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Conserved domains on  [gi|1889614189|ref|WP_182716864|]
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zinc-binding dehydrogenase [Pseudoalteromonas sp. SG45-2]

Protein Classification

zinc-binding dehydrogenase( domain architecture ID 10169636)

zinc-binding dehydrogenase belonging to the medium chain dehydrogenase/reductase (MDR) family

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
16-340 1.33e-128

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


:

Pssm-ID: 176232 [Multi-domain]  Cd Length: 325  Bit Score: 370.84  E-value: 1.33e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNEAIDLADAELPVPDCADNELLVKVEYVGLNPVDGQFAKTGFCKWQYPHILGLDAVGVVVKANKGVFPN-V 94
Cdd:cd08271     1 MKAWVLPKPGAALQLTLEEIEIPGPGAGEVLVKVHAAGLNPVDWKVIAWGPPAWSYPHVPGVDGAGVVVAVGAKVTGWkV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  95 GQRVMWHANIGEQGALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISL-DKIGISEGDTIFIEGGAGAVGQFAIQ 173
Cdd:cd08271    81 GDRVAYHASLARGGSFAEYTVVDARAVLPLPDSLSFEEAAALPCAGLTAYQALfKKLRIEAGRTILITGGAGGVGSFAVQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 174 YAKQRGADVFTTASKRNHKLVKQLGADVVFDYSDKKLCEKIRRELGPQGFDAVIDTIGGECTQRNIELMRFCGRIACLNP 253
Cdd:cd08271   161 LAKRAGLRVITTCSKRNFEYVKSLGADHVIDYNDEDVCERIKEITGGRGVDAVLDTVGGETAAALAPTLAFNGHLVCIQG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 254 LPYFDQDLMYHRAPNISVVSIGGAWLANSLCAQQRLSFMGNLLLEGAVSGDIKHPEITPVDFsaESVSQALNKQLAGGFT 333
Cdd:cd08271   241 RPDASPDPPFTRALSVHEVALGAAHDHGDPAAWQDLRYAGEELLELLAAGKLEPLVIEVLPF--EQLPEALRALKDRHTR 318

                  ....*..
gi 1889614189 334 GKQVVKV 340
Cdd:cd08271   319 GKIVVTI 325
 
Name Accession Description Interval E-value
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
16-340 1.33e-128

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176232 [Multi-domain]  Cd Length: 325  Bit Score: 370.84  E-value: 1.33e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNEAIDLADAELPVPDCADNELLVKVEYVGLNPVDGQFAKTGFCKWQYPHILGLDAVGVVVKANKGVFPN-V 94
Cdd:cd08271     1 MKAWVLPKPGAALQLTLEEIEIPGPGAGEVLVKVHAAGLNPVDWKVIAWGPPAWSYPHVPGVDGAGVVVAVGAKVTGWkV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  95 GQRVMWHANIGEQGALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISL-DKIGISEGDTIFIEGGAGAVGQFAIQ 173
Cdd:cd08271    81 GDRVAYHASLARGGSFAEYTVVDARAVLPLPDSLSFEEAAALPCAGLTAYQALfKKLRIEAGRTILITGGAGGVGSFAVQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 174 YAKQRGADVFTTASKRNHKLVKQLGADVVFDYSDKKLCEKIRRELGPQGFDAVIDTIGGECTQRNIELMRFCGRIACLNP 253
Cdd:cd08271   161 LAKRAGLRVITTCSKRNFEYVKSLGADHVIDYNDEDVCERIKEITGGRGVDAVLDTVGGETAAALAPTLAFNGHLVCIQG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 254 LPYFDQDLMYHRAPNISVVSIGGAWLANSLCAQQRLSFMGNLLLEGAVSGDIKHPEITPVDFsaESVSQALNKQLAGGFT 333
Cdd:cd08271   241 RPDASPDPPFTRALSVHEVALGAAHDHGDPAAWQDLRYAGEELLELLAAGKLEPLVIEVLPF--EQLPEALRALKDRHTR 318

                  ....*..
gi 1889614189 334 GKQVVKV 340
Cdd:cd08271   319 GKIVVTI 325
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
16-341 7.05e-75

NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and conversion, General function prediction only];


Pssm-ID: 440369 [Multi-domain]  Cd Length: 322  Bit Score: 233.50  E-value: 7.05e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNEAIDLADAELPVPDCADNELLVKVEYVGLNPVDGQFAK-TGFCKWQYPHILGLDAVGVVVKANKGVFP-N 93
Cdd:COG0604     1 MKAIVITEFGGPEVLELEEVPVPEPGPGEVLVRVKAAGVNPADLLIRRgLYPLPPGLPFIPGSDAAGVVVAVGEGVTGfK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  94 VGQRVMWHaniGEQGALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISL-DKIGISEGDTIFIEGGAGAVGQFAI 172
Cdd:COG0604    81 VGDRVAGL---GRGGGYAEYVVVPADQLVPLPDGLSFEEAAALPLAGLTAWQALfDRGRLKPGETVLVHGAAGGVGSAAV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 173 QYAKQRGADVFTTASK-RNHKLVKQLGADVVFDYSDKKLCEKIRRELGPQGFDAVIDTIGGECTQRNIELMRFCGRIACL 251
Cdd:COG0604   158 QLAKALGARVIATASSpEKAELLRALGADHVIDYREEDFAERVRALTGGRGVDVVLDTVGGDTLARSLRALAPGGRLVSI 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 252 ----NPLPYFDQDLMYHRApnisvVSIGGAWLANSLCAQQR--LSFMGNLLLEGAVsgdikHPEITPVdFSAESVSQALN 325
Cdd:COG0604   238 gaasGAPPPLDLAPLLLKG-----LTLTGFTLFARDPAERRaaLAELARLLAAGKL-----RPVIDRV-FPLEEAAEAHR 306
                         330
                  ....*....|....*.
gi 1889614189 326 KQLAGGFTGKQVVKVA 341
Cdd:COG0604   307 LLESGKHRGKVVLTVD 322
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
47-338 2.33e-32

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 122.11  E-value: 2.33e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189   47 VKVEYVGLNPVDGQFAkTGfckwQYP--HILGLDAVGVVVKANKGV--FpNVGQRVMWHAnigeQGALSEYTKVPNFAVS 122
Cdd:smart00829   1 IEVRAAGLNFRDVLIA-LG----LYPgeAVLGGECAGVVTRVGPGVtgL-AVGDRVMGLA----PGAFATRVVTDARLVV 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  123 VVPSGLNPGIAATLPCAGMAALISLDKIG-ISEGDTIFIEGGAGAVGQFAIQYAKQRGADVFTTA-SKRNHKLVKQLG-- 198
Cdd:smart00829  71 PIPDGWSFEEAATVPVVFLTAYYALVDLArLRPGESVLIHAAAGGVGQAAIQLARHLGAEVFATAgSPEKRDFLRALGip 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  199 ADVVFDYSDKKLCEKIRRELGPQGFDAVIDTIGGECTQRNIELMRFCGRIACL--------NPLPyfdqdlMYHRAPNIS 270
Cdd:smart00829 151 DDHIFSSRDLSFADEILRATGGRGVDVVLNSLSGEFLDASLRCLAPGGRFVEIgkrdirdnSQLA------MAPFRPNVS 224
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889614189  271 VVSIggawLANSLCAQ-QRLSFMGNLLLEGAVSGDIKHPEITPvdFSAESVSQALNKQLAGGFTGKQVV 338
Cdd:smart00829 225 YHAV----DLDALEEGpDRIRELLAEVLELFAEGVLRPLPVTV--FPISDAEDAFRYMQQGKHIGKVVL 287
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
16-249 1.77e-25

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 104.35  E-value: 1.77e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNEAIDLADAELPVPdcADNELLVKVEYVGLNPVDgQFAKTGFC-KWQYPHILGLDAVGVVVKANKGV--Fp 92
Cdd:PRK13771    1 MKAVILPGFKQGYRIEEVPDPKP--GKDEVVIKVNYAGLCYRD-LLQLQGFYpRMKYPVILGHEVVGTVEEVGENVkgF- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  93 NVGQRV--MWHANIGE----------------------QGALSEYTKVPNFAVSVVPSGLNPGIAATLPCagMAALI--S 146
Cdd:PRK13771   77 KPGDRVasLLYAPDGTceycrsgeeaycknrlgygeelDGFFAEYAKVKVTSLVKVPPNVSDEGAVIVPC--VTGMVyrG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 147 LDKIGISEGDTIFIEGGAGAVGQFAIQYAKQRGADVF-TTASKRNHKLVKQLGADVVfdySDKKLCEKIRReLGpqGFDA 225
Cdd:PRK13771  155 LRRAGVKKGETVLVTGAGGGVGIHAIQVAKALGAKVIaVTSSESKAKIVSKYADYVI---VGSKFSEEVKK-IG--GADI 228
                         250       260
                  ....*....|....*....|....
gi 1889614189 226 VIDTIGGECTQRNIELMRFCGRIA 249
Cdd:PRK13771  229 VIETVGTPTLEESLRSLNMGGKII 252
adh_fam_1 TIGR02817
zinc-binding alcohol dehydrogenase family protein; Members of this model form a distinct ...
22-258 4.24e-25

zinc-binding alcohol dehydrogenase family protein; Members of this model form a distinct subset of the larger family of oxidoreductases that includes zinc-binding alcohol dehydrogenases and NADPH:quinone reductases (pfam00107). While some current members of this family carry designations as putative alginate lyase, it seems no sequence with a direct characterization as such is detected by this model. [Energy metabolism, Fermentation]


Pssm-ID: 274313 [Multi-domain]  Cd Length: 336  Bit Score: 103.66  E-value: 4.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  22 PEPNEAID-LADAELPVPDCADNELLVKVEYVGLNPVDGQFAKTGFCKWQYPHILGLDAVGVVVKANKGV--FpNVGQRV 98
Cdd:TIGR02817   8 PLPITDPDaLVDIDLPKPKPGGRDLLVEVKAISVNPVDTKVRARMAPEAGQPKILGWDAAGVVVAVGDEVtlF-KPGDEV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  99 MWHANIGEQGALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISL-DKIGISEG-----DTIFIEGGAGAVGQFAI 172
Cdd:TIGR02817  87 WYAGDIDRPGSNAEFHLVDERIVGHKPKSLSFAEAAALPLTSITAWELLfDRLGINDPvagdkRALLIIGGAGGVGSILI 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 173 QYAKQ-RGADVFTTASK-RNHKLVKQLGADVVFDYSdKKLCEKIRReLGPQGFDAVIDTiggecTQRN------IELMRF 244
Cdd:TIGR02817 167 QLARQlTGLTVIATASRpESQEWVLELGAHHVIDHS-KPLKAQLEK-LGLEAVSYVFSL-----THTDqhfkeiVELLAP 239
                         250
                  ....*....|....
gi 1889614189 245 CGRIACLNPLPYFD 258
Cdd:TIGR02817 240 QGRFALIDDPAELD 253
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
166-278 3.78e-19

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 82.27  E-value: 3.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 166 AVGQFAIQYAKQRGADVFTTA-SKRNHKLVKQLGADVVFDYSDKKLCEKIRRELGPQGFDAVIDTIG-GECTQRNIELMR 243
Cdd:pfam00107   1 GVGLAAIQLAKAAGAKVIAVDgSEEKLELAKELGADHVINPKETDLVEEIKELTGGKGVDVVFDCVGsPATLEQALKLLR 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1889614189 244 FCGRIACL----NPLPYFDQDLMYHrapNISVV-SIGGAW 278
Cdd:pfam00107  81 PGGRVVVVglpgGPLPLPLAPLLLK---ELTILgSFLGSP 117
 
Name Accession Description Interval E-value
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
16-340 1.33e-128

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176232 [Multi-domain]  Cd Length: 325  Bit Score: 370.84  E-value: 1.33e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNEAIDLADAELPVPDCADNELLVKVEYVGLNPVDGQFAKTGFCKWQYPHILGLDAVGVVVKANKGVFPN-V 94
Cdd:cd08271     1 MKAWVLPKPGAALQLTLEEIEIPGPGAGEVLVKVHAAGLNPVDWKVIAWGPPAWSYPHVPGVDGAGVVVAVGAKVTGWkV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  95 GQRVMWHANIGEQGALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISL-DKIGISEGDTIFIEGGAGAVGQFAIQ 173
Cdd:cd08271    81 GDRVAYHASLARGGSFAEYTVVDARAVLPLPDSLSFEEAAALPCAGLTAYQALfKKLRIEAGRTILITGGAGGVGSFAVQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 174 YAKQRGADVFTTASKRNHKLVKQLGADVVFDYSDKKLCEKIRRELGPQGFDAVIDTIGGECTQRNIELMRFCGRIACLNP 253
Cdd:cd08271   161 LAKRAGLRVITTCSKRNFEYVKSLGADHVIDYNDEDVCERIKEITGGRGVDAVLDTVGGETAAALAPTLAFNGHLVCIQG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 254 LPYFDQDLMYHRAPNISVVSIGGAWLANSLCAQQRLSFMGNLLLEGAVSGDIKHPEITPVDFsaESVSQALNKQLAGGFT 333
Cdd:cd08271   241 RPDASPDPPFTRALSVHEVALGAAHDHGDPAAWQDLRYAGEELLELLAAGKLEPLVIEVLPF--EQLPEALRALKDRHTR 318

                  ....*..
gi 1889614189 334 GKQVVKV 340
Cdd:cd08271   319 GKIVVTI 325
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
16-341 7.05e-75

NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and conversion, General function prediction only];


Pssm-ID: 440369 [Multi-domain]  Cd Length: 322  Bit Score: 233.50  E-value: 7.05e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNEAIDLADAELPVPDCADNELLVKVEYVGLNPVDGQFAK-TGFCKWQYPHILGLDAVGVVVKANKGVFP-N 93
Cdd:COG0604     1 MKAIVITEFGGPEVLELEEVPVPEPGPGEVLVRVKAAGVNPADLLIRRgLYPLPPGLPFIPGSDAAGVVVAVGEGVTGfK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  94 VGQRVMWHaniGEQGALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISL-DKIGISEGDTIFIEGGAGAVGQFAI 172
Cdd:COG0604    81 VGDRVAGL---GRGGGYAEYVVVPADQLVPLPDGLSFEEAAALPLAGLTAWQALfDRGRLKPGETVLVHGAAGGVGSAAV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 173 QYAKQRGADVFTTASK-RNHKLVKQLGADVVFDYSDKKLCEKIRRELGPQGFDAVIDTIGGECTQRNIELMRFCGRIACL 251
Cdd:COG0604   158 QLAKALGARVIATASSpEKAELLRALGADHVIDYREEDFAERVRALTGGRGVDVVLDTVGGDTLARSLRALAPGGRLVSI 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 252 ----NPLPYFDQDLMYHRApnisvVSIGGAWLANSLCAQQR--LSFMGNLLLEGAVsgdikHPEITPVdFSAESVSQALN 325
Cdd:COG0604   238 gaasGAPPPLDLAPLLLKG-----LTLTGFTLFARDPAERRaaLAELARLLAAGKL-----RPVIDRV-FPLEEAAEAHR 306
                         330
                  ....*....|....*.
gi 1889614189 326 KQLAGGFTGKQVVKVA 341
Cdd:COG0604   307 LLESGKHRGKVVLTVD 322
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
16-338 7.00e-68

alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; Members identified as zinc-dependent alcohol dehydrogenases and quinone oxidoreductase. QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176191 [Multi-domain]  Cd Length: 309  Bit Score: 215.12  E-value: 7.00e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNEAIDLADAELPVPDCADNELLVKVEYVGLNPVDGQFAKTGFC---KWQYPHILGLDAVGVVVKANKGVFP 92
Cdd:cd05289     1 MKAVRIHEYGGPEVLELADVPTPEPGPGEVLVKVHAAGVNPVDLKIREGLLKaafPLTLPLIPGHDVAGVVVAVGPGVTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  93 -NVGQRVMWHANIGEQGALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISLDKIG-ISEGDTIFIEGGAGAVGQF 170
Cdd:cd05289    81 fKVGDEVFGMTPFTRGGAYAEYVVVPADELALKPANLSFEEAAALPLAGLTAWQALFELGgLKAGQTVLIHGAAGGVGSF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 171 AIQYAKQRGADVFTTASKRNHKLVKQLGADVVFDYSDkklcEKIRRELGPQGFDAVIDTIGGECTQRNIELMRFCGRIAC 250
Cdd:cd05289   161 AVQLAKARGARVIATASAANADFLRSLGADEVIDYTK----GDFERAAAPGGVDAVLDTVGGETLARSLALVKPGGRLVS 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 251 LNPLPYFDQDLMYHRAPNISV-VSIGGAwlanslcaqqRLSFMGNLLLEGAVsgdikHPEITPVdFSAESVSQALNKQLA 329
Cdd:cd05289   237 IAGPPPAEQAAKRRGVRAGFVfVEPDGE----------QLAELAELVEAGKL-----RPVVDRV-FPLEDAAEAHERLES 300

                  ....*....
gi 1889614189 330 GGFTGKQVV 338
Cdd:cd05289   301 GHARGKVVL 309
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
16-340 1.54e-63

enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176211 [Multi-domain]  Cd Length: 339  Bit Score: 205.12  E-value: 1.54e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNeAIDLADAELPVPDCADNELLVKVEYVGLNPVDGQFAKTGFCKwQYPHILGLDAVGVVVKANKGV--FPn 93
Cdd:cd08249     1 QKAAVLTGPG-GGLLVVVDVPVPKPGPDEVLVKVKAVALNPVDWKHQDYGFIP-SYPAILGCDFAGTVVEVGSGVtrFK- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  94 VGQRVMWHA-----NIGEQGALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISL-----------DKIGISEGDT 157
Cdd:cd08249    78 VGDRVAGFVhggnpNDPRNGAFQEYVVADADLTAKIPDNISFEEAATLPVGLVTAALALfqklglplpppKPSPASKGKP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 158 IFIEGGAGAVGQFAIQYAKQRGADVFTTASKRNHKLVKQLGADVVFDYSDKKLCEKIRRELGPqGFDAVIDTIGGECTQR 237
Cdd:cd08249   158 VLIWGGSSSVGTLAIQLAKLAGYKVITTASPKNFDLVKSLGADAVFDYHDPDVVEDIRAATGG-KLRYALDCISTPESAQ 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 238 NI-ELM--RFCGRIACLNPLPYFDqdlmyHRAPNISVVSIGGAWLANSLCAQQRLSFMGNLLLEGAV-SGDIKHPEITPV 313
Cdd:cd08249   237 LCaEALgrSGGGKLVSLLPVPEET-----EPRKGVKVKFVLGYTVFGEIPEDREFGEVFWKYLPELLeEGKLKPHPVRVV 311
                         330       340
                  ....*....|....*....|....*...
gi 1889614189 314 DFSAESVSQALNKQLAGGFTG-KQVVKV 340
Cdd:cd08249   312 EGGLEGVQEGLDLLRKGKVSGeKLVVRL 339
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
24-338 1.32e-55

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176228 [Multi-domain]  Cd Length: 319  Bit Score: 183.96  E-value: 1.32e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  24 PNEAIDLADAELPVPDCADNELLVKVEYVGLNPVDGQFAKTGFCKW---QYPHILGLDAVGVVVKANKGV--FPnVGQRV 98
Cdd:cd08267     8 SPEVLLLLEVEVPIPTPKPGEVLVKVHAASVNPVDWKLRRGPPKLLlgrPFPPIPGMDFAGEVVAVGSGVtrFK-VGDEV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  99 MWHANIGEQGALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISLDKIG-ISEGDTIFIEGGAGAVGQFAIQYAKQ 177
Cdd:cd08267    87 FGRLPPKGGGALAEYVVAPESGLAKKPEGVSFEEAAALPVAGLTALQALRDAGkVKPGQRVLINGASGGVGTFAVQIAKA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 178 RGADVFTTASKRNHKLVKQLGADVVFDYSDKKLCEKIRRElgpQGFDAVIDTIGGEctqrnielmrfcgriaclnPLPYF 257
Cdd:cd08267   167 LGAHVTGVCSTRNAELVRSLGADEVIDYTTEDFVALTAGG---EKYDVIFDAVGNS-------------------PFSLY 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 258 DQDLmyHRAPNISVVSIGG----------AWLANSLCAQQRLSFMG--------NLLLEGAVSGDIKhpeiTPVD--FSA 317
Cdd:cd08267   225 RASL--ALKPGGRYVSVGGgpsglllvllLLPLTLGGGGRRLKFFLakpnaedlEQLAELVEEGKLK----PVIDsvYPL 298
                         330       340
                  ....*....|....*....|.
gi 1889614189 318 ESVSQALNKQLAGGFTGKQVV 338
Cdd:cd08267   299 EDAPEAYRRLKSGRARGKVVI 319
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
16-340 2.71e-52

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176233 [Multi-domain]  Cd Length: 326  Bit Score: 175.44  E-value: 2.71e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNEAIDLADAELPVPDCADNELLVKVEYVGLNPVDGQ-FAKTGFCKWQYPHILGLDAVGVVVKANKGV--Fp 92
Cdd:cd08272     1 MKALVLESFGGPEVFELREVPRPQPGPGQVLVRVHASGVNPLDTKiRRGGAAARPPLPAILGCDVAGVVEAVGEGVtrF- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  93 NVGQRVMWHANI--GEQGALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISL-DKIGISEGDTIFIEGGAGAVGQ 169
Cdd:cd08272    80 RVGDEVYGCAGGlgGLQGSLAEYAVVDARLLALKPANLSMREAAALPLVGITAWEGLvDRAAVQAGQTVLIHGGAGGVGH 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 170 FAIQYAKQRGADVFTTASKRNHKLVKQLGADVVfDYSDKKLCEKIRRELGPQGFDAVIDTIGGECTQRNIELMRFCGRIA 249
Cdd:cd08272   160 VAVQLAKAAGARVYATASSEKAAFARSLGADPI-IYYRETVVEYVAEHTGGRGFDVVFDTVGGETLDASFEAVALYGRVV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 250 CLNPLPYFDQDLMYHRAPNISVVSIGGAWLANSLCAQQrlsfmGNLLLEGAV---SGDIKhPEITPVDFSAESVSQALNK 326
Cdd:cd08272   239 SILGGATHDLAPLSFRNATYSGVFTLLPLLTGEGRAHH-----GEILREAARlveRGQLR-PLLDPRTFPLEEAAAAHAR 312
                         330
                  ....*....|....
gi 1889614189 327 QLAGGFTGKQVVKV 340
Cdd:cd08272   313 LESGSARGKIVIDV 326
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
16-340 6.59e-46

Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye lens protein with NADP-dependent quinone reductase activity (QOR). It has been cited as a structural component in mammalian eyes, but also has homology to quinone reductases in unrelated species. QOR catalyzes the conversion of a quinone and NAD(P)H to a hydroquinone and NAD(P+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176215 [Multi-domain]  Cd Length: 325  Bit Score: 158.90  E-value: 6.59e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNEAIDLADAELPVPDCADNELLVKVEYVGLNPVD-----GQFAKTGFckwqYPHILGLDAVGVVVKANKGV 90
Cdd:cd08253     1 MRAIRYHEFGAPDVLRLGDLPVPTPGPGEVLVRVHASGVNPVDtyiraGAYPGLPP----LPYVPGSDGAGVVEAVGEGV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  91 FP-NVGQRVmW---HANIGEQGALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISL-DKIGISEGDTIFIEGGAG 165
Cdd:cd08253    77 DGlKVGDRV-WltnLGWGRRQGTAAEYVVVPADQLVPLPDGVSFEQGAALGIPALTAYRALfHRAGAKAGETVLVHGGSG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 166 AVGQFAIQYAKQRGADVFTTASKRNH-KLVKQLGADVVFDYSDKKLCEKIRRELGPQGFDAVIDTIGGECTQRNIELMRF 244
Cdd:cd08253   156 AVGHAAVQLARWAGARVIATASSAEGaELVRQAGADAVFNYRAEDLADRILAATAGQGVDVIIEVLANVNLAKDLDVLAP 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 245 CGRI---ACLNPLPYFDQDLMYHRAPNISVVSIGGAWLANSLCAQQRLSfmgNLLLEGAVSgdikhPEITPVdFSAESVS 321
Cdd:cd08253   236 GGRIvvyGSGGLRGTIPINPLMAKEASIRGVLLYTATPEERAAAAEAIA---AGLADGALR-----PVIARE-YPLEEAA 306
                         330
                  ....*....|....*....
gi 1889614189 322 QALNKQLAGGFTGKQVVKV 340
Cdd:cd08253   307 AAHEAVESGGAIGKVVLDP 325
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
16-339 2.66e-44

D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport and metabolism];


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 154.88  E-value: 2.66e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNEAIDLAdaELPVPDCADNELLVKVEYVGLNP-----VDGQFAKTgfckwQYPHILGLDAVGVVVKANKGV 90
Cdd:COG1064     1 MKAAVLTEPGGPLELE--EVPRPEPGPGEVLVKVEACGVCHsdlhvAEGEWPVP-----KLPLVPGHEIVGRVVAVGPGV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  91 --FpNVGQRVMWHANIG-----------EQ-------------GALSEYTKVP-NFAVSvVPSGLNPGIAATLPCAGMAA 143
Cdd:COG1064    74 tgF-KVGDRVGVGWVDScgtceycrsgrENlcengrftgyttdGGYAEYVVVPaRFLVK-LPDGLDPAEAAPLLCAGITA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 144 LISLDKIGISEGDTIFIEgGAGAVGQFAIQYAKQRGADVF---TTASKRnhKLVKQLGADVVFDYSDKKLCEKIRRElgp 220
Cdd:COG1064   152 YRALRRAGVGPGDRVAVI-GAGGLGHLAVQIAKALGAEVIavdRSPEKL--ELARELGADHVVNSSDEDPVEAVREL--- 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 221 QGFDAVIDTIGGECTQRN-IELMRFCGRIACL----NPLPYFDQDLMYHRapnISVVSiggawlanslcaqqrlSFMGNL 295
Cdd:COG1064   226 TGADVVIDTVGAPATVNAaLALLRRGGRLVLVglpgGPIPLPPFDLILKE---RSIRG----------------SLIGTR 286
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1889614189 296 -----LLEGAVSGDIKhPEITPvdFSAESVSQALNKQLAGGFTGKQVVK 339
Cdd:COG1064   287 adlqeMLDLAAEGKIK-PEVET--IPLEEANEALERLRAGKVRGRAVLD 332
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
17-250 3.13e-43

Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. 2-haloacrylate reductase, a member of this subgroup, catalyzes the NADPH-dependent reduction of a carbon-carbon double bond in organohalogen compounds. Although similar to QOR, Burkholderia 2-haloacrylate reductase does not act on the quinones 1,4-benzoquinone and 1,4-naphthoquinone. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176189 [Multi-domain]  Cd Length: 320  Bit Score: 151.82  E-value: 3.13e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  17 RAIVLPEPN--EAIDLADAELPVPdcADNELLVKVEYVGLNPVDGQFaKTGFCKWQYPHILGLDAVGVVVKANKGV--Fp 92
Cdd:cd05286     1 KAVRIHKTGgpEVLEYEDVPVPEP--GPGEVLVRNTAIGVNFIDTYF-RSGLYPLPLPFVLGVEGAGVVEAVGPGVtgF- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  93 NVGQRVMWHaniGEQGALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISLDKIG-ISEGDTIFIEGGAGAVGQFA 171
Cdd:cd05286    77 KVGDRVAYA---GPPGAYAEYRVVPASRLVKLPDGISDETAAALLLQGLTAHYLLRETYpVKPGDTVLVHAAAGGVGLLL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 172 IQYAKQRGADVFTTAS---KRnhKLVKQLGADVVFDYSDKKLCEKIRRELGPQGFDAVIDTIGGECTQRNIELMRFCGRI 248
Cdd:cd05286   154 TQWAKALGATVIGTVSseeKA--ELARAAGADHVINYRDEDFVERVREITGGRGVDVVYDGVGKDTFEGSLDSLRPRGTL 231

                  ..
gi 1889614189 249 AC 250
Cdd:cd05286   232 VS 233
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
43-338 7.51e-42

enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. Polyketide synthases produce polyketides in step by step mechanism that is similar to fatty acid synthesis. Enoyl reductase reduces a double to single bond. Erythromycin is one example of a polyketide generated by 3 complex enzymes (megasynthases). 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176179 [Multi-domain]  Cd Length: 293  Bit Score: 147.33  E-value: 7.51e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  43 NELLVKVEYVGLNPVDGQFAkTGFCKWQyPHILGLDAVGVVVKANKGV-FPNVGQRVMWHANigeqGALSEYTKVPNFAV 121
Cdd:cd05195     1 DEVEVEVKAAGLNFRDVLVA-LGLLPGD-ETPLGLECSGIVTRVGSGVtGLKVGDRVMGLAP----GAFATHVRVDARLV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 122 SVVPSGLNPGIAATLPCAGMAALISLDKIG-ISEGDTIFIEGGAGAVGQFAIQYAKQRGADVFTTAS---KRnhKLVKQL 197
Cdd:cd05195    75 VKIPDSLSFEEAATLPVAYLTAYYALVDLArLQKGESVLIHAAAGGVGQAAIQLAQHLGAEVFATVGseeKR--EFLREL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 198 GADV--VFDYSDKKLCEKIRRELGPQGFDAVIDTIGGECTQRNIELMRFCGRI-----------ACLNPLPyFDQDLMYH 264
Cdd:cd05195   153 GGPVdhIFSSRDLSFADGILRATGGRGVDVVLNSLSGELLRASWRCLAPFGRFveigkrdilsnSKLGMRP-FLRNVSFS 231
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1889614189 265 rapnisVVSIGGAWLANSLCAQQRLSFMGNLLLEGAVsgdikHPeITPVDFSAESVSQALNKQLAGGFTGKQVV 338
Cdd:cd05195   232 ------SVDLDQLARERPELLRELLREVLELLEAGVL-----KP-LPPTVVPSASEIDAFRLMQSGKHIGKVVL 293
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
44-278 1.56e-41

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 145.93  E-value: 1.56e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  44 ELLVKVEYVGLNPVD-GQFAKTGFCKWQYPHILGLDAVGVVVKANKGVFP-NVGQRVMWHANIGE--------------- 106
Cdd:cd05188     1 EVLVRVEAAGLCGTDlHIRRGGYPPPPKLPLILGHEGAGVVVEVGPGVTGvKVGDRVVVLPNLGCgtcelcrelcpgggi 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 107 -----QGALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISLDKIG-ISEGDTIFIEgGAGAVGQFAIQYAKQRGA 180
Cdd:cd05188    81 lgeglDGGFAEYVVVPADNLVPLPDGLSLEEAALLPEPLATAYHALRRAGvLKPGDTVLVL-GAGGVGLLAAQLAKAAGA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 181 DVFTTA-SKRNHKLVKQLGADVVFDYSDKKLcEKIRRELGPQGFDAVIDTIGGECTQRN-IELMRFCGRIACL-----NP 253
Cdd:cd05188   160 RVIVTDrSDEKLELAKELGADHVIDYKEEDL-EEELRLTGGGGADVVIDAVGGPETLAQaLRLLRPGGRIVVVggtsgGP 238
                         250       260
                  ....*....|....*....|....*.
gi 1889614189 254 LPYFDQDLMYHrapNISVV-SIGGAW 278
Cdd:cd05188   239 PLDDLRRLLFK---ELTIIgSTGGTR 261
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
16-339 5.17e-40

Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176203 [Multi-domain]  Cd Length: 323  Bit Score: 143.41  E-value: 5.17e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNEAIDLADAEL-PVPDcADNELLVKVEYVGLNpvdgqFAKTGFCKWQY------PHILGLDAVGVVVKANK 88
Cdd:cd08241     1 MKAVVCKELGGPEDLVLEEVpPEPG-APGEVRIRVEAAGVN-----FPDLLMIQGKYqvkpplPFVPGSEVAGVVEAVGE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  89 GV--FPnVGQRVMwhaNIGEQGALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISL-DKIGISEGDTIFIEGGAG 165
Cdd:cd08241    75 GVtgFK-VGDRVV---ALTGQGGFAEEVVVPAAAVFPLPDGLSFEEAAALPVTYGTAYHALvRRARLQPGETVLVLGAAG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 166 AVGQFAIQYAKQRGADVFTTAS---KRnhKLVKQLGADVVFDYSDKKLCEKIRRELGPQGFDAVIDTIGGECTQRNIELM 242
Cdd:cd08241   151 GVGLAAVQLAKALGARVIAAASseeKL--ALARALGADHVIDYRDPDLRERVKALTGGRGVDVVYDPVGGDVFEASLRSL 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 243 RFCGRIACL----NPLPYFDQDLMYHRapNISV--VSIGGAWLANSLCAQQRLSFMGNLLLEGAVsgdikHPEITPVdFS 316
Cdd:cd08241   229 AWGGRLLVIgfasGEIPQIPANLLLLK--NISVvgVYWGAYARREPELLRANLAELFDLLAEGKI-----RPHVSAV-FP 300
                         330       340
                  ....*....|....*....|...
gi 1889614189 317 AESVSQALNKQLAGGFTGKQVVK 339
Cdd:cd08241   301 LEQAAEALRALADRKATGKVVLT 323
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
16-254 2.47e-38

PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium chain dehydrogenase/reductase family member, acts in the apoptotic pathway. PIG3 reduces ortho-quinones, but its apoptotic activity has been attributed to oxidative stress generation, since overexpression of PIG3 accumulates reactive oxygen species. PIG3 resembles the MDR family member quinone reductases, which catalyze the reduction of quinone to hydroxyquinone. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176180 [Multi-domain]  Cd Length: 323  Bit Score: 138.73  E-value: 2.47e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNEAIDLADAELPVPDCADNELLVKVEYVGLNPVDgQFAKTGFckwqYPH------ILGLDAVGVVVKANKG 89
Cdd:cd05276     1 MKAIVIKEPGGPEVLELGEVPKPAPGPGEVLIRVAAAGVNRAD-LLQRQGL----YPPppgasdILGLEVAGVVVAVGPG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  90 VF-PNVGQRVMwhanigeqgAL------SEYTKVPnfAVSV--VPSGLNPGIAATLPCAGMAALISLDKIG-ISEGDTIF 159
Cdd:cd05276    76 VTgWKVGDRVC---------ALlagggyAEYVVVP--AGQLlpVPEGLSLVEAAALPEVFFTAWQNLFQLGgLKAGETVL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 160 IEGGAGAVGQFAIQYAKQRGADVFTTA-SKRNHKLVKQLGADVVFDYSDKKLCEKIRRELGPQGFDAVIDTIGGECTQRN 238
Cdd:cd05276   145 IHGGASGVGTAAIQLAKALGARVIATAgSEEKLEACRALGADVAINYRTEDFAEEVKEATGGRGVDVILDMVGGDYLARN 224
                         250
                  ....*....|....*.
gi 1889614189 239 IELMRFCGRIACLNPL 254
Cdd:cd05276   225 LRALAPDGRLVLIGLL 240
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
16-340 3.46e-37

Alcohol dehydrogenases of the MDR family; This group contains proteins related to the zinc-dependent alcohol dehydrogenases. However, while the group has structural zinc site characteristic of these enzymes, it lacks the consensus site for a catalytic zinc. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176227 [Multi-domain]  Cd Length: 342  Bit Score: 136.23  E-value: 3.46e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEP--NEAIDLADaeLPVPDCADNELLVKVEYVGLNPVDgQFAKTG--FCKWQYPHILGLDAVGVVVKANKGVF 91
Cdd:cd08266     1 MKAVVIRGHggPEVLEYGD--LPEPEPGPDEVLVRVKAAALNHLD-LWVRRGmpGIKLPLPHILGSDGAGVVEAVGPGVT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  92 P-NVGQRVMWHANI----------GEQ--------------GALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALIS 146
Cdd:cd08266    78 NvKPGQRVVIYPGIscgrceyclaGREnlcaqygilgehvdGGYAEYVAVPARNLLPIPDNLSFEEAAAAPLTFLTAWHM 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 147 L-DKIGISEGDTIFIEGGAGAVGQFAIQYAKQRGADVFTTASkRNHKL--VKQLGADVVFDYSDKKLCEKIRRELGPQGF 223
Cdd:cd08266   158 LvTRARLRPGETVLVHGAGSGVGSAAIQIAKLFGATVIATAG-SEDKLerAKELGADYVIDYRKEDFVREVRELTGKRGV 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 224 DAVIDTIGGECTQRNIELMRFCGRIACL----NPLPYFDQDLMYHRAPNIsvvsIGgawlanslcaqqrlSFMGNL---- 295
Cdd:cd08266   237 DVVVEHVGAATWEKSLKSLARGGRLVTCgattGYEAPIDLRHVFWRQLSI----LG--------------STMGTKaeld 298
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1889614189 296 -LLEGAVSGDIKhPEITPVdFSAESVSQALNKQLAGGFTGKQVVKV 340
Cdd:cd08266   299 eALRLVFRGKLK-PVIDSV-FPLEEAAEAHRRLESREQFGKIVLTP 342
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
16-251 5.02e-36

Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and metabolism, General function prediction only]; Threonine dehydrogenase or related Zn-dependent dehydrogenase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 440683 [Multi-domain]  Cd Length: 341  Bit Score: 132.95  E-value: 5.02e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNeaiDLADAELPVPDCADNELLVKVEYVG-----LNPVDGQFAKTgfckwQYPHILGLDAVGVVVKANKGV 90
Cdd:COG1063     1 MKALVLHGPG---DLRLEEVPDPEPGPGEVLVRVTAVGicgsdLHIYRGGYPFV-----RPPLVLGHEFVGEVVEVGEGV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  91 -FPNVGQRVMWHANI-------------------------GEQGALSEYTKVPNFAVSVVPSGLNPGIAA---TLPCAGM 141
Cdd:COG1063    73 tGLKVGDRVVVEPNIpcgecrycrrgrynlcenlqflgiaGRDGGFAEYVRVPAANLVKVPDGLSDEAAAlvePLAVALH 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 142 AAlislDKIGISEGDTIFIeGGAGAVGQFAIQYAKQRGADVFTTASKRNHKL--VKQLGADVVFDYSDKKLCEKIRRELG 219
Cdd:COG1063   153 AV----ERAGVKPGDTVLV-IGAGPIGLLAALAARLAGAARVIVVDRNPERLelARELGADAVVNPREEDLVEAVRELTG 227
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1889614189 220 PQGFDAVIDTIGGECTQRN-IELMRFCGRIACL 251
Cdd:COG1063   228 GRGADVVIEAVGAPAALEQaLDLVRPGGTVVLV 260
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
16-249 6.40e-35

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176235 [Multi-domain]  Cd Length: 350  Bit Score: 130.49  E-value: 6.40e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVL-----PEPNEAIDladaELPVPDCADNELLVKVEYVGLN-------------PVDGQFAKTGFCKW-------Q 70
Cdd:cd08274     1 MRAVLLtghggLDKLVYRD----DVPVPTPAPGEVLIRVGACGVNntdintregwystEVDGATDSTGAGEAgwwggtlS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  71 YPHILGLDAVGVVVKANKGVFPN-VGQRVMWHANI----------------GEQGALSEYTKVPNFAVSVVPSGLNPGIA 133
Cdd:cd08274    77 FPRIQGADIVGRVVAVGEGVDTArIGERVLVDPSIrdppeddpadidyigsERDGGFAEYTVVPAENAYPVNSPLSDVEL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 134 ATLPCAGMAALISLDKIGISEGDTIFIEGGAGAVGQFAIQYAKQRGADVFTTASKRNHKLVKQLGADVVFDYSDKKLCEK 213
Cdd:cd08274   157 ATFPCSYSTAENMLERAGVGAGETVLVTGASGGVGSALVQLAKRRGAIVIAVAGAAKEEAVRALGADTVILRDAPLLADA 236
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1889614189 214 irRELGPQGFDAVIDTIGGECTQRNIELMRFCGRIA 249
Cdd:cd08274   237 --KALGGEPVDVVADVVGGPLFPDLLRLLRPGGRYV 270
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
17-248 1.22e-34

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176236 [Multi-domain]  Cd Length: 337  Bit Score: 129.24  E-value: 1.22e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  17 RAIVLPEPNEAIDLADAELPVPDCADNELLVKVEYVGLNPVDgQFAKTGFC----KWqyPHILGLDAVGVVVKANKGVFP 92
Cdd:cd08275     1 RAVVLTGFGGLDKLKVEKEALPEPSSGEVRVRVEACGLNFAD-LMARQGLYdsapKP--PFVPGFECAGTVEAVGEGVKD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  93 N-VGQRVMWHANIGeqgALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISLDKIG-ISEGDTIFIEGGAGAVGQF 170
Cdd:cd08275    78 FkVGDRVMGLTRFG---GYAEVVNVPADQVFPLPDGMSFEEAAAFPVNYLTAYYALFELGnLRPGQSVLVHSAAGGVGLA 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889614189 171 AIQYAKQ-RGADVFTTASKRNHKLVKQLGADVVFDYSDKKLCEKIRrELGPQGFDAVIDTIGGECTQRNIELMRFCGRI 248
Cdd:cd08275   155 AGQLCKTvPNVTVVGTASASKHEALKENGVTHVIDYRTQDYVEEVK-KISPEGVDIVLDALGGEDTRKSYDLLKPMGRL 232
MDR4 cd08270
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
16-243 1.60e-34

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176231 [Multi-domain]  Cd Length: 305  Bit Score: 128.26  E-value: 1.60e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLpEPNEAIDLADAELPVPDCADNELLVKVEYVGLNPVDGQFAKTgfckWQYPHILGLDAVGVVVKANK-GVFPNV 94
Cdd:cd08270     1 MRALVV-DPDAPLRLRLGEVPDPQPAPHEALVRVAAISLNRGELKFAAE----RPDGAVPGWDAAGVVERAAAdGSGPAV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  95 GQRVmwhANIGEQGALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISLDKIGISEGDTIFIEGGAGAVGQFAIQY 174
Cdd:cd08270    76 GARV---VGLGAMGAWAELVAVPTGWLAVLPDGVSFAQAATLPVAGVTALRALRRGGPLLGRRVLVTGASGGVGRFAVQL 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1889614189 175 AKQRGADVFTTAS--KRNHKLVKQLGADVVFDYSDkklcekirreLGPQGFDAVIDTIGGECTQRNIELMR 243
Cdd:cd08270   153 AALAGAHVVAVVGspARAEGLRELGAAEVVVGGSE----------LSGAPVDLVVDSVGGPQLARALELLA 213
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
16-339 1.08e-33

Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member of the medium chain dehydrogenase/ reductase (MDR) family. Riticulons are endoplasmic reticulum associated proteins involved in membrane trafficking and neuroendocrine secretion. The MDR/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176210 [Multi-domain]  Cd Length: 350  Bit Score: 126.95  E-value: 1.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPE--PNEAIDLADaELPVPD-CADNELLVKVEYVGLNPVD----GQFAKTGFCKWQY-----------PHILGL 77
Cdd:cd08248     1 MKAWQIHSygGIDSLLLLE-NARIPViRKPNQVLIKVHAASVNPIDvlmrSGYGRTLLNKKRKpqsckysgiefPLTLGR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  78 DAVGVVVKANKGVFP-NVGQRVMWHANIGEQGALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISLDKIGISEGD 156
Cdd:cd08248    80 DCSGVVVDIGSGVKSfEIGDEVWGAVPPWSQGTHAEYVVVPENEVSKKPKNLSHEEAASLPYAGLTAWSALVNVGGLNPK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 157 T-----IFIEGGAGAVGQFAIQYAKQRGADVFTTASKRNHKLVKQLGADVVFDYSDKKLCEKIrRELGPqgFDAVIDTIG 231
Cdd:cd08248   160 NaagkrVLILGGSGGVGTFAIQLLKAWGAHVTTTCSTDAIPLVKSLGADDVIDYNNEDFEEEL-TERGK--FDVILDTVG 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 232 GECTQRNIELMRFCGRIACLNP--LPYFD---------QDLMYHRAPNISVVSIGGA--WLANSLCaqqrlsfmGNLLLE 298
Cdd:cd08248   237 GDTEKWALKLLKKGGTYVTLVSplLKNTDklglvggmlKSAVDLLKKNVKSLLKGSHyrWGFFSPS--------GSALDE 308
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1889614189 299 gaVSGDIKHPEITPV-D--FSAESVSQALNKQLAGGFTGKQVVK 339
Cdd:cd08248   309 --LAKLVEDGKIKPViDkvFPFEEVPEAYEKVESGHARGKTVIK 350
MDR_yhdh_yhfp cd05280
Yhdh and yhfp-like putative quinone oxidoreductases; Yhdh and yhfp-like putative quinone ...
16-250 1.12e-32

Yhdh and yhfp-like putative quinone oxidoreductases; Yhdh and yhfp-like putative quinone oxidoreductases (QOR). QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176183 [Multi-domain]  Cd Length: 325  Bit Score: 123.81  E-value: 1.12e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNEAIDLADAELPVPDCADNELLVKVEYVGLNPVDGqFAKTGFCK--WQYPHILGLDAVGVVVKANKGVFPn 93
Cdd:cd05280     1 FKALVVEEQDGGVSLFLRTLPLDDLPEGDVLIRVHYSSLNYKDA-LAATGNGGvtRNYPHTPGIDAAGTVVSSDDPRFR- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  94 VGQRVMWH-ANIGEQ--GALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISLDKI---GISEGDT-IFIEGGAGA 166
Cdd:cd05280    79 EGDEVLVTgYDLGMNtdGGFAEYVRVPADWVVPLPEGLSLREAMILGTAGFTAALSVHRLednGQTPEDGpVLVTGATGG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 167 VGQFAIQYAKQRGADVFTTASKRNHK-LVKQLGADVVFDYSDkkLCEKIRRELGPQGFDAVIDTIGGECTQRNIELMRFC 245
Cdd:cd05280   159 VGSIAVAILAKLGYTVVALTGKEEQAdYLKSLGASEVLDRED--LLDESKKPLLKARWAGAIDTVGGDVLANLLKQTKYG 236

                  ....*
gi 1889614189 246 GRIAC 250
Cdd:cd05280   237 GVVAS 241
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
47-338 2.33e-32

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 122.11  E-value: 2.33e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189   47 VKVEYVGLNPVDGQFAkTGfckwQYP--HILGLDAVGVVVKANKGV--FpNVGQRVMWHAnigeQGALSEYTKVPNFAVS 122
Cdd:smart00829   1 IEVRAAGLNFRDVLIA-LG----LYPgeAVLGGECAGVVTRVGPGVtgL-AVGDRVMGLA----PGAFATRVVTDARLVV 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  123 VVPSGLNPGIAATLPCAGMAALISLDKIG-ISEGDTIFIEGGAGAVGQFAIQYAKQRGADVFTTA-SKRNHKLVKQLG-- 198
Cdd:smart00829  71 PIPDGWSFEEAATVPVVFLTAYYALVDLArLRPGESVLIHAAAGGVGQAAIQLARHLGAEVFATAgSPEKRDFLRALGip 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  199 ADVVFDYSDKKLCEKIRRELGPQGFDAVIDTIGGECTQRNIELMRFCGRIACL--------NPLPyfdqdlMYHRAPNIS 270
Cdd:smart00829 151 DDHIFSSRDLSFADEILRATGGRGVDVVLNSLSGEFLDASLRCLAPGGRFVEIgkrdirdnSQLA------MAPFRPNVS 224
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889614189  271 VVSIggawLANSLCAQ-QRLSFMGNLLLEGAVSGDIKHPEITPvdFSAESVSQALNKQLAGGFTGKQVV 338
Cdd:smart00829 225 YHAV----DLDALEEGpDRIRELLAEVLELFAEGVLRPLPVTV--FPISDAEDAFRYMQQGKHIGKVVL 287
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
16-233 2.94e-32

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176234 [Multi-domain]  Cd Length: 331  Bit Score: 122.76  E-value: 2.94e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPE--PNEAIDLADAELPVPdcADNELLVKVEYVGLNPVDgQFAKTGFCKWQ--YPHILGLDAVGVVVKANKGVF 91
Cdd:cd08273     1 NREVVVTRrgGPEVLKVVEADLPEP--AAGEVVVKVEASGVSFAD-VQMRRGLYPDQppLPFTPGYDLVGRVDALGSGVT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  92 -PNVGQRVmwhANIGEQGALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISLDKIG-ISEGDTIFIEGGAGAVGQ 169
Cdd:cd08273    78 gFEVGDRV---AALTRVGGNAEYINLDAKYLVPVPEGVDAAEAVCLVLNYVTAYQMLHRAAkVLTGQRVLIHGASGGVGQ 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1889614189 170 FAIQYAKQRGADVFTTASKRNHKLVKQLGAdVVFDYSDKKLcekIRRELGPQGFDAVIDTIGGE 233
Cdd:cd08273   155 ALLELALLAGAEVYGTASERNHAALRELGA-TPIDYRTKDW---LPAMLTPGGVDVVFDGVGGE 214
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
16-248 3.66e-32

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. This group contains proteins that share the characteristic catalytic and structural zinc-binding sites of the zinc-dependent alcohol dehydrogenase family. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48), then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176220 [Multi-domain]  Cd Length: 332  Bit Score: 122.43  E-value: 3.66e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNEAIDLADAELPVPdcADNELLVKVEYVGLNPVDGQFAKTGFCKWQYPHILGLDAVGVVVKANKGVFP-NV 94
Cdd:cd08259     1 MKAAILHKPNKPLQIEEVPDPEP--GPGEVLIKVKAAGVCYRDLLFWKGFFPRGKYPLILGHEIVGTVEEVGEGVERfKP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  95 GQRVMWHANIGE------------------------QGALSEYTKVP-NFAVSVvPSGLNPGIAATLPCAGMAALISLDK 149
Cdd:cd08259    79 GDRVILYYYIPCgkceyclsgeenlcrnraeygeevDGGFAEYVKVPeRSLVKL-PDNVSDESAALAACVVGTAVHALKR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 150 IGISEGDTIFIEGGAGAVGQFAIQYAKQRGADVFT-TASKRNHKLVKQLGADVVFDysDKKLCEKIRRELGPqgfDAVID 228
Cdd:cd08259   158 AGVKKGDTVLVTGAGGGVGIHAIQLAKALGARVIAvTRSPEKLKILKELGADYVID--GSKFSEDVKKLGGA---DVVIE 232
                         250       260
                  ....*....|....*....|
gi 1889614189 229 TIGGECTQRNIELMRFCGRI 248
Cdd:cd08259   233 LVGSPTIEESLRSLNKGGRL 252
AL_MDR cd08252
Arginate lyase and other MDR family members; This group contains a structure identified as an ...
16-229 1.31e-31

Arginate lyase and other MDR family members; This group contains a structure identified as an arginate lyase. Other members are identified quinone reductases, alginate lyases, and other proteins related to the zinc-dependent dehydrogenases/reductases. QOR catalyzes the conversion of a quinone and NAD(P)H to a hydroquinone and NAD(P+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176214 [Multi-domain]  Cd Length: 336  Bit Score: 121.09  E-value: 1.31e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNEAID---LADAELPVPDCADNELLVKVEYVGLNPVDGQFAKTGFCKWQYPHILGLDAVGVVVKANKGV-- 90
Cdd:cd08252     1 MKAIGFTQPLPITDpdsLIDIELPKPVPGGRDLLVRVEAVSVNPVDTKVRAGGAPVPGQPKILGWDASGVVEAVGSEVtl 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  91 FpNVGQRVMWHANIGEQGALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISL-DKIGISEGD-----TIFIEGGA 164
Cdd:cd08252    81 F-KVGDEVYYAGDITRPGSNAEYQLVDERIVGHKPKSLSFAEAAALPLTSLTAWEALfDRLGISEDAenegkTLLIIGGA 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1889614189 165 GAVGQFAIQYAKQRGA-DVFTTASK-RNHKLVKQLGADVVFDYSDkkLCEKIRRELGPQGFDAVIDT 229
Cdd:cd08252   160 GGVGSIAIQLAKQLTGlTVIATASRpESIAWVKELGADHVINHHQ--DLAEQLEALGIEPVDYIFCL 224
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
16-340 5.68e-31

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176229 [Multi-domain]  Cd Length: 328  Bit Score: 119.24  E-value: 5.68e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNEAIDLADAELPVPDCADNELLVKVEYVGLNPVDgQFAKTGFCKWQ--YPHILGLDAVGVVVKANKGVFP- 92
Cdd:cd08268     1 MRAVRFHQFGGPEVLRIEELPVPAPGAGEVLIRVEAIGLNRAD-AMFRRGAYIEPppLPARLGYEAAGVVEAVGAGVTGf 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  93 NVGQRV--MWHANIGEQGALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISL-DKIGISEGDTIFIEGGAGAVGQ 169
Cdd:cd08268    80 AVGDRVsvIPAADLGQYGTYAEYALVPAAAVVKLPDGLSFVEAAALWMQYLTAYGALvELAGLRPGDSVLITAASSSVGL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 170 FAIQYAKQRGADVF--TTASKRNHKLvKQLGADVVFDYSDKKLCEKIRRELGPQGFDAVIDTIGGECTQRNIELMRFCGR 247
Cdd:cd08268   160 AAIQIANAAGATVIatTRTSEKRDAL-LALGAAHVIVTDEEDLVAEVLRITGGKGVDVVFDPVGGPQFAKLADALAPGGT 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 248 IA---CLNPLPY-FDQDLMYHRAPNISVVSIGGAWLanslcAQQRLSFMGNLLLEGAVSGDIKhPEITPVdFSAESVSQA 323
Cdd:cd08268   239 LVvygALSGEPTpFPLKAALKKSLTFRGYSLDEITL-----DPEARRRAIAFILDGLASGALK-PVVDRV-FPFDDIVEA 311
                         330
                  ....*....|....*..
gi 1889614189 324 LNKQLAGGFTGKQVVKV 340
Cdd:cd08268   312 HRYLESGQQIGKIVVTP 328
Mgc45594_like cd08250
Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of ...
15-233 1.92e-30

Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of undetermined function. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176212 [Multi-domain]  Cd Length: 329  Bit Score: 117.74  E-value: 1.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  15 TMRAIVLPE--PN--EAIDLADAELPVPdcADNELLVKVEYVGLNPVDGQFAKTGFCKW-QYPHILGLDAVGVVVKANKG 89
Cdd:cd08250     1 SFRKLVVHRlsPNfrEATSIVDVPVPLP--GPGEVLVKNRFVGINASDINFTAGRYDPGvKPPFDCGFEGVGEVVAVGEG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  90 VFP-NVGQRVMWHANigeqGALSEYTKVPNFAVSVVPSgLNPgIAATLPCAGMAALISLDKIG-ISEGDTIFIEGGAGAV 167
Cdd:cd08250    79 VTDfKVGDAVATMSF----GAFAEYQVVPARHAVPVPE-LKP-EVLPLLVSGLTASIALEEVGeMKSGETVLVTAAAGGT 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1889614189 168 GQFAIQYAKQRGADVF-TTASKRNHKLVKQLGADVVFDYSDKKLCEKIRRELgPQGFDAVIDTIGGE 233
Cdd:cd08250   153 GQFAVQLAKLAGCHVIgTCSSDEKAEFLKSLGCDRPINYKTEDLGEVLKKEY-PKGVDVVYESVGGE 218
CAD3 cd08297
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
16-340 4.39e-30

Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Cinnamyl alcohol dehydrogenases (CAD) reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176257 [Multi-domain]  Cd Length: 341  Bit Score: 117.25  E-value: 4.39e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNEAIDLADaELPVPDCADNELLVKVEYvglnpvdgqfakTGFC-------------KWQYPHILGLDAVGV 82
Cdd:cd08297     1 MKAAVVEEFGEKPYEVK-DVPVPEPGPGEVLVKLEA------------SGVChtdlhaalgdwpvKPKLPLIGGHEGAGV 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  83 VVKANKGVFP-NVGQRV----MWHA--------NIGEQ-------------GALSEYTKVPNFAVSVVPSGLNPGIAATL 136
Cdd:cd08297    68 VVAVGPGVSGlKVGDRVgvkwLYDAcgkceycrTGDETlcpnqknsgytvdGTFAEYAIADARYVTPIPDGLSFEQAAPL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 137 PCAGMAALISLDKIGISEGDTIFIEGGAGAVGQFAIQYAKQRGADVF---TTASKRnhKLVKQLGADVVFDYSDKKLCEK 213
Cdd:cd08297   148 LCAGVTVYKALKKAGLKPGDWVVISGAGGGLGHLGVQYAKAMGLRVIaidVGDEKL--ELAKELGADAFVDFKKSDDVEA 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 214 IRRELGPQGFDAVIDTIGG-ECTQRNIELMRFCGRIAC--LNPLPYFDQDLMYHRAPNISVVsigGAWLANSLCAQQRLS 290
Cdd:cd08297   226 VKELTGGGGAHAVVVTAVSaAAYEQALDYLRPGGTLVCvgLPPGGFIPLDPFDLVLRGITIV---GSLVGTRQDLQEALE 302
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1889614189 291 FmgnlllegAVSGDIKhPEITPVDFsaESVSQALNKQLAGGFTGKQVVKV 340
Cdd:cd08297   303 F--------AARGKVK-PHIQVVPL--EDLNEVFEKMEEGKIAGRVVVDF 341
quinone_oxidoreductase_like_1 cd08243
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
16-231 1.45e-29

Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176205 [Multi-domain]  Cd Length: 320  Bit Score: 115.40  E-value: 1.45e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVL--PEPNEAIDLAdaELPVPDCADNELLVKVEYVGLNPVDgQFAKTGFCKW-QYPHILGLDAVGVVVKANKGVFP 92
Cdd:cd08243     1 MKAIVIeqPGGPEVLKLR--EIPIPEPKPGWVLIRVKAFGLNRSE-IFTRQGHSPSvKFPRVLGIEAVGEVEEAPGGTFT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  93 nVGQRVMwhANIGE-----QGALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISLDK-IGISEGDTIFIEGGAGA 166
Cdd:cd08243    78 -PGQRVA--TAMGGmgrtfDGSYAEYTLVPNEQVYAIDSDLSWAELAALPETYYTAWGSLFRsLGLQPGDTLLIRGGTSS 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1889614189 167 VGQFAIQYAKQRGADVF-TTASKRNHKLVKQLGAD-VVFDysDKKLCEKIRRElgPQGFDAVIDTIG 231
Cdd:cd08243   155 VGLAALKLAKALGATVTaTTRSPERAALLKELGADeVVID--DGAIAEQLRAA--PGGFDKVLELVG 217
Zn_ADH_like2 cd08264
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
16-232 5.96e-29

Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase family. However, this subgroup does not contain the characteristic catalytic zinc site. Also, it contains an atypical structural zinc-binding pattern: DxxCxxCxxxxxxxC. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176225 [Multi-domain]  Cd Length: 325  Bit Score: 113.60  E-value: 5.96e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEP-NEAIDLADAELPVPdcADNELLVKVEYVGLNPVDgQFAKTGFCKWQYPHILGLDAVGVVVKANKGVFP-N 93
Cdd:cd08264     1 MKALVFEKSgIENLKVEDVKDPKP--GPGEVLIRVKMAGVNPVD-YNVINAVKVKPMPHIPGAEFAGVVEEVGDHVKGvK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  94 VGQRV-------------------MWHAN-----IGEQGALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISLDK 149
Cdd:cd08264    78 KGDRVvvynrvfdgtcdmclsgneMLCRNggiigVVSNGGYAEYIVVPEKNLFKIPDSISDELAASLPVAALTAYHALKT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 150 IGISEGDTIFIEGGAGAVGQFAIQYAKQRGADVFTTASKrnhKLVKQLGADVVFDYSDkkLCEKIRRelGPQGFDAVIDT 229
Cdd:cd08264   158 AGLGPGETVVVFGASGNTGIFAVQLAKMMGAEVIAVSRK---DWLKEFGADEVVDYDE--VEEKVKE--ITKMADVVINS 230

                  ...
gi 1889614189 230 IGG 232
Cdd:cd08264   231 LGS 233
AST1_like cd08247
AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast; This group ...
34-232 2.82e-28

AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast; This group contains members identified in targeting of yeast membrane proteins ATPase. AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast, identified as a multicopy suppressor of pma1 mutants which cause temperature sensitive growth arrest due to the inability of ATPase to target to the cell surface. This family is homologous to the medium chain family of dehydrogenases and reductases. Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of an beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176209 [Multi-domain]  Cd Length: 352  Bit Score: 112.36  E-value: 2.82e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  34 ELPVPDCA-DNELLVKVEYVGLNPVD-GQFAKTGFCKWQYPHILGLDAVGVVVKANKGVFPN--VGQRVM---WHANiGE 106
Cdd:cd08247    19 KLPLPNCYkDNEIVVKVHAAALNPVDlKLYNSYTFHFKVKEKGLGRDYSGVIVKVGSNVASEwkVGDEVCgiyPHPY-GG 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 107 QGALSEY----TKVPNFAVSVVPSGLNPGIAATLP-CAGMA--ALISLDKIGISeGDTIFIEGGAGAVGQFAIQYAKQRG 179
Cdd:cd08247    98 QGTLSQYllvdPKKDKKSITRKPENISLEEAAAWPlVLGTAyqILEDLGQKLGP-DSKVLVLGGSTSVGRFAIQLAKNHY 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1889614189 180 A--DVFTTASKRNHKLVKQLGADVVFDY----SDKKLCEKIRRELGPQGFDAVIDTIGG 232
Cdd:cd08247   177 NigTVVGTCSSRSAELNKKLGADHFIDYdahsGVKLLKPVLENVKGQGKFDLILDCVGG 235
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
26-335 1.66e-27

2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176645 [Multi-domain]  Cd Length: 323  Bit Score: 109.67  E-value: 1.66e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  26 EAIDLADAELPVPDCADNELLVKVEYVGLNPVD-----GQFAKtgfcKWQYPHILGLDAVGVVVKANKGVFP-NVGQRVm 99
Cdd:cd05282    10 LPLVLELVSLPIPPPGPGEVLVRMLAAPINPSDlitisGAYGS----RPPLPAVPGNEGVGVVVEVGSGVSGlLVGQRV- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 100 whANIGEQGALSEYTKVPNFAVSVVPSGLNPGIAATL---PcagMAA-LISLDKIGISEGDTIFIEGGAGAVGQFAIQYA 175
Cdd:cd05282    85 --LPLGGEGTWQEYVVAPADDLIPVPDSISDEQAAMLyinP---LTAwLMLTEYLKLPPGDWVIQNAANSAVGRMLIQLA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 176 KQRGADVFTTASKRNHK-LVKQLGADVVFDYSDKKLCEKIRRELGPQGFDAVIDTIGGECTQRNIELMRFCGRIACL--- 251
Cdd:cd05282   160 KLLGFKTINVVRRDEQVeELKALGADEVIDSSPEDLAQRVKEATGGAGARLALDAVGGESATRLARSLRPGGTLVNYgll 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 252 --NPLPYFDQDLmyhRAPNISVvsiGGAWLANSLCA--QQRLSFMGNLLLEGAVSGDIkHPEITPVdFSAESVSQALNKQ 327
Cdd:cd05282   240 sgEPVPFPRSVF---IFKDITV---RGFWLRQWLHSatKEAKQETFAEVIKLVEAGVL-TTPVGAK-FPLEDFEEAVAAA 311

                  ....*...
gi 1889614189 328 LAGGFTGK 335
Cdd:cd05282   312 EQPGRGGK 319
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
16-340 2.00e-27

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176237 [Multi-domain]  Cd Length: 336  Bit Score: 109.93  E-value: 2.00e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNEAIDLADAELPVPDCADNELLVKVEYVGLN-----PVDGQFAKTGfckwQYPHILGLDAVGVVVKANKGV 90
Cdd:cd08276     1 MKAWRLSGGGGLDNLKLVEEPVPEPGPGEVLVRVHAVSLNyrdllILNGRYPPPV----KDPLIPLSDGAGEVVAVGEGV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  91 --FpNVGQRVM------WHAN------------IGEQGALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISLDKI 150
Cdd:cd08276    77 trF-KVGDRVVptffpnWLDGpptaedeasalgGPIDGVLAEYVVLPEEGLVRAPDHLSFEEAATLPCAGLTAWNALFGL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 151 G-ISEGDTIFIeGGAGAVGQFAIQYAKQRGADVFTTASKrNHKL--VKQLGADVVFDYS-DKKLCEKIRRELGPQGFDAV 226
Cdd:cd08276   156 GpLKPGDTVLV-QGTGGVSLFALQFAKAAGARVIATSSS-DEKLerAKALGADHVINYRtTPDWGEEVLKLTGGRGVDHV 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 227 IDTIGGECTQRNIELMRFCGRIACLNPLPYFDQ-----DLMYHRApNISVVSIGgawlanSLCAQQRLsfmgNLLLEgav 301
Cdd:cd08276   234 VEVGGPGTLAQSIKAVAPGGVISLIGFLSGFEApvlllPLLTKGA-TLRGIAVG------SRAQFEAM----NRAIE--- 299
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1889614189 302 sgdiKHpEITPV-D--FSAESVSQALNKQLAGGFTGKQVVKV 340
Cdd:cd08276   300 ----AH-RIRPViDrvFPFEEAKEAYRYLESGSHFGKVVIRV 336
MDR_enoyl_red cd08244
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. ...
16-248 3.14e-27

Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176206 [Multi-domain]  Cd Length: 324  Bit Score: 108.99  E-value: 3.14e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPE--PNEAIDLADAELPVPdcADNELLVKVEYVGLNPVDGQF---AKTGFCKWQYPHILGLDAVGVVVKANKGV 90
Cdd:cd08244     1 MRAIRLHEfgPPEVLVPEDVPDPVP--GPGQVRIAVAAAGVHFVDTQLrsgWGPGPFPPELPYVPGGEVAGVVDAVGPGV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  91 FPN-VGQRVMWHANIGEQGaLSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISLDKIGISEGDTIFIEGGAGAVGQ 169
Cdd:cd08244    79 DPAwLGRRVVAHTGRAGGG-YAELAVADVDSLHPVPDGLDLEAAVAVVHDGRTALGLLDLATLTPGDVVLVTAAAGGLGS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 170 FAIQYAKQRGADVFTTA-SKRNHKLVKQLGADVVFDYSDKKLCEKIRRELGPQGFDAVIDTIGGECTQRNIELMRFCGRI 248
Cdd:cd08244   158 LLVQLAKAAGATVVGAAgGPAKTALVRALGADVAVDYTRPDWPDQVREALGGGGVTVVLDGVGGAIGRAALALLAPGGRF 237
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
16-251 4.46e-27

Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176222 [Multi-domain]  Cd Length: 337  Bit Score: 108.82  E-value: 4.46e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNEaidLADAELPVPDCADNELLVKVEYVGL-----------NPvdgqFAktgfckwQYPHILGLDAVGVVV 84
Cdd:cd08261     1 MKALVCEKPGR---LEVVDIPEPVPGAGEVLVRVKRVGIcgsdlhiyhgrNP----FA-------SYPRILGHELSGEVV 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  85 KANKGVFP-NVGQRVM---------WHA-NIG--------------EQGALSEYTKVPNFAVsVVPSGLNPGIAATLPCA 139
Cdd:cd08261    67 EVGEGVAGlKVGDRVVvdpyiscgeCYAcRKGrpnccenlqvlgvhRDGGFAEYIVVPADAL-LVPEGLSLDQAALVEPL 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 140 GMAALIsLDKIGISEGDTIFIEGgAGAVGQFAIQYAKQRGADVFTT---ASKRNhkLVKQLGADVVFDYSDKKLCEKIRR 216
Cdd:cd08261   146 AIGAHA-VRRAGVTAGDTVLVVG-AGPIGLGVIQVAKARGARVIVVdidDERLE--FARELGADDTINVGDEDVAARLRE 221
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1889614189 217 ELGPQGFDAVIDTIGGECTQRN-IELMRFCGRIACL 251
Cdd:cd08261   222 LTDGEGADVVIDATGNPASMEEaVELVAHGGRVVLV 257
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
16-249 1.77e-25

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 104.35  E-value: 1.77e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNEAIDLADAELPVPdcADNELLVKVEYVGLNPVDgQFAKTGFC-KWQYPHILGLDAVGVVVKANKGV--Fp 92
Cdd:PRK13771    1 MKAVILPGFKQGYRIEEVPDPKP--GKDEVVIKVNYAGLCYRD-LLQLQGFYpRMKYPVILGHEVVGTVEEVGENVkgF- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  93 NVGQRV--MWHANIGE----------------------QGALSEYTKVPNFAVSVVPSGLNPGIAATLPCagMAALI--S 146
Cdd:PRK13771   77 KPGDRVasLLYAPDGTceycrsgeeaycknrlgygeelDGFFAEYAKVKVTSLVKVPPNVSDEGAVIVPC--VTGMVyrG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 147 LDKIGISEGDTIFIEGGAGAVGQFAIQYAKQRGADVF-TTASKRNHKLVKQLGADVVfdySDKKLCEKIRReLGpqGFDA 225
Cdd:PRK13771  155 LRRAGVKKGETVLVTGAGGGVGIHAIQVAKALGAKVIaVTSSESKAKIVSKYADYVI---VGSKFSEEVKK-IG--GADI 228
                         250       260
                  ....*....|....*....|....
gi 1889614189 226 VIDTIGGECTQRNIELMRFCGRIA 249
Cdd:PRK13771  229 VIETVGTPTLEESLRSLNMGGKII 252
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
16-282 2.36e-25

NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol dehydrogenases and other sugar dehydrogenases of the medium-chain dehydrogenase/reductase family (MDR), which includes zinc-dependent alcohol dehydrogenase and related proteins. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Related proteins include threonine dehydrogenase, formaldehyde dehydrogenase, and butanediol dehydrogenase. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Horse liver alcohol dehydrogenase is a dimeric enzyme and each subunit has two domains. The NAD binding domain is in a Rossmann fold and the catalytic domain contains a zinc ion to which substrates bind. There is a cleft between the domains that closes upon formation of the ternary complex.


Pssm-ID: 176198 [Multi-domain]  Cd Length: 343  Bit Score: 104.23  E-value: 2.36e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNeaiDLADAELPVPDCADNELLVKVEYVGLNPVD-GQFAKTGfcKWQYPHILGLDAVGVVVKANKGVFP-N 93
Cdd:cd08236     1 MKALVLTGPG---DLRYEDIPKPEPGPGEVLVKVKACGICGSDiPRYLGTG--AYHPPLVLGHEFSGTVEEVGSGVDDlA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  94 VGQRV----MWHAN------------------IG--EQGALSEYTKVPNFAVSVVPSGLNPGIAATL-PCAgmAALISLD 148
Cdd:cd08236    76 VGDRVavnpLLPCGkceyckkgeyslcsnydyIGsrRDGAFAEYVSVPARNLIKIPDHVDYEEAAMIePAA--VALHAVR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 149 KIGISEGDTIFIEGgAGAVGQFAIQYAKQRGADVFTTASKRNHKLV--KQLGADVVFDYSDKKLcEKIRRELGPQGFDAV 226
Cdd:cd08236   154 LAGITLGDTVVVIG-AGTIGLLAIQWLKILGAKRVIAVDIDDEKLAvaRELGADDTINPKEEDV-EKVRELTEGRGADLV 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1889614189 227 IDTIGGECTQRN-IELMRFCGRIACLNpLPYfdQDLMYHRAPNISVV----SIGGAWLANS 282
Cdd:cd08236   232 IEAAGSPATIEQaLALARPGGKVVLVG-IPY--GDVTLSEEAFEKILrkelTIQGSWNSYS 289
adh_fam_1 TIGR02817
zinc-binding alcohol dehydrogenase family protein; Members of this model form a distinct ...
22-258 4.24e-25

zinc-binding alcohol dehydrogenase family protein; Members of this model form a distinct subset of the larger family of oxidoreductases that includes zinc-binding alcohol dehydrogenases and NADPH:quinone reductases (pfam00107). While some current members of this family carry designations as putative alginate lyase, it seems no sequence with a direct characterization as such is detected by this model. [Energy metabolism, Fermentation]


Pssm-ID: 274313 [Multi-domain]  Cd Length: 336  Bit Score: 103.66  E-value: 4.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  22 PEPNEAID-LADAELPVPDCADNELLVKVEYVGLNPVDGQFAKTGFCKWQYPHILGLDAVGVVVKANKGV--FpNVGQRV 98
Cdd:TIGR02817   8 PLPITDPDaLVDIDLPKPKPGGRDLLVEVKAISVNPVDTKVRARMAPEAGQPKILGWDAAGVVVAVGDEVtlF-KPGDEV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  99 MWHANIGEQGALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISL-DKIGISEG-----DTIFIEGGAGAVGQFAI 172
Cdd:TIGR02817  87 WYAGDIDRPGSNAEFHLVDERIVGHKPKSLSFAEAAALPLTSITAWELLfDRLGINDPvagdkRALLIIGGAGGVGSILI 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 173 QYAKQ-RGADVFTTASK-RNHKLVKQLGADVVFDYSdKKLCEKIRReLGPQGFDAVIDTiggecTQRN------IELMRF 244
Cdd:TIGR02817 167 QLARQlTGLTVIATASRpESQEWVLELGAHHVIDHS-KPLKAQLEK-LGLEAVSYVFSL-----THTDqhfkeiVELLAP 239
                         250
                  ....*....|....
gi 1889614189 245 CGRIACLNPLPYFD 258
Cdd:TIGR02817 240 QGRFALIDDPAELD 253
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
16-248 4.48e-25

L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some members in this subgroup. L-iditol 2-dehydrogenase catalyzes the NAD+-dependent conversion of L-iditol to L-sorbose in fructose and mannose metabolism. This enzyme is related to sorbitol dehydrogenase, alcohol dehydrogenase, and other medium chain dehydrogenase/reductases. The zinc-dependent alcohol dehydrogenase (ADH-Zn)-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) to highlight its broad range of activities and to distinguish from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal GroES-like catalytic domain. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176197 [Multi-domain]  Cd Length: 343  Bit Score: 103.44  E-value: 4.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNeaiDLADAELPVPDCADNELLVKVEYVGLNPVDGQFAKTGFCKWQYPHILGLDAVGVVVKANKGV--FPn 93
Cdd:cd08235     1 MKAAVLHGPN---DVRLEEVPVPEPGPGEVLVKVRACGICGTDVKKIRGGHTDLKPPRILGHEIAGEIVEVGDGVtgFK- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  94 VGQRVMWHANIG------------------------EQGALSEYTKVPNFAVsvVPSGLNPgIAATLPCAgMAALI---- 145
Cdd:cd08235    77 VGDRVFVAPHVPcgechyclrgnenmcpnykkfgnlYDGGFAEYVRVPAWAV--KRGGVLK-LPDNVSFE-EAALVepla 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 146 ----SLDKIGISEGDTIFIEGgAGAVGQFAIQYAKQRGAD-VFTT-ASKRNHKLVKQLGADVVFDYSDKKLCEKIRRELG 219
Cdd:cd08235   153 ccinAQRKAGIKPGDTVLVIG-AGPIGLLHAMLAKASGARkVIVSdLNEFRLEFAKKLGADYTIDAAEEDLVEKVRELTD 231
                         250       260       270
                  ....*....|....*....|....*....|
gi 1889614189 220 PQGFDAVIDTIGGECTQRN-IELMRFCGRI 248
Cdd:cd08235   232 GRGADVVIVATGSPEAQAQaLELVRKGGRI 261
PGDH cd05288
Prostaglandin dehydrogenases; Prostaglandins and related eicosanoids are metabolized by the ...
15-338 3.10e-24

Prostaglandin dehydrogenases; Prostaglandins and related eicosanoids are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto-13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176190 [Multi-domain]  Cd Length: 329  Bit Score: 101.02  E-value: 3.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  15 TMRAIVL---PEPNEAI-DLADAELPVPDCADNELLVKVEYVGLNPV------DGqfaktgfckWQY--PHILGL----D 78
Cdd:cd05288     1 SNRQVVLakrPEGPPPPdDFELVEVPLPELKDGEVLVRTLYLSVDPYmrgwmsDA---------KSYspPVQLGEpmrgG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  79 AVGVVVKANKGVFPnVGQRVMWHANIGEQGALSeytkvPNFAVSVVPSGLNPGIAATLPCAGM---AALISLDKIG-ISE 154
Cdd:cd05288    72 GVGEVVESRSPDFK-VGDLVSGFLGWQEYAVVD-----GASGLRKLDPSLGLPLSAYLGVLGMtglTAYFGLTEIGkPKP 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 155 GDTIFIEGGAGAVGQFAIQYAKQRGADVFTTAS---KRNHkLVKQLGADVVFDYSDKKLCEKIRRELgPQGFDAVIDTIG 231
Cdd:cd05288   146 GETVVVSAAAGAVGSVVGQIAKLLGARVVGIAGsdeKCRW-LVEELGFDAAINYKTPDLAEALKEAA-PDGIDVYFDNVG 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 232 GECTQRNIELMRFCGRIACL----------NPLPYFDQDLMYHRA--PNISVVSIGGAWlanslcaQQRLSFMGNLLLEG 299
Cdd:cd05288   224 GEILDAALTLLNKGGRIALCgaisqynatePPGPKNLGNIITKRLtmQGFIVSDYADRF-------PEALAELAKWLAEG 296
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1889614189 300 AvsgdIKHPEITPVDFsaESVSQALNKQLAGGFTGKQVV 338
Cdd:cd05288   297 K----LKYREDVVEGL--ENAPEAFLGLFTGKNTGKLVV 329
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
16-338 9.00e-24

D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related alcohol dehydrogenases. AraDH is a member of the medium chain dehydrogenase/reductase family and catalyzes the NAD(P)-dependent oxidation of D-arabinose and other pentoses, the initial step in the metabolism of d-arabinose into 2-oxoglutarate. Like the alcohol dehydrogenases, AraDH binds a zinc in the catalytic cleft as well as a distal structural zinc. AraDH forms homotetramers as a dimer of dimers. AraDH replaces a conserved catalytic His with replace with Arg, compared to the canonical ADH site. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176187 [Multi-domain]  Cd Length: 340  Bit Score: 99.94  E-value: 9.00e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNEAidLADAELPVPDCADNELLVKVEYVG-----LNPVDGQFAKTGfcKWQYPHILGLDAVGVVVKANKGV 90
Cdd:cd05284     1 MKAARLYEYGKP--LRLEDVPVPEPGPGQVLVRVGGAGvchsdLHVIDGVWGGIL--PYKLPFTLGHENAGWVEEVGSGV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  91 FP-NVGQRVMWHA------------------------NIGEQGALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALI 145
Cdd:cd05284    77 DGlKEGDPVVVHPpwgcgtcrycrrgeenycenarfpGIGTDGGFAEYLLVPSRRLVKLPRGLDPVEAAPLADAGLTAYH 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 146 SLDKIG--ISEGDTIFIEgGAGAVGQFAIQYAKQRGA------DVftTASKRnhKLVKQLGADVVFDySDKKLCEKIRRE 217
Cdd:cd05284   157 AVKKALpyLDPGSTVVVI-GVGGLGHIAVQILRALTPatviavDR--SEEAL--KLAERLGADHVLN-ASDDVVEEVREL 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 218 LGPQGFDAVIDTIGGECTQRN-IELMRFCGRIACLN-----PLPYFDqDLmyhrAPNISVVSiggawlanslcaqqrlSF 291
Cdd:cd05284   231 TGGRGADAVIDFVGSDETLALaAKLLAKGGRYVIVGygghgRLPTSD-LV----PTEISVIG----------------SL 289
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1889614189 292 MGNL-----LLEGAVSGDIKhPEITPVDFsaESVSQALNKQLAGGFTGKQVV 338
Cdd:cd05284   290 WGTRaelveVVALAESGKVK-VEITKFPL--EDANEALDRLREGRVTGRAVL 338
oxido_YhdH TIGR02823
putative quinone oxidoreductase, YhdH/YhfP family; This model represents a subfamily of ...
17-250 1.40e-23

putative quinone oxidoreductase, YhdH/YhfP family; This model represents a subfamily of pfam00107 as defined by Pfam, a superfamily in which some members are zinc-binding medium-chain alcohol dehydrogenases while others are quinone oxidoreductases with no bound zinc. This subfamily includes proteins studied crystallographically for insight into function: YhdH from Escherichia coli and YhfP from Bacillus subtilis. Members bind NADPH or NAD, but not zinc. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274315 [Multi-domain]  Cd Length: 323  Bit Score: 99.17  E-value: 1.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  17 RAIVLPEPNEAIDLADAELPVPDCADNELLVKVEYVGLNPVDGqFAKTGFCKW--QYPHILGLDAVGVVVKANKGVFpNV 94
Cdd:TIGR02823   1 KALVVEKEDGKVSAQVETLDLSDLPEGDVLIKVAYSSLNYKDA-LAITGKGGVvrSYPMIPGIDAAGTVVSSEDPRF-RE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  95 GQRVMWHA-NIGEQ--GALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISLDKI---GISEGD-TIFIEGGAGAV 167
Cdd:TIGR02823  79 GDEVIVTGyGLGVShdGGYSQYARVPADWLVPLPEGLSLREAMALGTAGFTAALSVMALernGLTPEDgPVLVTGATGGV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 168 GQFAIQYAKQRGADVFT-TASKRNHKLVKQLGADVVFDYSDkklCEKIRRELGPQGFDAVIDTIGGECTQRNIELMRFCG 246
Cdd:TIGR02823 159 GSLAVAILSKLGYEVVAsTGKAEEEDYLKELGASEVIDRED---LSPPGKPLEKERWAGAVDTVGGHTLANVLAQLKYGG 235

                  ....
gi 1889614189 247 RIAC 250
Cdd:TIGR02823 236 AVAA 239
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
71-247 2.72e-23

polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that is similar to fatty acid synthesis. Enoyl reductase reduces a double to single bond. Erythromycin is one example of a polyketide generated by 3 complex enzymes (megasynthases). 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176213 [Multi-domain]  Cd Length: 303  Bit Score: 97.88  E-value: 2.72e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  71 YPHILGLDAVGVVVKANKGVFP-NVGQRVMwhANIGEQ-GALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISLD 148
Cdd:cd08251    37 YPFTPGFEASGVVRAVGPHVTRlAVGDEVI--AGTGESmGGHATLVTVPEDQVVRKPASLSFEEACALPVVFLTVIDAFA 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 149 KIGISEGDTIFIEGGAGAVGQFAIQYAKQRGADVFTTASkRNHKL--VKQLGADVVFDYSDKKLCEKIRRELGPQGFDAV 226
Cdd:cd08251   115 RAGLAKGEHILIQTATGGTGLMAVQLARLKGAEIYATAS-SDDKLeyLKQLGVPHVINYVEEDFEEEIMRLTGGRGVDVV 193
                         170       180
                  ....*....|....*....|.
gi 1889614189 227 IDTIGGECTQRNIELMRFCGR 247
Cdd:cd08251   194 INTLSGEAIQKGLNCLAPGGR 214
MDR_yhfp_like cd08289
Yhfp putative quinone oxidoreductases; yhfp putative quinone oxidoreductases (QOR). QOR ...
17-233 3.27e-23

Yhfp putative quinone oxidoreductases; yhfp putative quinone oxidoreductases (QOR). QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176249 [Multi-domain]  Cd Length: 326  Bit Score: 98.17  E-value: 3.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  17 RAIVLPEPNEAIDLADAELPVPDCADNELLVKVEYVGLNPVDGQFAK-TGFCKWQYPHILGLDAVGVVVKANKGVFpNVG 95
Cdd:cd08289     2 QALVVEKDEDDVSVSVKNLTLDDLPEGDVLIRVAYSSVNYKDGLASIpGGKIVKRYPFIPGIDLAGTVVESNDPRF-KPG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  96 QRVM---WHANIGEQGALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISLDKI---GIS-EGDTIFIEGGAGAVG 168
Cdd:cd08289    81 DEVIvtsYDLGVSHHGGYSEYARVPAEWVVPLPKGLTLKEAMILGTAGFTAALSIHRLeenGLTpEQGPVLVTGATGGVG 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1889614189 169 QFAIQYAKQRGADVftTASKRN---HKLVKQLGADVVFDYSDkkLCEKIRRELGPQGFDAVIDTIGGE 233
Cdd:cd08289   161 SLAVSILAKLGYEV--VASTGKadaADYLKKLGAKEVIPREE--LQEESIKPLEKQRWAGAVDPVGGK 224
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
16-231 1.66e-22

L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine, via NAD(H)-dependent oxidation. THD is a member of the zinc-requiring, medium chain NAD(H)-dependent alcohol dehydrogenase family (MDR). MDRs have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose.


Pssm-ID: 176196 [Multi-domain]  Cd Length: 334  Bit Score: 96.06  E-value: 1.66e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNeaiDLADAELPVPDCADNELLVKVEYVGLNPVD-----GQFAKTgfckwqYPHILGLDAVGVVVKANKGV 90
Cdd:cd08234     1 MKALVYEGPG---ELEVEEVPVPEPGPDEVLIKVAACGICGTDlhiyeGEFGAA------PPLVPGHEFAGVVVAVGSKV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  91 --FpNVGQRVMWHANI----------GEQ--------------GALSEYTKVPNFAVSVVPSGLNPGIAAT---LPCagm 141
Cdd:cd08234    72 tgF-KVGDRVAVDPNIycgecfycrrGRPnlcenltavgvtrnGGFAEYVVVPAKQVYKIPDNLSFEEAALaepLSC--- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 142 aALISLDKIGISEGDTIFIEgGAGAVGQFAIQYAKQRGADVFT----TASKRnhKLVKQLGADVVFDYSDKKlcEKIRRE 217
Cdd:cd08234   148 -AVHGLDLLGIKPGDSVLVF-GAGPIGLLLAQLLKLNGASRVTvaepNEEKL--ELAKKLGATETVDPSRED--PEAQKE 221
                         250
                  ....*....|....
gi 1889614189 218 LGPQGFDAVIDTIG 231
Cdd:cd08234   222 DNPYGFDVVIEATG 235
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
15-248 2.57e-22

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 95.87  E-value: 2.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  15 TMRAIVLPEPNEAIDLADAELPVPDCADNELLVKVEYVGLNpvdgqfaKTGFCKWQ--YP------HILGLDAVGVVVKA 86
Cdd:PTZ00354    1 MMRAVTLKGFGGVDVLKIGESPKPAPKRNDVLIKVSAAGVN-------RADTLQRQgkYPpppgssEILGLEVAGYVEDV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  87 NKGV--FPNvGQRVMwhaNIGEQGALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISLDKIG-ISEGDTIFIEGG 163
Cdd:PTZ00354   74 GSDVkrFKE-GDRVM---ALLPGGGYAEYAVAHKGHVMHIPQGYTFEEAAAIPEAFLTAWQLLKKHGdVKKGQSVLIHAG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 164 AGAVGQFAIQYAKQRG-ADVFTTASKRNHKLVKQLGADVVFDYSD-KKLCEKIRRELGPQGFDAVIDTIGGECTQRNIEL 241
Cdd:PTZ00354  150 ASGVGTAAAQLAEKYGaATIITTSSEEKVDFCKKLAAIILIRYPDeEGFAPKVKKLTGEKGVNLVLDCVGGSYLSETAEV 229

                  ....*..
gi 1889614189 242 MRFCGRI 248
Cdd:PTZ00354  230 LAVDGKW 236
CurA COG2130
NADPH-dependent curcumin reductase CurA [Secondary metabolites biosynthesis, transport and ...
13-340 1.26e-21

NADPH-dependent curcumin reductase CurA [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 441733 [Multi-domain]  Cd Length: 333  Bit Score: 93.59  E-value: 1.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  13 PQTMRAIVLPE-PNEAIDLAD---AELPVPDCADNELLVKVEYVGL--------NPVDGQFAktgfckwqyPHILG--LD 78
Cdd:COG2130     2 MTTNRQIVLASrPEGEPTPEDfrlEEVPVPEPGDGEVLVRNLYLSVdpymrgrmSDAKSYAP---------PVELGevMR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  79 --AVGVVVKANKGVFPnVGQRVMwhANIGEQgalsEYTKVPNFAVSVVPSGLNPgIAATLPCAGMA---ALISLDKIG-I 152
Cdd:COG2130    73 ggAVGEVVESRHPDFA-VGDLVL--GMLGWQ----DYAVSDGAGLRKVDPSLAP-LSAYLGVLGMPgltAYFGLLDIGkP 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 153 SEGDTIFIEGGAGAVGQFAIQYAKQRGADVFTTA---SKRNHkLVKQLGADVVFDYSDKKLCEKIrRELGPQGFDAVIDT 229
Cdd:COG2130   145 KAGETVVVSAAAGAVGSVVGQIAKLKGCRVVGIAggaEKCRY-LVEELGFDAAIDYKAGDLAAAL-AAACPDGIDVYFDN 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 230 IGGECTQRNIELMRFCGRIAC-----------LNPLPYFDQDLMYHRApnisvvSIGG------------------AWLA 280
Cdd:COG2130   223 VGGEILDAVLPLLNTFARIAVcgaisqynatePPPGPRNLGQLLVKRL------RMQGfivfdhadrfpeflaelaGWVA 296
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1889614189 281 nslcaqqrlsfmgnlllegavSGDIKHPEiTPVD-FsaESVSQALNKQLAGGFTGKQVVKV 340
Cdd:COG2130   297 ---------------------EGKLKYRE-TVVEgL--ENAPEAFLGLFEGENFGKLLVKV 333
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
16-339 6.57e-21

6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, and other MDR family members; This group contains enzymes of the zinc-dependent alcohol dehydrogenase family, including members (aka MDR) identified as 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase and N-benzyl-3-pyrrolidinol dehydrogenase. 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase catalyzes the conversion of 6-Hydroxycyclohex-1-enecarbonyl-CoA and NAD+ to 6-Ketoxycyclohex-1-ene-1-carboxyl-CoA,NADH, and H+. This group displays the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176216 [Multi-domain]  Cd Length: 338  Bit Score: 91.92  E-value: 6.57e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNEAIdLADAELPVPDCADNELLVKVEYVGLNPVDGQFAKTGFCKWQYPHI-LGLDAVGVVVKANKGVFP-N 93
Cdd:cd08254     1 MKAWRFHKGSKGL-LVLEEVPVPEPGPGEVLVKVKAAGVCHSDLHILDGGVPTLTKLPLtLGHEIAGTVVEVGAGVTNfK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  94 VGQRVMWHAN------------------------IGEQGALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISLDK 149
Cdd:cd08254    80 VGDRVAVPAVipcgacalcrrgrgnlclnqgmpgLGIDGGFAEYIVVPARALVPVPDGVPFAQAAVATDAVLTPYHAVVR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 150 IG-ISEGDTIFIeGGAGAVGQFAIQYAKQRGADVftTASKRN-HKL--VKQLGADVVFDYSDKKLCEKIRRELgPQGFDA 225
Cdd:cd08254   160 AGeVKPGETVLV-IGLGGLGLNAVQIAKAMGAAV--IAVDIKeEKLelAKELGADEVLNSLDDSPKDKKAAGL-GGGFDV 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 226 VIDTIGGECTQRN-IELMRFCGRIACL----NPLPYFDQDLMYHRapnISVV-SIGGAW--LANSLcaqqrlsfmgNLLL 297
Cdd:cd08254   236 IFDFVGTQPTFEDaQKAVKPGGRIVVVglgrDKLTVDLSDLIARE---LRIIgSFGGTPedLPEVL----------DLIA 302
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1889614189 298 EGAVSgdikhPEITPVDFSaeSVSQALNKQLAGGFTGKQVVK 339
Cdd:cd08254   303 KGKLD-----PQVETRPLD--EIPEVLERLHKGKVKGRVVLV 337
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
16-339 1.96e-19

6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the zinc-dependent alcohol dehydrogenase-like family of medium chain dehydrogenases/reductases catalyzes the conversion of 6-hydroxyhexanoate and NAD(+) to 6-oxohexanoate + NADH and H+. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176202 [Multi-domain]  Cd Length: 350  Bit Score: 87.67  E-value: 1.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNEAIDLADAELPVPdcADNELLVKVEYVG-----LNPVDGQF----AKTGFCK---WQYPHILGLDAVGVV 83
Cdd:cd08240     1 MKAAAVVEPGKPLEEVEIDTPKP--PGTEVLVKVTACGvchsdLHIWDGGYdlggGKTMSLDdrgVKLPLVLGHEIVGEV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  84 VKAN---KGVfpNVGQRVM---WHA---------------------NIGEQGALSEYTKVPNFAVSVVPSGLNPGIAATL 136
Cdd:cd08240    79 VAVGpdaADV--KVGDKVLvypWIGcgecpvclagdenlcakgralGIFQDGGYAEYVIVPHSRYLVDPGGLDPALAATL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 137 PCAGMAALISLDKIGISEGDTIFIEGGAGAVGQFAIQYAKQRG------ADVfttaSKRNHKLVKQLGADVVFDYSDKKL 210
Cdd:cd08240   157 ACSGLTAYSAVKKLMPLVADEPVVIIGAGGLGLMALALLKALGpaniivVDI----DEAKLEAAKAAGADVVVNGSDPDA 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 211 CEKIrRELGPQGFDAVIDTIGGECT-QRNIELMRFCGRIACLN--------PLPyfdqdLMYHRApnisvVSIGGawlan 281
Cdd:cd08240   233 AKRI-IKAAGGGVDAVIDFVNNSATaSLAFDILAKGGKLVLVGlfggeatlPLP-----LLPLRA-----LTIQG----- 296
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1889614189 282 slcaqqrlSFMGNL-----LLEGAVSGDIKHPEITpvDFSAESVSQALNKQLAGGFTGKQVVK 339
Cdd:cd08240   297 --------SYVGSLeelreLVALAKAGKLKPIPLT--ERPLSDVNDALDDLKAGKVVGRAVLK 349
CAD_like cd08296
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
16-230 2.45e-19

Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family, reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADHs), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176256 [Multi-domain]  Cd Length: 333  Bit Score: 87.30  E-value: 2.45e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNEAIDLADAELPVPdcADNELLVKVEYVGLNPVDGQFAKTGFCKWQYPHILGLDAVGVVVKANKGV--FpN 93
Cdd:cd08296     1 YKAVQVTEPGGPLELVERDVPLP--GPGEVLIKVEACGVCHSDAFVKEGAMPGLSYPRVPGHEVVGRIDAVGEGVsrW-K 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  94 VGQRVM--WHAN-----------------------IGEQGALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISLD 148
Cdd:cd08296    78 VGDRVGvgWHGGhcgtcdacrrgdfvhcengkvtgVTRDGGYAEYMLAPAEALARIPDDLDAAEAAPLLCAGVTTFNALR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 149 KIGISEGDTIFIEgGAGAVGQFAIQYAKQRGADVFTTASKRN-HKLVKQLGADVVFDYSDKKLCEKIrRELGpqGFDAVI 227
Cdd:cd08296   158 NSGAKPGDLVAVQ-GIGGLGHLAVQYAAKMGFRTVAISRGSDkADLARKLGAHHYIDTSKEDVAEAL-QELG--GAKLIL 233

                  ...
gi 1889614189 228 DTI 230
Cdd:cd08296   234 ATA 236
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
166-278 3.78e-19

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 82.27  E-value: 3.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 166 AVGQFAIQYAKQRGADVFTTA-SKRNHKLVKQLGADVVFDYSDKKLCEKIRRELGPQGFDAVIDTIG-GECTQRNIELMR 243
Cdd:pfam00107   1 GVGLAAIQLAKAAGAKVIAVDgSEEKLELAKELGADHVINPKETDLVEEIKELTGGKGVDVVFDCVGsPATLEQALKLLR 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1889614189 244 FCGRIACL----NPLPYFDQDLMYHrapNISVV-SIGGAW 278
Cdd:pfam00107  81 PGGRVVVVglpgGPLPLPLAPLLLK---ELTILgSFLGSP 117
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
16-264 2.31e-18

(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent medium chain alcohol dehydrogenase, catalyzes the NAD(+)-dependent oxidation of (2R,3R)-2,3-butanediol and meso-butanediol to acetoin. BDH functions as a homodimer. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit.


Pssm-ID: 176195 [Multi-domain]  Cd Length: 351  Bit Score: 84.51  E-value: 2.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNeaiDLADAELPVPDCADNELLVKVEYVG-----LN---------PVDGQFAKTGFckwQYPHILGLDAVG 81
Cdd:cd08233     1 MKAARYHGRK---DIRVEEVPEPPVKPGEVKIKVAWCGicgsdLHeyldgpifiPTEGHPHLTGE---TAPVTLGHEFSG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  82 VVVKANKGVF-PNVGQRVMWHANI-------------------------GEQGALSEYTKVPNFAVSVVPSGLNPGIAAT 135
Cdd:cd08233    75 VVVEVGSGVTgFKVGDRVVVEPTIkcgtcgackrglynlcdslgfiglgGGGGGFAEYVVVPAYHVHKLPDNVPLEEAAL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 136 L-PCAgmAALISLDKIGISEGDTIFIeGGAGAVGQFAIQYAKQRGAD---VFTTASKRnHKLVKQLGADVVFDYSDKKLC 211
Cdd:cd08233   155 VePLA--VAWHAVRRSGFKPGDTALV-LGAGPIGLLTILALKAAGASkiiVSEPSEAR-RELAEELGATIVLDPTEVDVV 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1889614189 212 EKIRRELGPQGFDAVIDTIGGECT-QRNIELMRFCGRIACL----NPLPYFDQDLMYH 264
Cdd:cd08233   231 AEVRKLTGGGGVDVSFDCAGVQATlDTAIDALRPRGTAVNVaiweKPISFNPNDLVLK 288
CAD cd08245
Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases ...
17-250 4.01e-18

Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family, reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes, or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176207 [Multi-domain]  Cd Length: 330  Bit Score: 83.91  E-value: 4.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  17 RAIVLPEPNEAIDLAdaELPVPDCADNELLVKVEYVG-----LNPVDGQFAKTgfckwQYPHILGLDAVGVVVKANKGVF 91
Cdd:cd08245     1 KAAVVHAAGGPLEPE--EVPVPEPGPGEVLIKIEACGvchtdLHAAEGDWGGS-----KYPLVPGHEIVGEVVEVGAGVE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  92 P-NVGQRV--MWH--------------ANIGE---------QGALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALI 145
Cdd:cd08245    74 GrKVGDRVgvGWLvgscgrceycrrglENLCQkavntgyttQGGYAEYMVADAEYTVLLPDGLPLAQAAPLLCAGITVYS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 146 SLDKIGISEGDTIFIEGgAGAVGQFAIQYAKQRGADVFT-TASKRNHKLVKQLGADVVFDySDKKLCEKirRELGpqGFD 224
Cdd:cd08245   154 ALRDAGPRPGERVAVLG-IGGLGHLAVQYARAMGFETVAiTRSPDKRELARKLGADEVVD-SGAELDEQ--AAAG--GAD 227
                         250       260
                  ....*....|....*....|....*..
gi 1889614189 225 AVIDTI-GGECTQRNIELMRFCGRIAC 250
Cdd:cd08245   228 VILVTVvSGAAAEAALGGLRRGGRIVL 254
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
16-248 4.98e-18

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176224 [Multi-domain]  Cd Length: 367  Bit Score: 83.96  E-value: 4.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNEAIDLAdaELPVPDCADNELLVKVEYVG-----LNPVDGQFAKTGfckwqyPHILGLDAVGVVVKANKGV 90
Cdd:cd08263     1 MKAAVLKGPNPPLTIE--EIPVPRPKEGEILIRVAACGvchsdLHVLKGELPFPP------PFVLGHEISGEVVEVGPNV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  91 -----FPnVGQRVM--W-------------HANIGEQ-------------------------------GALSEYTKVPNF 119
Cdd:cd08263    73 enpygLS-VGDRVVgsFimpcgkcrycargKENLCEDffaynrlkgtlydgttrlfrldggpvymysmGGLAEYAVVPAT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 120 AVSVVPSGLNPGIAATLPCAGMAALISLDKIGISE-GDTIFIEgGAGAVGQFAIQYAKQRGADVFTTASKRNHKL--VKQ 196
Cdd:cd08263   152 ALAPLPESLDYTESAVLGCAGFTAYGALKHAADVRpGETVAVI-GVGGVGSSAIQLAKAFGASPIIAVDVRDEKLakAKE 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1889614189 197 LGADVVFDYSDKKLCEKIRRELGPQGFDAVIDTIGGECT-QRNIELMRFCGRI 248
Cdd:cd08263   231 LGATHTVNAAKEDAVAAIREITGGRGVDVVVEALGKPETfKLALDVVRDGGRA 283
CAD2 cd08298
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
16-274 1.11e-17

Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Cinnamyl alcohol dehydrogenases (CAD) reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176258 [Multi-domain]  Cd Length: 329  Bit Score: 82.62  E-value: 1.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVL--PEPNEAIDLADAELPVPDCADNELLVKVEYVG-----LNPVDGQFAKTGFckwqyPHILGLDAVGVVVKANK 88
Cdd:cd08298     1 MKAMVLekPGPIEENPLRLTEVPVPEPGPGEVLIKVEACGvcrtdLHIVEGDLPPPKL-----PLIPGHEIVGRVEAVGP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  89 GV--FpNVGQRV----MWHA------------NI-------GEQ--GALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGM 141
Cdd:cd08298    76 GVtrF-SVGDRVgvpwLGSTcgecrycrsgreNLcdnarftGYTvdGGYAEYMVADERFAYPIPEDYDDEEAAPLLCAGI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 142 AALISLDKIGISEGDTIFIEGgAGAVGQFAIQYAKQRGADVFTTASKRNH-KLVKQLGADVVFDYSDKKlcekirrelgP 220
Cdd:cd08298   155 IGYRALKLAGLKPGQRLGLYG-FGASAHLALQIARYQGAEVFAFTRSGEHqELARELGADWAGDSDDLP----------P 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1889614189 221 QGFDAVIDTIG-GECTQRNIELMRFCGRIAC----LNPLPYFDQDLMYHRAPNISVVSI 274
Cdd:cd08298   224 EPLDAAIIFAPvGALVPAALRAVKKGGRVVLagihMSDIPAFDYELLWGEKTIRSVANL 282
MDR_yhdh cd08288
Yhdh putative quinone oxidoreductases; Yhdh putative quinone oxidoreductases (QOR). QOR ...
16-232 7.21e-17

Yhdh putative quinone oxidoreductases; Yhdh putative quinone oxidoreductases (QOR). QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176248 [Multi-domain]  Cd Length: 324  Bit Score: 79.89  E-value: 7.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNEAIDLADAELPVPDCADNELLVKVEYVGLNPVDGqFAKTGFCKW--QYPHILGLDAVGVVVKANKGVFpN 93
Cdd:cd08288     1 FKALVLEKDDGGTSAELRELDESDLPEGDVTVEVHYSTLNYKDG-LAITGKGGIvrTFPLVPGIDLAGTVVESSSPRF-K 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  94 VGQRVM---WHanIGEQ--GALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALIS---LDKIGISEGD-TIFIEGGA 164
Cdd:cd08288    79 PGDRVVltgWG--VGERhwGGYAQRARVKADWLVPLPEGLSARQAMAIGTAGFTAMLCvmaLEDHGVTPGDgPVLVTGAA 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1889614189 165 GAVGQFAIQYAKQRGADVftTASK---RNHKLVKQLGADVVFDysdkklcekiRRELGPQG-------FDAVIDTIGG 232
Cdd:cd08288   157 GGVGSVAVALLARLGYEV--VASTgrpEEADYLRSLGASEIID----------RAELSEPGrplqkerWAGAVDTVGG 222
leukotriene_B4_DH_like cd08294
13-PGR is a bifunctional enzyme with delta-13 15-prostaglandin reductase and leukotriene B4 12 ...
80-340 9.81e-17

13-PGR is a bifunctional enzyme with delta-13 15-prostaglandin reductase and leukotriene B4 12 hydroxydehydrogenase activity; Prostaglandins and related eicosanoids are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto- 13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176254 [Multi-domain]  Cd Length: 329  Bit Score: 79.61  E-value: 9.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  80 VGVVVKANKGVFPnVGQRVM----W--HANIGEQGAlSEYTKVPNFAVSVVPSGLNPGiAATLPcaGMAALISLDKIG-I 152
Cdd:cd08294    67 VAKVIESKNSKFP-VGTIVVasfgWrtHTVSDGKDQ-PDLYKLPADLPDDLPPSLALG-VLGMP--GLTAYFGLLEICkP 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 153 SEGDTIFIEGGAGAVGQFAIQYAKQRGADV--FTTASKRNHKLvKQLGADVVFDYSDKKLCEKIrRELGPQGFDAVIDTI 230
Cdd:cd08294   142 KAGETVVVNGAAGAVGSLVGQIAKIKGCKVigCAGSDDKVAWL-KELGFDAVFNYKTVSLEEAL-KEAAPDGIDCYFDNV 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 231 GGECTQRNIELMRFCGRIA-----------CLNPLPYFDQDLMYHRapnISVVS-IGGAWLANSLCAQQRLSfmgNLLLE 298
Cdd:cd08294   220 GGEFSSTVLSHMNDFGRVAvcgsistyndkEPKKGPYVQETIIFKQ---LKMEGfIVYRWQDRWPEALKQLL---KWIKE 293
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1889614189 299 GAvsgdIKHPEITPVDFsaESVSQALNKQLAGGFTGKQVVKV 340
Cdd:cd08294   294 GK----LKYREHVTEGF--ENMPQAFIGMLKGENTGKAIVKV 329
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
17-231 1.00e-16

Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This group contains the hypothetical TM0436 alcohol dehydrogenase from Thermotoga maritima, proteins annotated as 5-exo-alcohol dehydrogenase, and other members of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family. MDR, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176193 [Multi-domain]  Cd Length: 361  Bit Score: 80.00  E-value: 1.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  17 RAIVLPEPNEAIDLAdaELPVPDCADNELLVKVEYVG-----LNPVDGQFAKTgfckwQYPHILGLDAVGVVVKANKGVF 91
Cdd:cd08231     2 RAAVLTGPGKPLEIR--EVPLPDLEPGAVLVRVRLAGvcgsdVHTVAGRRPRV-----PLPIILGHEGVGRVVALGGGVT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  92 PN-------VGQRVMW----------HANIGEQ---------------------GALSEYTKV-PNFAVSVVPSGLNPGI 132
Cdd:cd08231    75 TDvageplkVGDRVTWsvgapcgrcyRCLVGDPtkcenrkkygheascddphlsGGYAEHIYLpPGTAIVRVPDNVPDEV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 133 AATLPCAGMAALISLDKIG-ISEGDTIFIEGgAGAVGQFAIQYAKQRGAD--VFTTASKRNHKLVKQLGADVVFDYSDKK 209
Cdd:cd08231   155 AAPANCALATVLAALDRAGpVGAGDTVVVQG-AGPLGLYAVAAAKLAGARrvIVIDGSPERLELAREFGADATIDIDELP 233
                         250       260
                  ....*....|....*....|....*
gi 1889614189 210 LCEKIRREL---GPQGFDAVIDTIG 231
Cdd:cd08231   234 DPQRRAIVRditGGRGADVVIEASG 258
THR_DH_like cd08239
L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as ...
16-251 1.93e-15

L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as a threonine dehydrogenase. L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine via NAD(H)-dependent oxidation. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Zinc-dependent ADHs are medium chain dehydrogenase/reductase type proteins (MDRs) and have a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. In addition to alcohol dehydrogenases, this group includes quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176201 [Multi-domain]  Cd Length: 339  Bit Score: 76.20  E-value: 1.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEpNEAIDLADAELPVPdcADNELLVKVEYVGLNPVDGQFAKTGFCKWQYPHIL-GLDAVGVVVKANKGVF-PN 93
Cdd:cd08239     1 MRGAVFPG-DRTVELREFPVPVP--GPGEVLLRVKASGLCGSDLHYYYHGHRAPAYQGVIpGHEPAGVVVAVGPGVThFR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  94 VGQRVMWH-----------------------ANIGEQ--GALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISLD 148
Cdd:cd08239    78 VGDRVMVYhyvgcgacrncrrgwmqlctskrAAYGWNrdGGHAEYMLVPEKTLIPLPDDLSFADGALLLCGIGTAYHALR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 149 KIGISEGDTIFIEGgAGAVGQFAIQYAKQRGA-DVFTT-ASKRNHKLVKQLGADVVFDySDKKLCEKIRRELGPQGFDAV 226
Cdd:cd08239   158 RVGVSGRDTVLVVG-AGPVGLGALMLARALGAeDVIGVdPSPERLELAKALGADFVIN-SGQDDVQEIRELTSGAGADVA 235
                         250       260
                  ....*....|....*....|....*.
gi 1889614189 227 IDTIGGECTQRN-IELMRFCGRIACL 251
Cdd:cd08239   236 IECSGNTAARRLaLEAVRPWGRLVLV 261
crotonyl_coA_red cd08246
crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase ...
12-207 2.11e-15

crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase/reductase family, catalyzes the NADPH-dependent conversion of crotonyl-CoA to butyryl-CoA, a step in (2S)-methylmalonyl-CoA production for straight-chain fatty acid biosynthesis. Like enoyl reductase, another enzyme in fatty acid synthesis, crotonyl-CoA reductase is a member of the zinc-dependent alcohol dehydrogenase-like medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176208 [Multi-domain]  Cd Length: 393  Bit Score: 76.30  E-value: 2.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  12 IPQTMRA-IVLPE----PNEAIDLADaeLPVPDCADNELLVKVEYVGLN----------PVDGQFAKTGFCKWQYPHILG 76
Cdd:cd08246     9 VPEKMYAfAIRPErygdPAQAIQLED--VPVPELGPGEVLVAVMAAGVNynnvwaalgePVSTFAARQRRGRDEPYHIGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  77 LDAVGVVVKANKGVFP-NVGQRVMWHANIGEQ-------------------------GALSEYTKVPNFAVSVVPSGLNP 130
Cdd:cd08246    87 SDASGIVWAVGEGVKNwKVGDEVVVHCSVWDGndperaggdpmfdpsqriwgyetnyGSFAQFALVQATQLMPKPKHLSW 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 131 GIAATLPCAGMAA---LISLDKIGISEGDTIFIEGGAGAVGQFAIQYAKQRGAD-VFTTASKRNHKLVKQLGADVVFDYS 206
Cdd:cd08246   167 EEAAAYMLVGATAyrmLFGWNPNTVKPGDNVLIWGASGGLGSMAIQLARAAGANpVAVVSSEEKAEYCRALGAEGVINRR 246

                  .
gi 1889614189 207 D 207
Cdd:cd08246   247 D 247
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
23-340 4.24e-15

2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176250 [Multi-domain]  Cd Length: 341  Bit Score: 74.95  E-value: 4.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  23 EPNEAIDLADAELPvPDCADNELLVKVEYVGLNPVD-----GQFAKTGFCKWQYPHILGLDAVGVVVKANKGVF-PNVGQ 96
Cdd:cd08290    11 EPKEVLQLESYEIP-PPGPPNEVLVKMLAAPINPADinqiqGVYPIKPPTTPEPPAVGGNEGVGEVVKVGSGVKsLKPGD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  97 RVMwhANIGEQGALSEYTKVPNFAVSVVPSGLNPGIAATL---PCAgmaALISL-DKIGISEGDTIFIEGGAGAVGQFAI 172
Cdd:cd08290    90 WVI--PLRPGLGTWRTHAVVPADDLIKVPNDVDPEQAATLsvnPCT---AYRLLeDFVKLQPGDWVIQNGANSAVGQAVI 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 173 QYAKQRGADVFTTASKRN-----HKLVKQLGADVVFDYSD--KKLCEKIRRELGPQGFDAVIDTIGGECTQRnieLMRFC 245
Cdd:cd08290   165 QLAKLLGIKTINVVRDRPdleelKERLKALGADHVLTEEElrSLLATELLKSAPGGRPKLALNCVGGKSATE---LARLL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 246 GRIACL--------NPLPYFDQDLMYHrapNISVVsigGAWL------ANSlcaQQRLSfMGNLLLEGAVSGDIKHPEIT 311
Cdd:cd08290   242 SPGGTMvtyggmsgQPVTVPTSLLIFK---DITLR---GFWLtrwlkrANP---EEKED-MLEELAELIREGKLKAPPVE 311
                         330       340       350
                  ....*....|....*....|....*....|
gi 1889614189 312 PVDF-SAESVSQALNKQLAGGFTGKQVVKV 340
Cdd:cd08290   312 KVTDdPLEEFKDALANALKGGGGGKQVLVM 341
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
16-247 1.16e-14

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. This group has the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176221 [Multi-domain]  Cd Length: 345  Bit Score: 73.79  E-value: 1.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNEAIDLAdaELPVPDCADNELLVKVEyvglnpvdgqfaKTGFCK-----WQ-------YPHILGLDAVGVV 83
Cdd:cd08260     1 MRAAVYEEFGEPLEIR--EVPDPEPPPDGVVVEVE------------ACGVCRsdwhgWQghdpdvtLPHVPGHEFAGVV 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  84 VKANKGV--FpNVGQRVM---------------WHANIGEQ---------GALSEYTKVPNFAVSVV--PSGLNPGIAAT 135
Cdd:cd08260    67 VEVGEDVsrW-RVGDRVTvpfvlgcgtcpycraGDSNVCEHqvqpgfthpGSFAEYVAVPRADVNLVrlPDDVDFVTAAG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 136 LPCAGMAALISL-DKIGISEGDTIFIEgGAGAVGQFAIQYAKQRGADVftTASKRN-HKL--VKQLGADVVFDYSDKKLC 211
Cdd:cd08260   146 LGCRFATAFRALvHQARVKPGEWVAVH-GCGGVGLSAVMIASALGARV--IAVDIDdDKLelARELGAVATVNASEVEDV 222
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1889614189 212 EKIRRELGPQGFDAVIDTIGGECTQRN-IELMRFCGR 247
Cdd:cd08260   223 AAAVRDLTGGGAHVSVDALGIPETCRNsVASLRKRGR 259
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
34-249 1.26e-14

Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176230 [Multi-domain]  Cd Length: 312  Bit Score: 73.54  E-value: 1.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  34 ELPVPDCADNELLVKVEYVGL-----------NPVDGQFAKTGFckwqyphiLGLDAVGVVVKANKGVFP-NVGQRVmwh 101
Cdd:cd08269    11 EHPRPTPGPGQVLVRVEGCGVcgsdlpafnqgRPWFVYPAEPGG--------PGHEGWGRVVALGPGVRGlAVGDRV--- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 102 ANIGEqGALSEYTKVPNFAVSVVPSGLN--PGIAATLPCAgmaaLISLDKIGISEGDTIFIEGgAGAVGQFAIQYAKQRG 179
Cdd:cd08269    80 AGLSG-GAFAEYDLADADHAVPLPSLLDgqAFPGEPLGCA----LNVFRRGWIRAGKTVAVIG-AGFIGLLFLQLAAAAG 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1889614189 180 ADVFTTASKRNH--KLVKQLGADVVFDYSDKKLCEKIRRELGPQGFDAVIDTIGGECTqRN--IELMRFCGRIA 249
Cdd:cd08269   154 ARRVIAIDRRPArlALARELGATEVVTDDSEAIVERVRELTGGAGADVVIEAVGHQWP-LDlaGELVAERGRLV 226
B4_12hDH TIGR02825
leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 ...
25-249 1.88e-14

leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 12-hydroxydehydrogenase is an NADP-dependent enzyme of arachidonic acid metabolism, responsible for converting leukotriene B4 to the much less active metabolite 12-oxo-leukotriene B4. The BRENDA database lists leukotriene B4 12-hydroxydehydrogenase as one of the synonyms of 2-alkenal reductase (EC 1.3.1.74), while 1.3.1.48 is 15-oxoprostaglandin 13-reductase.


Pssm-ID: 131872 [Multi-domain]  Cd Length: 325  Bit Score: 73.11  E-value: 1.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  25 NEAIDLADAELPvpDCADNELLVKVEYVGLNPvdgqFAKTGFCKWQYPHILGLDAVGVVVKANKGVFPnVGQRVM----W 100
Cdd:TIGR02825  16 DSDFELKTVELP--PLNNGEVLLEALFLSVDP----YMRVAAKRLKEGDTMMGQQVARVVESKNVALP-KGTIVLaspgW 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 101 HANIGEQGalSEYTKVPNFAVSVVPSGLNPGiaaTLPCAGMAALISLDKI-GISEGDTIFIEGGAGAVGQFAIQYAKQRG 179
Cdd:TIGR02825  89 TSHSISDG--KDLEKLLTEWPDTLPLSLALG---TVGMPGLTAYFGLLEIcGVKGGETVMVNAAAGAVGSVVGQIAKLKG 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1889614189 180 ADVFTTA-SKRNHKLVKQLGADVVFDYSDKKLCEKIRRELGPQGFDAVIDTIGGECTQRNIELMRFCGRIA 249
Cdd:TIGR02825 164 CKVVGAAgSDEKVAYLKKLGFDVAFNYKTVKSLEETLKKASPDGYDCYFDNVGGEFSNTVIGQMKKFGRIA 234
ETR_like_1 cd08291
2-enoyl thioester reductase (ETR) like proteins, child 1; 2-enoyl thioester reductase (ETR) ...
16-242 3.66e-14

2-enoyl thioester reductase (ETR) like proteins, child 1; 2-enoyl thioester reductase (ETR) like proteins. ETR catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the 2-enoyl thioester reductase (ETR) like proteins. ETR catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176251 [Multi-domain]  Cd Length: 324  Bit Score: 72.25  E-value: 3.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNEAIDLADAELP---VPDCADNELLVKVEYVGLNPVD-----GQFAKTGfckwQYPHILGLDAVGVVVKAN 87
Cdd:cd08291     1 MKALLLEEYGKPLEVKELSLPepeVPEPGPGEVLIKVEAAPINPSDlgflkGQYGSTK----ALPVPPGFEGSGTVVAAG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  88 KGVFPN--VGQRVMWHAniGEQGALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISLDKIgISEGDTIFIE-GGA 164
Cdd:cd08291    77 GGPLAQslIGKRVAFLA--GSYGTYAEYAVADAQQCLPLPDGVSFEQGASSFVNPLTALGMLETA-REEGAKAVVHtAAA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 165 GAVGQFAIQYAKQRGADVFTTASKRNH-KLVKQLGADVVFDYSDKKLCEKIR---RELGPQ-GFDAVidtiGGECTQRNI 239
Cdd:cd08291   154 SALGRMLVRLCKADGIKVINIVRRKEQvDLLKKIGAEYVLNSSDPDFLEDLKeliAKLNATiFFDAV----GGGLTGQIL 229

                  ...
gi 1889614189 240 ELM 242
Cdd:cd08291   230 LAM 232
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
44-307 6.97e-14

2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family has members identified as 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide A dehydrogenase and alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176217 [Multi-domain]  Cd Length: 277  Bit Score: 70.76  E-value: 6.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  44 ELLVKVEYVGLNPVDGqfaktgfcKWQYPHILGLDAVGVVVKANKGVFP-NVGQRVMWHanigeqGALSEYTKVPNFAVS 122
Cdd:cd08255     1 DLVLDTALEGLSTGTE--------KLPLPLPPGYSSVGRVVEVGSGVTGfKPGDRVFCF------GPHAERVVVPANLLV 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 123 VVPSGLNPGIAATLPcAGMAALISLDKIGISEGDTIFIEGgAGAVGQFAIQYAKQRGA-DVFTT-ASKRNHKLVKQLGAD 200
Cdd:cd08255    67 PLPDGLPPERAALTA-LAATALNGVRDAEPRLGERVAVVG-LGLVGLLAAQLAKAAGArEVVGVdPDAARRELAEALGPA 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 201 --VVFDysdkklcekIRRELGPQGFDAVIDTIG-GECTQRNIELMRFCGRI-----ACLNPLPYfdQDLMYHRAPNI--S 270
Cdd:cd08255   145 dpVAAD---------TADEIGGRGADVVIEASGsPSALETALRLLRDRGRVvlvgwYGLKPLLL--GEEFHFKRLPIrsS 213
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1889614189 271 VVSIGGAWLAN-SLCAQQRLSFMGNLLLEGAVSGDIKH 307
Cdd:cd08255   214 QVYGIGRYDRPrRWTEARNLEEALDLLAEGRLEALITH 251
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
16-252 2.41e-13

Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. Formaldehyde dehydrogenase (aka ADH3) may be the ancestral form of alcohol dehydrogenase, which evolved to detoxify formaldehyde. This CD contains glutathione dependant FDH, glutathione independent FDH, and related alcohol dehydrogenases. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. Unlike typical FDH, Pseudomonas putida aldehyde-dismutating FDH (PFDH) is glutathione-independent. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176181 [Multi-domain]  Cd Length: 347  Bit Score: 70.00  E-value: 2.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNEaIDLADAELPVPDCADnELLVKVEYVGLNPVDGQFAKTGFCKWQYPHILGLDAVGVVVKANKGVFP-NV 94
Cdd:cd05278     1 MKALVYLGPGK-IGLEEVPDPKIQGPH-DAIVRVTATSICGSDLHIYRGGVPGAKHGMILGHEFVGEVVEVGSDVKRlKP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  95 GQRVMWHANI---------------------------GEQGALSEYTKVP--NFAVSVVPSGLNPGIAATLPCAGMAALI 145
Cdd:cd05278    79 GDRVSVPCITfcgrcrfcrrgyhahcenglwgwklgnRIDGGQAEYVRVPyaDMNLAKIPDGLPDEDALMLSDILPTGFH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 146 SLDKIGISEGDTIFIEGgAGAVGQFAIQYAKQRGADVFTTASKRNH--KLVKQLGADVVFDYSDKKLCEKIRRELGPQGF 223
Cdd:cd05278   159 GAELAGIKPGSTVAVIG-AGPVGLCAVAGARLLGAARIIAVDSNPErlDLAKEAGATDIINPKNGDIVEQILELTGGRGV 237
                         250       260       270
                  ....*....|....*....|....*....|
gi 1889614189 224 DAVIDTIGGECT-QRNIELMRFCGRIACLN 252
Cdd:cd05278   238 DCVIEAVGFEETfEQAVKVVRPGGTIANVG 267
ETR_like_2 cd08292
2-enoyl thioester reductase (ETR) like proteins, child 2; 2-enoyl thioester reductase (ETR) ...
16-242 3.99e-13

2-enoyl thioester reductase (ETR) like proteins, child 2; 2-enoyl thioester reductase (ETR) like proteins. ETR catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the 2-enoyl thioester reductase (ETR) like proteins. ETR catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176252 [Multi-domain]  Cd Length: 324  Bit Score: 69.28  E-value: 3.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIV---LPEPNEAIDLADAELPVPdcADNELLVKVEyvgLNP--------VDGQFaktGFcKWQYPHILGLDAVGVVV 84
Cdd:cd08292     1 MRAAVhtqFGDPADVLEIGEVPKPTP--GAGEVLVRTT---LSPihnhdlwtIRGTY---GY-KPELPAIGGSEAVGVVD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  85 KANKGV-FPNVGQRVmwhANIGEQGALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISLDKIGISEGDTIFIEGG 163
Cdd:cd08292    72 AVGEGVkGLQVGQRV---AVAPVHGTWAEYFVAPADGLVPLPDGISDEVAAQLIAMPLSALMLLDFLGVKPGQWLIQNAA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 164 AGAVGQFAIQYAKQRGADVFTTAskRNHKLVKQL---GADVVFDYSDKKLCEKIRRELGPQGFDAVIDTIGGECTQRNIE 240
Cdd:cd08292   149 GGAVGKLVAMLAAARGINVINLV--RRDAGVAELralGIGPVVSTEQPGWQDKVREAAGGAPISVALDSVGGKLAGELLS 226

                  ..
gi 1889614189 241 LM 242
Cdd:cd08292   227 LL 228
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
18-248 5.92e-13

Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. Aldose reductase catalyzes the NADP(H)-dependent conversion of glucose to sorbital, and SDH uses NAD(H) in the conversion of sorbitol to fructose. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176188 [Multi-domain]  Cd Length: 343  Bit Score: 68.67  E-value: 5.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  18 AIVLPEPNeaiDLADAELPVPDCADNELLVKVEYVGLNPVDGQFAKTG----FCKWQyPHILGLDAVGVVVKANKGVFP- 92
Cdd:cd05285     1 AAVLHGPG---DLRLEERPIPEPGPGEVLVRVRAVGICGSDVHYYKHGrigdFVVKE-PMVLGHESAGTVVAVGSGVTHl 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  93 NVGQRV---------------MWHANIGE----------QGALSEYTKVP-NFAVsVVPSGLNPGIAATL-PCA-GMAAl 144
Cdd:cd05285    77 KVGDRVaiepgvpcrtcefckSGRYNLCPdmrfaatppvDGTLCRYVNHPaDFCH-KLPDNVSLEEGALVePLSvGVHA- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 145 isLDKIGISEGDTIFIEgGAGAVGQFAIQYAKQRGAD--VFTTASKRNHKLVKQLGADVVFD---YSDKKLCEKIRRELG 219
Cdd:cd05285   155 --CRRAGVRPGDTVLVF-GAGPIGLLTAAVAKAFGATkvVVTDIDPSRLEFAKELGATHTVNvrtEDTPESAEKIAELLG 231
                         250       260       270
                  ....*....|....*....|....*....|
gi 1889614189 220 PQGFDAVIDTIGGE-CTQRNIELMRFCGRI 248
Cdd:cd05285   232 GKGPDVVIECTGAEsCIQTAIYATRPGGTV 261
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
16-248 6.35e-13

Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of an beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176219 [Multi-domain]  Cd Length: 306  Bit Score: 68.50  E-value: 6.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVL--PEPNEAidlADAELPVPDCADNELLVKVEYVGLNPVDGQFAKTGFCKWQYPHILGLDAVGVVVKANKGVFP- 92
Cdd:cd08258     1 MKALVKtgPGPGNV---ELREVPEPEPGPGEVLIKVAAAGICGSDLHIYKGDYDPVETPVVLGHEFSGTIVEVGPDVEGw 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  93 NVGQRVMWHAN-----------------------IGEQ--GALSEYTKVPNFAVSVVPSGLN-PGIAATLPCAgMAALIS 146
Cdd:cd08258    78 KVGDRVVSETTfstcgrcpycrrgdynlcphrkgIGTQadGGFAEYVLVPEESLHELPENLSlEAAALTEPLA-VAVHAV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 147 LDKIGISEGDTIFIEgGAGAVGQFAIQYAKQRGADVF---TTASKRNHKLVKQLGADVVfDYSDKKLCEKIRRELGPQGF 223
Cdd:cd08258   157 AERSGIRPGDTVVVF-GPGPIGLLAAQVAKLQGATVVvvgTEKDEVRLDVAKELGADAV-NGGEEDLAELVNEITDGDGA 234
                         250       260
                  ....*....|....*....|....*.
gi 1889614189 224 DAVIDTIGGECT-QRNIELMRFCGRI 248
Cdd:cd08258   235 DVVIECSGAVPAlEQALELLRKGGRI 260
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
16-251 7.32e-13

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 68.31  E-value: 7.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNEAIDLADAelPVPDCADNELLVKVEyvglnpvdgqfaKTGFC-------KW--------QYPHILGLDAV 80
Cdd:PRK05396    1 MKALVKLKAEPGLWLTDV--PVPEPGPNDVLIKVK------------KTAICgtdvhiyNWdewaqktiPVPMVVGHEFV 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  81 GVVVKANKGVF-PNVGQRVMWHANI------------------------GEQGALSEYTKVPNFAVSVVPSGLNPGIAAT 135
Cdd:PRK05396   67 GEVVEVGSEVTgFKVGDRVSGEGHIvcghcrncragrrhlcrntkgvgvNRPGAFAEYLVIPAFNVWKIPDDIPDDLAAI 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 136 LPCAGMA---ALiSLDKIGiseGDTIFIegGAGAVGQFAIQYAKQRGAD--VFTTASKRNHKLVKQLGADVVFDYSDKKL 210
Cdd:PRK05396  147 FDPFGNAvhtAL-SFDLVG---EDVLIT--GAGPIGIMAAAVAKHVGARhvVITDVNEYRLELARKMGATRAVNVAKEDL 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1889614189 211 cEKIRRELG-PQGFDAVIDTIG-GECTQRNIELMRFCGRIACL 251
Cdd:PRK05396  221 -RDVMAELGmTEGFDVGLEMSGaPSAFRQMLDNMNHGGRIAML 262
PRK09422 PRK09422
ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional
16-261 1.31e-12

ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional


Pssm-ID: 181842 [Multi-domain]  Cd Length: 338  Bit Score: 67.75  E-value: 1.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNEAIDLADAELPvpDCADNELLVKVEYVGLNPVD-----GQFA-KTGfckwqypHILGLDAVGVVVKANKG 89
Cdd:PRK09422    1 MKAAVVNKDHTGDVVVEKTLR--PLKHGEALVKMEYCGVCHTDlhvanGDFGdKTG-------RILGHEGIGIVKEVGPG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  90 VFP-NVGQRV--MW---------HANIGEQ--------------GALSEYTKVP-NFAVSVvPSGLNPGIAATLPCAGMA 142
Cdd:PRK09422   72 VTSlKVGDRVsiAWffegcghceYCTTGREtlcrsvknagytvdGGMAEQCIVTaDYAVKV-PEGLDPAQASSITCAGVT 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 143 ALISLDKIGISEGDTIFIEgGAGAVGQFAIQYAKQR-GADVftTASKRNH---KLVKQLGADVVFDYSDKKLCEKIRREL 218
Cdd:PRK09422  151 TYKAIKVSGIKPGQWIAIY-GAGGLGNLALQYAKNVfNAKV--IAVDINDdklALAKEVGADLTINSKRVEDVAKIIQEK 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1889614189 219 GPQGFDAVIDTIGGECTQRNIELMRFCGRIACLNpLPYFDQDL 261
Cdd:PRK09422  228 TGGAHAAVVTAVAKAAFNQAVDAVRAGGRVVAVG-LPPESMDL 269
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
42-230 2.03e-11

Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family, reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176186 [Multi-domain]  Cd Length: 337  Bit Score: 64.05  E-value: 2.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  42 DNELLVKVEYVGLNPVDGQFAKTGFCKWQYPHILGLDAVGVVVKANKGV--FpNVGQRV--------------------- 98
Cdd:cd05283    24 PDDVDIKITYCGVCHSDLHTLRNEWGPTKYPLVPGHEIVGIVVAVGSKVtkF-KVGDRVgvgcqvdscgtceqcksgeeq 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  99 -----------MWHANIGEQGALSEYTKVP-NFAVSVvPSGLNPGIAATLPCAGMAALISLDKIGISEGDTIfieG--GA 164
Cdd:cd05283   103 ycpkgvvtyngKYPDGTITQGGYADHIVVDeRFVFKI-PEGLDSAAAAPLLCAGITVYSPLKRNGVGPGKRV---GvvGI 178
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889614189 165 GAVGQFAIQYAKQRGADVF---TTASKRnhKLVKQLGADVVFDYSDKKLCEKIRRElgpqgFDAVIDTI 230
Cdd:cd05283   179 GGLGHLAVKFAKALGAEVTafsRSPSKK--EDALKLGADEFIATKDPEAMKKAAGS-----LDLIIDTV 240
MDR_like cd08242
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
16-233 3.18e-11

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family, including threonine dehydrogenase. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176204 [Multi-domain]  Cd Length: 319  Bit Score: 63.42  E-value: 3.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLpepNEAIDLADAELPVPDCADNELLVKVEYVGLNPVDGQFAKtGFckWQYPHILGLDAVGVVVKANKGVFpnVG 95
Cdd:cd08242     1 MKALVL---DGGLDLRVEDLPKPEPPPGEALVRVLLAGICNTDLEIYK-GY--YPFPGVPGHEFVGIVEEGPEAEL--VG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  96 QRVMWHANI-------------------------GEQGALSEYTKVPNFAVSVVPSGLNPGIAA-TLPCAgmAALISLDK 149
Cdd:cd08242    73 KRVVGEINIacgrceycrrglythcpnrtvlgivDRDGAFAEYLTLPLENLHVVPDLVPDEQAVfAEPLA--AALEILEQ 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 150 IGISEGDTIFIEgGAGAVGQFAIQYAKQRGADVfTTASKRNHKL--VKQLGADVVFDYSdkklcekirRELGPQGFDAVI 227
Cdd:cd08242   151 VPITPGDKVAVL-GDGKLGLLIAQVLALTGPDV-VLVGRHSEKLalARRLGVETVLPDE---------AESEGGGFDVVV 219

                  ....*.
gi 1889614189 228 DTIGGE 233
Cdd:cd08242   220 EATGSP 225
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
16-262 7.36e-11

NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol dehydrogenases; they exist as tetramers and exhibit specificity for NADP(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like other zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), tetrameric ADHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains; however, they do not have and a structural zinc in a lobe of the catalytic domain. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176245 [Multi-domain]  Cd Length: 351  Bit Score: 62.64  E-value: 7.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNEAidlADAELPVPDCADNELLVKVEYVGLNPVDGQFAKTGFCKWQYPHILGLDAVGVVVKANKGV--FpN 93
Cdd:cd08285     1 MKAFAMLGIGKV---GWIEKPIPVCGPNDAIVRPTAVAPCTSDVHTVWGGAPGERHGMILGHEAVGVVEEVGSEVkdF-K 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  94 VGQRVM-------WH---ANIGEQ-----------------GALSEYTKVPNFA--VSVVPSGLNPgiAATLPCAGMAA- 143
Cdd:cd08285    77 PGDRVIvpaitpdWRsvaAQRGYPsqsggmlggwkfsnfkdGVFAEYFHVNDADanLAPLPDGLTD--EQAVMLPDMMSt 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 144 -LISLDKIGISEGDTIFIEgGAGAVGQFAIQYAKQRGADVFTTASKRNH--KLVKQLGADVVFDYSDKKLCEKIRRELGP 220
Cdd:cd08285   155 gFHGAELANIKLGDTVAVF-GIGPVGLMAVAGARLRGAGRIIAVGSRPNrvELAKEYGATDIVDYKNGDVVEQILKLTGG 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1889614189 221 QGFDAVIDTIGGECT-QRNIELMRFCGRIACLNplpYFDQDLM 262
Cdd:cd08285   234 KGVDAVIIAGGGQDTfEQALKVLKPGGTISNVN---YYGEDDY 273
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
16-228 9.48e-11

Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine via NAD(H)- dependent oxidation. THD is a member of the zinc-requiring, medium chain NAD(H)-dependent alcohol dehydrogenase family (MDR). MDRs have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria) and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose.


Pssm-ID: 176184 [Multi-domain]  Cd Length: 341  Bit Score: 62.25  E-value: 9.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNEAIDLAdaELPVPDCADNELLVKVEyvglnpvdgqfaKTGFC-------KWQY--------PHILGLDAV 80
Cdd:cd05281     1 MKAIVKTKAGPGAELV--EVPVPKPGPGEVLIKVL------------AASICgtdvhiyEWDEwaqsrikpPLIFGHEFA 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  81 GVVVKANKGV-FPNVGQRV-----------------MWHA-------NIGEQGALSEYTKVPNFAVSVVPSGLNPGIAAT 135
Cdd:cd05281    67 GEVVEVGEGVtRVKVGDYVsaethivcgkcyqcrtgNYHVcqntkilGVDTDGCFAEYVVVPEENLWKNDKDIPPEIASI 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 136 LPCAGMA---ALISldkiGISeGDTIFIEGgAGAVGQFAIQYAKQRGAdVFTTASKRNH---KLVKQLGADVVFDYSDKK 209
Cdd:cd05281   147 QEPLGNAvhtVLAG----DVS-GKSVLITG-CGPIGLMAIAVAKAAGA-SLVIASDPNPyrlELAKKMGADVVINPREED 219
                         250
                  ....*....|....*....
gi 1889614189 210 LCEkIRRELGPQGFDAVID 228
Cdd:cd05281   220 VVE-VKSVTDGTGVDVVLE 237
FrmA COG1062
Zn-dependent alcohol/formaldehyde dehydrogenase [Energy production and conversion];
95-231 1.13e-10

Zn-dependent alcohol/formaldehyde dehydrogenase [Energy production and conversion];


Pssm-ID: 440682 [Multi-domain]  Cd Length: 355  Bit Score: 62.02  E-value: 1.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  95 GQRVMWHANigeQGALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGM----AALISLdkiGISEGDT--IFiegGAGAVG 168
Cdd:COG1062   118 GEPVGHFFG---QSSFAEYAVVPERSVVKVDKDVPLELAALLGCGVQtgagAVLNTA---KVRPGDTvaVF---GLGGVG 188
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1889614189 169 QFAIQYAKQRGAD----VFTTASKRnhKLVKQLGADVVFDYSDKKLCEKIrRELGPQGFDAVIDTIG 231
Cdd:COG1062   189 LSAVQGARIAGASriiaVDPVPEKL--ELARELGATHTVNPADEDAVEAV-RELTGGGVDYAFETTG 252
Zn_ADH_class_III cd08279
Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, ...
16-231 1.54e-10

Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, Class III ADH) are members of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. Class III ADH are also known as glutathione-dependent formaldehyde dehydrogenase (FDH), which convert aldehydes to corresponding carboxylic acid and alcohol. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176240 [Multi-domain]  Cd Length: 363  Bit Score: 61.79  E-value: 1.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNEAIDLADAELPVPdcADNELLVKVEYVGL-----NPVDGQFAKTgfckwqYPHILGLDAVGVVVKankgV 90
Cdd:cd08279     1 MRAAVLHEVGKPLEIEEVELDDP--GPGEVLVRIAAAGLchsdlHVVTGDLPAP------LPAVLGHEGAGVVEE----V 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  91 FPNV-----GQRVM----------WHANIGEQ----------------------------------GALSEYTKVPNFAV 121
Cdd:cd08279    69 GPGVtgvkpGDHVVlswipacgtcRYCSRGQPnlcdlgagilggqlpdgtrrftadgepvgamcglGTFAEYTVVPEASV 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 122 SVVPSGLNPGIAATLPCAGM----AALISldkIGISEGDTIFIEGgAGAVGQFAIQYAKQRGAD----VFTTASKRnhKL 193
Cdd:cd08279   149 VKIDDDIPLDRAALLGCGVTtgvgAVVNT---ARVRPGDTVAVIG-CGGVGLNAIQGARIAGASriiaVDPVPEKL--EL 222
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1889614189 194 VKQLGADVVFDYSDKKLCEKIRRELGPQGFDAVIDTIG 231
Cdd:cd08279   223 ARRFGATHTVNASEDDAVEAVRDLTDGRGADYAFEAVG 260
FDH_like_1 cd08283
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified ...
101-234 3.55e-10

Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified as glutathione-dependent formaldehyde dehydrogenase(FDH), a member of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like many zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these FDHs form dimers, with 4 zinc ions per dimer. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176243 [Multi-domain]  Cd Length: 386  Bit Score: 60.63  E-value: 3.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 101 HANIGEQGALSEYTKVP--NFAVSVVPSGLNP----GIAATLPCAGMAAlislDKIGISEGDTIFIeGGAGAVGQFAIQY 174
Cdd:cd08283   129 HLTGGYAGGQAEYVRVPfaDVGPFKIPDDLSDekalFLSDILPTGYHAA----ELAEVKPGDTVAV-WGCGPVGLFAARS 203
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1889614189 175 AKQRGA------DVFTTaskRNHKLVKQLGADVVfDYSD-KKLCEKIRRELGPQGFDAVIDTIGGEC 234
Cdd:cd08283   204 AKLLGAerviaiDRVPE---RLEMARSHLGAETI-NFEEvDDVVEALRELTGGRGPDVCIDAVGMEA 266
Zn_ADH2 cd08256
Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and ...
16-247 6.81e-10

Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and structural zinc-binding sites of the zinc-dependent alcohol dehydrogenases of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176218 [Multi-domain]  Cd Length: 350  Bit Score: 59.73  E-value: 6.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNeaiDLADAELPVPDCADNELLVKVEYVGLNPVD-----------GQFAKTGFCKwqYPHILGLDAVGVVV 84
Cdd:cd08256     1 MRAVVCHGPQ---DYRLEEVPVPRPGPGEILVKVEACGICAGDikcyhgapsfwGDENQPPYVK--PPMIPGHEFVGRVV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  85 KANKGVFPN---VGQRVM------------------W----HANIGEQ----GALSEYTKVPNFA-VSVVPSGLNPGIAA 134
Cdd:cd08256    76 ELGEGAEERgvkVGDRVIseqivpcwncrfcnrgqyWmcqkHDLYGFQnnvnGGMAEYMRFPKEAiVHKVPDDIPPEDAI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 135 TL-PCAgmAALISLDKIGISEGDTIFIeGGAGAVGQFAIQYAKQRGAD--VFTTASKRNHKLVKQLGADVVFDYSDKKLC 211
Cdd:cd08256   156 LIePLA--CALHAVDRANIKFDDVVVL-AGAGPLGLGMIGAARLKNPKklIVLDLKDERLALARKFGADVVLNPPEVDVV 232
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1889614189 212 EKIRRELGPQGFDAVIDTIGG-ECTQRNIELMRFCGR 247
Cdd:cd08256   233 EKIKELTGGYGCDIYIEATGHpSAVEQGLNMIRKLGR 269
double_bond_reductase_like cd08295
Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase; This ...
15-340 8.27e-10

Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase; This group includes proteins identified as the Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase. The Arabidopsis enzyme, a member of the medium chain dehydrogenase/reductase family, catalyzes the reduction of 7-8-double bond of phenylpropanal substrates as a plant defense mechanism. Prostaglandins and related eicosanoids (lipid mediators involved in host defense and inflamation) are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto-13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. Leukotriene B4 (LTB4) can be metabolized by LTB4 20-hydroxylase in inflamatory cells, and in other cells by bifunctional LTB4 12-HD/PGR. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of an beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176255 [Multi-domain]  Cd Length: 338  Bit Score: 59.26  E-value: 8.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  15 TMRAIVLPEPNEA---IDLADAELPVPDCADNELLVKVEYVGLNP--------VDGQFAKTGFCKWQYphilgLDAVGV- 82
Cdd:cd08295     7 ILKAYVTGFPKESdleLRTTKLTLKVPPGGSGDVLVKNLYLSCDPymrgrmkgHDDSLYLPPFKPGEV-----ITGYGVa 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  83 -VVKANKGVFpNVGQRVM----WhanigeqgalSEYTKVPN------FAVSVVPSGLNPGIaatLPCAGMAALISLDKIG 151
Cdd:cd08295    82 kVVDSGNPDF-KVGDLVWgftgW----------EEYSLIPRgqdlrkIDHTDVPLSYYLGL---LGMPGLTAYAGFYEVC 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 152 ISE-GDTIFIEGGAGAVGQFAIQYAKQRGADVFTTA-SKRNHKLVK-QLGADVVFDYSDKK-LCEKIRRELgPQGFDAVI 227
Cdd:cd08295   148 KPKkGETVFVSAASGAVGQLVGQLAKLKGCYVVGSAgSDEKVDLLKnKLGFDDAFNYKEEPdLDAALKRYF-PNGIDIYF 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 228 DTIGGECTQRNIELMRFCGRIACLNPLPYFDQDLMYHRAPNISVVSiggawlaNSLCAQQRLSFMGNLLL---EGAVSGD 304
Cdd:cd08295   227 DNVGGKMLDAVLLNMNLHGRIAACGMISQYNLEWPEGVRNLLNIIY-------KRVKIQGFLVGDYLHRYpefLEEMSGY 299
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1889614189 305 IKHPEITPV-DFSA--ESVSQALNKQLAGGFTGKQVVKV 340
Cdd:cd08295   300 IKEGKLKYVeDIADglESAPEAFVGLFTGSNIGKQVVKV 338
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
16-248 2.32e-09

Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; Glutathione-dependent formaldehyde dehydrogenases (FDHs) are members of the zinc-dependent/medium chain alcohol dehydrogenase family. Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD to formate and NADH. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. These tetrameric FDHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains and a structural zinc in a lobe of the catalytic domain. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176244 [Multi-domain]  Cd Length: 344  Bit Score: 58.04  E-value: 2.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVL--PEPNEAIDLADAELPVPDCAdnelLVKVEYVG-----LNPVDGQFAKTgfckwqYPHILGLDAVGVVVKANK 88
Cdd:cd08284     1 MKAVVFkgPGDVRVEEVPIPQIQDPTDA----IVKVTAAAicgsdLHIYRGHIPST------PGFVLGHEFVGEVVEVGP 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  89 GVFP-NVGQRVM--WHANIGE--------------------------QGALSEYTKVPNFAVSVV--PSGLNPG----IA 133
Cdd:cd08284    71 EVRTlKVGDRVVspFTIACGEcfycrrgqsgrcakgglfgyagspnlDGAQAEYVRVPFADGTLLklPDGLSDEaallLG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 134 ATLPCAGMAALisldKIGISEGDTIFIEGgAGAVGQFAIQYAKQRGAD-VFT---TASKRnhKLVKQLGADVVfDYSDKK 209
Cdd:cd08284   151 DILPTGYFGAK----RAQVRPGDTVAVIG-CGPVGLCAVLSAQVLGAArVFAvdpVPERL--ERAAALGAEPI-NFEDAE 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1889614189 210 LCEKIRRELGPQGFDAVIDTIGGECTQR-NIELMRFCGRI 248
Cdd:cd08284   223 PVERVREATEGRGADVVLEAVGGAAALDlAFDLVRPGGVI 262
ADH_zinc_N_2 pfam13602
Zinc-binding dehydrogenase;
197-338 9.10e-09

Zinc-binding dehydrogenase;


Pssm-ID: 433341 [Multi-domain]  Cd Length: 131  Bit Score: 53.10  E-value: 9.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 197 LGADVVFDYSDkklcEKIRRELGPQGFDAVIDTIGGECTQRNIELMRFCGRIACLNPLPYFDQDLMYHRAPNISVVSIGG 276
Cdd:pfam13602   1 LGADEVIDYRT----TDFVQATGGEGVDVVLDTVGGEAFEASLRVLPGGGRLVTIGGPPLSAGLLLPARKRGGRGVKYLF 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1889614189 277 AWLANSLcAQQRLSFMGNLLLEGAVsgdikHPEITPVdFSAESVSQALNKQLAGGFTGKQVV 338
Cdd:pfam13602  77 LFVRPNL-GADILQELADLIEEGKL-----RPVIDRV-FPLEEAAEAHRYLESGRARGKIVL 131
benzyl_alcohol_DH cd08278
Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol ...
15-231 1.80e-08

Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol dehydrogenase, but has some amino acid substitutions near the active site, which may determine the enzyme's specificity of oxidizing aromatic substrates. Also known as aryl-alcohol dehydrogenases, they catalyze the conversion of an aromatic alcohol + NAD+ to an aromatic aldehyde + NADH + H+. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176239 [Multi-domain]  Cd Length: 365  Bit Score: 55.20  E-value: 1.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  15 TMRAIVLPEPNEAIDLADAELPVPdcADNELLVKVEYVGLNPVDGQFAKTGFCKwQYPHILGLDAVGVVVKANKGVFP-N 93
Cdd:cd08278     2 KTTAAVVREPGGPFVLEDVELDDP--RPDEVLVRIVATGICHTDLVVRDGGLPT-PLPAVLGHEGAGVVEAVGSAVTGlK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  94 VGQRV-----------------------MWHANIG---EQG--ALSEYTKVP------------NFAVS------VVPSG 127
Cdd:cd08278    79 PGDHVvlsfascgecanclsghpaycenFFPLNFSgrrPDGstPLSLDDGTPvhghffgqssfaTYAVVhernvvKVDKD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 128 LNPGIAATLPC-----AGmAALISLdkiGISEGDTIFIEGgAGAVGQFAIQYAKQRGAD----VFTTASKRnhKLVKQLG 198
Cdd:cd08278   159 VPLELLAPLGCgiqtgAG-AVLNVL---KPRPGSSIAVFG-AGAVGLAAVMAAKIAGCTtiiaVDIVDSRL--ELAKELG 231
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1889614189 199 ADVVFDYSDKKLCEKIrRELGPQGFDAVIDTIG 231
Cdd:cd08278   232 ATHVINPKEEDLVAAI-REITGGGVDYALDTTG 263
PTGR2 cd08293
Prostaglandin reductase; Prostaglandins and related eicosanoids are metabolized by the ...
121-256 1.81e-08

Prostaglandin reductase; Prostaglandins and related eicosanoids are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto-13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176253 [Multi-domain]  Cd Length: 345  Bit Score: 55.09  E-value: 1.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 121 VSVVPSGLNPGIAATLPCAGMAALISLdkIGISE--------GDTIFIEGGAGAVGQFAIQYAKQRGADVFTTASKRNHK 192
Cdd:cd08293   115 EKVDPQLVDGHLSYFLGAVGLPGLTAL--IGIQEkghitpgaNQTMVVSGAAGACGSLAGQIGRLLGCSRVVGICGSDEK 192
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1889614189 193 ---LVKQLGADVVFDYSDKKLCEKIRrELGPQGFDAVIDTIGGECTQRNIELMR------FCGRIACLNP-LPY 256
Cdd:cd08293   193 cqlLKSELGFDAAINYKTDNVAERLR-ELCPEGVDVYFDNVGGEISDTVISQMNenshiiLCGQISQYNKdVPY 265
PLN03154 PLN03154
putative allyl alcohol dehydrogenase; Provisional
155-342 2.27e-08

putative allyl alcohol dehydrogenase; Provisional


Pssm-ID: 215606 [Multi-domain]  Cd Length: 348  Bit Score: 54.85  E-value: 2.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 155 GDTIFIEGGAGAVGQFAIQYAKQRGADVFTTA-SKRNHKLVK-QLGADVVFDYSDKKLCEKIRRELGPQGFDAVIDTIGG 232
Cdd:PLN03154  159 GDSVFVSAASGAVGQLVGQLAKLHGCYVVGSAgSSQKVDLLKnKLGFDEAFNYKEEPDLDAALKRYFPEGIDIYFDNVGG 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 233 ECTQRNIELMRFCGRIAclnplpyfdqdlmyhrapnisvvsIGGAWLANSLCAQQRLSFMGNLL-----LEGAVSGDIKH 307
Cdd:PLN03154  239 DMLDAALLNMKIHGRIA------------------------VCGMVSLNSLSASQGIHNLYNLIskrirMQGFLQSDYLH 294
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1889614189 308 --PE----------------ITPVDFSAESVSQALNKQLAGGFTGKQVVKVAK 342
Cdd:PLN03154  295 lfPQflenvsryykqgkivyIEDMSEGLESAPAALVGLFSGKNVGKQVIRVAK 347
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
43-125 4.74e-08

Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol dehydrogenases. Many of them contain an inserted zinc binding domain. This domain has a GroES-like structure.


Pssm-ID: 400513 [Multi-domain]  Cd Length: 106  Bit Score: 50.30  E-value: 4.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  43 NELLVKVEYVGLNPVDGQFAKTGFCKWQYPHILGLDAVGVVVKANKGV-FPNVGQRVMWHANI----------GE----- 106
Cdd:pfam08240   1 GEVLVKVKAAGICGSDLHIYKGGNPPVKLPLILGHEFAGEVVEVGPGVtGLKVGDRVVVEPLIpcgkceycreGRynlcp 80
                          90       100
                  ....*....|....*....|....*...
gi 1889614189 107 ---------QGALSEYTKVPnfAVSVVP 125
Cdd:pfam08240  81 ngrflgydrDGGFAEYVVVP--ERNLVP 106
Zn_ADH3 cd08265
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
34-231 2.21e-07

Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol dehydrogenase and has the catalytic and structural zinc-binding sites characteristic of this group. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176226 [Multi-domain]  Cd Length: 384  Bit Score: 52.13  E-value: 2.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  34 ELPVPDCADNELLVKVEYVGLNPVDGQFAKT---GFCKW----QYPHILGLDAVGVVVKANKGVF------PNVGQRVMW 100
Cdd:cd08265    43 DVPVPNLKPDEILIRVKACGICGSDIHLYETdkdGYILYpgltEFPVVIGHEFSGVVEKTGKNVKnfekgdPVTAEEMMW 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 101 ----HA----------NIGE-----QGALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGmaALISLDKI----------G 151
Cdd:cd08265   123 cgmcRAcrsgspnhckNLKElgfsaDGAFAEYIAVNARYAWEINELREIYSEDKAFEAG--ALVEPTSVaynglfirggG 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 152 ISEGDTIFIEGgAGAVGQFAIQYAKQRGAD---VFTTASKRnHKLVKQLGADVVFDYSDKKLC---EKIRRELGPQGFDA 225
Cdd:cd08265   201 FRPGAYVVVYG-AGPIGLAAIALAKAAGASkviAFEISEER-RNLAKEMGADYVFNPTKMRDClsgEKVMEVTKGWGADI 278

                  ....*.
gi 1889614189 226 VIDTIG 231
Cdd:cd08265   279 QVEAAG 284
PRK10083 PRK10083
putative oxidoreductase; Provisional
16-226 2.74e-07

putative oxidoreductase; Provisional


Pssm-ID: 182229 [Multi-domain]  Cd Length: 339  Bit Score: 51.67  E-value: 2.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEPNEaidLADAELPVPDCADNELLVKVEYVGLNPVDGQF--AKTGFCKwqYPHILGLDAVGVVVKANKGVFPN 93
Cdd:PRK10083    1 MKSIVIEKPNS---LAIEERPIPQPAAGEVRVKVKLAGICGSDSHIyrGHNPFAK--YPRVIGHEFFGVIDAVGEGVDAA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  94 -VGQRVM----------WHANIGEQ--------------GALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISlD 148
Cdd:PRK10083   76 rIGERVAvdpviscghcYPCSIGKPnvctslvvlgvhrdGGFSEYAVVPAKNAHRIPDAIADQYAVMVEPFTIAANVT-G 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 149 KIGISEGDTIFIEgGAGAVGQFAIQYAKQ-RGADVFTTASKRNHKL--VKQLGADVVFDYSDKKLCEKI-RRELGPQG-F 223
Cdd:PRK10083  155 RTGPTEQDVALIY-GAGPVGLTIVQVLKGvYNVKAVIVADRIDERLalAKESGADWVINNAQEPLGEALeEKGIKPTLiI 233

                  ...
gi 1889614189 224 DAV 226
Cdd:PRK10083  234 DAA 236
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
29-248 2.95e-07

L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of L-lodonate to 5-ketogluconate in the metabolism of L-Idonate to 6-P-gluconate. In E. coli, this GntII pathway is a subsidiary pathway to the canonical GntI system, which also phosphorylates and transports gluconate. L-ido 5-DH is found in an operon with a regulator indR, transporter idnT, 5-keto-D-gluconate 5-reductase, and Gnt kinase. L-ido 5-DH is a zinc-dependent alcohol dehydrogenase-like protein. The alcohol dehydrogenase ADH-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) which displays a broad range of activities and are distinguished from the smaller short chain dehydrogenases(~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal GroES-like catalytic domain. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176194 [Multi-domain]  Cd Length: 339  Bit Score: 51.47  E-value: 2.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  29 DLADAELPVPDCADNELLVKVEYVGLNPVD---GQFAKTGFCKWQYPHILGLDAVGVVVKANKGVF-PNVGQRVMWHA-- 102
Cdd:cd08232     8 DLRVEERPAPEPGPGEVRVRVAAGGICGSDlhyYQHGGFGTVRLREPMVLGHEVSGVVEAVGPGVTgLAPGQRVAVNPsr 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 103 -----------------NIG----------EQGALSEYTKVPNFAVSVVPSGLNPGIAATL-PCAgmAALISLDKIGISE 154
Cdd:cd08232    88 pcgtcdycragrpnlclNMRflgsamrfphVQGGFREYLVVDASQCVPLPDGLSLRRAALAePLA--VALHAVNRAGDLA 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 155 GDTIFIEGgAGAVGQFAIQYAKQRGAD--VFTTASKRNHKLVKQLGADVVFDYSDKKLCEKirrELGPQGFDAVIDTIGG 232
Cdd:cd08232   166 GKRVLVTG-AGPIGALVVAAARRAGAAeiVATDLADAPLAVARAMGADETVNLARDPLAAY---AADKGDFDVVFEASGA 241
                         250
                  ....*....|....*..
gi 1889614189 233 ECTQRN-IELMRFCGRI 248
Cdd:cd08232   242 PAALASaLRVVRPGGTV 258
Zn_ADH8 cd08262
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
16-251 4.60e-07

Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176223 [Multi-domain]  Cd Length: 341  Bit Score: 50.77  E-value: 4.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  16 MRAIVLPEpneaIDLADAELPVPDCADNELLVKVEYVGLNPVDGQFAK---------TGFCKWQYPH--ILGLDAVGVVV 84
Cdd:cd08262     1 MRAAVFRD----GPLVVRDVPDPEPGPGQVLVKVLACGICGSDLHATAhpeamvddaGGPSLMDLGAdiVLGHEFCGEVV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  85 KANKGV--FPNVGQRV----MWH----------ANIGEQGALSEYTKVPNFAVSVVPSGLNPGIAA-TLPCAgmAALISL 147
Cdd:cd08262    77 DYGPGTerKLKVGTRVtslpLLLcgqgascgigLSPEAPGGYAEYMLLSEALLLRVPDGLSMEDAAlTEPLA--VGLHAV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 148 DKIGISEGDTIFIEGgAGAVGQFAIQYAKQRGAD--VFTTASKRNHKLVKQLGADVVFDYsdkklcekiRRELGPQGFDA 225
Cdd:cd08262   155 RRARLTPGEVALVIG-CGPIGLAVIAALKARGVGpiVASDFSPERRALALAMGADIVVDP---------AADSPFAAWAA 224
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1889614189 226 VIDTIGG-------ECT------QRNIELMRFCGRIACL 251
Cdd:cd08262   225 ELARAGGpkpavifECVgapgliQQIIEGAPPGGRIVVV 263
PLN02586 PLN02586
probable cinnamyl alcohol dehydrogenase
39-230 3.09e-05

probable cinnamyl alcohol dehydrogenase


Pssm-ID: 166227 [Multi-domain]  Cd Length: 360  Bit Score: 45.25  E-value: 3.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  39 DCADNELLVKVEYVGLNPVDGQFAKTGFCKWQYPHILGLDAVGVVVKANKGVFP-NVGQRV------------------- 98
Cdd:PLN02586   34 ENGDEDVTVKILYCGVCHSDLHTIKNEWGFTRYPIVPGHEIVGIVTKLGKNVKKfKEGDRVgvgvivgsckscescdqdl 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  99 -------------MWHANIGEQGALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISLDKIGISEGDTIFIEGGAG 165
Cdd:PLN02586  114 enycpkmiftynsIGHDGTKNYGGYSDMIVVDQHFVLRFPDNLPLDAGAPLLCAGITVYSPMKYYGMTEPGKHLGVAGLG 193
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1889614189 166 AVGQFAIQYAKQRG--ADVFTTASKRNHKLVKQLGADVVFDYSDKklcEKIRRELGPqgFDAVIDTI 230
Cdd:PLN02586  194 GLGHVAVKIGKAFGlkVTVISSSSNKEDEAINRLGADSFLVSTDP---EKMKAAIGT--MDYIIDTV 255
PLN02178 PLN02178
cinnamyl-alcohol dehydrogenase
42-233 6.94e-05

cinnamyl-alcohol dehydrogenase


Pssm-ID: 177834 [Multi-domain]  Cd Length: 375  Bit Score: 44.24  E-value: 6.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189  42 DNELLVKVEYVGLNPVDGQFAKTGFCKWQYPHILGLDAVGVVVKANKGVFP-NVGQRVMWHANIGE-------------- 106
Cdd:PLN02178   31 ENDVTVKILFCGVCHSDLHTIKNHWGFSRYPIIPGHEIVGIATKVGKNVTKfKEGDRVGVGVIIGScqscescnqdleny 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 107 ------------------QGALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISLDKIGISE--GDTIFIEgGAGA 166
Cdd:PLN02178  111 cpkvvftynsrssdgtrnQGGYSDVIVVDHRFVLSIPDGLPSDSGAPLLCAGITVYSPMKYYGMTKesGKRLGVN-GLGG 189
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889614189 167 VGQFAIQYAKQRG--ADVFTTASKRNHKLVKQLGADVVFDYSDKklcEKIRRELGPqgFDAVIDTIGGE 233
Cdd:PLN02178  190 LGHIAVKIGKAFGlrVTVISRSSEKEREAIDRLGADSFLVTTDS---QKMKEAVGT--MDFIIDTVSAE 253
PLN02514 PLN02514
cinnamyl-alcohol dehydrogenase
107-230 9.14e-05

cinnamyl-alcohol dehydrogenase


Pssm-ID: 166155 [Multi-domain]  Cd Length: 357  Bit Score: 43.63  E-value: 9.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 107 QGALSEYTKVPNFAVSVVPSGLNPGIAATLPCAGMAALISLDKIGISE---GDTIFiegGAGAVGQFAIQYAKQRG--AD 181
Cdd:PLN02514  132 QGGFASAMVVDQKFVVKIPEGMAPEQAAPLLCAGVTVYSPLSHFGLKQsglRGGIL---GLGGVGHMGVKIAKAMGhhVT 208
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1889614189 182 VFTTASKRNHKLVKQLGADVVFDYSDKKLCEKIRRELgpqgfDAVIDTI 230
Cdd:PLN02514  209 VISSSDKKREEALEHLGADDYLVSSDAAEMQEAADSL-----DYIIDTV 252
FDH_like_ADH3 cd08287
formaldehyde dehydrogenase (FDH)-like; This group contains proteins identified as alcohol ...
101-261 2.29e-03

formaldehyde dehydrogenase (FDH)-like; This group contains proteins identified as alcohol dehydrogenases and glutathione-dependant formaldehyde dehydrogenases (FDH) of the zinc-dependent/medium chain alcohol dehydrogenase family. The MDR family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. FDH converts formaldehyde and NAD to formate and NADH. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176247 [Multi-domain]  Cd Length: 345  Bit Score: 39.60  E-value: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 101 HANIGEQGalsEYTKVPN-----FAVSVVPSGLNPGIAATLPCA-----GMAALISldkIGISEGDTIFIEGGaGAVGQF 170
Cdd:cd08287   111 AFVDGGQG---EYVRVPLadgtlVKVPGSPSDDEDLLPSLLALSdvmgtGHHAAVS---AGVRPGSTVVVVGD-GAVGLC 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614189 171 AIQYAKQRGADVFTTASKR--NHKLVKQLGA-DVVFDYSDKKLcEKIRRELGPQGFDAVIDTIGG-ECTQRNIELMRFCG 246
Cdd:cd08287   184 AVLAAKRLGAERIIAMSRHedRQALAREFGAtDIVAERGEEAV-ARVRELTGGVGADAVLECVGTqESMEQAIAIARPGG 262
                         170
                  ....*....|....*
gi 1889614189 247 RIACLNpLPYFDQDL 261
Cdd:cd08287   263 RVGYVG-VPHGGVEL 276
 
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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