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Conserved domains on  [gi|648449283|ref|WP_026141034|]
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MULTISPECIES: glycerol dehydrogenase [Aeromonas]

Protein Classification

glycerol dehydrogenase( domain architecture ID 10013226)

glycerol dehydrogenase catalyzes the NAD-dependent oxidation of glycerol to dihydroxyacetone

CATH:  3.40.50.1970
EC:  1.1.1.6
Gene Ontology:  GO:0008270|GO:0008888|GO:0030554
PubMed:  35751426
SCOP:  3001905

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
gldA PRK09423
glycerol dehydrogenase; Provisional
 5-369 1.01e-178

glycerol dehydrogenase; Provisional


:

Pssm-ID: 181843  Cd Length: 366  Bit Score: 500.50  E-value: 1.01e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283   5 PRTVTSPKKFIIGHDLLPQLHDHVKDFGDNALLVSDEFILERVREEALAGLLQAGLKGAVEKFNYECTDIEIRRLCDLAE 84
Cdd:PRK09423   2 DRIFISPSKYVQGKGALARLGEYLKPLGKRALVIADEFVLGIVGDRVEASLKEAGLTVVFEVFNGECSDNEIDRLVAIAE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  85 QQGANVIVGIGGGKTLDVAKAVAFYLRRPVVLFPTIASTDAPCTALAVIYNPAGEFERYLFLPQNPDVVIADTAIIAAAP 164
Cdd:PRK09423  82 ENGCDVVIGIGGGKTLDTAKAVADYLGVPVVIVPTIASTDAPTSALSVIYTEEGEFERYLFLPKNPDLVLVDTAIIAKAP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283 165 ARFFAAGVGDALATYFEARACYRADGINLVGKRPSRTGLGLARLCYELLGENIELAMDAVRHHVTTPALEQTIEATIYLS 244
Cdd:PRK09423 162 ARFLAAGIGDALATWFEARACSRSGGTTMAGGKPTLAALALAELCYETLLEDGLKAKLAVEAKVVTPALENVIEANTLLS 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283 245 GVGAEAGGLAAAHAVNNGMSVVPDLHRAQHGEKVVFGLLTQLVLERAPQAELDEVMRIIQLAGLPMTLQEMGLSQFVESE 324
Cdd:PRK09423 242 GLGFESGGLAAAHAIHNGLTALEDTHHLTHGEKVAFGTLTQLVLENRPKEEIEEVIDFCHAVGLPTTLADLGLKEDSDEE 321

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 648449283 325 WRQVAKLACDPLDTMGNMPMSVSEQDVYHAMIAANAMAERYRARH 369
Cdd:PRK09423 322 LRKVAEAACAEGETIHNMPFKVTPEDVAAAILAADAYGQRYKQEW 366
 
Name Accession Description Interval E-value
gldA PRK09423
glycerol dehydrogenase; Provisional
 5-369 1.01e-178

glycerol dehydrogenase; Provisional


Pssm-ID: 181843  Cd Length: 366  Bit Score: 500.50  E-value: 1.01e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283   5 PRTVTSPKKFIIGHDLLPQLHDHVKDFGDNALLVSDEFILERVREEALAGLLQAGLKGAVEKFNYECTDIEIRRLCDLAE 84
Cdd:PRK09423   2 DRIFISPSKYVQGKGALARLGEYLKPLGKRALVIADEFVLGIVGDRVEASLKEAGLTVVFEVFNGECSDNEIDRLVAIAE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  85 QQGANVIVGIGGGKTLDVAKAVAFYLRRPVVLFPTIASTDAPCTALAVIYNPAGEFERYLFLPQNPDVVIADTAIIAAAP 164
Cdd:PRK09423  82 ENGCDVVIGIGGGKTLDTAKAVADYLGVPVVIVPTIASTDAPTSALSVIYTEEGEFERYLFLPKNPDLVLVDTAIIAKAP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283 165 ARFFAAGVGDALATYFEARACYRADGINLVGKRPSRTGLGLARLCYELLGENIELAMDAVRHHVTTPALEQTIEATIYLS 244
Cdd:PRK09423 162 ARFLAAGIGDALATWFEARACSRSGGTTMAGGKPTLAALALAELCYETLLEDGLKAKLAVEAKVVTPALENVIEANTLLS 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283 245 GVGAEAGGLAAAHAVNNGMSVVPDLHRAQHGEKVVFGLLTQLVLERAPQAELDEVMRIIQLAGLPMTLQEMGLSQFVESE 324
Cdd:PRK09423 242 GLGFESGGLAAAHAIHNGLTALEDTHHLTHGEKVAFGTLTQLVLENRPKEEIEEVIDFCHAVGLPTTLADLGLKEDSDEE 321

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 648449283 325 WRQVAKLACDPLDTMGNMPMSVSEQDVYHAMIAANAMAERYRARH 369
Cdd:PRK09423 322 LRKVAEAACAEGETIHNMPFKVTPEDVAAAILAADAYGQRYKQEW 366
GlyDH cd08170
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ...
 11-361 2.07e-148

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: 422.98  E-value: 2.07e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  11 PKKFIIGHDLLPQLHDHVKDFGDNALLVSDEFILERVREEALAGLLQAGLKGAVEKFNYECTDIEIRRLCDLAEQQGANV 90
Cdd:cd08170    1 PSRYVQGPGALDRLGEYLAPLGKKALVIADPFVLDLVGERLEESLEKAGLEVVFEVFGGECSREEIERLAAIARANGADV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  91 IVGIGGGKTLDVAKAVAFYLRRPVVLFPTIASTDAPCTALAVIYNPAGEFERYLFLPQNPDVViadtaiiaaaparffaa 170
Cdd:cd08170   81 VIGIGGGKTIDTAKAVADYLGLPVVIVPTIASTDAPCSALSVIYTEDGEFDEYLFLPRNPDLVlvdteiiakapvrflva 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283 171 GVGDALATYFEARACYRADGINLVGKRPSRTGLGLARLCYELLGENIELAMDAVRHHVTTPALEQTIEATIYLSgvgaea 250
Cdd:cd08170  161 GMGDALATYFEARACARSGAPNMAGGRPTLAALALAELCYDTLLEYGVAAKAAVEAGVVTPALEAVIEANTLLSglgfes 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283 251 gglaaahaVNNGMSVVPDLHRAQHGEKVVFGLLTQLVLERAPQAELDEVMRIIQLAGLPMTLQEMGLSQFVESEWRQVAK 330
Cdd:cd08170  241 gglaaahaIHNGLTALPETHHLLHGEKVAFGTLVQLVLEGRPDEEIEEVIRFCRSVGLPVTLADLGLEDVTDEELRKVAE 320

                        330       340       350
                 ....*....|....*....|....*....|.
gi 648449283 331 LACDPLDTMGNMPMSVSEQDVYHAMIAANAM 361
Cdd:cd08170  321 AACAPGETIHNMPFPVTPEDVVDAILAADAL 351
GldA COG0371
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ...
 6-358 3.97e-124

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: 361.79  E-value: 3.97e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283   6 RTVTSPKKFIIGHDLLPQLHDHVKDFGDNALLVSDEFILERVREEALAGLLQAGLKGAVEKFNYECTDIEIRRLCDLAEQ 85
Cdd:COG0371    1 RVIILPRRYVQGEGALDELGEYLADLGKRALIITGPTALKAAGDRLEESLEDAGIEVEVEVFGGECSEEEIERLAEEAKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  86 QGANVIVGIGGGKTLDVAKAVAFYLRRPVVLFPTIASTDAPCTALAVIYNPAGEFERYLFLPQNPDVViadtaiiaaapa 165
Cdd:COG0371   81 QGADVIIGVGGGKALDTAKAVAYRLGLPVVSVPTIASTDAPASPLSVIYTEDGAFDGYSFLAKNPDLVlvdtdiiakapv 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283 166 rffaaGVGDALATYFEARACYRADGiNLVGKRPSRTGLGLARLCYELLGENIELAMDAVRHHVTTPALEQTIEATIYLSG 245
Cdd:COG0371  161 rllaaGIGDALAKWYEARDWSLAHR-DLAGEYYTEAAVALARLCAETLLEYGEAAIKAVEAGVVTPALERVVEANLLLSG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283 246 VGAEAGGLAAAH----AVNNGMSVVPDLHRAQHGEKVVFGLLTQLVLERAPQaELDEVMRIIQLAGLPMTLQEMGLSQFV 321
Cdd:COG0371  240 LAMGIGSSRPGSgaahAIHNGLTALPETHHALHGEKVAFGTLVQLVLEGRPE-EIEELLDFLRSVGLPTTLADLGLDDET 318

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 648449283 322 ESEWRQVAKLACDPLDTMGNMPMSVSEQDVYHAMIAA 358
Cdd:COG0371  319 EEELLTVAEAARPERYTILNLPFEVTPEAVEAAILAT 355
Fe-ADH pfam00465
Iron-containing alcohol dehydrogenase;
11-351 5.18e-37

Iron-containing alcohol dehydrogenase;


Pssm-ID: 425696 [Multi-domain]  Cd Length: 362  Bit Score: 136.96  E-value: 5.18e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283   11 PKKFIIGHDLLPQLHDHVKDFGDNALLVSDEFILER-VREEALAGLLQAGLKGAV-EKFNYECTDIEIRRLCDLAEQQGA 88
Cdd:pfam00465   1 PTRIVFGAGALAELGEELKRLGARALIVTDPGSLKSgLLDKVLASLEEAGIEVVVfDGVEPEPTLEEVDEAAALAREAGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283   89 NVIVGIGGGKTLDVAKAVAFYL------------------RRPVVLFPTIASTDAPCTALAVIYNPAGEFERYLFLPQ-N 149
Cdd:pfam00465  81 DVIIAVGGGSVIDTAKAIALLLtnpgdvwdylggkpltkpALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFSPKlL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  150 PDVVIADTAIIAAAPARFFAAGVGDALATYFEAracyradginLVGKRPSRTGLGLARLCYELLGENIELAMDAVRHhvt 229
Cdd:pfam00465 161 PDLAILDPELTLTLPPRLTAATGMDALAHAVEA----------YVSKGANPLTDALALEAIRLIAENLPRAVADGED--- 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  230 TPALEQTIEATiYLSGVGAEAGGLAAAHAVNNGMSVVPDL-HRAQHGEKVVFGL----------LTQLVL-------ERA 291
Cdd:pfam00465 228 LEARENMLLAS-TLAGLAFSNAGLGAAHALAHALGGRYGIpHGLANAILLPYVLrfnapaapekLAQLARalgedsdEEA 306

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  292 PQAELDEVMRIIQLAGLPMTLQEMGLSqfvESEWRQVAKLACDPLdTMGNMPMSVSEQDV 351
Cdd:pfam00465 307 AEEAIEALRELLRELGLPTTLSELGVT---EEDLDALAEAALRDR-SLANNPRPLTAEDI 362
 
Name Accession Description Interval E-value
gldA PRK09423
glycerol dehydrogenase; Provisional
 5-369 1.01e-178

glycerol dehydrogenase; Provisional


Pssm-ID: 181843  Cd Length: 366  Bit Score: 500.50  E-value: 1.01e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283   5 PRTVTSPKKFIIGHDLLPQLHDHVKDFGDNALLVSDEFILERVREEALAGLLQAGLKGAVEKFNYECTDIEIRRLCDLAE 84
Cdd:PRK09423   2 DRIFISPSKYVQGKGALARLGEYLKPLGKRALVIADEFVLGIVGDRVEASLKEAGLTVVFEVFNGECSDNEIDRLVAIAE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  85 QQGANVIVGIGGGKTLDVAKAVAFYLRRPVVLFPTIASTDAPCTALAVIYNPAGEFERYLFLPQNPDVVIADTAIIAAAP 164
Cdd:PRK09423  82 ENGCDVVIGIGGGKTLDTAKAVADYLGVPVVIVPTIASTDAPTSALSVIYTEEGEFERYLFLPKNPDLVLVDTAIIAKAP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283 165 ARFFAAGVGDALATYFEARACYRADGINLVGKRPSRTGLGLARLCYELLGENIELAMDAVRHHVTTPALEQTIEATIYLS 244
Cdd:PRK09423 162 ARFLAAGIGDALATWFEARACSRSGGTTMAGGKPTLAALALAELCYETLLEDGLKAKLAVEAKVVTPALENVIEANTLLS 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283 245 GVGAEAGGLAAAHAVNNGMSVVPDLHRAQHGEKVVFGLLTQLVLERAPQAELDEVMRIIQLAGLPMTLQEMGLSQFVESE 324
Cdd:PRK09423 242 GLGFESGGLAAAHAIHNGLTALEDTHHLTHGEKVAFGTLTQLVLENRPKEEIEEVIDFCHAVGLPTTLADLGLKEDSDEE 321

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 648449283 325 WRQVAKLACDPLDTMGNMPMSVSEQDVYHAMIAANAMAERYRARH 369
Cdd:PRK09423 322 LRKVAEAACAEGETIHNMPFKVTPEDVAAAILAADAYGQRYKQEW 366
GlyDH cd08170
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ...
 11-361 2.07e-148

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: 422.98  E-value: 2.07e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  11 PKKFIIGHDLLPQLHDHVKDFGDNALLVSDEFILERVREEALAGLLQAGLKGAVEKFNYECTDIEIRRLCDLAEQQGANV 90
Cdd:cd08170    1 PSRYVQGPGALDRLGEYLAPLGKKALVIADPFVLDLVGERLEESLEKAGLEVVFEVFGGECSREEIERLAAIARANGADV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  91 IVGIGGGKTLDVAKAVAFYLRRPVVLFPTIASTDAPCTALAVIYNPAGEFERYLFLPQNPDVViadtaiiaaaparffaa 170
Cdd:cd08170   81 VIGIGGGKTIDTAKAVADYLGLPVVIVPTIASTDAPCSALSVIYTEDGEFDEYLFLPRNPDLVlvdteiiakapvrflva 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283 171 GVGDALATYFEARACYRADGINLVGKRPSRTGLGLARLCYELLGENIELAMDAVRHHVTTPALEQTIEATIYLSgvgaea 250
Cdd:cd08170  161 GMGDALATYFEARACARSGAPNMAGGRPTLAALALAELCYDTLLEYGVAAKAAVEAGVVTPALEAVIEANTLLSglgfes 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283 251 gglaaahaVNNGMSVVPDLHRAQHGEKVVFGLLTQLVLERAPQAELDEVMRIIQLAGLPMTLQEMGLSQFVESEWRQVAK 330
Cdd:cd08170  241 gglaaahaIHNGLTALPETHHLLHGEKVAFGTLVQLVLEGRPDEEIEEVIRFCRSVGLPVTLADLGLEDVTDEELRKVAE 320

                        330       340       350
                 ....*....|....*....|....*....|.
gi 648449283 331 LACDPLDTMGNMPMSVSEQDVYHAMIAANAM 361
Cdd:cd08170  321 AACAPGETIHNMPFPVTPEDVVDAILAADAL 351
GldA COG0371
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ...
 6-358 3.97e-124

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: 361.79  E-value: 3.97e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283   6 RTVTSPKKFIIGHDLLPQLHDHVKDFGDNALLVSDEFILERVREEALAGLLQAGLKGAVEKFNYECTDIEIRRLCDLAEQ 85
Cdd:COG0371    1 RVIILPRRYVQGEGALDELGEYLADLGKRALIITGPTALKAAGDRLEESLEDAGIEVEVEVFGGECSEEEIERLAEEAKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  86 QGANVIVGIGGGKTLDVAKAVAFYLRRPVVLFPTIASTDAPCTALAVIYNPAGEFERYLFLPQNPDVViadtaiiaaapa 165
Cdd:COG0371   81 QGADVIIGVGGGKALDTAKAVAYRLGLPVVSVPTIASTDAPASPLSVIYTEDGAFDGYSFLAKNPDLVlvdtdiiakapv 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283 166 rffaaGVGDALATYFEARACYRADGiNLVGKRPSRTGLGLARLCYELLGENIELAMDAVRHHVTTPALEQTIEATIYLSG 245
Cdd:COG0371  161 rllaaGIGDALAKWYEARDWSLAHR-DLAGEYYTEAAVALARLCAETLLEYGEAAIKAVEAGVVTPALERVVEANLLLSG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283 246 VGAEAGGLAAAH----AVNNGMSVVPDLHRAQHGEKVVFGLLTQLVLERAPQaELDEVMRIIQLAGLPMTLQEMGLSQFV 321
Cdd:COG0371  240 LAMGIGSSRPGSgaahAIHNGLTALPETHHALHGEKVAFGTLVQLVLEGRPE-EIEELLDFLRSVGLPTTLADLGLDDET 318

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 648449283 322 ESEWRQVAKLACDPLDTMGNMPMSVSEQDVYHAMIAA 358
Cdd:COG0371  319 EEELLTVAEAARPERYTILNLPFEVTPEAVEAAILAT 355
GlyDH-like cd08550
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ...
 11-358 9.49e-94

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: 284.04  E-value: 9.49e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  11 PKKFIIGHDLLPQLHDHVKDFGDNALLVSDEFILERVREEALAGLLQAGLKGAVEKFNYECTDIEIRRLCDLAEQQGANV 90
Cdd:cd08550    1 PGRYIQEPGILAKAGEYIAPLGKKALIIGGKTALEAVGEKLEKSLEEAGIDYEVEVFGGECTEENIERLAEKAKEEGADV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  91 IVGIGGGKTLDVAKAVAFYLRRPVVLFPTIASTDAPCTALAVIYNPAGEFERYLFLPQNPDVVIADTAIIAAAPARFFAA 170
Cdd:cd08550   81 IIGIGGGKVLDTAKAVADRLGLPVVTVPTIAATCAAWSALSVLYDEEGEFLGYSLLKRSPDLVLVDTDIIAAAPVRYLAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283 171 GVGDALATYFEARACYRADGINLvgkrPSRTGLGLARLCYELLGENIELAMDAVRHHVTTPALEQTIEATIYL----SGV 246
Cdd:cd08550  161 GIGDTLAKWYEARPSSRGGPDDL----ALQAAVQLAKLAYDLLLEYGVQAVEDVRQGKVTPALEDVVDAIILLaglvGSL 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283 247 GAEAGGLAAAHAVNNGMSVVPDLHRAQHGEKVVFGLLTQLVLERAPQAELDEVMRIIQLAGLPMTLQEMGLSqFVESEWR 326
Cdd:cd08550  237 GGGGCRTAAAHAIHNGLTKLPETHGTLHGEKVAFGLLVQLALEGRSEEEIEELIEFLRRLGLPVTLEDLGLE-LTEEELR 315

                        330       340       350
                 ....*....|....*....|....*....|..
gi 648449283 327 QVAKLACDPLDTMGNMPMSVSEQDVYHAMIAA 358
Cdd:cd08550  316 KIAEYACDPPDMAHMLPFPVTPEMLAEAILAA 347
GlyDH-like cd08172
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ...
 64-357 4.86e-62

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: 202.36  E-value: 4.86e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  64 VEKFNYECTDIEIRRLCDLAEQQGANVIVGIGGGKTLDVAKAVAFYLRRPVVLFPTIASTDAPCTALAVIYNPAGEFERY 143
Cdd:cd08172   52 VLRYDGECSYEEIDRLAEEAKEHQADVIIGIGGGKVLDTAKAVADKLNIPLILIPTLASNCAAWTPLSVIYDEDGEFIGY 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283 144 LFLPQNPDVVIADTAIIAAAPARFFAAGVGDALATYFEARACYRADGINLVGKRPSRTGlglARLCYELLGENIELAMDA 223
Cdd:cd08172  132 DYFPRSAYLVLVDPRLLLDSPKDYFVAGIGDTLAKWYEADAILRQLEELPAFLQLARQA---AKLCRDILLKDSEQALAD 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283 224 VRHHVTTPALEQTIEATIYLSGV----GAEAGGLAAAHAVNNGMSVVPDLHRAQHGEKVVFGLLTQLVLERapqaELDEV 299
Cdd:cd08172  209 LEAGKLTPAFIKVVETIIALAGMvggfGDEYGRSAGAHAIHNGLTKLPETHHFLHGEKVAYGILVQLALEG----KWDEI 284

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648449283 300 MRIIQL---AGLPMTLQEMGLSQFVESEWRQVAKLACDPLDTMGNMPMSVSEQDVYHAMIA 357
Cdd:cd08172  285 KKLLPFyrrLGLPTSLADLGLTDDTEEALQKIAAFAASPEESIHLLPPDVTAEEVLQAIEK 345
GlyDH-like cd08171
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ...
 16-355 9.49e-49

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: 167.70  E-value: 9.49e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  16 IGHDLLPQLHDHVKDFGDNALLVSDEFILERVREEALAGLLQAGLKgAVEKFNY--ECTDIEIRRLCDLAEQQGANVIVG 93
Cdd:cd08171    6 IGEDAYDAIPKICSPYGKKVVVIGGKKALAAAKPKLRAALEGSGLE-ITDFIWYggEATYENVEKLKANPEVQEADMIFA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  94 IGGGKTLDVAKAVAFYLRRPVVLFPTIASTDAPCTALAVIYNPAGEFERYLFLPQNPDVVIADTAIIAAAPARFFAAGVG 173
Cdd:cd08171   85 VGGGKAIDTVKVLADRLNKPVFTFPTIASNCAAVTAVSVMYNPDGSFKEYYFLKRPPVHTFIDTEIIAEAPEKYLWAGIG 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283 174 DALATYFEARACYRADGINLvgkrPSRTGLGLARLCYELLGENIELAMDAVRHHVTTPALEQTIEATI----YLSGVGAE 249
Cdd:cd08171  165 DTLAKYYEVEFSARGDELDH----TNALGVAISKMCSEPLLKYGVQALEDCRANKVSDALEQVVLDIIvttgLVSNLVEP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283 250 AGGLAAAHAVNNGMSVVPDL-HRAQHGEKVVFGLLTQLVLERApQAELDEVMRIIQLAGLPMTLQEMGLSqfvESEWRQV 328
Cdd:cd08171  241 DYNSSLAHALYYGLTTLPQIeEEHLHGEVVSYGVLVLLTVDGQ-FEELEKVYAFNKSIGLPTCLADLGLT---VEDLEKV 316

                        330       340
                 ....*....|....*....|....*..
gi 648449283 329 AKLACDPLDtMGNMPMSVSEQDVYHAM 355
Cdd:cd08171  317 LDKALKTKD-LRHSPYPITKEMFEEAI 342
Fe-ADH pfam00465
Iron-containing alcohol dehydrogenase;
11-351 5.18e-37

Iron-containing alcohol dehydrogenase;


Pssm-ID: 425696 [Multi-domain]  Cd Length: 362  Bit Score: 136.96  E-value: 5.18e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283   11 PKKFIIGHDLLPQLHDHVKDFGDNALLVSDEFILER-VREEALAGLLQAGLKGAV-EKFNYECTDIEIRRLCDLAEQQGA 88
Cdd:pfam00465   1 PTRIVFGAGALAELGEELKRLGARALIVTDPGSLKSgLLDKVLASLEEAGIEVVVfDGVEPEPTLEEVDEAAALAREAGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283   89 NVIVGIGGGKTLDVAKAVAFYL------------------RRPVVLFPTIASTDAPCTALAVIYNPAGEFERYLFLPQ-N 149
Cdd:pfam00465  81 DVIIAVGGGSVIDTAKAIALLLtnpgdvwdylggkpltkpALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFSPKlL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  150 PDVVIADTAIIAAAPARFFAAGVGDALATYFEAracyradginLVGKRPSRTGLGLARLCYELLGENIELAMDAVRHhvt 229
Cdd:pfam00465 161 PDLAILDPELTLTLPPRLTAATGMDALAHAVEA----------YVSKGANPLTDALALEAIRLIAENLPRAVADGED--- 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  230 TPALEQTIEATiYLSGVGAEAGGLAAAHAVNNGMSVVPDL-HRAQHGEKVVFGL----------LTQLVL-------ERA 291
Cdd:pfam00465 228 LEARENMLLAS-TLAGLAFSNAGLGAAHALAHALGGRYGIpHGLANAILLPYVLrfnapaapekLAQLARalgedsdEEA 306

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  292 PQAELDEVMRIIQLAGLPMTLQEMGLSqfvESEWRQVAKLACDPLdTMGNMPMSVSEQDV 351
Cdd:pfam00465 307 AEEAIEALRELLRELGLPTTLSELGVT---EEDLDALAEAALRDR-SLANNPRPLTAEDI 362
DHQ_Fe-ADH cd07766
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ...
 11-333 1.32e-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: 98.59  E-value: 1.32e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  11 PKKFIIGHDLLPQLHDHVKDFGDNALLVSDEFILERVrEEALAGLLQAGLKGAVEKF-NYECTDIEIRRLCDLAEQQGAN 89
Cdd:cd07766    1 PTRIVFGEGAIAKLGEIKRRGFDRALVVSDEGVVKGV-GEKVADSLKKGLAVAIFDFvGENPTFEEVKNAVERARAAEAD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  90 VIVGIGGGKTLDVAKAVAFYLRR--PVVLFPTIASTDAPCTALAVIYNPAGEFERyLFLPQNPDVVIADTAIIAAAPARF 167
Cdd:cd07766   80 AVIAVGGGSTLDTAKAVAALLNRgiPFIIVPTTASTDSEVSPKSVITDKGGKNKQ-VGPHYNPDVVFVDTDITKGLPPRQ 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283 168 FAAGVGDALATYFEaRACYRADGINLVGKRPSRTGLGLarlcyellgenielamdavrHHvttpALEQTIEAtiylsgvg 247
Cdd:cd07766  159 VASGGVDALAHAVE-LEKVVEAATLAGMGLFESPGLGL--------------------AH----AIGHALTA-------- 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283 248 aeagglaaahavnngmsvvpdLHRAQHGEKVVFGLLTQLVLERAPQAELD-EVMRIIQLA---GLPMTLQEMGLSqfvES 323
Cdd:cd07766  206 ---------------------FEGIPHGEAVAVGLPYVLKVANDMNPEPEaAIEAVFKFLedlGLPTHLADLGVS---KE 261

                        330
                 ....*....|
gi 648449283 324 EWRQVAKLAC 333
Cdd:cd07766  262 DIPKLAEKAL 271
Gro1PDH cd08173
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ...
 4-133 6.59e-20

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: 89.53  E-value: 6.59e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283   4 LPRTVtspkkfIIGHDLLPQLHDHVKD--FGDNALLVSDEFILERVREEALAGLLQAGLKGAVEKFNYECTDIEIRRLCD 81
Cdd:cd08173    1 LPRNV------VVGHGAINKIGEVLKKllLGKRALIITGPNTYKIAGKRVEDLLESSGVEVVIVDIATIEEAAEVEKVKK 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 648449283  82 LAEQQGANVIVGIGGGKTLDVAKAVAFYLRRPVVLFPTIASTDAPCTALAVI 133
Cdd:cd08173   75 LIKESKADFIIGVGGGKVIDVAKYAAYKLNLPFISIPTSASHDGIASPFASI 126
PRK10586 PRK10586
putative oxidoreductase; Provisional
 66-349 1.57e-17

putative oxidoreductase; Provisional


Pssm-ID: 182570  Cd Length: 362  Bit Score: 82.85  E-value: 1.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  66 KFNYECTDIEIRRLCDLAEQQgANVIVGIGGGKTLDVAKAVAFYLRRPVVLFPTIASTDAPCTALAVIYNPAGEFERYLF 145
Cdd:PRK10586  66 LFRGHCSESDVAQLAAASGDD-RQVVIGVGGGALLDTAKALARRLGLPFVAIPTIAATCAAWTPLSVWYNDAGQALHFEI 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283 146 LPQNPDVVIADTAIIAAAPARFFAAGVGDALATYFEARacyradginLVGKRPS------RTGLGLARLCYELLGENIEL 219
Cdd:PRK10586 145 FDDANFLVLVEPRIILNAPQEYLLAGIGDTLAKWYEAV---------VLAPQPEtlpltvRLGINNALAIRDVLLNSSEQ 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283 220 AMDAVRHHVTTPALEQTIEATI----YLSGVGAEAGGLAAAHAVNNGMSVVPDLHRAQHGEKVVFGLLTQLVLerapqAE 295
Cdd:PRK10586 216 ALADQQNGQLTQDFCDVVDAIIagggMVGGLGERYTRVAAAHAVHNGLTVLPQTEKFLHGTKVAYGILVQSAL-----LG 290

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 648449283 296 LDEVMRIIQLA----GLPMTLQEMGLSQFVESEWRQVAKLACDPLDTMGNMPMSVSEQ 349
Cdd:PRK10586 291 QDDVLAQLIGAyqrfHLPTTLAELDVDINNQAEIDRVIAHTLRPVESIHYLPVTLTPD 348
G1PDH-like cd08174
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ...
 11-135 8.88e-17

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: 80.26  E-value: 8.88e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  11 PKKFIIGHDLLPQLHDHVKD---FGDNALLVSDEFILERVREEalaglLQAGLKGAVEKFN-YECTDIEIRrlcDLAEQQ 86
Cdd:cd08174    1 PLILKIEEGALEHLGKYLADrnqGFGKVAIVTGEGIDELLGED-----ILESLEEAGEIVTvEENTDNSAE---ELAEKA 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 648449283  87 ----GANVIVGIGGGKTLDVAKAVAFYLRRPVVLFPTIASTDAPCTALAVIYN 135
Cdd:cd08174   73 fslpKVDAIVGIGGGKVLDVAKYAAFLSKLPFISVPTSLSNDGIASPVAVLKV 125
egsA PRK00843
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
 11-124 1.54e-13

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


Pssm-ID: 179139  Cd Length: 350  Bit Score: 71.08  E-value: 1.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  11 PKKFIIGHDLLPQLHDHVKD--FGDNALLVS----DEFILERVREEalagllqagLKGA-------VEKFNYEctdiEIR 77
Cdd:PRK00843  11 PRDVVVGHGVLDDIGDVCSDlkLTGRALIVTgpttKKIAGDRVEEN---------LEDAgdvevviVDEATME----EVE 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 648449283  78 RLCDLAEQQGANVIVGIGGGKTLDVAKAVAFYLRRPVVLFPTIASTD 124
Cdd:PRK00843  78 KVEEKAKDVNAGFLIGVGGGKVIDVAKLAAYRLGIPFISVPTAASHD 124
Fe-ADH cd08551
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ...
 11-137 6.11e-13

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: 69.40  E-value: 6.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  11 PKKFIIGHDLLPQLHDHVKDFG-DNALLVSDEFILER-VREEALAGLLQAGLkgAVEKFNY---ECTDIEIRRLCDLAEQ 85
Cdd:cd08551    1 PTRIVFGAGALARLGEELKALGgKKVLLVTDPGLVKAgLLDKVLESLKAAGI--EVEVFDDvepNPTVETVEAAAELARE 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  86 QGANVIVGIGGGKTLDVAKAVAFYL------------------RRPVVLFPTIASTDAPCTALAVIYNPA 137
Cdd:cd08551   79 EGADLVIAVGGGSVLDTAKAIAVLAtnggsirdyegigkvpkpGLPLIAIPTTAGTGSEVTPNAVITDPE 148
Fe-ADH_2 pfam13685
Iron-containing alcohol dehydrogenase;
15-134 8.21e-13

Iron-containing alcohol dehydrogenase;


Pssm-ID: 404557 [Multi-domain]  Cd Length: 251  Bit Score: 67.71  E-value: 8.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283   15 IIGHDLLPQLHDHVKDFG-DNALLVSDEFIlervrEEALAGLLQAGLKGA------VEKFNYECTDIEIRRLCDLAEQQG 87
Cdd:pfam13685   1 VIGPGALGRLGEYLAELGfRRVALVADANT-----YAAAGRKVAESLKRAgievetRLEVAGNADMETAEKLVGALRERD 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 648449283   88 ANVIVGIGGGKTLDVAKAVAFYLRRPVVLFPTIASTDAPCTALAVIY 134
Cdd:pfam13685  76 ADAVVGVGGGTVIDLAKYAAFKLGKPFISVPTAASNDGFASPGASLT 122
Fe-ADH-like cd08183
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 11-137 4.31e-11

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: 63.67  E-value: 4.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  11 PKKFIIGHDLLPQLHDHVKDFGDNALLV--SDEFILERVrEEALAGLLQAGLKGAVEKFNYECTDIEIRRLCDLAEQQGA 88
Cdd:cd08183    1 PPRIVFGRGSLQELGELAAELGKRALLVtgRSSLRSGRL-ARLLEALEAAGIEVALFSVSGEPTVETVDAAVALAREAGC 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648449283  89 NVIVGIGGGKTLDVAKAVAF----------YL------------RRPVVLFPTIASTDAPCTALAVIYNPA 137
Cdd:cd08183   80 DVVIAIGGGSVIDAAKAIAAlltnegsvldYLevvgkgrpltepPLPFIAIPTTAGTGSEVTKNAVLSSPE 150
Fe-ADH-like cd08196
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 11-137 1.93e-10

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: 61.44  E-value: 1.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  11 PKKFIIGHDLLPQLHDHVKD-FGDNALLVSDEFilerVREEALAGLLQAGLKGA----VEKFNYECTDIEIRRLCDLAEQ 85
Cdd:cd08196    6 PVKIIFGEGILKELPDIIKElGGKRGLLVTDPS----FIKSGLAKRIVESLKGRivavFSDVEPNPTVENVDKCARLARE 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648449283  86 QGANVIVGIGGGKTLDVAKAVAF----------YL---------RRPVVLFPTIASTDAPCTALAVIYNPA 137
Cdd:cd08196   82 NGADFVIAIGGGSVLDTAKAAAClaktdgsiedYLegkkkipkkGLPLIAIPTTAGTGSEVTPVAVLTDKE 152
Fe-ADH-like cd08191
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 10-137 2.68e-10

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: 61.48  E-value: 2.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  10 SPKKFIIGHDLLPQLHDHVKDFGDNALLVSDEFILE-RVREEALAGLLQAGLkgAVEKFNYECTD---IEIRRLCDLAEQ 85
Cdd:cd08191    3 SPSRLLFGPGARRALGRVAARLGSRVLIVTDPRLAStPLVAELLAALTAAGV--AVEVFDGGQPElpvSTVADAAAAARA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  86 QGANVIVGIGGGKTLDVAKAVAFYLRR------------------PVVLFPTIASTDAPCTALAVIYNPA 137
Cdd:cd08191   81 FDPDVVIGLGGGSNMDLAKVVALLLAHggdprdyygedrvpgpvlPLIAVPTTAGTGSEVTPVAVLTDPA 150
EutG COG1454
Alcohol dehydrogenase, class IV [Energy production and conversion];
7-137 3.58e-10

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


Pssm-ID: 441063 [Multi-domain]  Cd Length: 381  Bit Score: 60.90  E-value: 3.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283   7 TVTSPKKFIIGHDLLPQLHDHVKDFG-DNALLVSDEFILER-VREEALAGLLQAGLKGAVekFNY---ECTDIEIRRLCD 81
Cdd:COG1454    4 TFRLPTRIVFGAGALAELGEELKRLGaKRALIVTDPGLAKLgLLDRVLDALEAAGIEVVV--FDDvepNPTVETVEAGAA 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648449283  82 LAEQQGANVIVGIGGGKTLDVAKAVAFYLRR------------------PVVLFPTIASTDAPCTALAVIYNPA 137
Cdd:COG1454   82 AAREFGADVVIALGGGSAIDAAKAIALLATNpgdledylgikkvpgpplPLIAIPTTAGTGSEVTPFAVITDPE 155
Fe-ADH-like cd08194
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 11-133 1.81e-09

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: 58.70  E-value: 1.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  11 PKKFIIGHDLLPQLHDHVKD-FGDNALLVSDEFILERVR-EEALAGLLQAGLKGAV-EKFNYECTDIEIRRLCDLAEQQG 87
Cdd:cd08194    1 PRTIIIGGGALEELGEEAASlGGKRALIVTDKVMVKLGLvDKVTQLLAEAGIAYAVfDDVVSEPTDEMVEEGLALYKEGG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648449283  88 ANVIVGIGGGKTLDVAKAVAF------YLRR------------PVVLFPTIASTDAPCTALAVI 133
Cdd:cd08194   81 CDFIVALGGGSPIDTAKAIAVlatnggPIRDymgprkvdkpglPLIAIPTTAGTGSEVTRFTVI 144
Fe-ADH-like cd14863
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 15-137 2.04e-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: 341485 [Multi-domain]  Cd Length: 380  Bit Score: 58.70  E-value: 2.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  15 IIGHDLLPQLHDHVKDFG-DNALLVSDEFILER-VREEALAGLLQAGLKGAV-EKFNYECTDIEIRRLCDLAEQQGANVI 91
Cdd:cd14863    9 IFGAGAVEQIGELLKELGcKKVLLVTDKGLKKAgIVDKIIDLLEEAGIEVVVfDDVEPDPPDEIVDEAAEIAREEGADGV 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648449283  92 VGIGGGKTLDVAKAVA-----------FYLRR--------PVVLFPTIASTDAPCTALAVIYNPA 137
Cdd:cd14863   89 IGIGGGSVLDTAKAIAvlltnpgpiidYALAGppvpkpgiPLIAIPTTAGTGSEVTPIAVITDEE 153
Fe-ADH-like cd08185
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 11-137 1.20e-08

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: 55.97  E-value: 1.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  11 PKKFIIGHDLLPQLHDHVKDFGDNALLVSDEfilervREEALAGLL---QAGLKGA-VEKFNYEC-----TDIEIRRLCD 81
Cdd:cd08185    4 PTRILFGAGKLNELGEEALRPGKKALIVTGK------GSSKKTGLLdrvKKLLEKAgVEVVVFDKvepnpLTTTVMEGAA 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648449283  82 LAEQQGANVIVGIGGGKTLDVAKAVAF----------YLR------------RPVVLFPTIASTDAPCTALAVIYNPA 137
Cdd:cd08185   78 LAKEEGCDFVIGLGGGSSMDAAKAIAFmatnpgdiwdYIFggtgkgpppekaLPIIAIPTTAGTGSEVDPWAVITNPE 155
HEPD cd08182
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ...
 11-134 1.26e-08

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: 56.08  E-value: 1.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  11 PKKFIIGHDLLPQLHDHVKDFGDN--ALLVSDEFILERVREEALAGLLQAGLKGAVEKF--NyecTDIE-IRRLCDLAEQ 85
Cdd:cd08182    1 PVKIIFGPGALAELKDLLGGLGARrvLLVTGPSAVRESGAADILDALGGRIPVVVFSDFspN---PDLEdLERGIELFRE 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648449283  86 QGANVIVGIGGGKTLDVAKAVAFYL--------------------RRPVVLFPTIASTDAPCTALAVIY 134
Cdd:cd08182   78 SGPDVIIAVGGGSVIDTAKAIAALLgspgenllllrtgekapeenALPLIAIPTTAGTGSEVTPFATIW 146
Fe-ADH-like cd14864
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 11-134 1.41e-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: 341486 [Multi-domain]  Cd Length: 376  Bit Score: 55.77  E-value: 1.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  11 PKKFIIGHDLLPQLHDHVKDFGDNALLVSDefilervREEALAGLLQAgLKGAVEKFNYEC----------TDIEIRRLC 80
Cdd:cd14864    4 PPNIVFGADSLERIGEEVKEYGSRFLLITD-------PVLKESGLADK-IVSSLEKAGISVivfdeipasaTSDTIDEAA 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648449283  81 DLAEQQGANVIVGIGGGKTLDVAKAVA-----------FYLRR-------PVVLFPTIASTDAPCTALAVIY 134
Cdd:cd14864   76 ELARKAGADGIIAVGGGKVLDTAKAVAilanndggaydFLEGAkpkkkplPLIAVPTTPRSGFEFSDRFPVV 147
PPD-like cd08181
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ...
 10-137 1.45e-08

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: 55.67  E-value: 1.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  10 SPKKFIIGHDLLPQLHDHVKDFGDNALLVSDefilervREEALA-GLLQAgLKGAVEKFNYECT---DIE-------IRR 78
Cdd:cd08181    3 MPTKVYFGKNCVEKHADELAALGKKALIVTG-------KHSAKKnGSLDD-VTEALEENGIEYFifdEVEenpsietVEK 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648449283  79 LCDLAEQQGANVIVGIGGGKTLDVAKAVAFYLRR-----------------PVVLFPTIASTDAPCTALAVIYNPA 137
Cdd:cd08181   75 GAELARKEGADFVIGIGGGSPLDAAKAIALLAANkdgdedlfqngkynpplPIVAIPTTAGTGSEVTPYSILTDHE 150
BDH cd08187
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ...
 10-138 3.99e-08

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: 54.36  E-value: 3.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  10 SPKKFIIGHDLLPQLHDHVKDFGDNALLV-SDEFI-----LERVREEalagllqagLKGAVEKFnYECTDIE-------I 76
Cdd:cd08187    6 NPTKIIFGKGAIEELGEEIKKYGKKVLLVyGGGSIkknglYDRVVAS---------LKEAGIEV-VEFGGVEpnprletV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  77 RRLCDLAEQQGANVIVGIGGGKTLDVAKAVA-----------FYLRR-------PVVLFPTIASTDAPCTALAVIYNPAG 138
Cdd:cd08187   76 REGIELAREENVDFILAVGGGSVIDAAKAIAagakydgdvwdFFTGKappekalPVGTVLTLAATGSEMNGGAVITNEET 155
HVD cd08193
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ...
 23-139 1.57e-07

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: 52.51  E-value: 1.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  23 QLHDHVKDFG-DNALLVSDEFILER-VREEALAGLLQAGLkgAVEKFnyecTDIE-------IRRLCDLAEQQGANVIVG 93
Cdd:cd08193   16 RLGELLRELGaRRVLLVTDPGLVKAgLADPALAALEAAGI--AVTVF----DDVVadppeavVEAAVEQAREAGADGVIG 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648449283  94 IGGGKTLDVAKAVAFYL------------------RRPVVLFPTIASTDAPCTALAVIYNPAGE 139
Cdd:cd08193   90 FGGGSSMDVAKLVALLAgsdqplddiygvgkatgpRLPLILVPTTAGTGSEVTPISIVTTGETE 153
Fe-ADH-like cd08189
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 15-137 7.96e-07

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: 50.54  E-value: 7.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  15 IIGHDLLPQLHDHVKDFG-DNALLVSDEFILER-VREEALAGLLQAGLKGAVekFN-------YECTDiEIRRLCdlaEQ 85
Cdd:cd08189    9 FEGAGSLLQLPEALKKLGiKRVLIVTDKGLVKLgLLDPLLDALKKAGIEYVV--FDgvvpdptIDNVE-EGLALY---KE 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648449283  86 QGANVIVGIGGGKTLDVAKAVA----------------FYLRRPVVLF---PTIASTDAPCTALAVIYNPA 137
Cdd:cd08189   83 NGCDAIIAIGGGSVIDCAKVIAaraanpkksvrklkglLKVRKKLPPLiavPTTAGTGSEATIAAVITDPE 153
Fe-ADH-like cd14865
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 10-137 1.86e-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: 341487 [Multi-domain]  Cd Length: 383  Bit Score: 49.46  E-value: 1.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  10 SPKKFIIGHDLLPQLHDHVKDFG-DNALLVSDEfileRVREEALAGLLQAGLKGAvekfnYECTDIE-----------IR 77
Cdd:cd14865    5 NPTKIVSGAGALENLPAELARLGaRRPLIVTDK----GLAAAGLLKKVEDALGDA-----IEIVGVFddvppdssvavVN 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648449283  78 RLCDLAEQQGANVIVGIGGGKTLDVAKAV----------------AFYLRRPVVLF---PTIASTDAPCTALAVIYNPA 137
Cdd:cd14865   76 EAAARAREAGADGIIAVGGGSVIDTAKGVnillseggddlddyggANRLTRPLKPLiaiPTTAGTGSEVTLVAVIKDEE 154
G1PDH_related cd08549
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ...
 31-179 1.52e-05

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: 46.40  E-value: 1.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  31 FGDNALLVSDEfILERVREEALAGLLQAGLKGAVEKFNYEC--------TDIEIRRLCD-LAEQQGANVIVGIGGGKTLD 101
Cdd:cd08549    6 VGDGAINKIEE-ILKKLNLKRVLIITGKNTKAKYCRFFYDQlktvcdivYYDNIDNLEDeLKKYTFYDCVIGIGGGRSID 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648449283 102 VAKAVAFYLRRPVVLFPTIASTDAPCTALAVIYNPAgefERYLFLPQNPDVVIADTAIIAAAPARFFAAGVGDALATY 179
Cdd:cd08549   85 TGKYLAYKLKIPFISVPTSASNDGIASPIVSLRIPG---VKKTFMADAPIAIIADTEIIKKSPRRLLSAGIGDLVSNI 159
Fe-ADH_KdnB-like cd08184
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ...
 90-136 2.79e-05

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: 45.72  E-value: 2.79e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648449283  90 VIVGIGGGKTLDVAKAVAFYLRRP------------------VVLFPTIASTDAPCTALAVIYNP 136
Cdd:cd08184   85 AVVGIGGGSTMDIAKAVSNMLTNPgsaadyqgwdlvknpgiyKIGVPTLSGTGAEASRTAVLTGP 149
Fe-ADH-like cd14862
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 10-133 4.31e-05

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: 44.91  E-value: 4.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  10 SPKKFIIGHDLLPQLHDHVkdfGDNALLVSDEFILE-RVREEALAGLLQAGLKGAVekFNyectDIE-------IRRLCD 81
Cdd:cd14862    5 SSPKIVFGEDALSHLEQLS---GKRALIVTDKVLVKlGLLKKVLKRLLQAGFEVEV--FD----EVEpeppletVLKGAE 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648449283  82 LAEQQGANVIVGIGGGKTLDVAKAVAFYLRRPV--------------------VLFPTIASTDAPCTALAVI 133
Cdd:cd14862   76 AMREFEPDLIIALGGGSVMDAAKAAWVLYERPDldpedispldllglrkkaklIAIPTTSGTGSEATWAIVL 147
G1PDH cd08175
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ...
 12-133 6.55e-05

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: 44.42  E-value: 6.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  12 KKFIIGHDLLPQLHDHVKDF--GDNALLVSDEFIlervreEALAGL-LQAGLKGAVEKFNYECTDIEIRRLCD------- 81
Cdd:cd08175    2 KEIVIGEGALKKLPEYLKELfgGKKVLVVADENT------YAAAGEeVEAALEEAGVTVCLLIFPGEGDLIADeaavgkv 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 648449283  82 -LAEQQGANVIVGIGGGkTL-DVAKAVAFYLRRPVVLFPTIASTDAPCTALAVI 133
Cdd:cd08175   76 lLELEKDTDLIIAVGSG-TInDLTKYAAYKLGIPYISVPTAPSMDGYTSSGAPI 128
PDDH cd08188
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ...
 6-107 2.57e-04

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: 42.50  E-value: 2.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283   6 RTVTSPKKFIIGHDLLPQLHDHVKDFG-DNALLVSDEF-----ILERVreeaLAGLLQAGLKGAV-EKFNYECTDIEIRR 78
Cdd:cd08188    1 FRFYIPPVNLFGPGCLKEIGDELKKLGgKKALIVTDKGlvklgLVKKV----TDVLEEAGIEYVIfDGVQPNPTVTNVNE 76

                         90       100
                 ....*....|....*....|....*....
gi 648449283  79 LCDLAEQQGANVIVGIGGGKTLDVAKAVA 107
Cdd:cd08188   77 GLELFKENGCDFIISVGGGSAHDCAKAIG 105
HOT cd08190
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ...
 34-132 5.02e-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: 41.76  E-value: 5.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  34 NALLVSDEFI-----LERVREealaGLLQAGLKgaVEKFNY---ECTDIEIRRLCDLAEQQGANVIVGIGGGKTLDVAKA 105
Cdd:cd08190   25 KVLVVTDPGLaklglVERVLE----SLEKAGIE--VVVYDGvrvEPTDESFEEAIEFAKEGDFDAFVAVGGGSVIDTAKA 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 648449283 106 VAFYLR-----------------------RPVVLFPTIASTDAPCTALAV 132
Cdd:cd08190   99 ANLYAThpgdfldyvnapigkgkpvpgplKPLIAIPTTAGTGSETTGVAI 148
Fe-ADH-like cd17814
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 14-107 2.61e-03

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: 39.45  E-value: 2.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  14 FIIGHDLLPQLHDHVKDFG-DNALLVSDEfilervreealaGLLQAGLKGAVEK------FNYEC--------TDIEIRR 78
Cdd:cd17814    7 FIFGVGARKLAGRYAKNLGaRKVLVVTDP------------GVIKAGWVDEVLDsleaegLEYVVfsdvtpnpRDFEVME 74

                         90       100
                 ....*....|....*....|....*....
gi 648449283  79 LCDLAEQQGANVIVGIGGGKTLDVAKAVA 107
Cdd:cd17814   75 GAELYREEGCDGIVAVGGGSPIDCAKGIG 103
DHQS cd08195
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ...
 15-119 7.73e-03

Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway for aromatic compounds synthesis; 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, which involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds, is found in bacteria, microbial eukaryotes, and plants, but not in mammals. Therefore, enzymes of this pathway are attractive targets for the development of non-toxic antimicrobial compounds, herbicides and anti-parasitic agents. The activity of DHQS requires nicotinamide adenine dinucleotide (NAD) as cofactor. A single active site in DHQS catalyzes five sequential reactions involving alcohol oxidation, phosphate elimination, carbonyl reduction, ring opening, and intramolecular aldol condensation. The binding of substrates and ligands induces domain conformational changes. In some fungi and protozoa, this domain is fused with the other four domains in shikimate pathway and forms a penta-domain AROM protein, which catalyzes steps 2-6 in the shikimate pathway.


Pssm-ID: 341474  Cd Length: 343  Bit Score: 37.81  E-value: 7.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648449283  15 IIGHDLLPQLHDHVKDF-GDNALLVSDEFILERVREEALAGLLQAGLKGAV------EKF-NYEctdiEIRRLCDLAEQQ 86
Cdd:cd08195    5 LIGSGLLDKLGELLELKkGSKVVIVTDENVAKLYGELLLKSLEAAGFKVEVivipagEKSkSLE----TVERIYDFLLEA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 648449283  87 GAN---VIVGIGGGKTLDVAkavAF----YLRR-PVVLFPT 119
Cdd:cd08195   81 GLDrdsLLIALGGGVVGDLA---GFvastYMRGiPFIQVPT 118
 
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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