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Conserved domains on  [gi|2463707570|ref|WP_276219713|]
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iron-containing alcohol dehydrogenase family protein [Dickeya fangzhongdai]

Protein Classification

iron-containing alcohol dehydrogenase family protein( domain architecture ID 10171094)

iron-containing alcohol dehydrogenase family protein may catalyze the iron-dependent reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P) to NAD(P)H; similar to Synechocystis sp oxidoreductase slr1167

CATH:  3.40.50.1970
Gene Ontology:  GO:0046872|GO:0030554
PubMed:  9685163|35751426
SCOP:  3001905

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GlyDH-like cd08550
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ...
 8-353 1.01e-129

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: 374.95  E-value: 1.01e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570   8 PATVLRGAGVSQQLGGICARLGSRVLVAGGHQALAAAQTLIIEQLRQSGVTlTAVEWSGEQCSVNQIERLCARVRETDSD 87
Cdd:cd08550     1 PGRYIQEPGILAKAGEYIAPLGKKALIIGGKTALEAVGEKLEKSLEEAGID-YEVEVFGGECTEENIERLAEKAKEEGAD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  88 VLLAVGGGKALDTGKAVAFQCGIPVVTLPTIAATCAAVTPLSVRYHDDGHFHDLHHLPVAPAAVVIDSALLARAPLRWLA 167
Cdd:cd08550    80 VIIGIGGGKVLDTAKAVADRLGLPVVTVPTIAATCAAWSALSVLYDEEGEFLGYSLLKRSPDLVLVDTDIIAAAPVRYLA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570 168 AGLGDTLAKWYEFRAIDNGGNDSGFAASSRANSEICFRLIEQYGEEACRAVTAGQHNDALDQVLDAIFLFAGLTSLMASG 247
Cdd:cd08550   160 AGIGDTLAKWYEARPSSRGGPDDLALQAAVQLAKLAYDLLLEYGVQAVEDVRQGKVTPALEDVVDAIILLAGLVGSLGGG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570 248 AHAAAAH-ALYEGFTVCDKTREFGHGLLVGFGNLCLLALEQRSDEELLAAIRLAQACAVPLTMAAICPDLSEEELTAIVR 326
Cdd:cd08550   240 GCRTAAAhAIHNGLTKLPETHGTLHGEKVAFGLLVQLALEGRSEEEIEELIEFLRRLGLPVTLEDLGLELTEEELRKIAE 319

                         330       340
                  ....*....|....*....|....*...
gi 2463707570 327 ASVDAPDMATM-PFTVAEQQVRQAIRRV 353
Cdd:cd08550   320 YACDPPDMAHMlPFPVTPEMLAEAILAA 347
 
Name Accession Description Interval E-value
GlyDH-like cd08550
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ...
 8-353 1.01e-129

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: 374.95  E-value: 1.01e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570   8 PATVLRGAGVSQQLGGICARLGSRVLVAGGHQALAAAQTLIIEQLRQSGVTlTAVEWSGEQCSVNQIERLCARVRETDSD 87
Cdd:cd08550     1 PGRYIQEPGILAKAGEYIAPLGKKALIIGGKTALEAVGEKLEKSLEEAGID-YEVEVFGGECTEENIERLAEKAKEEGAD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  88 VLLAVGGGKALDTGKAVAFQCGIPVVTLPTIAATCAAVTPLSVRYHDDGHFHDLHHLPVAPAAVVIDSALLARAPLRWLA 167
Cdd:cd08550    80 VIIGIGGGKVLDTAKAVADRLGLPVVTVPTIAATCAAWSALSVLYDEEGEFLGYSLLKRSPDLVLVDTDIIAAAPVRYLA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570 168 AGLGDTLAKWYEFRAIDNGGNDSGFAASSRANSEICFRLIEQYGEEACRAVTAGQHNDALDQVLDAIFLFAGLTSLMASG 247
Cdd:cd08550   160 AGIGDTLAKWYEARPSSRGGPDDLALQAAVQLAKLAYDLLLEYGVQAVEDVRQGKVTPALEDVVDAIILLAGLVGSLGGG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570 248 AHAAAAH-ALYEGFTVCDKTREFGHGLLVGFGNLCLLALEQRSDEELLAAIRLAQACAVPLTMAAICPDLSEEELTAIVR 326
Cdd:cd08550   240 GCRTAAAhAIHNGLTKLPETHGTLHGEKVAFGLLVQLALEGRSEEEIEELIEFLRRLGLPVTLEDLGLELTEEELRKIAE 319

                         330       340
                  ....*....|....*....|....*...
gi 2463707570 327 ASVDAPDMATM-PFTVAEQQVRQAIRRV 353
Cdd:cd08550   320 YACDPPDMAHMlPFPVTPEMLAEAILAA 347
GldA COG0371
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ...
 5-353 1.68e-108

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: 321.35  E-value: 1.68e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570   5 VFFPATVLRGAGVSQQLGGICARLGSRVLVAGGHQALAAAQTLIIEQLRQSGVTLTAVEWSGEqCSVNQIERLCARVRET 84
Cdd:COG0371     3 IILPRRYVQGEGALDELGEYLADLGKRALIITGPTALKAAGDRLEESLEDAGIEVEVEVFGGE-CSEEEIERLAEEAKEQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  85 DSDVLLAVGGGKALDTGKAVAFQCGIPVVTLPTIAATCAAVTPLSVRYHDDGHFHDLHHLPVAPAAVVIDSALLARAPLR 164
Cdd:COG0371    82 GADVIIGVGGGKALDTAKAVAYRLGLPVVSVPTIASTDAPASPLSVIYTEDGAFDGYSFLAKNPDLVLVDTDIIAKAPVR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570 165 WLAAGLGDTLAKWYEFRAIDNGGND---SGFAASSRANSEICFRLIEQYGEEACRAVTAGQHNDALDQVLDAIFLFAGLT 241
Cdd:COG0371   162 LLAAGIGDALAKWYEARDWSLAHRDlagEYYTEAAVALARLCAETLLEYGEAAIKAVEAGVVTPALERVVEANLLLSGLA 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570 242 SLMASGAHAAAAH-ALYEGFTVCDKTREFGHGLLVGFGNLCLLALEQRsDEELLAAIRLAQACAVPLTMAAI-CPDLSEE 319
Cdd:COG0371   242 MGIGSSRPGSGAAhAIHNGLTALPETHHALHGEKVAFGTLVQLVLEGR-PEEIEELLDFLRSVGLPTTLADLgLDDETEE 320

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 2463707570 320 ELTAIVRASV-DAPDMATMPFTVAEQQVRQAIRRV 353
Cdd:COG0371   321 ELLTVAEAARpERYTILNLPFEVTPEAVEAAILAT 355
gldA PRK09423
glycerol dehydrogenase; Provisional
 1-360 3.94e-73

glycerol dehydrogenase; Provisional


Pssm-ID: 181843  Cd Length: 366  Bit Score: 231.24  E-value: 3.94e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570   1 MMQQVFFPATVLRGAGVSQQLGGICARLGSRVLVAGGHQALAAAQTLIIEQLRQSGVTLTAVEWSGEqCSVNQIERLCAR 80
Cdd:PRK09423    1 MDRIFISPSKYVQGKGALARLGEYLKPLGKRALVIADEFVLGIVGDRVEASLKEAGLTVVFEVFNGE-CSDNEIDRLVAI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  81 VRETDSDVLLAVGGGKALDTGKAVAFQCGIPVVTLPTIAATCAAVTPLSVRYHDDGHFHDLHHLPVAPAAVVIDSALLAR 160
Cdd:PRK09423   80 AEENGCDVVIGIGGGKTLDTAKAVADYLGVPVVIVPTIASTDAPTSALSVIYTEEGEFERYLFLPKNPDLVLVDTAIIAK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570 161 APLRWLAAGLGDTLAKWYEFRA-IDNGGNDSGFAASSRAN---SEICFRLIEQYGEEACRAVTAGQHNDALDQVLDAIFL 236
Cdd:PRK09423  160 APARFLAAGIGDALATWFEARAcSRSGGTTMAGGKPTLAAlalAELCYETLLEDGLKAKLAVEAKVVTPALENVIEANTL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570 237 FAGL----TSLMASgahaaaaHALYEGFTVCDKTREFGHGLLVGFGNLCLLALEQRSDEELLAAIRLAQACAVPLTMAAI 312
Cdd:PRK09423  240 LSGLgfesGGLAAA-------HAIHNGLTALEDTHHLTHGEKVAFGTLTQLVLENRPKEEIEEVIDFCHAVGLPTTLADL 312

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 2463707570 313 -CPDLSEEELTAIVRASV-DAPDMATMPFTVAEQQVRQAIRRVEALAARV 360
Cdd:PRK09423  313 gLKEDSDEELRKVAEAACaEGETIHNMPFKVTPEDVAAAILAADAYGQRY 362
Fe-ADH pfam00465
Iron-containing alcohol dehydrogenase;
8-346 4.25e-38

Iron-containing alcohol dehydrogenase;


Pssm-ID: 425696 [Multi-domain]  Cd Length: 362  Bit Score: 139.66  E-value: 4.25e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570   8 PATVLRGAGVSQQLGGICARLGSRVL-VAGGHQALAAAQTLIIEQLRQSGVTLTAVEWSGEQCSVNQIERLCARVRETDS 86
Cdd:pfam00465   1 PTRIVFGAGALAELGEELKRLGARALiVTDPGSLKSGLLDKVLASLEEAGIEVVVFDGVEPEPTLEEVDEAAALAREAGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  87 DVLLAVGGGKALDTGKAVAFQCG------------------IPVVTLPTIAATCAAVTPLSVRYHDDGHFHD-LHHLPVA 147
Cdd:pfam00465  81 DVIIAVGGGSVIDTAKAIALLLTnpgdvwdylggkpltkpaLPLIAIPTTAGTGSEVTPLAVITDTETGEKLgIFSPKLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570 148 PAAVVIDSALLARAPLRWLAAGLGDTLAKWYEFRAIDNGgndsgfAASSRANSEICFRLIEQYGEeacRAVTAGQHNDAL 227
Cdd:pfam00465 161 PDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGA------NPLTDALALEAIRLIAENLP---RAVADGEDLEAR 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570 228 DQVLDAIFLfAGLtSLMASGAHAA--------AAHALYEGFT-------VCDKTREFGHGLLVGFGNLCLLALEQRSDEE 292
Cdd:pfam00465 232 ENMLLASTL-AGL-AFSNAGLGAAhalahalgGRYGIPHGLAnaillpyVLRFNAPAAPEKLAQLARALGEDSDEEAAEE 309

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2463707570 293 LLAAIR-LAQACAVPLTMAAIcpDLSEEELTAIVRASVDAPDMATMPFTVAEQQV 346
Cdd:pfam00465 310 AIEALReLLRELGLPTTLSEL--GVTEEDLDALAEAALRDRSLANNPRPLTAEDI 362
 
Name Accession Description Interval E-value
GlyDH-like cd08550
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ...
 8-353 1.01e-129

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: 374.95  E-value: 1.01e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570   8 PATVLRGAGVSQQLGGICARLGSRVLVAGGHQALAAAQTLIIEQLRQSGVTlTAVEWSGEQCSVNQIERLCARVRETDSD 87
Cdd:cd08550     1 PGRYIQEPGILAKAGEYIAPLGKKALIIGGKTALEAVGEKLEKSLEEAGID-YEVEVFGGECTEENIERLAEKAKEEGAD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  88 VLLAVGGGKALDTGKAVAFQCGIPVVTLPTIAATCAAVTPLSVRYHDDGHFHDLHHLPVAPAAVVIDSALLARAPLRWLA 167
Cdd:cd08550    80 VIIGIGGGKVLDTAKAVADRLGLPVVTVPTIAATCAAWSALSVLYDEEGEFLGYSLLKRSPDLVLVDTDIIAAAPVRYLA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570 168 AGLGDTLAKWYEFRAIDNGGNDSGFAASSRANSEICFRLIEQYGEEACRAVTAGQHNDALDQVLDAIFLFAGLTSLMASG 247
Cdd:cd08550   160 AGIGDTLAKWYEARPSSRGGPDDLALQAAVQLAKLAYDLLLEYGVQAVEDVRQGKVTPALEDVVDAIILLAGLVGSLGGG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570 248 AHAAAAH-ALYEGFTVCDKTREFGHGLLVGFGNLCLLALEQRSDEELLAAIRLAQACAVPLTMAAICPDLSEEELTAIVR 326
Cdd:cd08550   240 GCRTAAAhAIHNGLTKLPETHGTLHGEKVAFGLLVQLALEGRSEEEIEELIEFLRRLGLPVTLEDLGLELTEEELRKIAE 319

                         330       340
                  ....*....|....*....|....*...
gi 2463707570 327 ASVDAPDMATM-PFTVAEQQVRQAIRRV 353
Cdd:cd08550   320 YACDPPDMAHMlPFPVTPEMLAEAILAA 347
GldA COG0371
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ...
 5-353 1.68e-108

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: 321.35  E-value: 1.68e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570   5 VFFPATVLRGAGVSQQLGGICARLGSRVLVAGGHQALAAAQTLIIEQLRQSGVTLTAVEWSGEqCSVNQIERLCARVRET 84
Cdd:COG0371     3 IILPRRYVQGEGALDELGEYLADLGKRALIITGPTALKAAGDRLEESLEDAGIEVEVEVFGGE-CSEEEIERLAEEAKEQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  85 DSDVLLAVGGGKALDTGKAVAFQCGIPVVTLPTIAATCAAVTPLSVRYHDDGHFHDLHHLPVAPAAVVIDSALLARAPLR 164
Cdd:COG0371    82 GADVIIGVGGGKALDTAKAVAYRLGLPVVSVPTIASTDAPASPLSVIYTEDGAFDGYSFLAKNPDLVLVDTDIIAKAPVR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570 165 WLAAGLGDTLAKWYEFRAIDNGGND---SGFAASSRANSEICFRLIEQYGEEACRAVTAGQHNDALDQVLDAIFLFAGLT 241
Cdd:COG0371   162 LLAAGIGDALAKWYEARDWSLAHRDlagEYYTEAAVALARLCAETLLEYGEAAIKAVEAGVVTPALERVVEANLLLSGLA 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570 242 SLMASGAHAAAAH-ALYEGFTVCDKTREFGHGLLVGFGNLCLLALEQRsDEELLAAIRLAQACAVPLTMAAI-CPDLSEE 319
Cdd:COG0371   242 MGIGSSRPGSGAAhAIHNGLTALPETHHALHGEKVAFGTLVQLVLEGR-PEEIEELLDFLRSVGLPTTLADLgLDDETEE 320

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 2463707570 320 ELTAIVRASV-DAPDMATMPFTVAEQQVRQAIRRV 353
Cdd:COG0371   321 ELLTVAEAARpERYTILNLPFEVTPEAVEAAILAT 355
GlyDH cd08170
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ...
 14-356 4.77e-86

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: 263.89  E-value: 4.77e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  14 GAGVSQQLGGICARLGSRVLVAGGHQALAAAQTLIIEQLRQSGVTLTAVEWSGEqCSVNQIERLCARVRETDSDVLLAVG 93
Cdd:cd08170     7 GPGALDRLGEYLAPLGKKALVIADPFVLDLVGERLEESLEKAGLEVVFEVFGGE-CSREEIERLAAIARANGADVVIGIG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  94 GGKALDTGKAVAFQCGIPVVTLPTIAATCAAVTPLSVRYHDDGHFHDLHHLPVAPAAVVIDSALLARAPLRWLAAGLGDT 173
Cdd:cd08170    86 GGKTIDTAKAVADYLGLPVVIVPTIASTDAPCSALSVIYTEDGEFDEYLFLPRNPDLVLVDTEIIAKAPVRFLVAGMGDA 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570 174 LAKWYEFRAI--DNGGNDSGFAAS--SRANSEICFRLIEQYGEEACRAVTAGQHNDALDQVLDAIFLFAGL----TSLMA 245
Cdd:cd08170   166 LATYFEARACarSGAPNMAGGRPTlaALALAELCYDTLLEYGVAAKAAVEAGVVTPALEAVIEANTLLSGLgfesGGLAA 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570 246 SgahaaaaHALYEGFTVCDKTREFGHGLLVGFGNLCLLALEQRSDEELLAAIRLAQACAVPLTMAAI-CPDLSEEELTAI 324
Cdd:cd08170   246 A-------HAIHNGLTALPETHHLLHGEKVAFGTLVQLVLEGRPDEEIEEVIRFCRSVGLPVTLADLgLEDVTDEELRKV 318

                         330       340       350
                  ....*....|....*....|....*....|...
gi 2463707570 325 VRASVDAPD-MATMPFTVAEQQVRQAIRRVEAL 356
Cdd:cd08170   319 AEAACAPGEtIHNMPFPVTPEDVVDAILAADAL 351
GlyDH-like cd08171
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ...
 14-353 6.05e-86

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: 263.61  E-value: 6.05e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  14 GAGVSQQLGGICARLGSRVLVAGGHQALAAAQTLIIEQLRQSGVTLTAVEWSGEQCSVNQIERLCARVRETDSDVLLAVG 93
Cdd:cd08171     7 GEDAYDAIPKICSPYGKKVVVIGGKKALAAAKPKLRAALEGSGLEITDFIWYGGEATYENVEKLKANPEVQEADMIFAVG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  94 GGKALDTGKAVAFQCGIPVVTLPTIAATCAAVTPLSVRYHDDGHFHDLHHLPVAPAAVVIDSALLARAPLRWLAAGLGDT 173
Cdd:cd08171    87 GGKAIDTVKVLADRLNKPVFTFPTIASNCAAVTAVSVMYNPDGSFKEYYFLKRPPVHTFIDTEIIAEAPEKYLWAGIGDT 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570 174 LAKWYEFRAIDNGGNDSGFAASSRANSEICFRLIEQYGEEACRAVTAGQHNDALDQVLDAIFLFAGLTSLMA-----SGa 248
Cdd:cd08171   167 LAKYYEVEFSARGDELDHTNALGVAISKMCSEPLLKYGVQALEDCRANKVSDALEQVVLDIIVTTGLVSNLVepdynSS- 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570 249 haaAAHALYEGFTVC-DKTREFGHGLLVGFGNLCLLALEQRsDEELLAAIRLAQACAVPLTMAAIcpDLSEEELTAIVRA 327
Cdd:cd08171   246 ---LAHALYYGLTTLpQIEEEHLHGEVVSYGVLVLLTVDGQ-FEELEKVYAFNKSIGLPTCLADL--GLTVEDLEKVLDK 319

                         330       340
                  ....*....|....*....|....*.
gi 2463707570 328 SVDAPDMATMPFTVAEQQVRQAIRRV 353
Cdd:cd08171   320 ALKTKDLRHSPYPITKEMFEEAIKDL 345
gldA PRK09423
glycerol dehydrogenase; Provisional
 1-360 3.94e-73

glycerol dehydrogenase; Provisional


Pssm-ID: 181843  Cd Length: 366  Bit Score: 231.24  E-value: 3.94e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570   1 MMQQVFFPATVLRGAGVSQQLGGICARLGSRVLVAGGHQALAAAQTLIIEQLRQSGVTLTAVEWSGEqCSVNQIERLCAR 80
Cdd:PRK09423    1 MDRIFISPSKYVQGKGALARLGEYLKPLGKRALVIADEFVLGIVGDRVEASLKEAGLTVVFEVFNGE-CSDNEIDRLVAI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  81 VRETDSDVLLAVGGGKALDTGKAVAFQCGIPVVTLPTIAATCAAVTPLSVRYHDDGHFHDLHHLPVAPAAVVIDSALLAR 160
Cdd:PRK09423   80 AEENGCDVVIGIGGGKTLDTAKAVADYLGVPVVIVPTIASTDAPTSALSVIYTEEGEFERYLFLPKNPDLVLVDTAIIAK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570 161 APLRWLAAGLGDTLAKWYEFRA-IDNGGNDSGFAASSRAN---SEICFRLIEQYGEEACRAVTAGQHNDALDQVLDAIFL 236
Cdd:PRK09423  160 APARFLAAGIGDALATWFEARAcSRSGGTTMAGGKPTLAAlalAELCYETLLEDGLKAKLAVEAKVVTPALENVIEANTL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570 237 FAGL----TSLMASgahaaaaHALYEGFTVCDKTREFGHGLLVGFGNLCLLALEQRSDEELLAAIRLAQACAVPLTMAAI 312
Cdd:PRK09423  240 LSGLgfesGGLAAA-------HAIHNGLTALEDTHHLTHGEKVAFGTLTQLVLENRPKEEIEEVIDFCHAVGLPTTLADL 312

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 2463707570 313 -CPDLSEEELTAIVRASV-DAPDMATMPFTVAEQQVRQAIRRVEALAARV 360
Cdd:PRK09423  313 gLKEDSDEELRKVAEAACaEGETIHNMPFKVTPEDVAAAILAADAYGQRY 362
GlyDH-like cd08172
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ...
 24-353 1.07e-69

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: 221.62  E-value: 1.07e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  24 ICARLGSRVLVAGGHQALAAAQTLIiEQLRQSGVTLtaVEWSGEqCSVNQIERLCARVRETDSDVLLAVGGGKALDTGKA 103
Cdd:cd08172    18 LSEFGIKRPLIIHGEKSWQAAKPYL-PKLFEIEYPV--LRYDGE-CSYEEIDRLAEEAKEHQADVIIGIGGGKVLDTAKA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570 104 VAFQCGIPVVTLPTIAATCAAVTPLSVRYHDDGHFHDLHHLPVAPAAVVIDSALLARAPLRWLAAGLGDTLAKWYEFRAI 183
Cdd:cd08172    94 VADKLNIPLILIPTLASNCAAWTPLSVIYDEDGEFIGYDYFPRSAYLVLVDPRLLLDSPKDYFVAGIGDTLAKWYEADAI 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570 184 -DNGGNDSGFAASSRANSEICFRLIEQYGEEACRAVTAGQHNDALDQVLDAIFLFAGLTSLMA------SGahaaaAHAL 256
Cdd:cd08172   174 lRQLEELPAFLQLARQAAKLCRDILLKDSEQALADLEAGKLTPAFIKVVETIIALAGMVGGFGdeygrsAG-----AHAI 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570 257 YEGFTVCDKTREFGHGLLVGFGNLCLLALEQRSDE--ELLA---AIRLaqacavPLTMAAI-CPDLSEEELTAIVRASVd 330
Cdd:cd08172   249 HNGLTKLPETHHFLHGEKVAYGILVQLALEGKWDEikKLLPfyrRLGL------PTSLADLgLTDDTEEALQKIAAFAA- 321

                         330       340
                  ....*....|....*....|....*
gi 2463707570 331 APD--MATMPFTVAEQQVRQAIRRV 353
Cdd:cd08172   322 SPEesIHLLPPDVTAEEVLQAIEKL 346
Fe-ADH pfam00465
Iron-containing alcohol dehydrogenase;
8-346 4.25e-38

Iron-containing alcohol dehydrogenase;


Pssm-ID: 425696 [Multi-domain]  Cd Length: 362  Bit Score: 139.66  E-value: 4.25e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570   8 PATVLRGAGVSQQLGGICARLGSRVL-VAGGHQALAAAQTLIIEQLRQSGVTLTAVEWSGEQCSVNQIERLCARVRETDS 86
Cdd:pfam00465   1 PTRIVFGAGALAELGEELKRLGARALiVTDPGSLKSGLLDKVLASLEEAGIEVVVFDGVEPEPTLEEVDEAAALAREAGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  87 DVLLAVGGGKALDTGKAVAFQCG------------------IPVVTLPTIAATCAAVTPLSVRYHDDGHFHD-LHHLPVA 147
Cdd:pfam00465  81 DVIIAVGGGSVIDTAKAIALLLTnpgdvwdylggkpltkpaLPLIAIPTTAGTGSEVTPLAVITDTETGEKLgIFSPKLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570 148 PAAVVIDSALLARAPLRWLAAGLGDTLAKWYEFRAIDNGgndsgfAASSRANSEICFRLIEQYGEeacRAVTAGQHNDAL 227
Cdd:pfam00465 161 PDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGA------NPLTDALALEAIRLIAENLP---RAVADGEDLEAR 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570 228 DQVLDAIFLfAGLtSLMASGAHAA--------AAHALYEGFT-------VCDKTREFGHGLLVGFGNLCLLALEQRSDEE 292
Cdd:pfam00465 232 ENMLLASTL-AGL-AFSNAGLGAAhalahalgGRYGIPHGLAnaillpyVLRFNAPAAPEKLAQLARALGEDSDEEAAEE 309

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2463707570 293 LLAAIR-LAQACAVPLTMAAIcpDLSEEELTAIVRASVDAPDMATMPFTVAEQQV 346
Cdd:pfam00465 310 AIEALReLLRELGLPTTLSEL--GVTEEDLDALAEAALRDRSLANNPRPLTAEDI 362
PRK10586 PRK10586
putative oxidoreductase; Provisional
 30-358 1.63e-33

putative oxidoreductase; Provisional


Pssm-ID: 182570  Cd Length: 362  Bit Score: 127.53  E-value: 1.63e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  30 SRVLVAGGHQALAAAQTLIIEQLrqSGVTLTAVEWSGeQCSVNQIERLCARVrETDSDVLLAVGGGKALDTGKAVAFQCG 109
Cdd:PRK10586   35 SRAVWIYGERAIAAAQPYLPPAF--ELPGAKHILFRG-HCSESDVAQLAAAS-GDDRQVVIGVGGGALLDTAKALARRLG 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570 110 IPVVTLPTIAATCAAVTPLSVRYHDDGH------FHDLHHLpvapaaVVIDSALLARAPLRWLAAGLGDTLAKWYEFRAI 183
Cdd:PRK10586  111 LPFVAIPTIAATCAAWTPLSVWYNDAGQalhfeiFDDANFL------VLVEPRIILNAPQEYLLAGIGDTLAKWYEAVVL 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570 184 DNGGNDSGFAASSRANSEICFR--LIEQyGEEACRAVTAGQHNDALDQVLDAIFLFAGLT-SLMASGAHAAAAHALYEGF 260
Cdd:PRK10586  185 APQPETLPLTVRLGINNALAIRdvLLNS-SEQALADQQNGQLTQDFCDVVDAIIAGGGMVgGLGERYTRVAAAHAVHNGL 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570 261 TVCDKTREFGHGLLVGFGNLCLLALEQRsDEELLAAIRLAQACAVPLTMAAICPDL-SEEELTAIVRASVDAPD-MATMP 338
Cdd:PRK10586  264 TVLPQTEKFLHGTKVAYGILVQSALLGQ-DDVLAQLIGAYQRFHLPTTLAELDVDInNQAEIDRVIAHTLRPVEsIHYLP 342

                         330       340
                  ....*....|....*....|
gi 2463707570 339 FTVAEQQVRQAIRRVEALAA 358
Cdd:PRK10586  343 VTLTPDTLRAAFEKVESFKA 362
Gro1PDH cd08173
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ...
 7-176 1.38e-24

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: 102.63  E-value: 1.38e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570   7 FPATVLRGAGVSQQLGGICARL--GSRVLVAGGHQALAAAQTLIIEQLRQSGVTLTAVEWSGEQCSVNqIERLCARVRET 84
Cdd:cd08173     1 LPRNVVVGHGAINKIGEVLKKLllGKRALIITGPNTYKIAGKRVEDLLESSGVEVVIVDIATIEEAAE-VEKVKKLIKES 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  85 DSDVLLAVGGGKALDTGKAVAFQCGIPVVTLPTIAATCAAVTPLSVRYHDDGHfhdlHHLP-VAPAAVVIDSALLARAPL 163
Cdd:cd08173    80 KADFIIGVGGGKVIDVAKYAAYKLNLPFISIPTSASHDGIASPFASIKGGDKP----YSIKaKAPIAIIADTEIISKAPK 155

                         170
                  ....*....|...
gi 2463707570 164 RWLAAGLGDTLAK 176
Cdd:cd08173   156 RLLAAGCGDLISN 168
Fe-ADH_2 pfam13685
Iron-containing alcohol dehydrogenase;
14-177 1.36e-23

Iron-containing alcohol dehydrogenase;


Pssm-ID: 404557 [Multi-domain]  Cd Length: 251  Bit Score: 97.76  E-value: 1.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  14 GAGVSQQLGGICARLG-SRVLVAGGHQALAAAQTLIIEQLRQSGVTLTAVEWSGEQCSVNQIERLCARVRETDSDVLLAV 92
Cdd:pfam13685   3 GPGALGRLGEYLAELGfRRVALVADANTYAAAGRKVAESLKRAGIEVETRLEVAGNADMETAEKLVGALRERDADAVVGV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  93 GGGKALDTGKAVAFQCGIPVVTLPTIAATCAAVTPLSVRYHDdghfHDLHHLP-VAPAAVVIDSALLARAPLRWLAAGLG 171
Cdd:pfam13685  83 GGGTVIDLAKYAAFKLGKPFISVPTAASNDGFASPGASLTVD----GKKRSIPaAAPFGVIADTDVIAAAPRRLLASGVG 158


                  ....*.
gi 2463707570 172 DTLAKW 177
Cdd:pfam13685 159 DLLAKI 164
DHQ_Fe-ADH cd07766
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ...
 8-179 7.39e-23

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: 96.28  E-value: 7.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570   8 PATVLRGAGVSQQLGGICARLGSRVLV-AGGHQALAAAQTliIEQLRQSGVTLTAVEWSGEQCSVNQIERLCARVRETDS 86
Cdd:cd07766     1 PTRIVFGEGAIAKLGEIKRRGFDRALVvSDEGVVKGVGEK--VADSLKKGLAVAIFDFVGENPTFEEVKNAVERARAAEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  87 DVLLAVGGGKALDTGKAVAF--QCGIPVVTLPTIAATCAAVTPLSVRYHDDGHF--HDLHHLPVapaAVVIDSALLARAP 162
Cdd:cd07766    79 DAVIAVGGGSTLDTAKAVAAllNRGIPFIIVPTTASTDSEVSPKSVITDKGGKNkqVGPHYNPD---VVFVDTDITKGLP 155

                         170
                  ....*....|....*..
gi 2463707570 163 LRWLAAGLGDTLAKWYE 179
Cdd:cd07766   156 PRQVASGGVDALAHAVE 172
egsA PRK00843
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
 7-176 1.85e-19

NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed


Pssm-ID: 179139  Cd Length: 350  Bit Score: 88.03  E-value: 1.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570   7 FPATVLRGAGVSQQLGGICARL--GSRVLVAGGHQALAAAQTLIIEQLRQSGVtltAVEWSGEQCSVNQIERLCARVRET 84
Cdd:PRK00843   10 LPRDVVVGHGVLDDIGDVCSDLklTGRALIVTGPTTKKIAGDRVEENLEDAGD---VEVVIVDEATMEEVEKVEEKAKDV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  85 DSDVLLAVGGGKALDTGKAVAFQCGIPVVTLPT------IAATCAAV----TPLSVRYHddghfhdlhhlpvAPAAVVID 154
Cdd:PRK00843   87 NAGFLIGVGGGKVIDVAKLAAYRLGIPFISVPTaashdgIASPRASIkgggKPVSVKAK-------------PPLAVIAD 153

                         170       180
                  ....*....|....*....|..
gi 2463707570 155 SALLARAPLRWLAAGLGDTLAK 176
Cdd:PRK00843  154 TEIIAKAPYRLLAAGCGDIISN 175
Fe-ADH-like cd08183
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 8-130 1.36e-16

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: 80.24  E-value: 1.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570   8 PATVLRGAGVSQQLGGICARLGSRVL-VAGGHQALAAAQTLIIEQLRQSGVTLTAVEWSGEQcSVNQIERLCARVRETDS 86
Cdd:cd08183     1 PPRIVFGRGSLQELGELAAELGKRALlVTGRSSLRSGRLARLLEALEAAGIEVALFSVSGEP-TVETVDAAVALAREAGC 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2463707570  87 DVLLAVGGGKALDTGKAVA----------------------FQCGIPVVTLPTIAATCAAVTPLSV 130
Cdd:cd08183    80 DVVIAIGGGSVIDAAKAIAalltnegsvldylevvgkgrplTEPPLPFIAIPTTAGTGSEVTKNAV 145
G1PDH-like cd08174
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ...
 14-334 2.16e-16

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: 79.10  E-value: 2.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  14 GAGVSQQLGGICARL---GSRVLVA-GGHQALAAAQTlIIEQLRQSGVTLTAvewsgEQCSVNQIERLCARVRETD-SDV 88
Cdd:cd08174     7 EEGALEHLGKYLADRnqgFGKVAIVtGEGIDELLGED-ILESLEEAGEIVTV-----EENTDNSAEELAEKAFSLPkVDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  89 LLAVGGGKALDTGKAVAFQCGIPVVTLPTIAATCAAVTPLSVRYHDDGHfhdlHHLPVA-PAAVVIDSALLARAPLRWLA 167
Cdd:cd08174    81 IVGIGGGKVLDVAKYAAFLSKLPFISVPTSLSNDGIASPVAVLKVDGKR----KSLGAKmPYGVIVDLDVIKSAPRRLIL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570 168 AGLGDTLAK------W-YEFRAidNGGNDSGFAA-SSRAnseicfrlieqygeeACRAV----TAGQHNDA-LDQVLDAI 234
Cdd:cd08174   157 AGIGDLISNitalydWkLAEEK--GGEPVDDFAYlLSRT---------------AADSLlntpGKDIKDDEfLKELAESL 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570 235 FL------FAGlTSLMASGAhaaaahalyegftvC-------DKT--REFGHGLLVGFGNLCLLALEQRSDEELLAAIRL 299
Cdd:cd08174   220 VLsgiameIAG-SSRPASGS--------------EhlishalDKLfpGPALHGIQVGLGTYFMSFLQGQRYEEIRDVLKR 284

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 2463707570 300 aqaCAVPLTMAAIcpDLSEEELTAIVRAsvdAPDM 334
Cdd:cd08174   285 ---TGFPLNPSDL--GLTKEEFIEAVKL---APST 311
HEPD cd08182
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ...
 8-175 8.77e-14

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: 71.49  E-value: 8.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570   8 PATVLRGAGVSQQLGGICARLGSR--VLVAGGHqalAAAQTLIIEQLRQSGVTLTAVEWSGEQC--SVNQIERLCARVRE 83
Cdd:cd08182     1 PVKIIFGPGALAELKDLLGGLGARrvLLVTGPS---AVRESGAADILDALGGRIPVVVFSDFSPnpDLEDLERGIELFRE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  84 TDSDVLLAVGGGKALDTGKAVAFQCG--------------------IPVVTLPTIAATCAAVTPLSVRYHDDGHF-HDLH 142
Cdd:cd08182    78 SGPDVIIAVGGGSVIDTAKAIAALLGspgenllllrtgekapeenaLPLIAIPTTAGTGSEVTPFATIWDEAEGKkYSLA 157

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2463707570 143 HLPVAPAAVVIDSALLARAPLR-WLAAGLgDTLA 175
Cdd:cd08182   158 HPSLYPDAAILDPELTLSLPLYlTASTGL-DALS 190
EutG COG1454
Alcohol dehydrogenase, class IV [Energy production and conversion];
1-175 1.24e-12

Alcohol dehydrogenase, class IV [Energy production and conversion];


Pssm-ID: 441063 [Multi-domain]  Cd Length: 381  Bit Score: 68.22  E-value: 1.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570   1 MMQQVFFPATVLRGAGVSQQLGGICARLG-SRVLVAGGhQALAAAQTL--IIEQLRQSGVTltAVEWSG--EQCSVNQIE 75
Cdd:COG1454     1 MMFTFRLPTRIVFGAGALAELGEELKRLGaKRALIVTD-PGLAKLGLLdrVLDALEAAGIE--VVVFDDvePNPTVETVE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  76 RLCARVRETDSDVLLAVGGGKALDTGKAVAFQC------------------GIPVVTLPTIAATCAAVTPLSVRYHDDGH 137
Cdd:COG1454    78 AGAAAAREFGADVVIALGGGSAIDAAKAIALLAtnpgdledylgikkvpgpPLPLIAIPTTAGTGSEVTPFAVITDPETG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2463707570 138 F-HDLHHLPVAPAAVVIDSALLARAPlRWLAAGLG-DTLA 175
Cdd:COG1454   158 VkKGIADPELLPDVAILDPELTLTLP-PSLTAATGmDALT 196
G1PDH_related cd08549
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ...
 8-322 1.67e-12

Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and archeal glycerol-1-phosphate dehydrogenase-like oxidoreductases. These proteins have similarity with 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. It also contains archaeal Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) that plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids.


Pssm-ID: 341479 [Multi-domain]  Cd Length: 331  Bit Score: 67.59  E-value: 1.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570   8 PATVLRGAGVSQQLGGICARLGS-RVLVAGGHQALAAAQTLIIEQLRQsgvtLTAVEwSGEQCSVNQIERLCARVRetds 86
Cdd:cd08549     1 PRYTIVGDGAINKIEEILKKLNLkRVLIITGKNTKAKYCRFFYDQLKT----VCDIV-YYDNIDNLEDELKKYTFY---- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  87 DVLLAVGGGKALDTGKAVAFQCGIPVVTLPTIAAT---CAAVTPLSVRYHDDGHFHDlhhlpvAPAAVVIDSALLARAPL 163
Cdd:cd08549    72 DCVIGIGGGRSIDTGKYLAYKLKIPFISVPTSASNdgiASPIVSLRIPGVKKTFMAD------APIAIIADTEIIKKSPR 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570 164 RWLAAGLGDTLAKW-----YEFRAIDNGGNDSGFAAS-SRANSEICFRLIEQY--GEEACRAVTagqhnDALDQVLDAIf 235
Cdd:cd08549   146 RLLSAGIGDLVSNItavldWKLAHKEKGEKYSEFAAIlSKTSAKELVSYVLKAsdLEEYHRVLV-----KALVGSGIAM- 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570 236 LFAGlTSLMASGAHAAAAHALyEGFTVCDKTREFGHGLLVGFGNLCLLALEQRSDEELLAA---IRLAQA---CAVPLTM 309
Cdd:cd08549   220 AIAG-SSRPASGSEHLFSHAL-DKLKEEYLNINVLHGEQVGVGTIIMSYLHEKENKKLSGLherIKMILKkvgAPTTAKQ 297

                         330
                  ....*....|...
gi 2463707570 310 AAICPDLSEEELT 322
Cdd:cd08549   298 LGIDEDLIIEALT 310
Fe-ADH cd08551
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ...
 8-162 4.20e-12

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: 66.70  E-value: 4.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570   8 PATVLRGAGVSQQLGGICARLG-SRVLVAGGhQALAAAQTL--IIEQLRQSGVTLT---AVEwsgEQCSVNQIERLCARV 81
Cdd:cd08551     1 PTRIVFGAGALARLGEELKALGgKKVLLVTD-PGLVKAGLLdkVLESLKAAGIEVEvfdDVE---PNPTVETVEAAAELA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  82 RETDSDVLLAVGGGKALDTGKAVAFQC------------------GIPVVTLPTIAATCAAVTPLSVRYHDDGHFHD-LH 142
Cdd:cd08551    77 REEGADLVIAVGGGSVLDTAKAIAVLAtnggsirdyegigkvpkpGLPLIAIPTTAGTGSEVTPNAVITDPETGRKMgIV 156

                         170       180
                  ....*....|....*....|
gi 2463707570 143 HLPVAPAAVVIDSALLARAP 162
Cdd:cd08551   157 SPYLLPDVAILDPELTLSLP 176
Fe-ADH-like cd08191
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 8-130 5.83e-12

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: 66.10  E-value: 5.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570   8 PATVLRGAGVSQQLGGICARLGSRVLVAgGHQALAAAQTL--IIEQLRQSGVTLTAVEWSGEQCSVNQIERLCARVRETD 85
Cdd:cd08191     4 PSRLLFGPGARRALGRVAARLGSRVLIV-TDPRLASTPLVaeLLAALTAAGVAVEVFDGGQPELPVSTVADAAAAARAFD 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2463707570  86 SDVLLAVGGGKALDTGKAVAFQC------------------GIPVVTLPTIAATCAAVTPLSV 130
Cdd:cd08191    83 PDVVIGLGGGSNMDLAKVVALLLahggdprdyygedrvpgpVLPLIAVPTTAGTGSEVTPVAV 145
Fe-ADH-like cd08196
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 8-157 7.50e-12

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: 65.68  E-value: 7.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570   8 PATVLRGAGVSQQLGGICARLG--SRVLVAGGHQALAAAQTLIIEQLRQSGVTL-TAVEwsgEQCSVNQIERLCARVRET 84
Cdd:cd08196     6 PVKIIFGEGILKELPDIIKELGgkRGLLVTDPSFIKSGLAKRIVESLKGRIVAVfSDVE---PNPTVENVDKCARLAREN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  85 DSDVLLAVGGGKALDTGKAVAFQC-------------------GIPVVTLPTIAATCAAVTPLSV-RYHDDGHFHDLHHL 144
Cdd:cd08196    83 GADFVIAIGGGSVLDTAKAAACLAktdgsiedylegkkkipkkGLPLIAIPTTAGTGSEVTPVAVlTDKEKGKKAPLVSP 162

                         170
                  ....*....|...
gi 2463707570 145 PVAPAAVVIDSAL 157
Cdd:cd08196   163 GFYPDIAIVDPEL 175
BDH cd08187
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ...
 8-175 2.38e-10

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: 61.30  E-value: 2.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570   8 PATVLRGAGVSQQLGGICARLGSRVLVA-GGhqalAAAQTL-----IIEQLRQSGVTLtaVEWSG-----EQCSVNQIER 76
Cdd:cd08187     7 PTKIIFGKGAIEELGEEIKKYGKKVLLVyGG----GSIKKNglydrVVASLKEAGIEV--VEFGGvepnpRLETVREGIE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  77 LCarvRETDSDVLLAVGGGKALDTGKAVA-----------FQCG-------IPVVTLPTIAAT-----CAAVtplsVRYH 133
Cdd:cd08187    81 LA---REENVDFILAVGGGSVIDAAKAIAagakydgdvwdFFTGkappekaLPVGTVLTLAATgsemnGGAV----ITNE 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2463707570 134 DDGHFHDLHHLPVAPAAVVIDSALLARAPLRWLAAGLGDTLA 175
Cdd:cd08187   154 ETKEKLGFGSPLLRPKFSILDPELTYTLPKYQTAAGIVDIFS 195
Fe-ADH-like cd14864
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 7-175 1.20e-09

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: 59.24  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570   7 FPATVLRGAGVSQQLGGICARLGSRVLVAGGhQALAAAQTL--IIEQLRQSGVTLTAVEWSGEQCSVNQIERLCARVRET 84
Cdd:cd14864     3 IPPNIVFGADSLERIGEEVKEYGSRFLLITD-PVLKESGLAdkIVSSLEKAGISVIVFDEIPASATSDTIDEAAELARKA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  85 DSDVLLAVGGGKALDTGKAVA---------------FQC---GIPVVTLPTIAATCAAVTPLSVRYHD-DGHFHDLHHLP 145
Cdd:cd14864    82 GADGIIAVGGGKVLDTAKAVAilanndggaydflegAKPkkkPLPLIAVPTTPRSGFEFSDRFPVVDSrSREVKLLKAQP 161

                         170       180       190
                  ....*....|....*....|....*....|
gi 2463707570 146 VAPAAVVIDSALLARAPLRWLAAGLGDTLA 175
Cdd:cd14864   162 GLPKAVIVDPNLMASLTGNQTAAMALAALA 191
G1PDH cd08175
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ...
 14-176 1.34e-09

Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in an NADH-dependent manner; Glycerol-1-phosphate dehydrogenase (G1PDH) 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 a Ni++ ion. In Bacillus subtilis, it has been described as AraM gene in L-arabinose (ara) operon. AraM protein forms homodimer.


Pssm-ID: 341454  Cd Length: 340  Bit Score: 58.68  E-value: 1.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  14 GAGVSQQLGGICARLG---SRVLVAGGHQALAAAQTLIiEQLRQSGVTLTAVEWSGEQcSVNQIERLCARVRET---DSD 87
Cdd:cd08175     7 GEGALKKLPEYLKELFggkKVLVVADENTYAAAGEEVE-AALEEAGVTVCLLIFPGEG-DLIADEAAVGKVLLElekDTD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  88 VLLAVGGGKALDTGKAVAFQCGIPVVTLPTiAAT----CAAVTPLSVryhdDGhfhdL-HHLP-VAPAAVVIDSALLARA 161
Cdd:cd08175    85 LIIAVGSGTINDLTKYAAYKLGIPYISVPT-APSmdgyTSSGAPIIV----DG----VkKTFPaHAPKAIFADLDVLANA 155

                         170
                  ....*....|....*
gi 2463707570 162 PLRWLAAGLGDTLAK 176
Cdd:cd08175   156 PQRMIAAGFGDLLGK 170
MAR cd08177
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ...
 8-117 2.21e-09

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: 58.28  E-value: 2.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570   8 PATVLRGAGVSQQLGGICARLG-SRVLV-AGGHQALAAAQtlIIEQLRQSGvtltAVEWSG--EQCSVNQIERLCARVRE 83
Cdd:cd08177     1 PQRVVFGAGTLAELAEELERLGaRRALVlSTPRQRALAER--VAALLGDRV----AGVFDGavMHVPVEVAERALAAARE 74

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2463707570  84 TDSDVLLAVGGGKALDTGKAVAFQCGIPVVTLPT 117
Cdd:cd08177    75 AGADGLVAIGGGSAIGLAKAIALRTGLPIVAVPT 108
PPD-like cd08181
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ...
 6-130 4.28e-09

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: 57.21  E-value: 4.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570   6 FFPATVLRGAGVSQQLGGICARLGSRVL-VAGGHQALAA-AQTLIIEQLRQSGVTLTAVEWSGEQCSVNQIERLCARVRE 83
Cdd:cd08181     2 YMPTKVYFGKNCVEKHADELAALGKKALiVTGKHSAKKNgSLDDVTEALEENGIEYFIFDEVEENPSIETVEKGAELARK 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2463707570  84 TDSDVLLAVGGGKALDTGKAVA------------FQCG-----IPVVTLPTIAATCAAVTPLSV 130
Cdd:cd08181    82 EGADFVIGIGGGSPLDAAKAIAllaankdgdedlFQNGkynppLPIVAIPTTAGTGSEVTPYSI 145
Fe-ADH-like cd14863
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 7-175 1.06e-08

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: 56.39  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570   7 FPATVLRGAGVSQQLGGICARLGSR--VLVAG-GHQALAAAQtLIIEQLRQSGvtLTAVEWSGEQ--CSVNQIERLCARV 81
Cdd:cd14863     4 QLTPVIFGAGAVEQIGELLKELGCKkvLLVTDkGLKKAGIVD-KIIDLLEEAG--IEVVVFDDVEpdPPDEIVDEAAEIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  82 RETDSDVLLAVGGGKALDTGKAVA-------------------FQCGIPVVTLPTIAATCAAVTPLSVRY-HDDGHFHDL 141
Cdd:cd14863    81 REEGADGVIGIGGGSVLDTAKAIAvlltnpgpiidyalagppvPKPGIPLIAIPTTAGTGSEVTPIAVITdEENGVKKSL 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2463707570 142 HHLPVAPAAVVIDSALLARAPLRWLAA-GLgDTLA 175
Cdd:cd14863   161 LGPFLVPDLAILDPELTVGLPPSLTAAtGM-DALS 194
Fe-ADH-like cd08185
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 6-130 3.47e-07

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: 51.34  E-value: 3.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570   6 FFPATVLRGAGVSQQLGGICARLGSRVLVAGGHQALAAAQTL--IIEQLRQSGVT-----------LTAVewsgeqcsvn 72
Cdd:cd08185     2 YQPTRILFGAGKLNELGEEALRPGKKALIVTGKGSSKKTGLLdrVKKLLEKAGVEvvvfdkvepnpLTTT---------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  73 qIERLCARVRETDSDVLLAVGGGKALDTGKAVAFQCG----------------------IPVVTLPTIAATCAAVTPLSV 130
Cdd:cd08185    72 -VMEGAALAKEEGCDFVIGLGGGSSMDAAKAIAFMATnpgdiwdyifggtgkgpppekaLPIIAIPTTAGTGSEVDPWAV 150
Fe-ADH-like cd08194
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 8-126 5.52e-07

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: 50.99  E-value: 5.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570   8 PATVLRGAGVSQQLGGICARL-GSRVLVAGGHQALAAAQTLIIEQ-LRQSGVTlTAV--EWSGEQCSVNqIERLCARVRE 83
Cdd:cd08194     1 PRTIIIGGGALEELGEEAASLgGKRALIVTDKVMVKLGLVDKVTQlLAEAGIA-YAVfdDVVSEPTDEM-VEEGLALYKE 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2463707570  84 TDSDVLLAVGGGKALDTGKAVAF------------------QCGIPVVTLPTIAATCAAVT 126
Cdd:cd08194    79 GGCDFIVALGGGSPIDTAKAIAVlatnggpirdymgprkvdKPGLPLIAIPTTAGTGSEVT 139
Fe-ADH-like cd14865
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 4-168 7.79e-07

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: 50.62  E-value: 7.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570   4 QVFFPATVLRGAGVSQQLGGICARLG-SRVLVAGGHQALAAAQTLIIEQLRQSGVTLTAVEWSGEQ-CSVNQIERLCARV 81
Cdd:cd14865     2 EFFNPTKIVSGAGALENLPAELARLGaRRPLIVTDKGLAAAGLLKKVEDALGDAIEIVGVFDDVPPdSSVAVVNEAAARA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  82 RETDSDVLLAVGGGKALDTGKAVA--FQCG-----------------IPVVTLPTIAATCAAVTPLSVRYHDDGH----F 138
Cdd:cd14865    82 REAGADGIIAVGGGSVIDTAKGVNilLSEGgddlddygganrltrplKPLIAIPTTAGTGSEVTLVAVIKDEEKKvkllF 161

                         170       180       190
                  ....*....|....*....|....*....|
gi 2463707570 139 HDlHHLpvAPAAVVIDSALLARAPLRWLAA 168
Cdd:cd14865   162 VS-PFL--LPDVAILDPRLTLSLPPKLTAA 188
Fe-ADH-like cd14866
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 8-176 1.68e-06

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: 49.54  E-value: 1.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570   8 PATVLRGAGVSQQLGGICARLGSR--VLVAGGHqalAAAQTLIIEQLRQS-GVTLTAVEWSGEQCS-VNQIERLCARVRE 83
Cdd:cd14866     5 PLRLFSGRGALARLGRELDRLGARraLVVCGSS---VGANPDLMDPVRAAlGDRLAGVFDGVRPHSpLETVEAAAEALRE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  84 TDSDVLLAVGGGKALDTGKAVAFQCG---------------------------IPVVTLPTIAATCAAVTPLSVRYHDDG 136
Cdd:cd14866    82 ADADAVVAVGGGSAIVTARAASILLAedrdvrelctrraedglmvsprldapkLPIFVVPTTPTTADVKAGSAVTDPPAG 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2463707570 137 HFHDLHHLPVAPAAVVIDSALLARAPLRWLAAGLGDTLAK 176
Cdd:cd14866   162 QRLALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDM 201
YqdH COG1979
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
1-121 4.14e-06

Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];


Pssm-ID: 441582 [Multi-domain]  Cd Length: 387  Bit Score: 48.14  E-value: 4.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570   1 MMQQVFF-PATVLRGAGVSQQLGGICARLGSRVLVA-GGHQA-----LAAaqtlIIEQLRQSGVTLtaVEWSGeqcsvnq 73
Cdd:COG1979     1 MNNFTFYnPTKIIFGKGQIAKLGEEIPKYGKKVLLVyGGGSIkknglYDQ----VKAALKEAGIEV--VEFGG------- 67

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2463707570  74 IE---------RLCARVRETDSDVLLAVGGGKALDTGKAVAF------------------QCGIPVVTLPTIAAT 121
Cdd:COG1979    68 VEpnprletvrKGVELCKEEGIDFILAVGGGSVIDGAKAIAAgakydgdpwdiltgkapvEKALPLGTVLTLPAT 142
Fe-ADH-like cd14861
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ...
 7-157 4.16e-06

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: 48.28  E-value: 4.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570   7 FPATVLRGAGVSQQLGGICARLG-SRVLV---AGghqaLAAAQ--TLIIEQLRQSGvtLTAVEWSGEQC--SVNQIERLC 78
Cdd:cd14861     2 YPTRIRFGAGAIAELPEELKALGiRRPLLvtdPG----LAALGivDRVLEALGAAG--LSPAVFSDVPPnpTEADVEAGV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  79 ARVRETDSDVLLAVGGGKALDTGKAVAFQCG----------------------IPVVTLPTIAATCAAVTPLSVRYHDDG 136
Cdd:cd14861    76 AAYREGGCDGIIALGGGSAIDAAKAIALMAThpgplwdyedgeggpaaitpavPPLIAIPTTAGTGSEVGRAAVITDDDT 155

                         170       180
                  ....*....|....*....|....*.
gi 2463707570 137 H-----FHDlhhlPVAPAAVVIDSAL 157
Cdd:cd14861   156 GrkkiiFSP----KLLPKVAICDPEL 177
HVD cd08193
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ...
 8-130 6.17e-06

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: 47.51  E-value: 6.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570   8 PATVLRGAGVSQQLGGICARLG-SRVLV---AGGHQA-LAAAqtlIIEQLRQSGVTLTAVEWSGEQCSVNQIERLCARVR 82
Cdd:cd08193     4 VPRIICGAGAAARLGELLRELGaRRVLLvtdPGLVKAgLADP---ALAALEAAGIAVTVFDDVVADPPEAVVEAAVEQAR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2463707570  83 ETDSDVLLAVGGGKALDTGKAVAFQCG------------------IPVVTLPTIAATCAAVTPLSV 130
Cdd:cd08193    81 EAGADGVIGFGGGSSMDVAKLVALLAGsdqplddiygvgkatgprLPLILVPTTAGTGSEVTPISI 146
Fe-ADH-like cd08186
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ...
 14-105 5.96e-05

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: 44.56  E-value: 5.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  14 GAGVSQQLGGICARLG-SRVLVAGGHQA--LAAAQTLIIEQLRQSGVTLTAVEWSGEQCSVNQIERLCARVRETDSDVLL 90
Cdd:cd08186     7 GVGAIAKIKDILKDLGiDKVIIVTGRSSykKSGAWDDVEKALEENGIEYVVYDKVTPNPTVDQADEAAKLARDFGADAVI 86

                          90
                  ....*....|....*
gi 2463707570  91 AVGGGKALDTGKAVA 105
Cdd:cd08186    87 AIGGGSPIDTAKSVA 101
Fe-ADH-like cd08189
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 10-125 1.42e-04

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: 43.23  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  10 TVLRGAGVSQQLGGICARLG-SRVLVAGGhQALAAAQTL--IIEQLRQSGVTLTAveWSGEQC--SVNQIERLCARVRET 84
Cdd:cd08189     7 ELFEGAGSLLQLPEALKKLGiKRVLIVTD-KGLVKLGLLdpLLDALKKAGIEYVV--FDGVVPdpTIDNVEEGLALYKEN 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2463707570  85 DSDVLLAVGGGKALDTGKAVA----------------FQC---GIPVVTLPTIA-----ATCAAV 125
Cdd:cd08189    84 GCDAIIAIGGGSVIDCAKVIAaraanpkksvrklkglLKVrkkLPPLIAVPTTAgtgseATIAAV 148
HOT cd08190
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ...
 14-130 9.96e-04

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: 40.99  E-value: 9.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  14 GAGVSQQLGGICARLG-SRVLVAG--GHQALAAAQTlIIEQLRQSGVTltAVEWSG---EQcSVNQIERLCARVRETDSD 87
Cdd:cd08190     7 GPGATRELGMDLKRLGaKKVLVVTdpGLAKLGLVER-VLESLEKAGIE--VVVYDGvrvEP-TDESFEEAIEFAKEGDFD 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2463707570  88 VLLAVGGGKALDTGKAVAF-----------------------QCGIPVVTLPTIAATCAAVTPLSV 130
Cdd:cd08190    83 AFVAVGGGSVIDTAKAANLyathpgdfldyvnapigkgkpvpGPLKPLIAIPTTAGTGSETTGVAI 148
EEVS cd08199
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the ...
 87-171 1.79e-03

2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the cyclization of sedoheptulose 7-phosphate to 2-epi-5-epi-valiolone in the biosynthesis of C(7)N-aminocyclitol-containing products. The cyclization product, 2-epi-5-epi-valiolone ((2S,3S,4S,5R)-5-(hydroxymethyl)cyclohexanon-2,3,4,5-tetrol), is a precursor of the valienamine moiety. The valienamine unit is responsible for their biological activities as various glycosidic hydrolases inhibitors. Two important microbial secondary metabolites, validamycin and acarbose, are used in agricultural and biomedical applications. Validamycin A is an antifungal antibiotic which has a strong trehalase inhibitory activity and has been used to control sheath blight disease in rice caused by Rhizoctonia solani. Acarbose is an alpha-glucosidase inhibitor used for the treatment of type II insulin-independent diabetes. Salbostatin produced by Streptomyces albus also belongs to this family. It exhibits strong trehalase inhibitory activity.


Pssm-ID: 341478  Cd Length: 349  Bit Score: 39.82  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  87 DVLLAVGGGKALDTgkaVAFQC-----GIPVVTLPT--IAATCAAVtplSVRY---HDD-----GHFHdlhhlpvAPAAV 151
Cdd:cd08199    89 EPVIAIGGGVLLDV---VGFAAslyrrGVPYIRVPTtlLGLVDAGV---GIKTgvnFGGhknrlGAYY-------PPVAT 155

                          90       100
                  ....*....|....*....|
gi 2463707570 152 VIDSALLARAPLRWLAAGLG 171
Cdd:cd08199   156 LLDRSFLKTLPRRHIRNGLA 175
Fe-ADH_KdnB-like cd08184
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ...
 70-130 2.57e-03

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: 39.56  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  70 SVNQIERLCARVRETDS---DVLLAVGGGKALDTGKAVAFQC------------------GIPVVTLPTIAATCAAVTPL 128
Cdd:cd08184    64 KTDQIDALRAQIRAENDklpAAVVGIGGGSTMDIAKAVSNMLtnpgsaadyqgwdlvknpGIYKIGVPTLSGTGAEASRT 143


                  ..
gi 2463707570 129 SV 130
Cdd:cd08184   144 AV 145
PRK15454 PRK15454
ethanolamine utilization ethanol dehydrogenase EutG;
38-162 3.12e-03

ethanolamine utilization ethanol dehydrogenase EutG;


Pssm-ID: 185351 [Multi-domain]  Cd Length: 395  Bit Score: 39.24  E-value: 3.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463707570  38 HQALAAAQtlIIEQLRQSGVTLTAveW---SGEQCsVNQIERLCARVRETDSDVLLAVGGGKALDTGKAVA--------- 105
Cdd:PRK15454   61 HQAGMTAG--LTRSLAVKGIAMTL--WpcpVGEPC-ITDVCAAVAQLRESGCDGVIAFGGGSVLDAAKAVAllvtnpdst 135

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2463707570 106 ---------FQCGIPVVTLPTIAATCAAVTPLSVRYHD-DGHFHDLHHLPVAPAAVVIDSALLARAP 162
Cdd:PRK15454  136 laemsetsvLQPRLPLIAIPTTAGTGSETTNVTVIIDAvSGRKQVLAHASLMPDVAILDAALTEGVP 202
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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