKFSILDPVNTFTVPKNHTIY-GMvDMMSHVFEQYFhHTENTPYQDRMCEGLLRTVIETAPKLINDLENYELR 241
Cdd:cd14863 160 LLGPFLVPDLAILDPELTVGLPPSLTAAtGM-DALSHAIEAYT-SKLANPMTDALALQAIRLIVKNLPRAVKDGDNLEAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 242 ETILFTGTIAlnGMlSMGARGDWASHNIEHAVSAVYDIPHAGGLAILFPNWMKHVIQENPGRFKQLAvRVFDVDPAGKTD 321
Cdd:cd14863 238 ENMLLASNLA--GI-AFNNAGTHIGHAIAHALGALYHIPHGLACALALPVVLEFNAEAYPEKVKKIA-KALGVSFPGESD 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515928379 322 EEVGLEGIEKLSAFWTSLGAPNRLADYDINDEKIDLIADrAMARGEFGQF--KKLNKEDVLAILNA 385
Cdd:cd14863 314 EELGEAVADAIREFMKELGIPSLFEDYGIDKEDLDKIAE-AVLKDPFAMFnpRPITEEEVAEILEA 378
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
4-383 |
9.64e-68 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341475 [Multi-domain] Cd Length: 367 Bit Score: 218.22 E-value: 9.64e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 4 FTYWNPTKLIFGKGEVSALSDELKHYG-KNVLLVyGGGSIKRNGLYDQVVSILKESGAAIteLAGVEPNPRLTTVRKGVE 82
Cdd:cd08196 1 WSYYQPVKIIFGEGILKELPDIIKELGgKRGLLV-TDPSFIKSGLAKRIVESLKGRIVAV--FSDVEPNPTVENVDKCAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 83 LCKENQIDFILAVGGGSVIDATKAIAAGAKYDGDAWDI------VTRKHVPMEAIPfgtvlTLAATGSEMNSGSVITNWE 156
Cdd:cd08196 78 LARENGADFVIAIGGGSVLDTAKAAACLAKTDGSIEDYlegkkkIPKKGLPLIAIP-----TTAGTGSEVTPVAVLTDKE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 157 TNEKYGWGSPAVFPKFSILDPVNTFTVPKNHT-IYGMvDMMSHVFEQYF--HHtenTPYQDRMCEGLLRTVIETAPKLIN 233
Cdd:cd08196 153 KGKKAPLVSPGFYPDIAIVDPELTYSMPPKVTaSTGI-DALCHAIEAYWsiNH---QPISDALALEAAKLVLENLEKAYN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 234 DLENYELRETILFTGTIAlnGmLSMGARGDWASHNIEHAVSAVYDIPHAGGLAILFPNWMKHVIQENPGRFKQLAVRVfd 313
Cdd:cd08196 229 NPNDKEAREKMALASLLA--G-LAFSQTRTTASHACSYPLTSHFGIPHGEACALTLPSFIRLNAEALPGRLDELAKQL-- 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515928379 314 vdpaGKTDEEVGLEGIEKLSAfwtSLGAPNRLADYDINDEKIDLIADRAMARGEFGQF-KKLNKEDVLAIL 383
Cdd:cd08196 304 ----GFKDAEELADKIEELKK---RIGLRTRLSELGITEEDLEEIVEESFHPNRANNNpVEVTKEDLEKLL 367
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
9-383 |
7.17e-63 |
|
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1,3-propanediol dehydrogenase (PPD) which is a member of the iron-containing alcohol dehydrogenase superfamily, and exhibits a dehydroquinate synthase-like fold. Protein sequence similarity search and other biochemical evidences suggest that they are close to the iron-containing 1,3-propanediol dehydrogenase (EC 1.1.1.202). 1,3-propanediol dehydrogenase catalyzes the oxidation of propane-1,3-diol to 3-hydroxypropanal with the simultaneous reduction of NADP+ to NADPH. The protein structure of Thermotoga maritima TM0920 gene contains one NADP+ and one iron ion.
Pssm-ID: 341460 [Multi-domain] Cd Length: 358 Bit Score: 205.51 E-value: 7.17e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 9 PTKLIFGKGEVSALSDELKHYGKNVLLVYGGGSIKRNGLYDQVVSILKESGAAITELAGVEPNPRLTTVRKGVELCKENQ 88
Cdd:cd08181 4 PTKVYFGKNCVEKHADELAALGKKALIVTGKHSAKKNGSLDDVTEALEENGIEYFIFDEVEENPSIETVEKGAELARKEG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 89 IDFILAVGGGSVIDATKAIAAGAKYDGDAWD----IVTRKHVPMEAIPfgtvlTLAATGSEMNSGSVITNWETNEKYGWG 164
Cdd:cd08181 84 ADFVIGIGGGSPLDAAKAIALLAANKDGDEDlfqnGKYNPPLPIVAIP-----TTAGTGSEVTPYSILTDHEKGTKKSFG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 165 SPAVFPKFSILDPVNTFTVPKNHTIYGMVDMMSHVFEQYFhHTENTPYQDRMCEGLLRTVIETAPKLINDLENYELRETI 244
Cdd:cd08181 159 NPLIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGYL-SVKATPLSDALALEALRLIGECLPNLLGDELDEEDREKL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 245 LFTGTIAlnGMLSMGArGDWASHNIEHAVSAVYDIPHAGGLAILFPNWMKHVIQENPGRFKQLAvrvfdvdpagktdEEV 324
Cdd:cd08181 238 MYASTLA--GMVIAQT-GTTLPHGLGYPLTYFKGIPHGRANGILLPAYLKLCEKQEPEKVDKIL-------------KLL 301
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 325 GLEGIEKLSAFWTSLGAPNRladyDINDEKIDLIADRAMARGEFGQF-KKLNKEDVLAIL 383
Cdd:cd08181 302 GFGSIEEFQKFLNRLLGKKE----ELSEEELEKYADEAMKAKNKKNTpGNVTKEDILRIY 357
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
6-366 |
2.00e-59 |
|
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in bacteria; NADPH-dependent butanol dehydrogenase (BDH) is involved in the butanol and ethanol formation pathway of some bacteria. The fermentation process is characterized by an acid producing growth phase, followed by a solvent producing phase. The latter phase is associated with the induction of solventogenic enzymes such as butanol dehydrogenase. The activity of the enzyme requires NADPH as cofactor, as well as divalent ions zinc or iron. This family is a member of the iron-containing alcohol dehydrogenase superfamily. Protein structure has a dehydroquinate synthase-like fold.
Pssm-ID: 341458 [Multi-domain] Cd Length: 379 Bit Score: 197.03 E-value: 2.00e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 6 YWNPTKLIFGKGEVSALSdELKhyGKNVLLVYGGGSIKRNGLYDQVVSILKESGAAITELAGVEPNPRLTTVRKGVELCK 85
Cdd:cd08179 2 FFVPRDIYFGEGALEYLK-TLK--GKRAFIVTGGGSMKRNGFLDKVEDYLKEAGMEVKVFEGVEPDPSVETVEKGAEAMR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 86 ENQIDFILAVGGGSVIDATKAIAAGAKYDGDAWDIVT--------RKHVPMEAIPfgtvlTLAATGSEMNSGSVITNWET 157
Cdd:cd08179 79 EFEPDWIIAIGGGSVIDAAKAMWVFYEYPELTFEDALvpfplpelRKKARFIAIP-----STSGTGSEVTRASVITDTEK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 158 NEKYGWGSPAVFPKFSILDPVNTFTVPKNHTIY-GMvDMMSHVFEQYFHHTeNTPYQDRMCEGLLRTVIETAPKLINDLE 236
Cdd:cd08179 154 GIKYPLASFEITPDVAILDPELTMTMPPHVTANtGM-DALTHAIEAYVSTL-ANDFTDALALGAILDIFENLPKSYNGGK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 237 NYELRETILFTGTIA----LNGMLSMgargdwaSHNIEHAVSAVYDIPHagGL--AILFPNwmkhVIQENPGRFKqlAVR 310
Cdd:cd08179 232 DLEAREKMHNASCLAgmafSNSGLGI-------VHSMAHKGGAFFGIPH--GLanAILLPY----VIEFNSKDPE--ARA 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 311 VFDVDPAGKTDEEVGLEGIEKLSAFWTSLGAPNRLADYDINDE----KIDLIADRAMARG 366
Cdd:cd08179 297 RYAALLIGLTDEELVEDLIEAIEELNKKLGIPLSFKEAGIDEDeffaKLDEMAENAMNDA 356
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
7-384 |
3.22e-58 |
|
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between L-lactaldehyde and L-1,2-propanediol in Escherichia coli and other enterobacteria; Lactadehyde:propanediol oxidoreductase (LPO) is a member of the group III iron-activated dehydrogenases which catalyze the interconversion between L-lactaldehyde and L-1,2-propanediol in Escherichia coli and other enterobacteria. L-fucose and L-rhamnose are used by Escherichia coli through an inducible pathway mediated by the fucose regulon comprising four linked operons fucO, fucA, fucPIK, and fucR. The fucA-encoded aldolase catalyzes the formation of dihydroxyacetone phosphate and L-lactaldehyde. Under anaerobic conditions, with NADH as a cofactor, lactaldehyde is converted by a fucO-encoded lactadehyde:propanediol oxidoreductase (LPO) to L-1,2-propanediol, which is excreted as a fermentation product. In mutant strains, E. coli adapted to grow on L-1,2-propanediol, FucO catalyzes the oxidation of the polyol to L-lactaldehyde. FucO is induced regardless of the respiratory conditions of the culture, remains fully active in the absence of oxygen. In the presence of oxygen, this enzyme becomes oxidatively inactivated by a metal-catalyzed oxidation mechanism. FucO is an iron-dependent metalloenzyme that is inactivated by other metals, such as zinc, copper, or cadmium. This enzyme can also reduce glycol aldehyde with similar efficiency. Beside L-1,2-propanediol, the enzyme is also able to oxidize methanol as an alternative substrate.
Pssm-ID: 341455 [Multi-domain] Cd Length: 378 Bit Score: 193.92 E-value: 3.22e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 7 WNPTkLIFGKGEVSALSDELKHYG-KNVLLVYGGGSIKrNGLYDQVVSILKESGAAITELAGVEPNPRLTTVRKGVELCK 85
Cdd:cd08176 5 LNPT-SYFGWGAIEEIGEEAKKRGfKKALIVTDKGLVK-FGIVDKVTDVLKEAGIAYTVFDEVKPNPTIENVMAGVAAYK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 86 ENQIDFILAVGGGSVIDATKAIAAGAKYDG------DAWDIVTRKHVPMEAIPfgtvlTLAATGSEMNSGSVITNWETNE 159
Cdd:cd08176 83 ESGADGIIAVGGGSSIDTAKAIGIIVANPGadvrslEGVAPTKNPAVPIIAVP-----TTAGTGSEVTINYVITDTEKKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 160 KYGWGSPAVFPKFSILDPVNTFTVPKNHTIY-GMvDMMSHVFEQYFhHTENTPYQDRMCEGLLRTVIETAPKLINDLENY 238
Cdd:cd08176 158 KFVCVDPHDIPTVAIVDPDLMSSMPKGLTAAtGM-DALTHAIEGYI-TKGAWELSDMLALKAIELIAKNLRKAVANPNNV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 239 ELRETILFTGTIAlnGM-LSMGARGdwASHNIEHAVSAVYDIPHagGL--AILFPNWMKHVIQENPGRFKQLAvRVFDVD 315
Cdd:cd08176 236 EARENMALAQYIA--GMaFSNVGLG--IVHSMAHPLSAFYDTPH--GVanAILLPYVMEFNAPATGEKYRDIA-RAMGVD 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515928379 316 PAGKTDEEVG---LEGIEKLSafwTSLGAPNRLADYDINDEKIDLIADRAMArgEF---GQFKKLNKEDVLAILN 384
Cdd:cd08176 309 TTGMSDEEAAeaaVDAVKKLS---KDVGIPQKLSELGVKEEDIEALAEDALN--DVctpGNPREATKEDIIALYK 378
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
4-387 |
5.43e-56 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341487 [Multi-domain] Cd Length: 383 Bit Score: 188.13 E-value: 5.43e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 4 FTYWNPTKLIFGKGEVSALSDELKHYG-KNVLLVYGGGsIKRNGLYDQVVSILKESGAAITELAGVEPNPRLTTVRKGVE 82
Cdd:cd14865 1 FEFFNPTKIVSGAGALENLPAELARLGaRRPLIVTDKG-LAAAGLLKKVEDALGDAIEIVGVFDDVPPDSSVAVVNEAAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 83 LCKENQIDFILAVGGGSVIDATKAIAAGAKYDGDAWD------IVTRKHVPMEAIPfgtvlTLAATGSEMNSGSVITNWE 156
Cdd:cd14865 80 RAREAGADGIIAVGGGSVIDTAKGVNILLSEGGDDLDdygganRLTRPLKPLIAIP-----TTAGTGSEVTLVAVIKDEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 157 TNEKYGWGSPAVFPKFSILDPVNTFTVPKNHT-IYGMvDMMSHVFEQYfHHTENTPYQDRMCEGLLRTVIETAPKLINDL 235
Cdd:cd14865 155 KKVKLLFVSPFLLPDVAILDPRLTLSLPPKLTaATGM-DALTHAIEAY-TSLQKNPISDALALQAIRLISENLPKAVKNG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 236 ENYELRETILFTGTIA----LNGMLSMgargdwaSHNIEHAVSAVYDIPHAGGLAILFPNWMKHVIQENPGRFKQLAVR- 310
Cdd:cd14865 233 KDLEARLALAIAATMAgiafSNSMVGL-------VHAIAHAVGAVAGVPHGLANSILLPHVMRYNLDAAAERYAELALAl 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515928379 311 VFDVDPAGKTDEEVGLEGIEKLSAFWTSLGAPNRLADYDINDEKIDLIADRAMARGE-FGQFKKLNKEDVLAILNASL 387
Cdd:cd14865 306 AYGVTPAGRRAEEAIEAAIDLVRRLHELCGLPTRLRDVGVPEEQLEAIAELALNDGAiLFNPREVDPEDILAILEAAY 383
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
4-384 |
4.34e-54 |
|
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) dehydrogenase, a key enzyme in the microbial production of 1,3-PD that has been previously characterized as the product of dhaT gene in Klebsiella pneumoniae. 1,3-PD dehydrogenase is a member of the family III metal-dependent polyol dehydrogenases, which are shown to require a divalent metal ion for catalysis. However, some members of this family showed a dependence on Fe(2+) or Zn(2+) for activity.
Pssm-ID: 341467 [Multi-domain] Cd Length: 377 Bit Score: 183.10 E-value: 4.34e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 4 FTYWNPTKLIFGKGEVSALSDELKHYG-KNVLLVYGGGSIKrNGLYDQVVSILKESGAAITELAGVEPNPRLTTVRKGVE 82
Cdd:cd08188 1 FRFYIPPVNLFGPGCLKEIGDELKKLGgKKALIVTDKGLVK-LGLVKKVTDVLEEAGIEYVIFDGVQPNPTVTNVNEGLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 83 LCKENQIDFILAVGGGSVIDATKAIAAGAKYDGDAWD-----IVTRKHVPMEAIPfgtvlTLAATGSEMNSGSVITNWET 157
Cdd:cd08188 80 LFKENGCDFIISVGGGSAHDCAKAIGILATNGGEIEDyegvdKSKKPGLPLIAIN-----TTAGTASEVTRFAVITDEER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 158 NEKYGWGSPAVFPKFSILDPVNTFTVPKNHTIY-GMvDMMSHVFEQYFhHTENTPYQDRMCEGLLRTVIETAPKLINDLE 236
Cdd:cd08188 155 HVKMVIVDWNVTPTIAVNDPELMLGMPPSLTAAtGM-DALTHAIEAYV-STGATPLTDALALEAIRLIAENLPKAVANGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 237 NYELRETIL---FTGTIALN----GMLsmgargdwasHNIEHAVSAVYDIPHagGL--AILFPNWMKHVIQENPGRFKQL 307
Cdd:cd08188 233 DLEARENMAyaqFLAGMAFNnaglGYV----------HAMAHQLGGFYNLPH--GVcnAILLPHVMEFNLPACPERFADI 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515928379 308 AvRVFDVDPAGKTDEEVGLEGIEKLSAFWTSLGAPNRLADYDINDEKIDLIADRAMARG-EFGQFKKLNKEDVLAILN 384
Cdd:cd08188 301 A-RALGENTEGLSDEEAAEAAIEAIRKLSRRVGIPSGLKELGVKEEDFPLLAENALKDAcGPTNPRQATKEDVIAIYR 377
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
9-364 |
7.34e-53 |
|
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to iron-containing alcohol dehydrogenase (Fe-ADH), most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.
Pssm-ID: 341483 [Multi-domain] Cd Length: 374 Bit Score: 179.63 E-value: 7.34e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 9 PTKLIFGKGEVSALSDELKHYG-KNVLLVYGGGsIKRNGLYDQVVSILKESGAAITELAGVEPNPRLTTVRKGVELCKEN 87
Cdd:cd14861 3 PTRIRFGAGAIAELPEELKALGiRRPLLVTDPG-LAALGIVDRVLEALGAAGLSPAVFSDVPPNPTEADVEAGVAAYREG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 88 QIDFILAVGGGSVIDATKAIAAGAKYDGDAWD---------IVTRKHVPMEAIPfgtvlTLAATGSEMNSGSVITNWETN 158
Cdd:cd14861 82 GCDGIIALGGGSAIDAAKAIALMATHPGPLWDyedgeggpaAITPAVPPLIAIP-----TTAGTGSEVGRAAVITDDDTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 159 EKYGWGSPAVFPKFSILDPVNTFTVPKNHTIY-GMvDMMSHVFEQYFHHTENtPyqdrMCEGL----LRTVIETAPKLIN 233
Cdd:cd14861 157 RKKIIFSPKLLPKVAICDPELTLGLPPRLTAAtGM-DALTHCIEAYLSPGFH-P----MADGIalegLRLISEWLPRAVA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 234 DLENYELREtilftgtialnGML---SMGA----RGDWASHNIEHAVSAVYDIPHagGL--AILFPNWMKHVIQENPGRF 304
Cdd:cd14861 231 DGSDLEARG-----------EMMmaaLMGAvafqKGLGAVHALAHALGALYGLHH--GLlnAILLPYVLRFNRPAVEDKL 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 305 KQLAVRvfdVDPAGKTDEEVgLEGIEKLSAfwtSLGAPNRLADYDINDEKIDLIADRAMA 364
Cdd:cd14861 298 ARLARA---LGLGLGGFDDF-IAWVEDLNE---RLGLPATLSELGVTEDDLDELAELALA 350
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
10-365 |
2.08e-52 |
|
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol dehydrogenase (ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. The ADH of hyperthermophilic archaeon Thermococcus hydrothermalis oxidizes a series of primary aliphatic and aromatic alcohols, preferentially from C2 to C8, but is also active towards methanol and glycerol, and is stereospecific for monoterpenes. It has been suggested that the type III ADHs in microorganisms are involved in acetaldehyde detoxication rather than in alcohol turnover.
Pssm-ID: 341465 [Multi-domain] Cd Length: 380 Bit Score: 178.61 E-value: 2.08e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 10 TKLIFGKGEVSALSDELKHYG-KNVLLVYGGGSIKRNGLYDQVVSILKESGAAITELAGVEPNPRLTTVRKGVELCKENQ 88
Cdd:cd08186 2 TTLYFGVGAIAKIKDILKDLGiDKVIIVTGRSSYKKSGAWDDVEKALEENGIEYVVYDKVTPNPTVDQADEAAKLARDFG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 89 IDFILAVGGGSVIDATKAIAAGAKY-DGDAWDIVTRKHVPMEAIPFGTVLTLAATGSEMNSGSVITNWETNEKYGWGSPA 167
Cdd:cd08186 82 ADAVIAIGGGSPIDTAKSVAVLLAYgGKTARDLYGFRFAPERALPLVAINLTHGTGSEVDRFAVATIPEKGYKPGIAYDC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 168 VFPKFSILDPVNTFTVPKNHTIYGMVDMMSHVFEQYFHHTENtPYQDRMCEGLLRTVIETAPKLINDLENYELRETILFT 247
Cdd:cd08186 162 IYPLYAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATTKVSS-PYVITLAKEAIRLIAEYLPRALANPKDLEARYWLLYA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 248 GTIA----LNGMLSMGargdwasHNIEHAVSAVY-DIPHAGGLAILFPNWMKHViqeNPGRFKQLAVRVFDVDPAGKTDE 322
Cdd:cd08186 241 SMIAgiaiDNGLLHLT-------HALEHPLSGLKpELPHGLGLALLGPAVVKYI---YKAVPETLADILRPIVPGLKGTP 310
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 515928379 323 EVGLEGIEKLSAFWTSLGAPNRLADYDINDEKIDLIADRAMAR 365
Cdd:cd08186 311 DEAEKAARGVEEFLFSVGFTEKLSDYGFTEDDVDRLVELAFTT 353
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
7-385 |
1.26e-51 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized.
Pssm-ID: 341468 [Multi-domain] Cd Length: 378 Bit Score: 176.51 E-value: 1.26e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 7 WNPTKLIFGKGEVSALSDELKHYG-KNVLLVYGGGSIKRnGLYDQVVSILKESGAAITELAGVEPNPRLTTVRKGVELCK 85
Cdd:cd08189 3 WPEPELFEGAGSLLQLPEALKKLGiKRVLIVTDKGLVKL-GLLDPLLDALKKAGIEYVVFDGVVPDPTIDNVEEGLALYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 86 ENQIDFILAVGGGSVIDATKAIAAGAKYDGDawDI--------VTRKHVPMEAIPfgtvlTLAATGSEMNSGSVITNWET 157
Cdd:cd08189 82 ENGCDAIIAIGGGSVIDCAKVIAARAANPKK--SVrklkgllkVRKKLPPLIAVP-----TTAGTGSEATIAAVITDPET 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 158 NEKYGWGSPAVFPKFSILDPVNTFTVPKNHTIY-GMvDMMSHVFEQY--FHHTENTpyqDRMCEGLLRTVIETAPKLIND 234
Cdd:cd08189 155 HEKYAINDPKLIPDAAVLDPELTLGLPPAITAAtGM-DALTHAVEAYisRSATKET---DEYALEAVKLIFENLPKAYED 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 235 LENYELREtilftgtialnGMLsmgargdWAS---------------HNIEHAVSAVYDIPHAGGLAILFPnwmkHVIQE 299
Cdd:cd08189 231 GSDLEARE-----------NML-------LASyyaglaftrayvgyvHAIAHQLGGLYGVPHGLANAVVLP----HVLEF 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 300 N----PGRFKQLAVRVfDVDPAGKTDEEVGLEGIEKLSAFWTSLGAPNRLAdyDINDEKIDLIADRAMARGEFGQF--KK 373
Cdd:cd08189 289 YgpaaEKRLAELADAA-GLGDSGESDSEKAEAFIAAIRELNRRMGIPTTLE--ELKEEDIPEIAKRALKEANPLYPvpRI 365
|
410
....*....|..
gi 515928379 374 LNKEDVLAILNA 385
Cdd:cd08189 366 MDRKDCEELLRK 377
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-366 |
7.87e-51 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.
Pssm-ID: 341473 [Multi-domain] Cd Length: 378 Bit Score: 174.64 E-value: 7.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 9 PTKLIFGKGEVSALSDELKH-YGKNVLLVyGGGSIKRNGLYDQVVSILKESGAAITELAGVEPNPRLTTVRKGVELCKEN 87
Cdd:cd08194 1 PRTIIIGGGALEELGEEAASlGGKRALIV-TDKVMVKLGLVDKVTQLLAEAGIAYAVFDDVVSEPTDEMVEEGLALYKEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 88 QIDFILAVGGGSVIDATKAIAAGAKYDGDAWDIVTRKHVPMEAIPFGTVLTLAATGSEMNSGSVITNWETNEKYGWGSPA 167
Cdd:cd08194 80 GCDFIVALGGGSPIDTAKAIAVLATNGGPIRDYMGPRKVDKPGLPLIAIPTTAGTGSEVTRFTVITDTETDVKMLLKGPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 168 VFPKFSILDPVNTFTVPKNHTIYGMVDMMSHVFEQYFHHTENtPYQDRMCEGLLRTVIETAPKLINDLENYELRETILFT 247
Cdd:cd08194 160 LLPAVAIVDPELTLSMPPRVTAATGIDALTHAIEAYVSRKAQ-PLTDTLALSAIKLIGRNLRRAYADGDDLEAREAMMLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 248 GT---IALNGmlsmgargdwASHNIEHAVS----AVYDIPHagGL--AILFPNWMKHVIQENPGRFKQLAvRVFDVDPAG 318
Cdd:cd08194 239 ALeagIAFSN----------SSVALVHGMSrpigALFHVPH--GLsnAMLLPAVTEFSLPGAPERYAEIA-RAMGIATEG 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 515928379 319 KTDEEVGLEGIEKLSAFWTSLGAPnRLADYDINDEK----IDLIADRAMARG 366
Cdd:cd08194 306 DSDEEAAEKLVEALERLCADLEIP-TLREYGIDEEEfeaaLDKMAEDALASG 356
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
9-384 |
6.66e-50 |
|
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde (PnAA) to hydroxyethylphosphoate (HEP); Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde (PnAA) to hydroxyethylphosphoate (HEP) with either NADH or NADPH as a cofactor, although NADH is the preferred cofactor. PnAA is a biosynthetic intermediate for several phosphonates such as the antibiotic fosfomycin, phosphinothricin tripeptide (PTT), and 2-aminoethylphosphonate (AEP). This enzyme is named PhpC in PTT biosynthesis pathway in Streptomyces hygroscopicus and S. viridochromogenes.
Pssm-ID: 341461 [Multi-domain] Cd Length: 370 Bit Score: 172.02 E-value: 6.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 9 PTKLIFGKGEVSALSDELKHYG-KNVLLVYGGGSIKRNGLYDQVVSILKESgaAITELAGVEPNPRLTTVRKGVELCKEN 87
Cdd:cd08182 1 PVKIIFGPGALAELKDLLGGLGaRRVLLVTGPSAVRESGAADILDALGGRI--PVVVFSDFSPNPDLEDLERGIELFRES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 88 QIDFILAVGGGSVIDATKAIAAGAKYDGDAWDIVTRKHVPME--AIPFGTVLTLAATGSEMNSGSVItnW--ETNEKYGW 163
Cdd:cd08182 79 GPDVIIAVGGGSVIDTAKAIAALLGSPGENLLLLRTGEKAPEenALPLIAIPTTAGTGSEVTPFATI--WdeAEGKKYSL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 164 GSPAVFPKFSILDPVNTFTVPKNHTIYGMVDMMSHVFEQYF-HHTenTPYQDRMCEGLLRTVIETAPKLINDLENYELRE 242
Cdd:cd08182 157 AHPSLYPDAAILDPELTLSLPLYLTASTGLDALSHAIESIWsVNA--NPESRAYALRAIRLILENLPLLLENLPNLEARE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 243 TIL---------F--TGTIalngmlsmgargdwASHNIEHAVSAVYDIPHagGLA--ILFPNWMKHVIQENPGRFKQLAV 309
Cdd:cd08182 235 AMAeasllaglaIsiTKTT--------------AAHAISYPLTSRYGVPH--GHAcaLTLPAVLRYNAGADDECDDDPRG 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515928379 310 RvFDVDPAGKTDEEvglEGIEKLSAFWTSLGAPNRLADYDINDEKIDLIADRAMARGEFGQF-KKLNKEDVLAILN 384
Cdd:cd08182 299 R-EILLALGASDPA---EAAERLRALLESLGLPTRLSEYGVTAEDLEALAASVNTPERLKNNpVRLSEEDLLRLLE 370
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
5-363 |
7.40e-47 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341484 [Multi-domain] Cd Length: 375 Bit Score: 163.93 E-value: 7.40e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 5 TYWNPTKLIFGKGEVSALSDelkHYGKNVLLVYGGGsIKRNGLYDQVVSILKESGAAITELAGVEPNPRLTTVRKGVELC 84
Cdd:cd14862 2 WYFSSPKIVFGEDALSHLEQ---LSGKRALIVTDKV-LVKLGLLKKVLKRLLQAGFEVEVFDEVEPEPPLETVLKGAEAM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 85 KENQIDFILAVGGGSVIDATKAiaagakydgdAWDIVTRKHVPMEAIPFGTVL------------TLAATGSEMNSGSVI 152
Cdd:cd14862 78 REFEPDLIIALGGGSVMDAAKA----------AWVLYERPDLDPEDISPLDLLglrkkakliaipTTSGTGSEATWAIVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 153 TNWETNEKYGWGSPAVFPKFSILDPVNTFTVPKNHTIYGMVDMMSHVFEQYFHHTENtPYQDRMCEGLLRTVIETAPKLI 232
Cdd:cd14862 148 TDTEEPRKIAVANPELVPDVAILDPEFVLGMPPKLTAGTGLDALAHAVEAYLSTWSN-DFSDALALKAIELIFKYLPRAY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 233 NDLENYELRETILFTGTIA----LNGMLSMGargdwasHNIEHAVSAVYDIPHagGLAI-LFpnwMKHVIQEN----PGR 303
Cdd:cd14862 227 KDGDDLEAREKMHNAATIAglafGNSQAGLA-------HALGHSLGAVFHVPH--GIAVgLF---LPYVIEFYakvtDER 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515928379 304 FKQLAVrvfdVDPAGKTDEEVGLEGIEKLSAFWTSLGAPNRLADYDIN----DEKIDLIADRAM 363
Cdd:cd14862 295 YDLLKL----LGIEARDEEEALKKLVEAIRELYKEVGQPLSIKDLGISeeefEEKLDELVEYAM 354
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-383 |
7.00e-46 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341462 [Multi-domain] Cd Length: 377 Bit Score: 161.52 E-value: 7.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 9 PTKLIFGKGEVSALSDELKHYGKNVLLVYGGGSIkRNGLYDQVVSILKESGAAITELAGVEpNPRLTTVRKGVELCKENQ 88
Cdd:cd08183 1 PPRIVFGRGSLQELGELAAELGKRALLVTGRSSL-RSGRLARLLEALEAAGIEVALFSVSG-EPTVETVDAAVALAREAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 89 IDFILAVGGGSVIDATKAIAAGAKYDG---DAWDIV------TRKHVPMEAIPfgtvlTLAATGSEMNSGSVITNWETNE 159
Cdd:cd08183 79 CDVVIAIGGGSVIDAAKAIAALLTNEGsvlDYLEVVgkgrplTEPPLPFIAIP-----TTAGTGSEVTKNAVLSSPEHGV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 160 KYGWGSPAVFPKFSILDPVNTFTVPKNHTIY-GMvDMMSHVFEQYFHHTENtPYQDRMC-EGLLRtVIETAPKLINDLEN 237
Cdd:cd08183 154 KVSLRSPSMLPDVALVDPELTLSLPPEVTAAsGL-DALTQLIEPYVSRKAN-PLTDALArEGLRL-AARSLRRAYEDGED 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 238 YELRETI----LFTGtIAL-NGMLsmGargdwASHNIEHAVSAVYDIPHagGL--AILFPnwmkHVIQEN--------PG 302
Cdd:cd08183 231 LEAREDMalasLLGG-LALaNAGL--G-----AVHGLAGPLGGMFGAPH--GAicAALLP----PVLEANlralrerePD 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 303 RFKQLAVRVFDVDPAGkTDEEVGLEGIEKLSAFWTSLGAPnRLADYDINDEKIDLIADRAMARGEF-GQFKKLNKEDVLA 381
Cdd:cd08183 297 SPALARYRELAGILTG-DPDAAAEDGVEWLEELCEELGIP-RLSEYGLTEEDFPEIVEKARGSSSMkGNPIELSDEELLE 374
|
..
gi 515928379 382 IL 383
Cdd:cd08183 375 IL 376
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
13-364 |
2.33e-43 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341489 [Multi-domain] Cd Length: 374 Bit Score: 154.62 E-value: 2.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 13 IFGKGEVSALSDELKHYG-KNVLLVYGGGSIKrNGLYDQVVSILKESGAAITELAGVEPNPRLTTVRKGVELCKENQIDF 91
Cdd:cd17814 8 IFGVGARKLAGRYAKNLGaRKVLVVTDPGVIK-AGWVDEVLDSLEAEGLEYVVFSDVTPNPRDFEVMEGAELYREEGCDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 92 ILAVGGGSVIDATKAIAAGA-------KYDGdaWDIVTRKHVPMEAIPfgtvlTLAATGSEMNSGSVITNWETNEKYGWG 164
Cdd:cd17814 87 IVAVGGGSPIDCAKGIGIVVsngghilDYEG--VDKVRRPLPPLICIP-----TTAGSSADVSQFAIITDTERRVKMAII 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 165 SPAVFPKFSILDPVNTFTVPKNHTIYGMVDMMSHVFEQYFhHTENTPYQDRMCEGLLRTVIETAPKLINDLENYELRETI 244
Cdd:cd17814 160 SKTLVPDVSLIDPETLTTMDPELTACTGMDALTHAIEAYV-SNASSPLTDLHALEAIRLISENLPKAVADPDDLEAREKM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 245 LFTGTIAlnGM----LSMGargdwASHNIEHAVSAVYDIPHagGL--AILFPnwmkHVIQEN----PGRFKQLAvRVFDV 314
Cdd:cd17814 239 MLASLQA--GLafsnASLG-----AVHAMAHSLGGLLDLPH--GEcnALLLP----HVIRFNfpaaPERYRKIA-EAMGL 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 515928379 315 DPAGKTDEEVGLEGIEKLSAFWTSLGAPNRLADYDINDEKIDLIADRAMA 364
Cdd:cd17814 305 DVDGLDDEEVAERLIEAIRDLREDLGIPETLSELGVDEEDIPELAKRAMK 354
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-387 |
3.62e-41 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized.
Pssm-ID: 341470 [Multi-domain] Cd Length: 392 Bit Score: 149.30 E-value: 3.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 9 PTKLIFGKGEVSALSDELKHYGKNVLLVyGGGSIKRNGLYDQVVSILKESGAAITELAGVEPNPRLTTVRKGVELCKENQ 88
Cdd:cd08191 4 PSRLLFGPGARRALGRVAARLGSRVLIV-TDPRLASTPLVAELLAALTAAGVAVEVFDGGQPELPVSTVADAAAAARAFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 89 IDFILAVGGGSVIDATKAIAAGAKYDGDAWDIVTRKHVPMEAIPFGTVLTLAATGSEMNSGSVITNWETNEKYGWGSPAV 168
Cdd:cd08191 83 PDVVIGLGGGSNMDLAKVVALLLAHGGDPRDYYGEDRVPGPVLPLIAVPTTAGTGSEVTPVAVLTDPARGMKVGVSSPYL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 169 FPKFSILDPVNTFTVPKNHTIYGMVDMMSHVFEQY----FHHTE----------NTPYQDRMCEGLLRTVIETAPKLIND 234
Cdd:cd08191 163 RPAVAIVDPELTLTCPPGVTADSGIDALTHAIESYtardFPPFPrldpdpvyvgKNPLTDLLALEAIRLIGRHLPRAVRD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 235 LENYELRETILFTGTIAlnGMlSMGARGDWASHNIEHAVSAVYDIPHAGGLAILFPnwmkHVIQEN-PGRFKQLAV--RV 311
Cdd:cd08191 243 GDDLEARSGMALAALLA--GL-AFGTAGTAAAHALQYPIGALTHTSHGVGNGLLLP----YVMRFNrPARAAELAEiaRA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 312 FDVDPAGkTDEEVGLEGIEKLSAFWTSLGAPNRLADYDINDEKIDLIADRAMArgefgqFKKLNK--------EDVLAIL 383
Cdd:cd08191 316 LGVTTAG-TSEEAADRAIERVEELLARIGIPTTLADLGVTEADLPGLAEKALS------VTRLIAnnprppteEDLLRIL 388
|
....
gi 515928379 384 NASL 387
Cdd:cd08191 389 RAAF 392
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
10-364 |
2.56e-39 |
|
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This family contains hydroxyacid-oxoacid transhydrogenase (HOT), also known as D-2-hydroxyglutarate transhydrogenase. It catalyzes the conversion of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA), coupled to the stoichiometric conversion of alpha-ketoglutarate to D-2-hydroxyglutarate in gamma-Hydroxybutyrate catabolism. Unlike many other alcohols, which are oxidized by NAD-linked dehydrogenases, gamma-hydroxybutyrate is metabolized to succinate semialdehyde by hydroxyacid-oxoacid transhydrogenase which does not require free NAD or NADP; instead, it uses alpha-ketoglutarate as an acceptor, converting it to d-2-hydroxyglutarate. Alpha-ketoglutarate serves as an intermediate acceptor to regenerate NAD(P) required for the oxidation of GHB. HOT also catalyzes the reversible oxidation of a hydroxyacid obligatorily coupled to the reduction of an oxoacid, and requires no cofactor. In mammals, the HOT enzyme is located in mitochondria, and is expressed with an N-terminal mitochondrial targeting sequence. HOT enzyme is member of the metal-containing alcohol dehydrogenase family. It typically contains an iron although other metal ions may be used.
Pssm-ID: 341469 [Multi-domain] Cd Length: 412 Bit Score: 144.61 E-value: 2.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 10 TKLIFGKGEVSALSDELKHYG-KNVLLVYGGGsIKRNGLYDQVVSILKESGAAITELAGVEPNPRLTTVRKGVELCKENQ 88
Cdd:cd08190 2 SNIRFGPGATRELGMDLKRLGaKKVLVVTDPG-LAKLGLVERVLESLEKAGIEVVVYDGVRVEPTDESFEEAIEFAKEGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 89 IDFILAVGGGSVIDATKAIAAGAKYDGDAWD----------IVTRKHVPMEAIPfgtvlTLAATGSEMNSGSVITNWETN 158
Cdd:cd08190 81 FDAFVAVGGGSVIDTAKAANLYATHPGDFLDyvnapigkgkPVPGPLKPLIAIP-----TTAGTGSETTGVAIFDLEELK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 159 EKYGWGSPAVFPKFSILDPVNTFTVPKNHTIY-GMvDMMSHVFEQY-----------FHHTENTPYQ------DRMCEGL 220
Cdd:cd08190 156 VKTGISSRYLRPTLAIVDPLLTLTLPPRVTASsGF-DVLCHALESYtarpynarprpANPDERPAYQgsnpisDVWAEKA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 221 LRTVIETAPKLINDLENYELRETILFTGTIAlnGMlSMGARGDWASHNIEHAVSAV-------------YDIPHAGGLAI 287
Cdd:cd08190 235 IELIGKYLRRAVNDGDDLEARSNMLLASTLA--GI-GFGNAGVHLPHAMAYPIAGLvkdyrppgypvdhPHVPHGLSVAL 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515928379 288 LFPNWMKHVIQENPGRFKQLAvRVFDVDPAGKTDEEVGLEGIEKLSAFWTSLGAPNRLADYDINDEKIDLIADRAMA 364
Cdd:cd08190 312 TAPAVFRFTAPACPERHLEAA-ELLGADTSGASDRDAGEVLADALIKLMRDIGIPNGLSALGYSEDDIPALVEGTLP 387
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
9-362 |
2.58e-38 |
|
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol dehydrogenase bifunctional two-domain protein (AAD); This alcohol dehydrogenase domain is located on the C-terminal of a bifunctional two-domain protein. The N-terminal of the protein contains an acetaldehyde-CoA dehydrogenase domain. This protein is involved in pyruvate metabolism whereby pyruvate is converted to acetyl-CoA and formate by pyruvate formate-lysase (PFL). Under anaerobic condition, acetyl-CoA is reduced to acetaldehyde and ethanol by this two-domain protein. Acetyl-CoA is first converted into an enzyme-bound thiohemiacetal by the N-terminal acetaldehyde dehydrogenase domain. The enzyme-bound thiohemiacetal is subsequently reduced by the C-terminal NAD+-dependent alcohol dehydrogenase domain. In E. coli, this protein is called AdhE and has been shown to have pyruvate formate-lyase (PFL) deactivase activity, which leads to the inactivation of PFL, a key enzyme in anaerobic metabolism. In Escherichia coli and Entamoeba histolytica, this enzyme forms homopolymeric peptides composed of more than 20 protomers associated in a helical rod-like structure.
Pssm-ID: 341457 [Multi-domain] Cd Length: 400 Bit Score: 141.94 E-value: 2.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 9 PTKLIFGKGEVSALSDELKHyGKNVLLVYGGGSIKrNGLYDQVVSILKESGAAITELAGVEPNPRLTTVRKGVELCKENQ 88
Cdd:cd08178 3 PPKIYFEPGCLPYLLLELPG-VKRAFIVTDRVLYK-LGYVDKVLDVLEARGVETEVFSDVEPDPTLSTVRKGLEAMNAFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 89 IDFILAVGGGSVIDATKAIAAGAKYDGDAW-DIVTR---------------KHVPMEAIPfgtvlTLAATGSEMNSGSVI 152
Cdd:cd08178 81 PDVIIALGGGSAMDAAKIMWLFYEHPETKFeDLAQRfmdirkrvykfpklgKKAKLVAIP-----TTSGTGSEVTPFAVI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 153 TNWETNEKYGWGSPAVFPKFSILDPVNTFTVPKNHTIYGMVDMMSHVFEQYFhHTENTPYQDRMCEGLLRTVIETAPKLI 232
Cdd:cd08178 156 TDDKTGKKYPLADYALTPDMAIVDPELVMTMPKRLTADTGIDALTHAIEAYV-SVMASDYTDGLALQAIKLIFEYLPRSY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 233 NDLENYELRETILFTGTIAlnGM------LSMGargdwasHNIEHAVSAVYDIPHagGL--AILFPnwmkHVI----QEN 300
Cdd:cd08178 235 NNGNDIEAREKMHNAATIA--GMafanafLGIC-------HSLAHKLGAAFHIPH--GRanAILLP----HVIrynaTDP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 301 PGRF-----------KQLAVRVFD-VDPAGKTDEE---VGLEGIEKLSAfwtSLGAPNRLADYDINDE----KIDLIADR 361
Cdd:cd08178 300 PTKQaafpqykyyvaKERYAEIADlLGLGGKTPEEkveSLIKAIEDLKK---DLGIPTSIREAGIDEAdflaAVDKLAED 376
|
.
gi 515928379 362 A 362
Cdd:cd08178 377 A 377
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
9-385 |
5.19e-38 |
|
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic microbes; Maleylacetate reductase (MAR) plays an important role in the degradation of aromatic compounds in aerobic microbes. In fungi and yeasts, the enzyme is involved in the catabolism of compounds such as phenol, tyrosine, benzoate, 4-hydroxybenzoate and resorcinol. In bacteria, the enzyme contributes to the degradation of resorcinol, 2,4-dihydroxybenzoate ([beta]-resorcylate) and 2,6-dihydroxybenzoate ([gamma]-resorcylate) via hydroxyquinol and maleylacetate. Maleylacetate reductase (MAR) catalyzes NADH- or NADPH-dependent reduction, at the carbon-carbon double bond, of maleylacetate or 2-chloromaleylacetate to 3-oxoadipate. In the case of 2-chloromaleylacetate, MAR initially catalyzes the NAD(P)H-dependent dechlorination to maleylacetate, which is then reduced to 3-oxoadipate. This enzyme is a homodimer. It is inhibited by thiol-blocking reagents such as p-chloromercuribenzoate and Hg++, indicating that the cysteine residue is probably necessary for the catalytic activity of maleylacetate reductase.
Pssm-ID: 341471 [Multi-domain] Cd Length: 380 Bit Score: 140.46 E-value: 5.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 9 PTKLIFGKGEVSALSDELKHYG-KNVLLVYGGgSIKRN-GLYDQVVSILKESGAAITElaGVEPNPRLTTVRKGVELCKE 86
Cdd:cd08192 1 LERVSYGPGAVEALLHELATLGaSRVFIVTSK-SLATKtDVIKRLEEALGDRHVGVFS--GVRQHTPREDVLEAARAVRE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 87 NQIDFILAVGGGSVIDATKAIA------------AGAKYDGDAWD-IVTRKHVPMEAIPfgTvlTLAatGSEMNSGSVIT 153
Cdd:cd08192 78 AGADLLVSLGGGSPIDAAKAVAlalaedvtdvdqLDALEDGKRIDpNVTGPTLPHIAIP--T--TLS--GAEFTAGAGAT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 154 NWETNEKYGWGSPAVFPKFSILDPVNTFTVPKN---HTiyGM--VDmmsHVFEQYFhHTENTPYQDRMCEGLLRTVIETA 228
Cdd:cd08192 152 DDDTGHKQGFAHPELGPDAVILDPELTLHTPERlwlST--GIraVD---HAVETLC-SPQATPFVDALALKALRLLFEGL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 229 PKLINDLENYELReTILFTGTI-ALNGMLSMGARGdwASHNIEHAVSAVYDIPHAGGLAILFPNWMKHVIQENPGRFKQL 307
Cdd:cd08192 226 PRSKADPEDLEAR-LKCQLAAWlSLFGLGSGVPMG--ASHAIGHQLGPLYGVPHGITSCIMLPAVLRFNAPVNAERQRLI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 308 AVRVFDVDPAGKTDEE-VGlegiEKLSAFWTSLGAPNRLADYDINDEKIDLIADRAMAR--GEFGQFKKLNKEDVLAILN 384
Cdd:cd08192 303 ARALGLVTGGLGREAAdAA----DAIDALIRELGLPRTLRDVGVGRDQLEKIAENALTDvwCRTNPRPITDKDDVLEILE 378
|
.
gi 515928379 385 A 385
Cdd:cd08192 379 S 379
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
9-383 |
2.53e-37 |
|
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol in glycerol metabolism; 1,3-propanediol dehydrogenase (PPD) plays a role in glycerol metabolism of some bacteria in anaerobic conditions. In this degradation pathway, glycerol is converted in a two-step process to 1,3-propanediol (1,3-PD) which is then excreted into the extracellular medium. The first reaction involves the transformation of glycerol into 3-hydroxypropionaldehyde (3-HPA) by a coenzyme B-12-dependent dehydratase. The second reaction involves the dismutation of the 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol by the NADH-linked 1,3-propanediol dehydrogenase (PPD). The enzyme requires iron ion for its function. Because many genes in this pathway are present in the propanediol utilization (pdu) operon, they are also named pdu genes. PPD is a member of the iron-containing alcohol dehydrogenase superfamily. The PPD structure has a dehydroquinate synthase-like fold.
Pssm-ID: 341459 [Multi-domain] Cd Length: 333 Bit Score: 137.62 E-value: 2.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 9 PTKLIFGKGEVSALsDELKhyGKNVLLVyGGGSIKRNGLYDQVVSILKESgAAITELAGVEPNPRLTTVRKGVELCKENQ 88
Cdd:cd08180 4 KTKIYSGEDSLERL-KELK--GKRVFIV-TDPFMVKSGMVDKVTDELDKS-NEVEIFSDVVPDPSIEVVAKGLAKILEFK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 89 IDFILAVGGGSVIDATKAIAAGAKydgdaWDIVTRKHVPMEAIPfgtvlTLAATGSEMNSGSVITNWETNEKYGWGSPAV 168
Cdd:cd08180 79 PDTIIALGGGSAIDAAKAIIYFAL-----KQKGNIKKPLFIAIP-----TTSGTGSEVTSFAVITDPEKGIKYPLVDDSM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 169 FPKFSILDPVNTFTVPKNHTIY-GMvDMMSHVFEQYFhHTENTPYQDRMCEGLLRTVIETAPKLINDLENYELRETILFT 247
Cdd:cd08180 149 LPDIAILDPELVKSVPPKVTADtGM-DVLTHALEAYV-STNANDFTDALAEKAIKLVFENLPRAYRDGDDLEAREKMHNA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 248 GTIAlnGM----LSMGargdwASHNIEHAVSAVYDIPHagGL--AILFPnwmkHVIqenpgrfkqlavrvfdvdpagktd 321
Cdd:cd08180 227 SCMA--GIafnnAGLG-----INHSLAHALGGRFHIPH--GRanAILLP----YVI------------------------ 269
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515928379 322 eEVGLEGIEKLSAfwtSLGAPNRLADYDINDE----KIDLIADRAMARGEF-GQFKKLNKEDVLAIL 383
Cdd:cd08180 270 -EFLIAAIRRLNK---KLGIPSTLKELGIDEEefekAIDEMAEAALADRCTaTNPRKPTAEDLIELL 332
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
9-362 |
2.14e-36 |
|
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); This superfamily consists of two subgroups: the dehydroquinate synthase (DHQS)-like, and a large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. Dehydroquinate synthase-like group includes dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase. The alcohol dehydrogenases (ADHs) in this superfamily contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases; insect-type, or short-chain alcohol dehydrogenases; iron-containing alcohol dehydrogenases, and others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.
Pssm-ID: 341447 [Multi-domain] Cd Length: 271 Bit Score: 133.64 E-value: 2.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 9 PTKLIFGKGEVSALSDELKHYGKNVLLVYGGGSIKrnGLYDQVVSILKEsGAAITELAGVEPNPRLTTVRKGVELCKENQ 88
Cdd:cd07766 1 PTRIVFGEGAIAKLGEIKRRGFDRALVVSDEGVVK--GVGEKVADSLKK-GLAVAIFDFVGENPTFEEVKNAVERARAAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 89 IDFILAVGGGSVIDATKAIAAGAKYDgdawdivtrkhvpmeaIPFGTVLTLAATGSEMNSGSVITNWETNEKYgwGSPAV 168
Cdd:cd07766 78 ADAVIAVGGGSTLDTAKAVAALLNRG----------------IPFIIVPTTASTDSEVSPKSVITDKGGKNKQ--VGPHY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 169 FPKFSILDPVNTFTVPKNHTIYGMVDMMSHVFEqyfhhtentpyqdrmcegllrtvietapklindlenyelRETILFTG 248
Cdd:cd07766 140 NPDVVFVDTDITKGLPPRQVASGGVDALAHAVE---------------------------------------LEKVVEAA 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 249 TIALNGMLSMGarGDWASHNIEHAVSAVYDIPHAGGLAILFPnwmkHVIQENPgrfkqlavrvfDVDPAGKTDeevgleg 328
Cdd:cd07766 181 TLAGMGLFESP--GLGLAHAIGHALTAFEGIPHGEAVAVGLP----YVLKVAN-----------DMNPEPEAA------- 236
|
330 340 350
....*....|....*....|....*....|....
gi 515928379 329 IEKLSAFWTSLGAPNRLADYDINDEKIDLIADRA 362
Cdd:cd07766 237 IEAVFKFLEDLGLPTHLADLGVSKEDIPKLAEKA 270
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
9-363 |
6.37e-35 |
|
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor; 5-hydroxyvalerate dehydrogenase (HVD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the cyclopentanol metabolism biochemical pathway. It catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor. This cyclopentanol (cpn) degradation pathway is present in some bacteria which can use cyclopentanol as sole carbon source. In Comamonas sp. strain NCIMB 9872, this enzyme is encoded by the CpnD gene.
Pssm-ID: 341472 [Multi-domain] Cd Length: 379 Bit Score: 132.25 E-value: 6.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 9 PTKLIFGKGEVSALSDELKHYG-KNVLLVYGGGsIKRNGLYDQVVSILKESGAAITELAGVEPNPRLTTVRKGVELCKEN 87
Cdd:cd08193 4 VPRIICGAGAAARLGELLRELGaRRVLLVTDPG-LVKAGLADPALAALEAAGIAVTVFDDVVADPPEAVVEAAVEQAREA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 88 QIDFILAVGGGSVIDATKAIAAGAKYD---GDAW--DIVTRKHVPMEAIPfgtvlTLAATGSEMNSGSVITNwETNEKYG 162
Cdd:cd08193 83 GADGVIGFGGGSSMDVAKLVALLAGSDqplDDIYgvGKATGPRLPLILVP-----TTAGTGSEVTPISIVTT-GETEKKG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 163 WGSPAVFPKFSILDPVNTFTVPKNHTIYGMVDMMSHVFEQYFHHTENTPYQDRM-CEGL--LRTVIETApklINDLENYE 239
Cdd:cd08193 157 VVSPQLLPDVALLDAELTLGLPPHVTAATGIDAMVHAIEAYTSRHKKNPISDALaREALrlLGANLRRA---VEDGSDLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 240 LRETILFTGTIAlnGML----SMGargdwASHNIEHAVSAVYDIPHagGL--AILFPNWMKHVIQENPGRFKQLAvRVFD 313
Cdd:cd08193 234 AREAMLLGSMLA--GQAfanaPVA-----AVHALAYPLGGHFHVPH--GLsnALVLPHVLRFNLPAAEALYAELA-RALL 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 515928379 314 VDPAGKTDEEVGLEGIEKLSAFWTSLGAPNRLADYDINDEKIDLIADRAM 363
Cdd:cd08193 304 PGLAFGSDAAAAEAFIDALEELVEASGLPTRLRDVGVTEEDLPMLAEDAM 353
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
8-385 |
4.43e-31 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341486 [Multi-domain] Cd Length: 376 Bit Score: 121.64 E-value: 4.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 8 NPTKLIFGKGEVSALSDELKHYGKNVLLVYGGGSiKRNGLYDQVVSILKESGAAITELAGVEPNPRLTTVRKGVELCKEN 87
Cdd:cd14864 3 IPPNIVFGADSLERIGEEVKEYGSRFLLITDPVL-KESGLADKIVSSLEKAGISVIVFDEIPASATSDTIDEAAELARKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 88 QIDFILAVGGGSVIDATKAIAAGAKYDGDAWDIVTRKHVPMEAIPFGTVLTLAATGSEMNSGSVITNWETNEKYGWGSPA 167
Cdd:cd14864 82 GADGIIAVGGGKVLDTAKAVAILANNDGGAYDFLEGAKPKKKPLPLIAVPTTPRSGFEFSDRFPVVDSRSREVKLLKAQP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 168 VFPKFSILDPVNTFTVPKNHTIYGMVDMMSHVFEQYFHHTeNTPYQDRMCEGLLRTVIETAPKLINDLENYELRETILFT 247
Cdd:cd14864 162 GLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSKK-SNFFSDALALKAIELVSENLDGALADPKNTPAEELLAQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 248 GtiALNGML-SMGARGdwASHNIEHAVSAVYDIPHAGGLAILFPNWMKHVIQENPGRFKQLAvRVFDVDPAGKTDEEVG- 325
Cdd:cd14864 241 G--CLAGLAaSSSSPG--LATALALAVNSRYKVSKSLVASILLPHVIEYAATSAPDKYAKIA-RALGEDVEGASPEEAAi 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515928379 326 --LEGIEKLSAfwtSLGAPNRLADYDINDeKIDLIADRAMARGEFGQF-KKLNKEDVLAILNA 385
Cdd:cd14864 316 aaVEGVRRLIA---QLNLPTRLKDLDLAS-SLEQLAAIAEDAPKLNGLpRSMSSDDIFDILKA 374
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
9-362 |
1.19e-29 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 121.06 E-value: 1.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 9 PTKLIFGKGEVSALSDELKHyGKNVLLVYGGGSIKrNGLYDQVVSILK--ESGAAITELAGVEPNPRLTTVRKGVELCKE 86
Cdd:PRK13805 460 PKKIYFERGSLPYLLDELDG-KKRAFIVTDRFMVE-LGYVDKVTDVLKkrENGVEYEVFSEVEPDPTLSTVRKGAELMRS 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 87 NQIDFILAVGGGSVIDATKAIaagakydgdaW------------------DIvtRKHV---P-------MEAIPfgtvlT 138
Cdd:PRK13805 538 FKPDTIIALGGGSPMDAAKIM----------WlfyehpetdfedlaqkfmDI--RKRIykfPklgkkakLVAIP-----T 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 139 LAATGSEMNSGSVITNWETNEKYGWGSPAVFPKFSILDPVNTFTVPKNHTIYGMVDMMSHVFEQYFhHTENTPYQDRMCE 218
Cdd:PRK13805 601 TSGTGSEVTPFAVITDDKTGVKYPLADYELTPDVAIVDPNLVMTMPKSLTADTGIDALTHALEAYV-SVMASDYTDGLAL 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 219 GLLRTVIETAPKLI-NDLENYELRETILFTGTIAlnGM------LSMgargdwaSHNIEHAVSAVYDIPHagGL--AILF 289
Cdd:PRK13805 680 QAIKLVFEYLPRSYkNGAKDPEAREKMHNASTIA--GMafanafLGI-------CHSMAHKLGAEFHIPH--GRanAILL 748
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 290 PnwmkHVIQEN------------------PGRFKQLAVRVFdvdPAGKTDEE-VG--LEGIEKLSAfwtSLGAPNRLADY 348
Cdd:PRK13805 749 P----HVIRYNatdppkqaafpqyeypraDERYAEIARHLG---LPGSTTEEkVEslIKAIEELKA---ELGIPMSIKEA 818
|
410
....*....|....*...
gi 515928379 349 DIN----DEKIDLIADRA 362
Cdd:PRK13805 819 GVDeadfLAKLDELAELA 836
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
1-387 |
4.82e-29 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 116.21 E-value: 4.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 1 MDRFTYWNPTKLIFGKGEVSALSDELKHYGKNVLLVYGGGSIKRNGLYDQVVSILKESGAAITELAGVEPNPRLTTVRKG 80
Cdd:PRK09860 1 MAASTFFIPSVNVIGADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 81 VELCKENQIDFILAVGGGSVIDATKAIAAGAKYDGDAWDI--VTRKHVPMeaIPFGTVLTLAATGSEMNSGSVITNWETN 158
Cdd:PRK09860 81 LKLLKENNCDSVISLGGGSPHDCAKGIALVAANGGDIRDYegVDRSAKPQ--LPMIAINTTAGTASEMTRFCIITDEARH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 159 EKYGWGSPAVFPKFSILDPVNTFTVPKNHTIYGMVDMMSHVFEQYFhHTENTPYQDRMCEGLLRTVIETAPKLINDLENY 238
Cdd:PRK09860 159 IKMAIVDKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYV-SIAATPITDACALKAVTMIAENLPLAVEDGSNA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 239 ELRETILFTGTIAlnGMLSMGARGDWAsHNIEHAVSAVYDIPHAGGLAILFPNWMKHVIQENPGRFKQLAvRVFDVDPAG 318
Cdd:PRK09860 238 KAREAMAYAQFLA--GMAFNNASLGYV-HAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCA-AAMGVNVTG 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515928379 319 KTDEEVGLEGIEKLSAFWTSLGAPNRLADYDINDEKIDLIADRAM--ARGeFGQFKKLNKEDVLAILNASL 387
Cdd:PRK09860 314 KNDAEGAEACINAIRELAKKVDIPAGLRDLNVKEEDFAVLATNALkdACG-FTNPIQATHEEIVAIYRAAM 383
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
14-382 |
5.08e-29 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 116.25 E-value: 5.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 14 FGKGEVSALSDELKHYG-KNVLLVYGGGSIKrNGLYDQVVSILKESGAAITELAGVEPNPRLTTVRKGVELCKENQIDFI 92
Cdd:PRK10624 13 FGRGAIGALTDEVKRRGfKKALIVTDKTLVK-CGVVAKVTDVLDAAGLAYEIYDGVKPNPTIEVVKEGVEVFKASGADYL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 93 LAVGGGSVIDATKAIAAgAKYDGDAWDIV-------TRKH-VPMEAIPfgtvlTLAATGSEMNSGSVITNWETNEKYGWG 164
Cdd:PRK10624 92 IAIGGGSPQDTCKAIGI-ISNNPEFADVRslegvapTKKPsVPIIAIP-----TTAGTAAEVTINYVITDEEKRRKFVCV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 165 SPAVFPKFSILDPVNTFTVPKNHTIYGMVDMMSHVFEQYFhhtenTPYQDRMCEGLLRTVIETAPKLINDL--ENYELRE 242
Cdd:PRK10624 166 DPHDIPQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYI-----TRGAWALTDMLHLKAIEIIAGALRGAvaGDKEAGE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 243 TILFTGTIAlnGM----LSMGargdwASHNIEHAVSAVYDIPHAGGLAILFPNWMKHVIQENPGRFKQLAvRVFDVDPAG 318
Cdd:PRK10624 241 GMALGQYIA--GMgfsnVGLG-----LVHGMAHPLGAFYNTPHGVANAILLPHVMEYNADFTGEKYRDIA-RAMGVKVEG 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515928379 319 KTDEEVGLEGIEKLSAFWTSLGAPNRLADYDINDEKIDLIADRAMA---RGefGQFKKLNKEDVLAI 382
Cdd:PRK10624 313 MSLEEARNAAVEAVKALNRDVGIPPHLRDVGVKEEDIPALAQAAFDdvcTG--GNPREATLEDIVEL 377
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
4-385 |
1.23e-26 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341488 [Multi-domain] Cd Length: 384 Bit Score: 109.63 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 4 FTYWnPTKLIFGKGEVSALSDELKHYGKNVLLVYGGGSIKRNG-LYDQVVSILKESGAAIteLAGVEPNPRLTTVRKGVE 82
Cdd:cd14866 1 HDYP-PLRLFSGRGALARLGRELDRLGARRALVVCGSSVGANPdLMDPVRAALGDRLAGV--FDGVRPHSPLETVEAAAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 83 LCKENQIDFILAVGGGSVIDATKAIAAGAKYDGDAWDIVTRKH--------------VPMEAIPfgTVLtlaaTGSEMNS 148
Cdd:cd14866 78 ALREADADAVVAVGGGSAIVTARAASILLAEDRDVRELCTRRAedglmvsprldapkLPIFVVP--TTP----TTADVKA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 149 GSVITNWETNEKYGWGSPAVFPKFSILDPVNTFTVPKNHTIYGMVDMMSHVFEQYFHHTENtPYQDRMCEGLLRTVIETA 228
Cdd:cd14866 152 GSAVTDPPAGQRLALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEGLYSRHAD-PLADATLMHALRLLADGL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 229 PKLInDLENYELRETILF----TGTIALNGMLSMgargdwaSHNIEHAVSAVYDIPHAGGLAILFPNWMKHVIQENPGRF 304
Cdd:cd14866 231 PRLA-DDDDPAARADLVLaavlAGYGTDHTGGGV-------IHALGHAIGARYGVQNGVVHAILLPHVLRFNAPATDGRL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 305 KQLAvRVFDVDPAGktDEEVGLEGIEKLSAFWTSLGAPNRLADYDINDEKIDLIA-----DRAMARGEFGQfkkLNKEDV 379
Cdd:cd14866 303 DRLA-EALGVADAG--DEASAAAVVDAVEALLDALGVPTRLRDLGVSREDLPAIAeaamdDWFMDNNPRPV---PTAEEL 376
|
....*.
gi 515928379 380 LAILNA 385
Cdd:cd14866 377 EALLEA 382
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
5-347 |
1.77e-24 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 103.57 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 5 TYWNPTKLIFGKGEVSALSDELKHYGKNVLLVYGGGSIKRNGLYDQVVSILKESGAAITELAGVEPNPRLTTVRKGVELC 84
Cdd:PRK15454 23 TFSVPPVTLCGPGAVSSCGQQAQTRGLKHLFVMADSFLHQAGMTAGLTRSLAVKGIAMTLWPCPVGEPCITDVCAAVAQL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 85 KENQIDFILAVGGGSVIDATKAIAAGAKYDGDAWDIVTRKHVPMEAIPFGTVLTLAATGSEMNSGSVITNWETNEKYGWG 164
Cdd:PRK15454 103 RESGCDGVIAFGGGSVLDAAKAVALLVTNPDSTLAEMSETSVLQPRLPLIAIPTTAGTGSETTNVTVIIDAVSGRKQVLA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 165 SPAVFPKFSILDPVNTFTVPKNHTIYGMVDMMSHVFEQYfHHTENTPYQDRMCEGLLRTVIETAPKLINDLENYELRETI 244
Cdd:PRK15454 183 HASLMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAY-SALNATPFTDSLAIGAIAMIGKSLPKAVGYGHDLAARESM 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 245 LFTGTIAlnGMlSMGARGDWASHNIEHAVSAVYDIPHAGGLAILFPNWMKHVIQENPGRFKQLAVRVFDvdpaGKTDEev 324
Cdd:PRK15454 262 LLASCMA--GM-AFSSAGLGLCHAMAHQPGAALHIPHGLANAMLLPTVMEFNRMVCRERFSQIGRALRT----KKSDD-- 332
|
330 340
....*....|....*....|...
gi 515928379 325 gLEGIEKLSAFWTSLGAPNRLAD 347
Cdd:PRK15454 333 -RDAINAVSELIAEVGIGKRLGD 354
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
9-383 |
1.35e-20 |
|
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and conversion]; Glycerol dehydrogenase or related enzyme, iron-containing ADH family is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440140 [Multi-domain] Cd Length: 355 Bit Score: 91.77 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 9 PTKLIFGKGEVSALSDELKHYGKNVLLVYGGGSIKRNGlyDQVVSILKESGAAItELAGVEPNPRLTTVRKGVELCKENQ 88
Cdd:COG0371 6 PRRYVQGEGALDELGEYLADLGKRALIITGPTALKAAG--DRLEESLEDAGIEV-EVEVFGGECSEEEIERLAEEAKEQG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 89 IDFILAVGGGSVIDATKAIAAGAKydgdawdivtrkhvpmeaIPFGTVLTLAAT---GSemnSGSVITNwetnekyGWGS 165
Cdd:COG0371 83 ADVIIGVGGGKALDTAKAVAYRLG------------------LPVVSVPTIASTdapAS---PLSVIYT-------EDGA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 166 pavFPKFSILdPVNTFTV----------PKNHTIYGMVDMMSHVFEQYF----HHTENTPYQDR----MCEGLLRTVIET 227
Cdd:COG0371 135 ---FDGYSFL-AKNPDLVlvdtdiiakaPVRLLAAGIGDALAKWYEARDwslaHRDLAGEYYTEaavaLARLCAETLLEY 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 228 APKLINDLENYELRE--------TILFTGTialnGMLSMGARGDWAS-HNIEHAVSAVYDIPHAG-----GLAILFpnwm 293
Cdd:COG0371 211 GEAAIKAVEAGVVTPalervveaNLLLSGL----AMGIGSSRPGSGAaHAIHNGLTALPETHHALhgekvAFGTLV---- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 294 khviqenpgrfkQLAVRvfdvdpaGKTDEevglegIEKLSAFWTSLGAPNRLADYDIND---EKIDLIADRAMARGEF-- 368
Cdd:COG0371 283 ------------QLVLE-------GRPEE------IEELLDFLRSVGLPTTLADLGLDDeteEELLTVAEAARPERYTil 337
|
410
....*....|....*
gi 515928379 369 GQFKKLNKEDVLAIL 383
Cdd:COG0371 338 NLPFEVTPEAVEAAI 352
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
9-364 |
3.04e-19 |
|
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic microbes; Maleylacetate reductase (MAR) plays an important role in the degradation of aromatic compounds in aerobic microbes. In fungi and yeasts, the enzyme is involved in the catabolism of compounds such as phenol, tyrosine, benzoate, 4-hydroxybenzoate and resorcinol. In bacteria, the enzyme contributes to the degradation of resorcinol, 2,4-dihydroxybenzoate ([beta]-resorcylate) and 2,6-dihydroxybenzoate ([gamma]-resorcylate) via hydroxyquinol and maleylacetate. Maleylacetate reductase catalyzes NADH- or NADPH-dependent reduction, at the carbon-carbon double bond, of maleylacetate or 2-chloromaleylacetate to 3-oxoadipate. In the case of 2-chloromaleylacetate, MAR initially catalyzes the NAD(P)H-dependent dechlorination to maleylacetate, which is then reduced to 3-oxoadipate. This enzyme is a homodimer and is inhibited by thiol-blocking reagents such as p-chloromercuribenzoate and Hg++, indicating that the cysteine residue is probably necessary for the catalytic activity of maleylacetate reductase.
Pssm-ID: 341456 [Multi-domain] Cd Length: 337 Bit Score: 87.56 E-value: 3.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 9 PTKLIFGKGEVSALSDELKHYGKNVLLVYGGGSikRNGLYDQVVSILKESGAAIteLAGVEPNPRLTTVRKGVELCKENQ 88
Cdd:cd08177 1 PQRVVFGAGTLAELAEELERLGARRALVLSTPR--QRALAERVAALLGDRVAGV--FDGAVMHVPVEVAERALAAAREAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 89 IDFILAVGGGSVIDATKAIAAgakydgdawdivtRKHVPMEAIPfgTvlTLAatGSEMNSgsvitNW-ETNE--KYGWGS 165
Cdd:cd08177 77 ADGLVAIGGGSAIGLAKAIAL-------------RTGLPIVAVP--T--TYA--GSEMTP-----IWgETEDgvKTTGRD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 166 PAVFPKFSILDPVNTFTVPKNHTIYGMVDMMSHVFEQYFHHTENtPYQDRMCEGLLRTVIETAPKLINDLENYELRETIL 245
Cdd:cd08177 133 PRVLPRTVIYDPDLTLGLPAALSVASGLNALAHAVEALYAPDAN-PITSLLAEEGIRALARALPRLVADPSDLEARSDAL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 246 ---FTGTIALnGMLSMGARgdwasHNIEHAVSAVYDIPHAGGLAILFPnwmkHVIQEN----PGRFKQLAVRVFDVDPAG 318
Cdd:cd08177 212 ygaWLAGVVL-GSVGMGLH-----HKLCHVLGGTFDLPHAETHAVVLP----HVLAYNapaaPDAMARLARALGGGDAAG 281
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 515928379 319 ktdeevgleGIEKLSAfwtSLGAPNRLADYDINDEKIDLIADRAMA 364
Cdd:cd08177 282 ---------GLYDLAR---RLGAPTSLRDLGMPEDDIDRAADLALA 315
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
13-272 |
5.49e-13 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 68.10 E-value: 5.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 13 IFGKGEVSALSDEL-KHYGKNVLLVYGGGSIKRNGlyDQVVSILKESGAAITELAGVEPNPRLTTVRKGVELCKENQIDF 91
Cdd:pfam13685 1 VIGPGALGRLGEYLaELGFRRVALVADANTYAAAG--RKVAESLKRAGIEVETRLEVAGNADMETAEKLVGALRERDADA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 92 ILAVGGGSVIDATKAIAAgakydgdawdivtRKHVPMEAIPfgtvlTLAATGSEMNSGSVITnwETNEKYGWgsPAVFPK 171
Cdd:pfam13685 79 VVGVGGGTVIDLAKYAAF-------------KLGKPFISVP-----TAASNDGFASPGASLT--VDGKKRSI--PAAAPF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 172 FSILDPVNTFTVPKNHTIYGMVDMMSHVFEQYFHHTENT-PYQDRMCEGLLRTVIETAPKLINDLENYELRETILFTGTI 250
Cdd:pfam13685 137 GVIADTDVIAAAPRRLLASGVGDLLAKITAVADWELAHAeEVAAPLALLSAAMVMNFADRPLRDPGDIEALAELLSALAM 216
|
250 260
....*....|....*....|..
gi 515928379 251 alnGMLSMGARGDWASHNIEHA 272
Cdd:pfam13685 217 ---GGAGSSRPASGSEHLISHA 235
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
9-385 |
7.91e-12 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site. Some subfamilies have yet to be characterized.
Pssm-ID: 341480 [Multi-domain] Cd Length: 347 Bit Score: 66.02 E-value: 7.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 9 PTKLIFGKGEVSALSDELKHYGKNVLLVYGGGSIKRNGlyDQVVSILKESGAaITELAGVEPNPRLTTVRKGVELCKENQ 88
Cdd:cd08550 1 PGRYIQEPGILAKAGEYIAPLGKKALIIGGKTALEAVG--EKLEKSLEEAGI-DYEVEVFGGECTEENIERLAEKAKEEG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 89 IDFILAVGGGSVIDATKAIAAGAKydgdawdivtrkhVPMEAIPfgtvlTLAATGSEMNSGSVITNWETNEKYGWGSPAv 168
Cdd:cd08550 78 ADVIIGIGGGKVLDTAKAVADRLG-------------LPVVTVP-----TIAATCAAWSALSVLYDEEGEFLGYSLLKR- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 169 FPKFSILDPVNTFTVPKNHTIYGMVDMMSHVFEQYFHHTENTP--------YQDRMCeglLRTVIETAPKLINDLEN--- 237
Cdd:cd08550 139 SPDLVLVDTDIIAAAPVRYLAAGIGDTLAKWYEARPSSRGGPDdlalqaavQLAKLA---YDLLLEYGVQAVEDVRQgkv 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 238 -YELRET----ILFTGTIalNGMLSMGARGDwASHNIEHAVSAVYDIPHAG-----GLAILFpnwmkhviqenpgrfkQL 307
Cdd:cd08550 216 tPALEDVvdaiILLAGLV--GSLGGGGCRTA-AAHAIHNGLTKLPETHGTLhgekvAFGLLV----------------QL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 308 AVrvfdvdpAGKTDEEvglegIEKLSAFWTSLGAPNRLAD--YDINDEKIDLIADRAMARGEFGQFK--KLNKEDVL-AI 382
Cdd:cd08550 277 AL-------EGRSEEE-----IEELIEFLRRLGLPVTLEDlgLELTEEELRKIAEYACDPPDMAHMLpfPVTPEMLAeAI 344
|
...
gi 515928379 383 LNA 385
Cdd:cd08550 345 LAA 347
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
9-142 |
9.07e-12 |
|
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in glycerol dissmilation; Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341449 [Multi-domain] Cd Length: 351 Bit Score: 65.51 E-value: 9.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 9 PTKLIFGKGEVSALSDELKHYGKNVLLVYGGGSIKRNGlyDQVVSILKESGAAITELA-GVEPNPrlTTVRKGVELCKEN 87
Cdd:cd08170 1 PSRYVQGPGALDRLGEYLAPLGKKALVIADPFVLDLVG--ERLEESLEKAGLEVVFEVfGGECSR--EEIERLAAIARAN 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 515928379 88 QIDFILAVGGGSVIDATKAIAAGAKydgdawdivtrkhvpmeaIPFGTVLTLAAT 142
Cdd:cd08170 77 GADVVIGIGGGKTIDTAKAVADYLG------------------LPVVIVPTIAST 113
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
9-108 |
2.95e-09 |
|
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme; Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH, EC 1.1.1.261) plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids. It catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme. The activity is zinc-dependent. One characteristic feature of archaea is that their cellular membrane has an ether linkage between the glycerol backbone and the hydrocarbon residues. The polar lipids of the members of Archaea consist of di- and tetra-ethers of glycerol with isoprenoid alcohols bound at the sn-2 and sn-3 positions of the glycerol moiety. The archaeal polar lipids have the enantiomeric configuration of a glycerophosphate backbone [sn-glycerol-1-phosphate (G-1-P)] that is the mirror image structure of the bacterial or eukaryal counterpart [sn-glycerol- 3-phosphate (G-3-P)]. The absolute stereochemistry of the glycerol moiety in all archaeal polar lipids is opposite to that of glycerol ester lipids in bacteria and eukarya.
Pssm-ID: 341452 Cd Length: 343 Bit Score: 57.95 E-value: 2.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 9 PTKLIFGKGEVSALSDELK--HYGKNVLLVYGGGSIKRNGlyDQVVSILKESGA--AITELAGVEpnpRLTTVRKGVELC 84
Cdd:cd08173 2 PRNVVVGHGAINKIGEVLKklLLGKRALIITGPNTYKIAG--KRVEDLLESSGVevVIVDIATIE---EAAEVEKVKKLI 76
|
90 100
....*....|....*....|....
gi 515928379 85 KENQIDFILAVGGGSVIDATKAIA 108
Cdd:cd08173 77 KESKADFIIGVGGGKVIDVAKYAA 100
|
|
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
81-385 |
6.83e-09 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341451 [Multi-domain] Cd Length: 346 Bit Score: 56.76 E-value: 6.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 81 VELCKENQIDFILAVGGGSVIDATKAIAAGAKydgdawdivtrkhvpmeaIPFGTVLTLAATGSEMNSGSVITNWE-TNE 159
Cdd:cd08172 68 AEEAKEHQADVIIGIGGGKVLDTAKAVADKLN------------------IPLILIPTLASNCAAWTPLSVIYDEDgEFI 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 160 KYgwgspAVFPK---FSILDP---VNTftvPKNHTIYGMVDMMSHVFE---QYFHHTENTPYQD------RMCEGLLRTV 224
Cdd:cd08172 130 GY-----DYFPRsayLVLVDPrllLDS---PKDYFVAGIGDTLAKWYEadaILRQLEELPAFLQlarqaaKLCRDILLKD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 225 IETApklINDLENYELR-------ETIlftgtIALNGMLsmGARGDW-----ASHNIEHAVSAVYDIPHA--G---GLAI 287
Cdd:cd08172 202 SEQA---LADLEAGKLTpafikvvETI-----IALAGMV--GGFGDEygrsaGAHAIHNGLTKLPETHHFlhGekvAYGI 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 288 LFpnwmkhviqenpgrfkQLAVRvfdvdpaGKTDEevglegIEKLSAFWTSLGAPNRLAD---YDINDEKIDLIADRAMA 364
Cdd:cd08172 272 LV----------------QLALE-------GKWDE------IKKLLPFYRRLGLPTSLADlglTDDTEEALQKIAAFAAS 322
|
330 340
....*....|....*....|...
gi 515928379 365 RGEFGQ--FKKLNKEDVLAILNA 385
Cdd:cd08172 323 PEESIHllPPDVTAEEVLQAIEK 345
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
9-208 |
2.04e-08 |
|
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N biosynthesis; This family contains iron-containing alcohol dehydrogenase-like proteins, many of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the iron-containing alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron or zinc ions. This family also includes Shewanella oneidensis KdnB which is required for biosynthesis of 8-Amino-3,8-dideoxy-D-manno-octulosonic acid (Kdo8N), a unique amino sugar that has thus far only been observed on the lipopolysaccharides of marine bacteria belonging to the genus Shewanella, and thought to be important for the integrity of the bacterial cell outer membrane. KdnB requires NAD(P) and zinc ion for activity.
Pssm-ID: 341463 [Multi-domain] Cd Length: 348 Bit Score: 55.35 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 9 PTKLIFGKGEVSALSDELK-----HYGKNVLLV----YGGGSIKR--NGLYDQVVSIlkesgAAITElagvepnPRLTTV 77
Cdd:cd08184 1 VPKYLFGRGSFDQLGELLAerrksNNDYVVFFIddvfKGKPLLDRlpLQNGDLLIFV-----DTTDE-------PKTDQI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 78 RKGVELCKENQI---DFILAVGGGSVIDATKAIA-------AGAKYDGdaWDIVTRKHVPMEAIPfgtvlTLAATGSEMN 147
Cdd:cd08184 69 DALRAQIRAENDklpAAVVGIGGGSTMDIAKAVSnmltnpgSAADYQG--WDLVKNPGIYKIGVP-----TLSGTGAEAS 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515928379 148 SGSVITNweTNEKYGWGSPAVFPKFSILDPVNTFTVPKNHTIYGMVDMmshvfeqYFHHTE 208
Cdd:cd08184 142 RTAVLTG--PEKKLGINSDYTVFDQVILDPELIATVPRDQYFYTGMDC-------YIHCVE 193
|
|
| gldA |
PRK09423 |
glycerol dehydrogenase; Provisional |
1-112 |
2.60e-08 |
|
glycerol dehydrogenase; Provisional
Pssm-ID: 181843 Cd Length: 366 Bit Score: 55.21 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 1 MDRfTYWNPTKLIFGKGEVSALSDELKHYGKNVLLVYGGGSIKRNGlyDQVVSILKESGAAITEL--------AGVEpnp 72
Cdd:PRK09423 1 MDR-IFISPSKYVQGKGALARLGEYLKPLGKRALVIADEFVLGIVG--DRVEASLKEAGLTVVFEvfngecsdNEID--- 74
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 515928379 73 RLttvrkgVELCKENQIDFILAVGGGSVIDATKAIAAGAK 112
Cdd:PRK09423 75 RL------VAIAEENGCDVVIGIGGGKTLDTAKAVADYLG 108
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
9-132 |
3.75e-08 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 54.51 E-value: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 9 PTKLIFGKG---EVSALSDELkHYGKNVLLVYGGGSIKRNGlyDQVVSILKESGAAITELAGvepNPRLTTVRKGVELCK 85
Cdd:PRK00843 11 PRDVVVGHGvldDIGDVCSDL-KLTGRALIVTGPTTKKIAG--DRVEENLEDAGDVEVVIVD---EATMEEVEKVEEKAK 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 515928379 86 ENQIDFILAVGGGSVIDATKAIAagakydgdawdivTRKHVPMEAIP 132
Cdd:PRK00843 85 DVNAGFLIGVGGGKVIDVAKLAA-------------YRLGIPFISVP 118
|
|
| GlyDH-like |
cd08171 |
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
21-364 |
1.04e-07 |
|
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341450 Cd Length: 345 Bit Score: 53.29 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 21 ALSDELKHYGKNVLLVygGGSIKRNGLYDQVVSILKESGAAIT--ELAGVEPNprLTTVRKGVELCKENQIDFILAVGGG 98
Cdd:cd08171 13 AIPKICSPYGKKVVVI--GGKKALAAAKPKLRAALEGSGLEITdfIWYGGEAT--YENVEKLKANPEVQEADMIFAVGGG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 99 SVIDATKAIAAgakydgdawdivtrkhvpMEAIPFGTVLTLAATGSEMNSGSVItnweTNEKygwGSpavFPKFSILD-- 176
Cdd:cd08171 89 KAIDTVKVLAD------------------RLNKPVFTFPTIASNCAAVTAVSVM----YNPD---GS---FKEYYFLKrp 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 177 PVNTF-------TVPKNHTIYGMVDMMSHVFEQYF-------HHTENTPYQ-DRMC-EGLLR---TVIETApklINDLEN 237
Cdd:cd08171 141 PVHTFidteiiaEAPEKYLWAGIGDTLAKYYEVEFsargdelDHTNALGVAiSKMCsEPLLKygvQALEDC---RANKVS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 238 YELRETILftgTIALN-GMLSMGARGDWASHnIEHAV-SAVYDIPHAGGlailfpnwmKHVIQE--NPGRFKQLAVrvfd 313
Cdd:cd08171 218 DALEQVVL---DIIVTtGLVSNLVEPDYNSS-LAHALyYGLTTLPQIEE---------EHLHGEvvSYGVLVLLTV---- 280
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 515928379 314 vdpAGKTDEevglegIEKLSAFWTSLGAPNRLADYDINDEKIDLIADRAMA 364
Cdd:cd08171 281 ---DGQFEE------LEKVYAFNKSIGLPTCLADLGLTVEDLEKVLDKALK 322
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
92-382 |
4.12e-07 |
|
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes the reduction of succinic simialdehyde to 4-hydroxybutyrate in the succinic degradation pathway; 4-hydroxybutyrate dehydrogenase (4HBD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the succinate metabolism biochemical pathway. It catalyzes the reduction of succinic simialdehide to 4-hydroxybutyrate in the succinate degradation pathway This succinate degradation pathway is present in some bacteria which can use succinate as sole carbon source.
Pssm-ID: 341482 Cd Length: 371 Bit Score: 51.45 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 92 ILAVGGGSVIDATKAIAagAKYDGDAWDIVTRKHVPMEAIPFGTVLTLAATGSEMNSGSVITNWETNEKYGWGSPAVFPK 171
Cdd:cd14860 82 VIAIGGGTVIDIAKLLA--LKGISPVLDLFDGKIPLIKEKELIIVPTTCGTGSEVTNISIVELTSLGTKKGLAVDELYAD 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 172 FSILDPVNTFTVPKNHTIYGMVDMMSHVFEQYFhHTENTPYQD----RMCEGLLRTVIETApklindLENYELRETILFT 247
Cdd:cd14860 160 KAVLIPELLKGLPYKVFATSSIDALIHAIESYL-SPKATPYTEmfsyKAIEMILEGYQEIA------EKGEEARFPLLGD 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 248 GTIALN--GmLSMGARGDWASHNIEHAVSAVYDIPHAGGLAILFPNWMKHVIQENP-GRFKQLAVRVFDVDpagKTDEEV 324
Cdd:cd14860 233 FLIASNyaG-IAFGNAGCAAVHALSYPLGGKYHVPHGEANYAVFTGVLKNYQEKNPdGEIKKLNEFLAKIL---GCDEED 308
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515928379 325 GLEGIEKLsafwtsLG---APNRLADYDINDEKIDLIADRAMARgefgQ-------FKKLNKEDVLAI 382
Cdd:cd14860 309 VYDELEEL------LNkilPKKPLHEYGMKEEEIDEFADSVMEN----QqrllannYVPLDREDVAEI 366
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
9-132 |
7.10e-07 |
|
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like proteins have not been characterized. The protein sequences have high similarity with that of glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion.
Pssm-ID: 341453 [Multi-domain] Cd Length: 332 Bit Score: 50.60 E-value: 7.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515928379 9 PTKLIFGKGEVSALSDEL---KHYGKNVLLVYGGGSIKRngLYDQVVSILKESGAAITELAGVEPNprLTTVRKgvELCK 85
Cdd:cd08174 1 PLILKIEEGALEHLGKYLadrNQGFGKVAIVTGEGIDEL--LGEDILESLEEAGEIVTVEENTDNS--AEELAE--KAFS 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 515928379 86 ENQIDFILAVGGGSVIDATKAIAAGAKydgdawdivtrkhVPMEAIP 132
Cdd:cd08174 75 LPKVDAIVGIGGGKVLDVAKYAAFLSK-------------LPFISVP 108
|
|
| |
