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Conserved domains on  [gi|974005217|ref|NP_001305675|]
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reticulon-4-interacting protein 1, mitochondrial isoform 2 [Homo sapiens]

Protein Classification

RTN4I1 domain-containing protein( domain architecture ID 10169543)

RTN4I1 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
1-294 1.89e-174

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: 485.96  E-value: 1.89e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217   1 MKRDPLHVKIKGEEFPLTLGRDVSGVVMECGLDVKYFKPGDEVWAAVPPWKQGTLSEFVVVSGNEVSHKPKSLTHTQAAS 80
Cdd:cd08248   59 KKRKPQSCKYSGIEFPLTLGRDCSGVVVDIGSGVKSFEIGDEVWGAVPPWSQGTHAEYVVVPENEVSKKPKNLSHEEAAS 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  81 LPYVALTAWSAINKVGGLNDKNCTGKRVLILGASGGVGTFAIQVMKAWDAHVTAVCSQDASELVRKLGADDVIDYKSGSV 160
Cdd:cd08248  139 LPYAGLTAWSALVNVGGLNPKNAAGKRVLILGGSGGVGTFAIQLLKAWGAHVTTTCSTDAIPLVKSLGADDVIDYNNEDF 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 161 EEQLKSLKPFDFILDNVGGSTETWAPDFLKKwsGATYVTLVTPFLLNMDRLGIADGMLQTGVTVGSKALKHFWKGVHYRW 240
Cdd:cd08248  219 EEELTERGKFDVILDTVGGDTEKWALKLLKK--GGTYVTLVSPLLKNTDKLGLVGGMLKSAVDLLKKNVKSLLKGSHYRW 296
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 974005217 241 AFFMASGPCLDDIAELVDAGKIRPVIEQTFPFSKVPEAFLKVERGHARGKTVIN 294
Cdd:cd08248  297 GFFSPSGSALDELAKLVEDGKIKPVIDKVFPFEEVPEAYEKVESGHARGKTVIK 350
 
Name Accession Description Interval E-value
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
1-294 1.89e-174

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: 485.96  E-value: 1.89e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217   1 MKRDPLHVKIKGEEFPLTLGRDVSGVVMECGLDVKYFKPGDEVWAAVPPWKQGTLSEFVVVSGNEVSHKPKSLTHTQAAS 80
Cdd:cd08248   59 KKRKPQSCKYSGIEFPLTLGRDCSGVVVDIGSGVKSFEIGDEVWGAVPPWSQGTHAEYVVVPENEVSKKPKNLSHEEAAS 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  81 LPYVALTAWSAINKVGGLNDKNCTGKRVLILGASGGVGTFAIQVMKAWDAHVTAVCSQDASELVRKLGADDVIDYKSGSV 160
Cdd:cd08248  139 LPYAGLTAWSALVNVGGLNPKNAAGKRVLILGGSGGVGTFAIQLLKAWGAHVTTTCSTDAIPLVKSLGADDVIDYNNEDF 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 161 EEQLKSLKPFDFILDNVGGSTETWAPDFLKKwsGATYVTLVTPFLLNMDRLGIADGMLQTGVTVGSKALKHFWKGVHYRW 240
Cdd:cd08248  219 EEELTERGKFDVILDTVGGDTEKWALKLLKK--GGTYVTLVSPLLKNTDKLGLVGGMLKSAVDLLKKNVKSLLKGSHYRW 296
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 974005217 241 AFFMASGPCLDDIAELVDAGKIRPVIEQTFPFSKVPEAFLKVERGHARGKTVIN 294
Cdd:cd08248  297 GFFSPSGSALDELAKLVEDGKIKPVIDKVFPFEEVPEAYEKVESGHARGKTVIK 350
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
12-295 7.18e-74

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: 229.26  E-value: 7.18e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  12 GEEFPLTLGRDVSGVVMECGLDVKYFKPGDEVWAAVPPwkqGTLSEFVVVSGNEVSHKPKSLTHTQAASLPYVALTAWSA 91
Cdd:COG0604   54 PPGLPFIPGSDAAGVVVAVGEGVTGFKVGDRVAGLGRG---GGYAEYVVVPADQLVPLPDGLSFEEAAALPLAGLTAWQA 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  92 INKVGGLNDknctGKRVLILGASGGVGTFAIQVMKAWDAHVTAVCSQDAS-ELVRKLGADDVIDYKSGSVEEQLKSL--- 167
Cdd:COG0604  131 LFDRGRLKP----GETVLVHGAAGGVGSAAVQLAKALGARVIATASSPEKaELLRALGADHVIDYREEDFAERVRALtgg 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 168 KPFDFILDNVGGSTETWAPDFLKKwsGATYVTLVTPfllnmdrlgiadgmlqTGVTVGSKALKHFWKGVHYRWAFFMASG 247
Cdd:COG0604  207 RGVDVVLDTVGGDTLARSLRALAP--GGRLVSIGAA----------------SGAPPPLDLAPLLLKGLTLTGFTLFARD 268
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 974005217 248 P-----CLDDIAELVDAGKIRPVIEQTFPFSKVPEAFLKVERGHARGKTVINV 295
Cdd:COG0604  269 PaerraALAELARLLAAGKLRPVIDRVFPLEEAAEAHRLLESGKHRGKVVLTV 321
adh_fam_1 TIGR02817
zinc-binding alcohol dehydrogenase family protein; Members of this model form a distinct ...
4-294 7.75e-40

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: 141.80  E-value: 7.75e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217    4 DPLHVKIK-----GEEFPLTLGRDVSGVVMECGLDVKYFKPGDEVWAAVPPWKQGTLSEFVVVSGNEVSHKPKSLTHTQA 78
Cdd:TIGR02817  42 NPVDTKVRarmapEAGQPKILGWDAAGVVVAVGDEVTLFKPGDEVWYAGDIDRPGSNAEFHLVDERIVGHKPKSLSFAEA 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217   79 ASLPYVALTAWSAI-NKVGGLNDKNCTGKRVLILGASGGVGTFAIQVMKAW-DAHVTAVCSQ-DASELVRKLGADDVIDY 155
Cdd:TIGR02817 122 AALPLTSITAWELLfDRLGINDPVAGDKRALLIIGGAGGVGSILIQLARQLtGLTVIATASRpESQEWVLELGAHHVIDH 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  156 kSGSVEEQLKSLKPFDfiLDNVGGSTETwapdflkkwsgATYVTLVTPFLLNMDRLGIADGMLQTGVT-VGSKALKHFWK 234
Cdd:TIGR02817 202 -SKPLKAQLEKLGLEA--VSYVFSLTHT-----------DQHFKEIVELLAPQGRFALIDDPAELDISpFKRKSISLHWE 267
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 974005217  235 GVHYRWAF----FMASGPCLDDIAELVDAGKIRPVIEQTfpFSKVPEAFLK-----VERGHARGKTVIN 294
Cdd:TIGR02817 268 FMFTRSMFqtadMIEQHHLLNRVARLVDAGKIRTTLAET--FGTINAANLKrahalIESGKARGKIVLE 334
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
16-293 4.86e-38

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 135.59  E-value: 4.86e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217    16 PLTLGRDVSGVVMECGLDVKYFKPGDEVWAAVPpwkqGTLSEFVVVSGNEVSHKPKSLTHTQAASLPYVALTAWSAINKV 95
Cdd:smart00829  23 EAVLGGECAGVVTRVGPGVTGLAVGDRVMGLAP----GAFATRVVTDARLVVPIPDGWSFEEAATVPVVFLTAYYALVDL 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217    96 GGLNDknctGKRVLILGASGGVGTFAIQVMKAWDAHVTA-VCSQDASELVRKLG--ADDVIDYKSGSVEEQLKSL---KP 169
Cdd:smart00829  99 ARLRP----GESVLIHAAAGGVGQAAIQLARHLGAEVFAtAGSPEKRDFLRALGipDDHIFSSRDLSFADEILRAtggRG 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217   170 FDFILDNVGGstetwapDFLKK-WSgatyvtLVTPF--LLNMDRLGIADGmlqtgvtvGSKALKHFWKGVHYRwAF---F 243
Cdd:smart00829 175 VDVVLNSLSG-------EFLDAsLR------CLAPGgrFVEIGKRDIRDN--------SQLAMAPFRPNVSYH-AVdldA 232
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 974005217   244 MASGP-----CLDDIAELVDAGKIRPVIEQTFPFSKVPEAFLKVERGHARGKTVI 293
Cdd:smart00829 233 LEEGPdrireLLAEVLELFAEGVLRPLPVTVFPISDAEDAFRYMQQGKHIGKVVL 287
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
19-295 1.17e-30

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 117.44  E-value: 1.17e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  19 LGRDVSGVVMECGLDVKYFKPGDEVWAAVPpwkQGTLSEFVVVSGNEVSHKPKSLTHTQAASLPYVALTAWSAINKVGGL 98
Cdd:PTZ00354  62 LGLEVAGYVEDVGSDVKRFKEGDRVMALLP---GGGYAEYAVAHKGHVMHIPQGYTFEEAAAIPEAFLTAWQLLKKHGDV 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  99 NdkncTGKRVLILGASGGVGTFAIQVMKAWDAH-VTAVCSQDASELVRKLGADDVIDYK--SGSVEEQLKSLKP--FDFI 173
Cdd:PTZ00354 139 K----KGQSVLIHAGASGVGTAAAQLAEKYGAAtIITTSSEEKVDFCKKLAAIILIRYPdeEGFAPKVKKLTGEkgVNLV 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 174 LDNVGGS-----TETWAPDflKKW------SGATYVTL-VTPFLlnMDRLGIADGMLQTGvTVGSKA--LKHFWKgvhyr 239
Cdd:PTZ00354 215 LDCVGGSylsetAEVLAVD--GKWivygfmGGAKVEKFnLLPLL--RKRASIIFSTLRSR-SDEYKAdlVASFER----- 284
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 974005217 240 waffmasgpcldDIAELVDAGKIRPVIEQTFPFSKVPEAFLKVERGHARGKTVINV 295
Cdd:PTZ00354 285 ------------EVLPYMEEGEIKPIVDRTYPLEEVAEAHTFLEQNKNIGKVVLTV 328
ADH_zinc_N_2 pfam13602
Zinc-binding dehydrogenase;
147-293 3.03e-25

Zinc-binding dehydrogenase;


Pssm-ID: 433341 [Multi-domain]  Cd Length: 131  Bit Score: 97.78  E-value: 3.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  147 LGADDVIDYKSGSVEEQLKSlKPFDFILDNVGGSTETWAPDFLKKwsGATYVTLVTPFLLnmdrlgiadgmlqtgVTVGS 226
Cdd:pfam13602   1 LGADEVIDYRTTDFVQATGG-EGVDVVLDTVGGEAFEASLRVLPG--GGRLVTIGGPPLS---------------AGLLL 62
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 974005217  227 KALKHFWKGVHYRWAFFMASGP--CLDDIAELVDAGKIRPVIEQTFPFSKVPEAFLKVERGHARGKTVI 293
Cdd:pfam13602  63 PARKRGGRGVKYLFLFVRPNLGadILQELADLIEEGKLRPVIDRVFPLEEAAEAHRYLESGRARGKIVL 131
 
Name Accession Description Interval E-value
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
1-294 1.89e-174

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: 485.96  E-value: 1.89e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217   1 MKRDPLHVKIKGEEFPLTLGRDVSGVVMECGLDVKYFKPGDEVWAAVPPWKQGTLSEFVVVSGNEVSHKPKSLTHTQAAS 80
Cdd:cd08248   59 KKRKPQSCKYSGIEFPLTLGRDCSGVVVDIGSGVKSFEIGDEVWGAVPPWSQGTHAEYVVVPENEVSKKPKNLSHEEAAS 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  81 LPYVALTAWSAINKVGGLNDKNCTGKRVLILGASGGVGTFAIQVMKAWDAHVTAVCSQDASELVRKLGADDVIDYKSGSV 160
Cdd:cd08248  139 LPYAGLTAWSALVNVGGLNPKNAAGKRVLILGGSGGVGTFAIQLLKAWGAHVTTTCSTDAIPLVKSLGADDVIDYNNEDF 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 161 EEQLKSLKPFDFILDNVGGSTETWAPDFLKKwsGATYVTLVTPFLLNMDRLGIADGMLQTGVTVGSKALKHFWKGVHYRW 240
Cdd:cd08248  219 EEELTERGKFDVILDTVGGDTEKWALKLLKK--GGTYVTLVSPLLKNTDKLGLVGGMLKSAVDLLKKNVKSLLKGSHYRW 296
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 974005217 241 AFFMASGPCLDDIAELVDAGKIRPVIEQTFPFSKVPEAFLKVERGHARGKTVIN 294
Cdd:cd08248  297 GFFSPSGSALDELAKLVEDGKIKPVIDKVFPFEEVPEAYEKVESGHARGKTVIK 350
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
14-293 5.98e-88

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: 264.81  E-value: 5.98e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  14 EFPLTLGRDVSGVVMECGLDVKYFKPGDEVWAAVPPWKQGTLSEFVVVSGNEVSHKPKSLTHTQAASLPYVALTAWSAIN 93
Cdd:cd05289   58 TLPLIPGHDVAGVVVAVGPGVTGFKVGDEVFGMTPFTRGGAYAEYVVVPADELALKPANLSFEEAAALPLAGLTAWQALF 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  94 KVGGLNdkncTGKRVLILGASGGVGTFAIQVMKAWDAHVTAVCSQDASELVRKLGADDVIDYKSGSVEEQLKsLKPFDFI 173
Cdd:cd05289  138 ELGGLK----AGQTVLIHGAAGGVGSFAVQLAKARGARVIATASAANADFLRSLGADEVIDYTKGDFERAAA-PGGVDAV 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 174 LDNVGGSTETWAPDFLKKwsGATYVTLVTPfllnmdrlgiadgmlqtgvtvGSKALKHFWKGVHYRWAFFMASGPCLDDI 253
Cdd:cd05289  213 LDTVGGETLARSLALVKP--GGRLVSIAGP---------------------PPAEQAAKRRGVRAGFVFVEPDGEQLAEL 269
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 974005217 254 AELVDAGKIRPVIEQTFPFSKVPEAFLKVERGHARGKTVI 293
Cdd:cd05289  270 AELVEAGKLRPVVDRVFPLEDAAEAHERLESGHARGKVVL 309
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
15-293 1.44e-87

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: 264.08  E-value: 1.44e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  15 FPLTLGRDVSGVVMECGLDVKYFKPGDEVWAAVPPWKQGTLSEFVVVSGNEVSHKPKSLTHTQAASLPYVALTAWSAINK 94
Cdd:cd08267   58 FPPIPGMDFAGEVVAVGSGVTRFKVGDEVFGRLPPKGGGALAEYVVAPESGLAKKPEGVSFEEAAALPVAGLTALQALRD 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  95 VGGLndknCTGKRVLILGASGGVGTFAIQVMKAWDAHVTAVCSQDASELVRKLGADDVIDYKSGSVEEQLKSLKPFDFIL 174
Cdd:cd08267  138 AGKV----KPGQRVLINGASGGVGTFAVQIAKALGAHVTGVCSTRNAELVRSLGADEVIDYTTEDFVALTAGGEKYDVIF 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 175 DNVGGSTET--WAPDFLKKwsGATYVTLvtpfllnmdrlgiadGMLQTGVTVGSKALKHFWKGVHYRWAFFMASGPC--L 250
Cdd:cd08267  214 DAVGNSPFSlyRASLALKP--GGRYVSV---------------GGGPSGLLLVLLLLPLTLGGGGRRLKFFLAKPNAedL 276
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 974005217 251 DDIAELVDAGKIRPVIEQTFPFSKVPEAFLKVERGHARGKTVI 293
Cdd:cd08267  277 EQLAELVEEGKLKPVIDSVYPLEDAPEAYRRLKSGRARGKVVI 319
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
12-295 7.18e-74

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: 229.26  E-value: 7.18e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  12 GEEFPLTLGRDVSGVVMECGLDVKYFKPGDEVWAAVPPwkqGTLSEFVVVSGNEVSHKPKSLTHTQAASLPYVALTAWSA 91
Cdd:COG0604   54 PPGLPFIPGSDAAGVVVAVGEGVTGFKVGDRVAGLGRG---GGYAEYVVVPADQLVPLPDGLSFEEAAALPLAGLTAWQA 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  92 INKVGGLNDknctGKRVLILGASGGVGTFAIQVMKAWDAHVTAVCSQDAS-ELVRKLGADDVIDYKSGSVEEQLKSL--- 167
Cdd:COG0604  131 LFDRGRLKP----GETVLVHGAAGGVGSAAVQLAKALGARVIATASSPEKaELLRALGADHVIDYREEDFAERVRALtgg 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 168 KPFDFILDNVGGSTETWAPDFLKKwsGATYVTLVTPfllnmdrlgiadgmlqTGVTVGSKALKHFWKGVHYRWAFFMASG 247
Cdd:COG0604  207 RGVDVVLDTVGGDTLARSLRALAP--GGRLVSIGAA----------------SGAPPPLDLAPLLLKGLTLTGFTLFARD 268
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 974005217 248 P-----CLDDIAELVDAGKIRPVIEQTFPFSKVPEAFLKVERGHARGKTVINV 295
Cdd:COG0604  269 PaerraALAELARLLAAGKLRPVIDRVFPLEEAAEAHRLLESGKHRGKVVLTV 321
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
5-295 8.09e-58

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: 188.15  E-value: 8.09e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217   5 PLHVKIK------GEEFPLTLGRDVSGVVMECGLDVKYFKPGDEVWAAVPPWK--QGTLSEFVVVSGNEVSHKPKSLTHT 76
Cdd:cd08272   41 PLDTKIRrggaaaRPPLPAILGCDVAGVVEAVGEGVTRFRVGDEVYGCAGGLGglQGSLAEYAVVDARLLALKPANLSMR 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  77 QAASLPYVALTAWSAINKVGGLNdkncTGKRVLILGASGGVGTFAIQVMKAWDAHVTAVCSQDASELVRKLGADDVIDYK 156
Cdd:cd08272  121 EAAALPLVGITAWEGLVDRAAVQ----AGQTVLIHGGAGGVGHVAVQLAKAAGARVYATASSEKAAFARSLGADPIIYYR 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 157 SGSVEEQLKSL--KPFDFILDNVGGSTETWAPDFLKKWSGAtyVTLVTPFLLNmdrLGIADG---------MLQTGVTvg 225
Cdd:cd08272  197 ETVVEYVAEHTggRGFDVVFDTVGGETLDASFEAVALYGRV--VSILGGATHD---LAPLSFrnatysgvfTLLPLLT-- 269
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 974005217 226 SKALKHFwkgvhyrwaffmasGPCLDDIAELVDAGKIRPVI-EQTFPFSKVPEAFLKVERGHARGKTVINV 295
Cdd:cd08272  270 GEGRAHH--------------GEILREAARLVERGQLRPLLdPRTFPLEEAAAAHARLESGSARGKIVIDV 326
AST1_like cd08247
AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast; This group ...
5-295 6.38e-46

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: 158.20  E-value: 6.38e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217   5 PLHVKIKGEEFPL------TLGRDVSGVVMECGLDVKY-FKPGDEVWAAVPP--WKQGTLSEFVVV----SGNEVSHKPK 71
Cdd:cd08247   42 PVDLKLYNSYTFHfkvkekGLGRDYSGVIVKVGSNVASeWKVGDEVCGIYPHpyGGQGTLSQYLLVdpkkDKKSITRKPE 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  72 SLTHTQAASLPYVALTAWSAINKVGGLNDKNctgKRVLILGASGGVGTFAIQVMKAwdaH-----VTAVCSQDASELVRK 146
Cdd:cd08247  122 NISLEEAAAWPLVLGTAYQILEDLGQKLGPD---SKVLVLGGSTSVGRFAIQLAKN---HynigtVVGTCSSRSAELNKK 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 147 LGADDVIDYKSGSVEEQLKSL-------KPFDFILDNVGGStetwapDFL--------KKWSGATYVTLVTPFLLNMdrl 211
Cdd:cd08247  196 LGADHFIDYDAHSGVKLLKPVlenvkgqGKFDLILDCVGGY------DLFphinsilkPKSKNGHYVTIVGDYKANY--- 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 212 giADGMLQTGVTVGSKALKHFW----KGVHYRWAFFMASGPCLDDIAELVDAGKIRPVIEQTFPFSKVPEAFLKVERGHA 287
Cdd:cd08247  267 --KKDTFNSWDNPSANARKLFGslglWSYNYQFFLLDPNADWIEKCAELIADGKVKPPIDSVYPFEDYKEAFERLKSNRA 344

                 ....*...
gi 974005217 288 RGKTVINV 295
Cdd:cd08247  345 KGKVVIKV 352
AL_MDR cd08252
Arginate lyase and other MDR family members; This group contains a structure identified as an ...
11-294 2.18e-45

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: 156.15  E-value: 2.18e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  11 KGEEFPLTLGRDVSGVVMECGLDVKYFKPGDEVWAAVPPWKQGTLSEFVVVSGNEVSHKPKSLTHTQAASLPYVALTAWS 90
Cdd:cd08252   55 PVPGQPKILGWDASGVVEAVGSEVTLFKVGDEVYYAGDITRPGSNAEYQLVDERIVGHKPKSLSFAEAAALPLTSLTAWE 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  91 AINKVGGL--NDKNCtGKRVLILGASGGVGTFAIQVMKAW-DAHVTAVCS-QDASELVRKLGADDVIDYKSgSVEEQLKS 166
Cdd:cd08252  135 ALFDRLGIseDAENE-GKTLLIIGGAGGVGSIAIQLAKQLtGLTVIATASrPESIAWVKELGADHVINHHQ-DLAEQLEA 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 167 L--KPFDFILDnvggsteTWAPDflKKWSGATyvTLVTPFllnmDRLGIADGmlqTGVTVGSKALKHfwKGVHYRWAF-F 243
Cdd:cd08252  213 LgiEPVDYIFC-------LTDTD--QHWDAMA--ELIAPQ----GHICLIVD---PQEPLDLGPLKS--KSASFHWEFmF 272
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 974005217 244 ---------MAS-GPCLDDIAELVDAGKIRPVIEQTF-PFSkvPEAFLK----VERGHARGKTVIN 294
Cdd:cd08252  273 trsmfqtpdMIEqHEILNEVADLLDAGKLKTTLTETLgPIN--AENLREahalLESGKTIGKIVLE 336
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
14-293 2.77e-45

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: 155.73  E-value: 2.77e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  14 EFPLTLGRDVSGVVMECGLDVKYFKPGDEVWAAVPpwkQGTLSEFVVVSGNEVSHKPKSLTHTQAASLPYVALTAWSAIN 93
Cdd:cd08241   56 PLPFVPGSEVAGVVEAVGEGVTGFKVGDRVVALTG---QGGFAEEVVVPAAAVFPLPDGLSFEEAAALPVTYGTAYHALV 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  94 KVGGLndknCTGKRVLILGASGGVGTFAIQVMKAWDAHVTAVCSQDAS-ELVRKLGADDVIDYKSGSVEEQLKSL---KP 169
Cdd:cd08241  133 RRARL----QPGETVLVLGAAGGVGLAAVQLAKALGARVIAAASSEEKlALARALGADHVIDYRDPDLRERVKALtggRG 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 170 FDFILDNVGGSTetwAPDFLK--KWSGatyvtlvtpfllnmdRL---GIADG---------MLQTGVTVgskalkhfwKG 235
Cdd:cd08241  209 VDVVYDPVGGDV---FEASLRslAWGG---------------RLlviGFASGeipqipanlLLLKNISV---------VG 261
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 974005217 236 VHyrWAFFMASGP-----CLDDIAELVDAGKIRPVIEQTFPFSKVPEAFLKVERGHARGKTVI 293
Cdd:cd08241  262 VY--WGAYARREPellraNLAELFDLLAEGKIRPHVSAVFPLEQAAEALRALADRKATGKVVL 322
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
15-295 7.23e-45

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: 155.05  E-value: 7.23e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  15 FPLTLGRDVSGVVMECGLDVKYFKPGDEVWAAVP-----PWKQGTLSEFVVVSGNEVSHKPKSLTHTQAASLPYVALTAW 89
Cdd:cd08249   54 YPAILGCDFAGTVVEVGSGVTRFKVGDRVAGFVHggnpnDPRNGAFQEYVVADADLTAKIPDNISFEEAATLPVGLVTAA 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  90 SAINKVGGLN------DKNCTGKRVLILGASGGVGTFAIQVMKAWDAHVTAVCSQDASELVRKLGADDVIDYKSGSVEEQ 163
Cdd:cd08249  134 LALFQKLGLPlpppkpSPASKGKPVLIWGGSSSVGTLAIQLAKLAGYKVITTASPKNFDLVKSLGADAVFDYHDPDVVED 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 164 LKSL--KPFDFILDNVgGSTETWAP--DFLKKWSGATYVTLVTPFLLNMDRLGIADGMLQTGVTVGSKALKHFWKGVHYR 239
Cdd:cd08249  214 IRAAtgGKLRYALDCI-STPESAQLcaEALGRSGGGKLVSLLPVPEETEPRKGVKVKFVLGYTVFGEIPEDREFGEVFWK 292
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 974005217 240 WaffmasgpclddIAELVDAGKIRPVIEQTFP--FSKVPEAFLKVERGHARG-KTVINV 295
Cdd:cd08249  293 Y------------LPELLEEGKLKPHPVRVVEggLEGVQEGLDLLRKGKVSGeKLVVRL 339
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
19-293 1.03e-44

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: 154.14  E-value: 1.03e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  19 LGRDVSGVVMECGLDVKYFKPGDEVWAAVPpwkQGTLSEFVVVSGNEVSHKPKSLTHTQAASLPYVALTAWSAINKVGGL 98
Cdd:cd05276   61 LGLEVAGVVVAVGPGVTGWKVGDRVCALLA---GGGYAEYVVVPAGQLLPVPEGLSLVEAAALPEVFFTAWQNLFQLGGL 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  99 NdkncTGKRVLILGASGGVGTFAIQVMKAWDAHVTAVC-SQDASELVRKLGADDVIDYKSGSVEEQLKSL---KPFDFIL 174
Cdd:cd05276  138 K----AGETVLIHGGASGVGTAAIQLAKALGARVIATAgSEEKLEACRALGADVAINYRTEDFAEEVKEAtggRGVDVIL 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 175 DNVGGST-----ETWAPD-------FLkkwsGATYVTLVTPFLLnMDRLGIadgmlqTGVTVGS-----KA--LKHFWKG 235
Cdd:cd05276  214 DMVGGDYlarnlRALAPDgrlvligLL----GGAKAELDLAPLL-RKRLTL------TGSTLRSrsleeKAalAAAFREH 282
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 974005217 236 VhyrWAffmasgpclddiaeLVDAGKIRPVIEQTFPFSKVPEAFLKVERGHARGKTVI 293
Cdd:cd05276  283 V---WP--------------LFASGRIRPVIDKVFPLEEAAEAHRRMESNEHIGKIVL 323
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
6-293 1.41e-43

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 151.42  E-value: 1.41e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217   6 LHVkIKGE----EFPLTLGRDVSGVVMECGLDVKYFKPGDEVwaAVPPWK--------------------------QGTL 55
Cdd:COG1064   42 LHV-AEGEwpvpKLPLVPGHEIVGRVVAVGPGVTGFKVGDRV--GVGWVDscgtceycrsgrenlcengrftgyttDGGY 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  56 SEFVVVSGNEVSHKPKSLTHTQAASLPYVALTAWSAInKVGGLNDknctGKRVLILGAsGGVGTFAIQVMKAWDAHVTAV 135
Cdd:COG1064  119 AEYVVVPARFLVKLPDGLDPAEAAPLLCAGITAYRAL-RRAGVGP----GDRVAVIGA-GGLGHLAVQIAKALGAEVIAV 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 136 -CSQDASELVRKLGADDVIDYKSGSVEEQLKSLKPFDFILDNVgGSTETWAP--DFLKKwsGATYVTL--------VTPF 204
Cdd:COG1064  193 dRSPEKLELARELGADHVVNSSDEDPVEAVRELTGADVVIDTV-GAPATVNAalALLRR--GGRLVLVglpggpipLPPF 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 205 LLNMDRLGIAdgmlqtGVTVGSKALkhfwkgvhyrwaffmasgpcLDDIAELVDAGKIRPVIEqTFPFSKVPEAFLKVER 284
Cdd:COG1064  270 DLILKERSIR------GSLIGTRAD--------------------LQEMLDLAAEGKIKPEVE-TIPLEEANEALERLRA 322

                 ....*....
gi 974005217 285 GHARGKTVI 293
Cdd:COG1064  323 GKVRGRAVL 331
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
7-259 7.45e-42

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: 145.16  E-value: 7.45e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217   7 HVKIKGEEFPLTLGRDVSGVVMECGLDVKYFKPGDEVWAAVPPW--------------------KQGTLSEFVVVSGNEV 66
Cdd:cd05188   21 GGYPPPPKLPLILGHEGAGVVVEVGPGVTGVKVGDRVVVLPNLGcgtcelcrelcpgggilgegLDGGFAEYVVVPADNL 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  67 SHKPKSLTHTQAASLPYVALTAWSAINKVGGLNdkncTGKRVLILGAsGGVGTFAIQVMKAWDAHVTAVC-SQDASELVR 145
Cdd:cd05188  101 VPLPDGLSLEEAALLPEPLATAYHALRRAGVLK----PGDTVLVLGA-GGVGLLAAQLAKAAGARVIVTDrSDEKLELAK 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 146 KLGADDVIDYKSGSVEEQLKSLKP--FDFILDNVGG-STETWAPDFLKKwsGATYVTLVTPfllnmdrlgiadgmlqTGV 222
Cdd:cd05188  176 ELGADHVIDYKEEDLEEELRLTGGggADVVIDAVGGpETLAQALRLLRP--GGRIVVVGGT----------------SGG 237
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 974005217 223 TVGSKALKHFWKGVHYRWAFfmasGPCLDDIAELVDA 259
Cdd:cd05188  238 PPLDDLRRLLFKELTIIGST----GGTREDFEEALDL 270
adh_fam_1 TIGR02817
zinc-binding alcohol dehydrogenase family protein; Members of this model form a distinct ...
4-294 7.75e-40

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: 141.80  E-value: 7.75e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217    4 DPLHVKIK-----GEEFPLTLGRDVSGVVMECGLDVKYFKPGDEVWAAVPPWKQGTLSEFVVVSGNEVSHKPKSLTHTQA 78
Cdd:TIGR02817  42 NPVDTKVRarmapEAGQPKILGWDAAGVVVAVGDEVTLFKPGDEVWYAGDIDRPGSNAEFHLVDERIVGHKPKSLSFAEA 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217   79 ASLPYVALTAWSAI-NKVGGLNDKNCTGKRVLILGASGGVGTFAIQVMKAW-DAHVTAVCSQ-DASELVRKLGADDVIDY 155
Cdd:TIGR02817 122 AALPLTSITAWELLfDRLGINDPVAGDKRALLIIGGAGGVGSILIQLARQLtGLTVIATASRpESQEWVLELGAHHVIDH 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  156 kSGSVEEQLKSLKPFDfiLDNVGGSTETwapdflkkwsgATYVTLVTPFLLNMDRLGIADGMLQTGVT-VGSKALKHFWK 234
Cdd:TIGR02817 202 -SKPLKAQLEKLGLEA--VSYVFSLTHT-----------DQHFKEIVELLAPQGRFALIDDPAELDISpFKRKSISLHWE 267
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 974005217  235 GVHYRWAF----FMASGPCLDDIAELVDAGKIRPVIEQTfpFSKVPEAFLK-----VERGHARGKTVIN 294
Cdd:TIGR02817 268 FMFTRSMFqtadMIEQHHLLNRVARLVDAGKIRTTLAET--FGTINAANLKrahalIESGKARGKIVLE 334
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
13-295 7.98e-39

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: 138.87  E-value: 7.98e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  13 EEFPLTLGRDVSGVVMECGLDVKYFKPGDEVWA--AVPPWKQGTLSEFVVVSGNEVSHKPKSLTHTQAASLPYVALTAWS 90
Cdd:cd08253   55 PPLPYVPGSDGAGVVEAVGEGVDGLKVGDRVWLtnLGWGRRQGTAAEYVVVPADQLVPLPDGVSFEQGAALGIPALTAYR 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  91 AINKVGGLNdkncTGKRVLILGASGGVGTFAIQVMKAWDAHVTAVCSQDAS-ELVRKLGADDVIDYKSGSVEEQLKSL-- 167
Cdd:cd08253  135 ALFHRAGAK----AGETVLVHGGSGAVGHAAVQLARWAGARVIATASSAEGaELVRQAGADAVFNYRAEDLADRILAAta 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 168 -KPFDFILDNVGGSTETWAPDFLKKwsGATYVTlvtpfllnmdrlgIADGMLQTGVTVGSkalkHFWKGVHYRWAFFMAS 246
Cdd:cd08253  211 gQGVDVIIEVLANVNLAKDLDVLAP--GGRIVV-------------YGSGGLRGTIPINP----LMAKEASIRGVLLYTA 271
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 974005217 247 GP-----CLDDIAELVDAGKIRPVIEQTFPFSKVPEAFLKVERGHARGKTVINV 295
Cdd:cd08253  272 TPeeraaAAEAIAAGLADGALRPVIAREYPLEEAAAAHEAVESGGAIGKVVLDP 325
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
16-293 4.86e-38

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 135.59  E-value: 4.86e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217    16 PLTLGRDVSGVVMECGLDVKYFKPGDEVWAAVPpwkqGTLSEFVVVSGNEVSHKPKSLTHTQAASLPYVALTAWSAINKV 95
Cdd:smart00829  23 EAVLGGECAGVVTRVGPGVTGLAVGDRVMGLAP----GAFATRVVTDARLVVPIPDGWSFEEAATVPVVFLTAYYALVDL 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217    96 GGLNDknctGKRVLILGASGGVGTFAIQVMKAWDAHVTA-VCSQDASELVRKLG--ADDVIDYKSGSVEEQLKSL---KP 169
Cdd:smart00829  99 ARLRP----GESVLIHAAAGGVGQAAIQLARHLGAEVFAtAGSPEKRDFLRALGipDDHIFSSRDLSFADEILRAtggRG 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217   170 FDFILDNVGGstetwapDFLKK-WSgatyvtLVTPF--LLNMDRLGIADGmlqtgvtvGSKALKHFWKGVHYRwAF---F 243
Cdd:smart00829 175 VDVVLNSLSG-------EFLDAsLR------CLAPGgrFVEIGKRDIRDN--------SQLAMAPFRPNVSYH-AVdldA 232
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 974005217   244 MASGP-----CLDDIAELVDAGKIRPVIEQTFPFSKVPEAFLKVERGHARGKTVI 293
Cdd:smart00829 233 LEEGPdrireLLAEVLELFAEGVLRPLPVTVFPISDAEDAFRYMQQGKHIGKVVL 287
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
14-295 1.02e-37

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: 135.87  E-value: 1.02e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  14 EFPLTLGRDVSGVVMECGLDVKYFKPGDEVWAAVPPWKQGTLSEFVVVSGNEVSHKPKSLTHTQAASLPYVALTAWSAIN 93
Cdd:cd08271   55 SYPHVPGVDGAGVVVAVGAKVTGWKVGDRVAYHASLARGGSFAEYTVVDARAVLPLPDSLSFEEAAALPCAGLTAYQALF 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  94 KVGGLNdkncTGKRVLILGASGGVGTFAIQVMKAWDAHVTAVCSQDASELVRKLGADDVIDYKSGSVEEQLKSL---KPF 170
Cdd:cd08271  135 KKLRIE----AGRTILITGGAGGVGSFAVQLAKRAGLRVITTCSKRNFEYVKSLGADHVIDYNDEDVCERIKEItggRGV 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 171 DFILDNVGGST-ETWAPdFLKkwSGATYVTLVTPFLLNMDRlgiadgMLQTGVTVGSKALKHFWK-GVHYRWAFFMASGp 248
Cdd:cd08271  211 DAVLDTVGGETaAALAP-TLA--FNGHLVCIQGRPDASPDP------PFTRALSVHEVALGAAHDhGDPAAWQDLRYAG- 280
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 974005217 249 clDDIAELVDAGKIRPVIEQTFPFSKVPEAFLKVERGHARGKTVINV 295
Cdd:cd08271  281 --EELLELLAAGKLEPLVIEVLPFEQLPEALRALKDRHTRGKIVVTI 325
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
14-295 1.95e-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: 135.46  E-value: 1.95e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  14 EFPLTLGRDVSGVVMECGLDVKYFKPGDEVWAAVPPW------------------------KQGTLSEFVVVSGNEVSHK 69
Cdd:cd08266   56 PLPHILGSDGAGVVEAVGPGVTNVKPGQRVVIYPGIScgrceyclagrenlcaqygilgehVDGGYAEYVAVPARNLLPI 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  70 PKSLTHTQAASLPYVALTAWSAINKVGGLNdkncTGKRVLILGASGGVGTFAIQVMKAWDAHV-TAVCSQDASELVRKLG 148
Cdd:cd08266  136 PDNLSFEEAAAAPLTFLTAWHMLVTRARLR----PGETVLVHGAGSGVGSAAIQIAKLFGATViATAGSEDKLERAKELG 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 149 ADDVIDYKSGSVEEQLKSL---KPFDFILDNVGGstETWAPDFLKKWSGATYVTlvtpfllnmdrlgiadgmlqTGVTVG 225
Cdd:cd08266  212 ADYVIDYRKEDFVREVRELtgkRGVDVVVEHVGA--ATWEKSLKSLARGGRLVT--------------------CGATTG 269
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 974005217 226 SKA---LKH-FWKGVHYRWAFfMASGPCLDDIAELVDAGKIRPVIEQTFPFSKVPEAFLKVERGHARGKTVINV 295
Cdd:cd08266  270 YEApidLRHvFWRQLSILGST-MGTKAELDEALRLVFRGKLKPVIDSVFPLEEAAEAHRRLESREQFGKIVLTP 342
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
14-295 3.54e-37

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: 134.59  E-value: 3.54e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  14 EFPLTLGRDVSGVVMECGLDVKYFKPGDEV-------WAAVPPWK-----------QGTLSEFVVVSGNEVSHKPKSLTH 75
Cdd:cd08276   56 KDPLIPLSDGAGEVVAVGEGVTRFKVGDRVvptffpnWLDGPPTAedeasalggpiDGVLAEYVVLPEEGLVRAPDHLSF 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  76 TQAASLPYVALTAWSAINKVGGLNdkncTGKRVLILGaSGGVGTFAIQVMKAWDAHVTAVCSQDA-SELVRKLGADDVID 154
Cdd:cd08276  136 EEAATLPCAGLTAWNALFGLGPLK----PGDTVLVQG-TGGVSLFALQFAKAAGARVIATSSSDEkLERAKALGADHVIN 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 155 YKSGS-VEEQLKSLKP---FDFILDNVGGST-----ETWAPD-------FLkkwSGATYVTLVTPFLLNMDRLgiadgml 218
Cdd:cd08276  211 YRTTPdWGEEVLKLTGgrgVDHVVEVGGPGTlaqsiKAVAPGgvisligFL---SGFEAPVLLLPLLTKGATL------- 280
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 974005217 219 qTGVTVGSKALkhfwkgvhyrwaffmasgpcLDDIAELVDAGKIRPVIEQTFPFSKVPEAFLKVERGHARGKTVINV 295
Cdd:cd08276  281 -RGIAVGSRAQ--------------------FEAMNRAIEAHRIRPVIDRVFPFEEAKEAYRYLESGSHFGKVVIRV 336
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
3-293 3.78e-36

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: 131.15  E-value: 3.78e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217   3 RDPLHVKIKGEEFPLTLGRDVSGVVMECGLDVKYFKPGDEVWAAVPpwkqGTLSEFVVVSGNEVSHKPKSLTHTQAASLP 82
Cdd:cd05195   15 RDVLVALGLLPGDETPLGLECSGIVTRVGSGVTGLKVGDRVMGLAP----GAFATHVRVDARLVVKIPDSLSFEEAATLP 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  83 YVALTAWSAINKVGGLndknCTGKRVLILGASGGVGTFAIQVMKAWDAHVTAVCSQDA-SELVRKLG--ADDVIDYKSGS 159
Cdd:cd05195   91 VAYLTAYYALVDLARL----QKGESVLIHAAAGGVGQAAIQLAQHLGAEVFATVGSEEkREFLRELGgpVDHIFSSRDLS 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 160 VEEQLKSL---KPFDFILDNVGGST--ETWApdflkkwsgatyvtLVTPF--LLNMDRLGIADGmlqtgvtvGSKALKHF 232
Cdd:cd05195  167 FADGILRAtggRGVDVVLNSLSGELlrASWR--------------CLAPFgrFVEIGKRDILSN--------SKLGMRPF 224
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 974005217 233 WKGVHYR---WAFFMASGP-----CLDDIAELVDAGKIRPVIEQTFPFSKVPEAFLKVERGHARGKTVI 293
Cdd:cd05195  225 LRNVSFSsvdLDQLARERPellreLLREVLELLEAGVLKPLPPTVVPSASEIDAFRLMQSGKHIGKVVL 293
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
16-295 1.36e-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: 128.09  E-value: 1.36e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  16 PLTLGRDVSGVVMECGLDVKYFKPGDEVWAAVPpwkQGTLSEFVVVSGNEVSHKPKSLTHTQAASLPYVALTAWSAINKV 95
Cdd:cd08275   57 PFVPGFECAGTVEAVGEGVKDFKVGDRVMGLTR---FGGYAEVVNVPADQVFPLPDGMSFEEAAAFPVNYLTAYYALFEL 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  96 GGLNDknctGKRVLILGASGGVGTFAIQVMKAWDaHVTAV--CSQDASELVRKLGADDVIDYKSGSVEEQLK--SLKPFD 171
Cdd:cd08275  134 GNLRP----GQSVLVHSAAGGVGLAAGQLCKTVP-NVTVVgtASASKHEALKENGVTHVIDYRTQDYVEEVKkiSPEGVD 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 172 FILDNVGGstetwaPDFLKKWsgatyvTLVTPfllnMDRL---GIADgmLQTGVTVGS-KALKHFWK------------- 234
Cdd:cd08275  209 IVLDALGG------EDTRKSY------DLLKP----MGRLvvyGAAN--LVTGEKRSWfKLAKKWWNrpkvdpmklisen 270
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 974005217 235 ----GVHYRWAFFMASG--PCLDDIAELVDAGKIRPVIEQTFPFSKVPEAFLKVERGHARGKTVINV 295
Cdd:cd08275  271 ksvlGFNLGWLFEERELltEVMDKLLKLYEEGKIKPKIDSVFPFEEVGEAMRRLQSRKNIGKVVLTP 337
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
14-295 2.36e-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: 176229 [Multi-domain]  Cd Length: 328  Bit Score: 121.94  E-value: 2.36e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  14 EFPLTLGRDVSGVVMECGLDVKYFKPGDEVwaAVPPW----KQGTLSEFVVVSGNEVSHKPKSLTHTQAASLPYVALTAW 89
Cdd:cd08268   56 PLPARLGYEAAGVVEAVGAGVTGFAVGDRV--SVIPAadlgQYGTYAEYALVPAAAVVKLPDGLSFVEAAALWMQYLTAY 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  90 SAINKVGGLNDknctGKRVLILGASGGVGTFAIQVMKAWDAHVTAVC-SQDASELVRKLGADDVIDYKSGSVEEQLKSL- 167
Cdd:cd08268  134 GALVELAGLRP----GDSVLITAASSSVGLAAIQIANAAGATVIATTrTSEKRDALLALGAAHVIVTDEEDLVAEVLRIt 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 168 --KPFDFILDNVGGstetwaPDFlkkwsgatyvtlvTPFLLNMDRLGI-----ADGMLQTGVTVGSKALKHFWKGVHYRW 240
Cdd:cd08268  210 ggKGVDVVFDPVGG------PQF-------------AKLADALAPGGTlvvygALSGEPTPFPLKAALKKSLTFRGYSLD 270
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 974005217 241 AFFM---ASGPCLDDIAELVDAGKIRPVIEQTFPFSKVPEAFLKVERGHARGKTVINV 295
Cdd:cd08268  271 EITLdpeARRRAIAFILDGLASGALKPVVDRVFPFDDIVEAHRYLESGQQIGKIVVTP 328
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
14-293 3.62e-31

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: 117.91  E-value: 3.62e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  14 EFPLTLGRDVSGVVMECGLDVKYFKPGDEVWAAVPPwKQGTLSEFVVVSGNEVSHKPKSLTHTQAASLPYVALTAWSAIN 93
Cdd:cd08251   36 PYPFTPGFEASGVVRAVGPHVTRLAVGDEVIAGTGE-SMGGHATLVTVPEDQVVRKPASLSFEEACALPVVFLTVIDAFA 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  94 KvGGLNDknctGKRVLILGASGGVGTFAIQVMKAWDA--HVTAvCSQDASELVRKLGADDVIDYKSGSVEEQLKSL---K 168
Cdd:cd08251  115 R-AGLAK----GEHILIQTATGGTGLMAVQLARLKGAeiYATA-SSDDKLEYLKQLGVPHVINYVEEDFEEEIMRLtggR 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 169 PFDFILDNVGGSTETWAPDFLKKwsGATYVTLVTPFLLNMDRLGIAdgMLQTGVTVGSKALKHFWKGVHYRWAFFMAsgp 248
Cdd:cd08251  189 GVDVVINTLSGEAIQKGLNCLAP--GGRYVEIAMTALKSAPSVDLS--VLSNNQSFHSVDLRKLLLLDPEFIADYQA--- 261
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 974005217 249 cldDIAELVDAGKIRPVIEQTFPFSKVPEAFLKVERGHARGKTVI 293
Cdd:cd08251  262 ---EMVSLVEEGELRPTVSRIFPFDDIGEAYRYLSDRENIGKVVV 303
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
19-295 1.17e-30

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 117.44  E-value: 1.17e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  19 LGRDVSGVVMECGLDVKYFKPGDEVWAAVPpwkQGTLSEFVVVSGNEVSHKPKSLTHTQAASLPYVALTAWSAINKVGGL 98
Cdd:PTZ00354  62 LGLEVAGYVEDVGSDVKRFKEGDRVMALLP---GGGYAEYAVAHKGHVMHIPQGYTFEEAAAIPEAFLTAWQLLKKHGDV 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  99 NdkncTGKRVLILGASGGVGTFAIQVMKAWDAH-VTAVCSQDASELVRKLGADDVIDYK--SGSVEEQLKSLKP--FDFI 173
Cdd:PTZ00354 139 K----KGQSVLIHAGASGVGTAAAQLAEKYGAAtIITTSSEEKVDFCKKLAAIILIRYPdeEGFAPKVKKLTGEkgVNLV 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 174 LDNVGGS-----TETWAPDflKKW------SGATYVTL-VTPFLlnMDRLGIADGMLQTGvTVGSKA--LKHFWKgvhyr 239
Cdd:PTZ00354 215 LDCVGGSylsetAEVLAVD--GKWivygfmGGAKVEKFnLLPLL--RKRASIIFSTLRSR-SDEYKAdlVASFER----- 284
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 974005217 240 waffmasgpcldDIAELVDAGKIRPVIEQTFPFSKVPEAFLKVERGHARGKTVINV 295
Cdd:PTZ00354 285 ------------EVLPYMEEGEIKPIVDRTYPLEEVAEAHTFLEQNKNIGKVVLTV 328
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
14-293 9.15e-28

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: 109.45  E-value: 9.15e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  14 EFPLTLGRDVSGVVMECGLDVKYFKPGDEV-WAAVPpwkqGTLSEFVVVSGNEVSHKPKSLTHTQAASLPYVALTAWSAI 92
Cdd:cd05286   53 PLPFVLGVEGAGVVEAVGPGVTGFKVGDRVaYAGPP----GAYAEYRVVPASRLVKLPDGISDETAAALLLQGLTAHYLL 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  93 NKVGGLNdkncTGKRVLILGASGGVGTFAIQVMKAWDAHVTAVCSQDAS-ELVRKLGADDVIDYKSGSVEEQLKSL---K 168
Cdd:cd05286  129 RETYPVK----PGDTVLVHAAAGGVGLLLTQWAKALGATVIGTVSSEEKaELARAAGADHVINYRDEDFVERVREItggR 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 169 PFDFILDNVGGSteTWAPDFLKKWSGATYVTL------VTPFllNMDRLGiadgmlQTGVTVGSKALKHFwkgVHYRWAF 242
Cdd:cd05286  205 GVDVVYDGVGKD--TFEGSLDSLRPRGTLVSFgnasgpVPPF--DLLRLS------KGSLFLTRPSLFHY---IATREEL 271
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 974005217 243 FMASGpcldDIAELVDAGKIRPVIEQTFPFSKVPEAFLKVERGHARGKTVI 293
Cdd:cd05286  272 LARAA----ELFDAVASGKLKVEIGKRYPLADAAQAHRDLESRKTTGKLLL 318
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
15-293 4.25e-26

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: 105.04  E-value: 4.25e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  15 FPLTLGRDVSGVVMECGLDVKYFKPGDEVwAAVPPWkqGTLSEFVVVSGNEVSHKPKSLTHTQAASLPYVALTAWSAINK 94
Cdd:cd08273   57 LPFTPGYDLVGRVDALGSGVTGFEVGDRV-AALTRV--GGNAEYINLDAKYLVPVPEGVDAAEAVCLVLNYVTAYQMLHR 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  95 VGglndKNCTGKRVLILGASGGVGTFAIQVMKAWDAHVTAVCSQDASELVRKLGAdDVIDYKSGSVEEQLKSLKPFDFIL 174
Cdd:cd08273  134 AA----KVLTGQRVLIHGASGGVGQALLELALLAGAEVYGTASERNHAALRELGA-TPIDYRTKDWLPAMLTPGGVDVVF 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 175 DNVGGstetwaPDFLKKWSG-ATYVTLVTpFLLNMDRLGiaDGMLQTGVTVGSKALKHFW-----KGVHY---RWAFFMA 245
Cdd:cd08273  209 DGVGG------ESYEESYAAlAPGGTLVC-YGGNSSLLQ--GRRSLAALGSLLARLAKLKllptgRRATFyyvWRDRAED 279
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 974005217 246 SGPCLDDIAELVD---AGKIRPVIEQTFPFSKVPEAFLKVERGHARGKTVI 293
Cdd:cd08273  280 PKLFRQDLTELLDllaKGKIRPKIAKRLPLSEVAEAHRLLESGKVVGKIVL 330
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
16-294 1.68e-25

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: 103.55  E-value: 1.68e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  16 PLTLGRDVSGVVMECGLDVKYFKPGDEV--WAAVPPWK----------------------QGTLSEFVVVSGNEVSHKPK 71
Cdd:cd08259   55 PLILGHEIVGTVEEVGEGVERFKPGDRVilYYYIPCGKceyclsgeenlcrnraeygeevDGGFAEYVKVPERSLVKLPD 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  72 SLTHTQAASLPYVALTAWSAINKVGglnDKncTGKRVLILGASGGVGTFAIQVMKAWDAHVTAVC-SQDASELVRKLGAD 150
Cdd:cd08259  135 NVSDESAALAACVVGTAVHALKRAG---VK--KGDTVLVTGAGGGVGIHAIQLAKALGARVIAVTrSPEKLKILKELGAD 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 151 DVIDykSGSVEEQLKSLKPFDFILDNVGgsTETWAPDFLKKWSGATYVTL--VTPFLLNMdRLGIAdgMLQTGVTVGSka 228
Cdd:cd08259  210 YVID--GSKFSEDVKKLGGADVVIELVG--SPTIEESLRSLNKGGRLVLIgnVTPDPAPL-RPGLL--ILKEIRIIGS-- 280
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 974005217 229 lkhfwkgvhyrwaffmaSGPCLDDIAE---LVDAGKIRPVIEQTFPFSKVPEAFLKVERGHARGKTVIN 294
Cdd:cd08259  281 -----------------ISATKADVEEalkLVKEGKIKPVIDRVVSLEDINEALEDLKSGKVVGRIVLK 332
quinone_oxidoreductase_like_1 cd08243
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
14-293 2.23e-25

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: 102.69  E-value: 2.23e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  14 EFPLTLGRDVSGVVMECGLDvkYFKPGDEVWAAV----PPWkQGTLSEFVVVSGNEVSHKPKSLTHTQAASLPYVALTAW 89
Cdd:cd08243   55 KFPRVLGIEAVGEVEEAPGG--TFTPGQRVATAMggmgRTF-DGSYAEYTLVPNEQVYAIDSDLSWAELAALPETYYTAW 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  90 SAINKVGGLndknCTGKRVLILGASGGVGTFAIQVMKAWDAHVTA-VCSQDASELVRKLGADDV-IDykSGSVEEQLKSL 167
Cdd:cd08243  132 GSLFRSLGL----QPGDTLLIRGGTSSVGLAALKLAKALGATVTAtTRSPERAALLKELGADEVvID--DGAIAEQLRAA 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 168 -KPFDFILDNVGGSTetwAPDFLKkwsgatyvtLVTPFllnmdrlGIAdgmLQTGVTVGSKALKHF------WKGVH-YR 239
Cdd:cd08243  206 pGGFDKVLELVGTAT---LKDSLR---------HLRPG-------GIV---CMTGLLGGQWTLEDFnpmddiPSGVNlTL 263
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 974005217 240 WAFFMASGP--CLDDIAELVDAGKIRPVIEQTFPFSKVPEAFLKVERGHARGKTVI 293
Cdd:cd08243  264 TGSSSGDVPqtPLQELFDFVAAGHLDIPPSKVFTFDEIVEAHAYMESNRAFGKVVV 319
ADH_zinc_N_2 pfam13602
Zinc-binding dehydrogenase;
147-293 3.03e-25

Zinc-binding dehydrogenase;


Pssm-ID: 433341 [Multi-domain]  Cd Length: 131  Bit Score: 97.78  E-value: 3.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  147 LGADDVIDYKSGSVEEQLKSlKPFDFILDNVGGSTETWAPDFLKKwsGATYVTLVTPFLLnmdrlgiadgmlqtgVTVGS 226
Cdd:pfam13602   1 LGADEVIDYRTTDFVQATGG-EGVDVVLDTVGGEAFEASLRVLPG--GGRLVTIGGPPLS---------------AGLLL 62
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 974005217  227 KALKHFWKGVHYRWAFFMASGP--CLDDIAELVDAGKIRPVIEQTFPFSKVPEAFLKVERGHARGKTVI 293
Cdd:pfam13602  63 PARKRGGRGVKYLFLFVRPNLGadILQELADLIEEGKLRPVIDRVFPLEEAAEAHRYLESGRARGKIVL 131
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
16-294 4.06e-24

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: 99.63  E-value: 4.06e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  16 PLTLGRDVSGVVMECGLDVKYFKPGDEV--WAAVPPWK----------------------QGTLSEFVVVSGNEVSHKPK 71
Cdd:cd08254   57 PLTLGHEIAGTVVEVGAGVTNFKVGDRVavPAVIPCGAcalcrrgrgnlclnqgmpglgiDGGFAEYIVVPARALVPVPD 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  72 SLTHTQAASLPYVALTAWSAINKVGGLNDknctGKRVLILGAsGGVGTFAIQVMKAWDAHVTAV-CSQDASELVRKLGAD 150
Cdd:cd08254  137 GVPFAQAAVATDAVLTPYHAVVRAGEVKP----GETVLVIGL-GGLGLNAVQIAKAMGAAVIAVdIKEEKLELAKELGAD 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 151 DVIDYK---SGSVEEQLKSLKpFDFILDNVG-GSTETWAPDFLKkwSGATYVtLVTpflLNMDRLGIadgMLQTGVTVGS 226
Cdd:cd08254  212 EVLNSLddsPKDKKAAGLGGG-FDVIFDFVGtQPTFEDAQKAVK--PGGRIV-VVG---LGRDKLTV---DLSDLIAREL 281
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 974005217 227 KALKHFWkgvhyrwaffmasgpCL-DDIAELVD---AGKIRPVIEqTFPFSKVPEAFLKVERGHARGKTVIN 294
Cdd:cd08254  282 RIIGSFG---------------GTpEDLPEVLDliaKGKLDPQVE-TRPLDEIPEVLERLHKGKVKGRVVLV 337
CAD cd08245
Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases ...
12-293 5.10e-24

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: 99.32  E-value: 5.10e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  12 GEEFPLTLGRDVSGVVMECGLDVKYFKPGDEV---W---------------------AAVPPWK-QGTLSEFVVVSGNEV 66
Cdd:cd08245   50 GSKYPLVPGHEIVGEVVEVGAGVEGRKVGDRVgvgWlvgscgrceycrrglenlcqkAVNTGYTtQGGYAEYMVADAEYT 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  67 SHKPKSLTHTQAASLPYVALTAWSAInKVGGLNDknctGKRVLILGAsGGVGTFAIQVMKAWDAHVTAVC-SQDASELVR 145
Cdd:cd08245  130 VLLPDGLPLAQAAPLLCAGITVYSAL-RDAGPRP----GERVAVLGI-GGLGHLAVQYARAMGFETVAITrSPDKRELAR 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 146 KLGADDVIDykSGSVEEQLKSLKPFDFILDNVggSTETWAPDFLK--KWSG--------ATYVTLVTPFLLNMDRLGIAd 215
Cdd:cd08245  204 KLGADEVVD--SGAELDEQAAAGGADVILVTV--VSGAAAEAALGglRRGGrivlvglpESPPFSPDIFPLIMKRQSIA- 278
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 974005217 216 gmlqtGVTVGSKALkhfwkgvhyrwaffmasgpcLDDIAELVDAGKIRPVIEqTFPFSKVPEAFLKVERGHARGKTVI 293
Cdd:cd08245  279 -----GSTHGGRAD--------------------LQEALDFAAEGKVKPMIE-TFPLDQANEAYERMEKGDVRFRFVL 330
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
15-293 1.44e-23

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 98.19  E-value: 1.44e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  15 FPLTLGRDVSGVVMECGLDVKYFKPGDEVWAA--VPPWK----------------------QGTLSEFVVVSGNEVSHKP 70
Cdd:PRK13771  54 YPVILGHEVVGTVEEVGENVKGFKPGDRVASLlyAPDGTceycrsgeeaycknrlgygeelDGFFAEYAKVKVTSLVKVP 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  71 KSLTHTQAASLPYVALTAWSAInKVGGLNDknctGKRVLILGASGGVGTFAIQVMKAWDAHVTAVCS-QDASELVRKLgA 149
Cdd:PRK13771 134 PNVSDEGAVIVPCVTGMVYRGL-RRAGVKK----GETVLVTGAGGGVGIHAIQVAKALGAKVIAVTSsESKAKIVSKY-A 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 150 DDVIDYKSGSveEQLKSLKPFDFILDNVGGST--ETwapdfLKK-WSGATYVTL--VTPFLLNMDRLG--IADGMLQTGV 222
Cdd:PRK13771 208 DYVIVGSKFS--EEVKKIGGADIVIETVGTPTleES-----LRSlNMGGKIIQIgnVDPSPTYSLRLGyiILKDIEIIGH 280
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 974005217 223 TVGSKAlkhfwkgvhyrwaffmasgpCLDDIAELVDAGKIRPVIEQTFPFSKVPEAFLKVERGHARGKTVI 293
Cdd:PRK13771 281 ISATKR--------------------DVEEALKLVAEGKIKPVIGAEVSLSEIDKALEELKDKSRIGKILV 331
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
14-293 2.19e-23

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: 97.35  E-value: 2.19e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  14 EFPLTLGRDVSGVVMECGLDVKYFKPGDEVwaaVPPWKQGTLSEFVVVSGNEVSHKPKSLTHTQAASLpYV-ALTAWSAI 92
Cdd:cd05282   55 PLPAVPGNEGVGVVVEVGSGVSGLLVGQRV---LPLGGEGTWQEYVVAPADDLIPVPDSISDEQAAML-YInPLTAWLML 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  93 NKVGGLNdkncTGKRVLILGASGGVGTFAIQVMKAWDAHVTAVCSQDAS-ELVRKLGADDVIDYKSGSVEEQLKSL---K 168
Cdd:cd05282  131 TEYLKLP----PGDWVIQNAANSAVGRMLIQLAKLLGFKTINVVRRDEQvEELKALGADEVIDSSPEDLAQRVKEAtggA 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 169 PFDFILDNVGGStetwapdflkkwSGATYVTLVTPF--LLNmdrLGIADGMLQT-GVTVGSK---ALKHFWkgvHYRWaf 242
Cdd:cd05282  207 GARLALDAVGGE------------SATRLARSLRPGgtLVN---YGLLSGEPVPfPRSVFIFkdiTVRGFW---LRQW-- 266
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 974005217 243 fMASGP------CLDDIAELVDAGKIRPVIEQTFPFSKVPEAFLKVERGHARGKTVI 293
Cdd:cd05282  267 -LHSATkeakqeTFAEVIKLVEAGVLTTPVGAKFPLEDFEEAVAAAEQPGRGGKVLL 322
MDR4 cd08270
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
20-295 2.27e-23

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: 97.06  E-value: 2.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  20 GRDVSGVVMECGLDVKYFKPGDEVWAAVPPwkqGTLSEFVVVSGNEVSHKPKSLTHTQAASLPYVALTAWSAINKVGGLn 99
Cdd:cd08270   56 GWDAAGVVERAAADGSGPAVGARVVGLGAM---GAWAELVAVPTGWLAVLPDGVSFAQAATLPVAGVTALRALRRGGPL- 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 100 dkncTGKRVLILGASGGVGTFAIQVMKAWDAHVTAVCSQDA-SELVRKLGADDVIdyksgsVEEQLKSLKPFDFILDNVG 178
Cdd:cd08270  132 ----LGRRVLVTGASGGVGRFAVQLAALAGAHVVAVVGSPArAEGLRELGAAEVV------VGGSELSGAPVDLVVDSVG 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 179 GSTETWAPDFLKKwsGATYVTlvtpfllnmdrLGIADG------MLQTGVTVGSKALKHFWKGVhyrwafFMASGPCLDD 252
Cdd:cd08270  202 GPQLARALELLAP--GGTVVS-----------VGSSSGepavfnPAAFVGGGGGRRLYTFFLYD------GEPLAADLAR 262
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 974005217 253 IAELVDAGKIRPVIEQTFPFSKVPEAFLKVERGHARGKTVINV 295
Cdd:cd08270  263 LLGLVAAGRLDPRIGWRGSWTEIDEAAEALLARRFRGKAVLDV 305
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
15-295 1.05e-22

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: 96.21  E-value: 1.05e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  15 FPLTLGRDVSGVVMECGLDVKYFKPGDEV------WAAVPPWKQ----------GTLSEFVVVSGNEVSHKPKSLTHTQA 78
Cdd:cd08274   77 FPRIQGADIVGRVVAVGEGVDTARIGERVlvdpsiRDPPEDDPAdidyigserdGGFAEYTVVPAENAYPVNSPLSDVEL 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  79 ASLPYVALTAWSAINKvGGLNdkncTGKRVLILGASGGVGTFAIQVMKAWDAHVTAVCSQDASELVRKLGADDVIdYKSG 158
Cdd:cd08274  157 ATFPCSYSTAENMLER-AGVG----AGETVLVTGASGGVGSALVQLAKRRGAIVIAVAGAAKEEAVRALGADTVI-LRDA 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 159 SVEEQLKSLK--PFDFILDNVGGSTetwAPDFLKKW-SGATYVTlvtpfllnmdrLG-IADGMLQTGV-TVGSKALKHFW 233
Cdd:cd08274  231 PLLADAKALGgePVDVVADVVGGPL---FPDLLRLLrPGGRYVT-----------AGaIAGPVVELDLrTLYLKDLTLFG 296
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 974005217 234 KGVHYRWAFfmasgpclDDIAELVDAGKIRPVIEQTFPFSKVPEA---FLkvERGHArGKTVINV 295
Cdd:cd08274  297 STLGTREVF--------RRLVRYIEEGEIRPVVAKTFPLSEIREAqaeFL--EKRHV-GKLVLVP 350
CAD3 cd08297
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
15-293 3.27e-22

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: 94.52  E-value: 3.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  15 FPLTLGRDVSGVVMECGLDVKYFKPGDEVwaAVPP--------------WKQ-------------GTLSEFVVVSGNEVS 67
Cdd:cd08297   56 LPLIGGHEGAGVVVAVGPGVSGLKVGDRV--GVKWlydacgkceycrtgDETlcpnqknsgytvdGTFAEYAIADARYVT 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  68 HKPKSLTHTQAASLPYVALTAWSAINKVGGlndknCTGKRVLILGASGGVGTFAIQVMKAWDAHVTAVCSQDAS-ELVRK 146
Cdd:cd08297  134 PIPDGLSFEQAAPLLCAGVTVYKALKKAGL-----KPGDWVVISGAGGGLGHLGVQYAKAMGLRVIAIDVGDEKlELAKE 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 147 LGADDVIDYKSGSVEEQLK----------------SLKPFDfildnvggstetWAPDFLKKwsGATYVTL---------V 201
Cdd:cd08297  209 LGADAFVDFKKSDDVEAVKeltggggahavvvtavSAAAYE------------QALDYLRP--GGTLVCVglppggfipL 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 202 TPFLLNMDRLGIadgmlqTGVTVGSKAlkhfwkgvhyrwaffmasgpcldDIAELVD---AGKIRPVIeQTFPFSKVPEA 278
Cdd:cd08297  275 DPFDLVLRGITI------VGSLVGTRQ-----------------------DLQEALEfaaRGKVKPHI-QVVPLEDLNEV 324
                        330
                 ....*....|....*
gi 974005217 279 FLKVERGHARGKTVI 293
Cdd:cd08297  325 FEKMEEGKIAGRVVV 339
crotonyl_coA_red cd08246
crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase ...
20-295 2.73e-21

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: 92.48  E-value: 2.73e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  20 GRDVSGVVMECGLDVKYFKPGDEV------WAAVPPWKQ-------------------GTLSEFVVVSGNEVSHKPKSLT 74
Cdd:cd08246   86 GSDASGIVWAVGEGVKNWKVGDEVvvhcsvWDGNDPERAggdpmfdpsqriwgyetnyGSFAQFALVQATQLMPKPKHLS 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  75 HTQAASLPYVALTAWSAINKVGGLNDKncTGKRVLILGASGGVGTFAIQVMKAWDAHVTAVCSQDA-SELVRKLGADDVI 153
Cdd:cd08246  166 WEEAAAYMLVGATAYRMLFGWNPNTVK--PGDNVLIWGASGGLGSMAIQLARAAGANPVAVVSSEEkAEYCRALGAEGVI 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 154 DYK---------SGSVEEQ---LKSLKPF-DFILDNVGGSTetwAPDFLKKWSGATyvTLVTPFLLNMDRlgiadGMLQT 220
Cdd:cd08246  244 NRRdfdhwgvlpDVNSEAYtawTKEARRFgKAIWDILGGRE---DPDIVFEHPGRA--TFPTSVFVCDRG-----GMVVI 313
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 221 -GVTVGSKA---LKHFW------KGVHYrwaffmASGPCLDDIAELVDAGKIRPVIEQTFPFSKVPEAFLKVERG-HARG 289
Cdd:cd08246  314 cAGTTGYNHtydNRYLWmrqkriQGSHF------ANDREAAEANRLVMKGRIDPCLSKVFSLDETPDAHQLMHRNqHHVG 387

                 ....*.
gi 974005217 290 KTVINV 295
Cdd:cd08246  388 NMAVLV 393
PGDH cd05288
Prostaglandin dehydrogenases; Prostaglandins and related eicosanoids are metabolized by the ...
37-293 1.39e-20

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: 89.85  E-value: 1.39e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  37 FKPGDEVwAAVPPWKqgtlsEFVVVSGNEVSHKpksLTHTQAASLPY-------VALTAWSAINKVGGLNDknctGKRVL 109
Cdd:cd05288   84 FKVGDLV-SGFLGWQ-----EYAVVDGASGLRK---LDPSLGLPLSAylgvlgmTGLTAYFGLTEIGKPKP----GETVV 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 110 ILGASGGVGTFAIQVMKAWDAHVTAVCSQD--ASELVRKLGADDVIDYKSGSVEEQLKSLKPfDFI---LDNVGGSTETW 184
Cdd:cd05288  151 VSAAAGAVGSVVGQIAKLLGARVVGIAGSDekCRWLVEELGFDAAINYKTPDLAEALKEAAP-DGIdvyFDNVGGEILDA 229
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 185 APDFLKK-----WSGA--TYVTLVTPFLLNMDRLGIADGMLQtGVTVGSkalkhfwkgvhyrwaFFMASGPCLDDIAELV 257
Cdd:cd05288  230 ALTLLNKggriaLCGAisQYNATEPPGPKNLGNIITKRLTMQ-GFIVSD---------------YADRFPEALAELAKWL 293
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 974005217 258 DAGKIRPVIEQTFPFSKVPEAFLKVERGHARGKTVI 293
Cdd:cd05288  294 AEGKLKYREDVVEGLENAPEAFLGLFTGKNTGKLVV 329
MDR_enoyl_red cd08244
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. ...
14-293 2.21e-20

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: 89.35  E-value: 2.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  14 EFPLTLGRDVSGVVMECGLDVkyfkpgDEVW-----AAVPPWKQGTLSEFVVVSGNEVSHKPKSLTHTQAASLPYVALTA 88
Cdd:cd08244   58 ELPYVPGGEVAGVVDAVGPGV------DPAWlgrrvVAHTGRAGGGYAELAVADVDSLHPVPDGLDLEAAVAVVHDGRTA 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  89 wSAINKVGGLNdkncTGKRVLILGASGGVGTFAIQVMKAWDAHVTAVCSQDA-SELVRKLGADDVIDYK----SGSVEEQ 163
Cdd:cd08244  132 -LGLLDLATLT----PGDVVLVTAAAGGLGSLLVQLAKAAGATVVGAAGGPAkTALVRALGADVAVDYTrpdwPDQVREA 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 164 LKSlKPFDFILDNVGGSTETWAPDFLKkwSGATYVTlvtpfllnmdrLGIADGmLQTGVTVGSKALkhfwKGVHYRWAF- 242
Cdd:cd08244  207 LGG-GGVTVVLDGVGGAIGRAALALLA--PGGRFLT-----------YGWASG-EWTALDEDDARR----RGVTVVGLLg 267
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 974005217 243 -FMASGPCLDDIAE---LVDAGKIRPVIEQTFPFSKVPEAFLKVERGHARGKTVI 293
Cdd:cd08244  268 vQAERGGLRALEARalaEAAAGRLVPVVGQTFPLERAAEAHAALEARSTVGKVLL 322
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
6-293 5.81e-20

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: 88.39  E-value: 5.81e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217   6 LHV------KIKGEEFPLTLGRDVSGVVMECGLDVKYFKPGDEVwAAVPPWKQGT------------------------- 54
Cdd:cd05284   42 LHVidgvwgGILPYKLPFTLGHENAGWVEEVGSGVDGLKEGDPV-VVHPPWGCGTcrycrrgeenycenarfpgigtdgg 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  55 LSEFVVVSGNEVSHKPKSLTHTQAASLPYVALTAWSAINKvggLNDKNCTGKRVLILGAsGGVGTFAIQVMKAW-DAHVT 133
Cdd:cd05284  121 FAEYLLVPSRRLVKLPRGLDPVEAAPLADAGLTAYHAVKK---ALPYLDPGSTVVVIGV-GGLGHIAVQILRALtPATVI 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 134 AV-CSQDASELVRKLGADDVIDyKSGSVEEQLKSL---KPFDFILDNVG-GSTETWAPDFLKKwsGATYV--------TL 200
Cdd:cd05284  197 AVdRSEEALKLAERLGADHVLN-ASDDVVEEVRELtggRGADAVIDFVGsDETLALAAKLLAK--GGRYVivgygghgRL 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 201 VTPFllnmdrlgiadgMLQTGVTV-GSkalkhFWkgvhyrwaffmASGPCLDDIAELVDAGKIRPVIEqTFPFSKVPEAF 279
Cdd:cd05284  274 PTSD------------LVPTEISViGS-----LW-----------GTRAELVEVVALAESGKVKVEIT-KFPLEDANEAL 324
                        330
                 ....*....|....
gi 974005217 280 LKVERGHARGKTVI 293
Cdd:cd05284  325 DRLREGRVTGRAVL 338
Zn_ADH_like2 cd08264
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
9-181 6.12e-20

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: 87.79  E-value: 6.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217   9 KIKGEEFPLTLGRDVSGVVMECGLDVKYFKPGDEV---------------------------WAAVppwKQGTLSEFVVV 61
Cdd:cd08264   48 AVKVKPMPHIPGAEFAGVVEEVGDHVKGVKKGDRVvvynrvfdgtcdmclsgnemlcrnggiIGVV---SNGGYAEYIVV 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  62 SGNEVSHKPKSLTHTQAASLPYVALTAWSAINKVGglndkNCTGKRVLILGASGGVGTFAIQVMKAWDAHVTAVCSQDas 141
Cdd:cd08264  125 PEKNLFKIPDSISDELAASLPVAALTAYHALKTAG-----LGPGETVVVFGASGNTGIFAVQLAKMMGAEVIAVSRKD-- 197
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 974005217 142 eLVRKLGADDVIDYKsgSVEEQLKSL-KPFDFILDNVGGST 181
Cdd:cd08264  198 -WLKEFGADEVVDYD--EVEEKVKEItKMADVVINSLGSSF 235
MDR_yhdh_yhfp cd05280
Yhdh and yhfp-like putative quinone oxidoreductases; Yhdh and yhfp-like putative quinone ...
14-206 1.01e-19

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: 87.21  E-value: 1.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  14 EFPLTLGRDVSGVVMECglDVKYFKPGDEVwaAVPPW-----KQGTLSEFVVVSGNEVSHKPKSLTHTQAASLPYVALTA 88
Cdd:cd05280   56 NYPHTPGIDAAGTVVSS--DDPRFREGDEV--LVTGYdlgmnTDGGFAEYVRVPADWVVPLPEGLSLREAMILGTAGFTA 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  89 WSAINKvggLNDKNCTGKR--VLILGASGGVGTFAIQVMKAWDAHVTAVC-SQDASELVRKLGADDVIDyKSGSVEEQLK 165
Cdd:cd05280  132 ALSVHR---LEDNGQTPEDgpVLVTGATGGVGSIAVAILAKLGYTVVALTgKEEQADYLKSLGASEVLD-REDLLDESKK 207
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 974005217 166 SLKP--FDFILDNVGGSTETWAPDFLKKW---------SGATYVTLVTPFLL 206
Cdd:cd05280  208 PLLKarWAGAIDTVGGDVLANLLKQTKYGgvvascgnaAGPELTTTVLPFIL 259
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
6-296 3.79e-19

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: 85.96  E-value: 3.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217   6 LHVKIKGEEFPLTLGRDVSGVVMECGLDVKYFKPGDEVwaAVPP---------------------------WKQGTLSEF 58
Cdd:COG1063   44 YRGGYPFVRPPLVLGHEFVGEVVEVGEGVTGLKVGDRV--VVEPnipcgecrycrrgrynlcenlqflgiaGRDGGFAEY 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  59 VVVsgnevshkPKSLTHTQAASLPYVAL-------TAWSAINKVGglndkNCTGKRVLILGAsGGVGTFAIQVMKAWDA- 130
Cdd:COG1063  122 VRV--------PAANLVKVPDGLSDEAAalveplaVALHAVERAG-----VKPGDTVLVIGA-GPIGLLAALAARLAGAa 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 131 HVTAV-CSQDASELVRKLGADDVIDYKSGSVEEQLKSL---KPFDFILDNVG-GSTETWAPDFLKKwsGATYVtLVtpfl 205
Cdd:COG1063  188 RVIVVdRNPERLELARELGADAVVNPREEDLVEAVRELtggRGADVVIEAVGaPAALEQALDLVRP--GGTVV-LV---- 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 206 lnmdrlgiadGMLQTGVTVGSKALkhFWKGVHYRWAfFMASGPCLDDIAELVDAGKI--RPVIEQTFPFSKVPEAFlkvE 283
Cdd:COG1063  261 ----------GVPGGPVPIDLNAL--VRKELTLRGS-RNYTREDFPEALELLASGRIdlEPLITHRFPLDDAPEAF---E 324
                        330
                 ....*....|...
gi 974005217 284 RGHARGKTVINVV 296
Cdd:COG1063  325 AAADRADGAIKVV 337
Mgc45594_like cd08250
Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of ...
16-181 3.91e-19

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: 85.77  E-value: 3.91e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  16 PLTLGRDVSGVVMECGLDVKYFKPGDevwaAVPPWKQGTLSEFVVVSGNEVshKPKSLTHTQAASLPYVALTAWSAINKV 95
Cdd:cd08250   61 PFDCGFEGVGEVVAVGEGVTDFKVGD----AVATMSFGAFAEYQVVPARHA--VPVPELKPEVLPLLVSGLTASIALEEV 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  96 GGLNdkncTGKRVLILGASGGVGTFAIQVMKAWDAHVTAVCSQDA-SELVRKLGADDVIDYKSGSVEEQLKSLKP--FDF 172
Cdd:cd08250  135 GEMK----SGETVLVTAAAGGTGQFAVQLAKLAGCHVIGTCSSDEkAEFLKSLGCDRPINYKTEDLGEVLKKEYPkgVDV 210

                 ....*....
gi 974005217 173 ILDNVGGST 181
Cdd:cd08250  211 VYESVGGEM 219
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
15-293 4.27e-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 (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: 85.63  E-value: 4.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  15 FPLTLGRDVSGVVMECGLDVKYFKPGDEV---------------------------WAAVPPWK-----QGTLSEFVVVS 62
Cdd:cd05283   53 YPLVPGHEIVGIVVAVGSKVTKFKVGDRVgvgcqvdscgtceqcksgeeqycpkgvVTYNGKYPdgtitQGGYADHIVVD 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  63 GNEVSHKPKSLTHTQAASLPYVALTAWSAI--NKVGglndkncTGKRVLILGAsGGVGTFAIQVMKAWDAHVTAVcSQDA 140
Cdd:cd05283  133 ERFVFKIPEGLDSAAAAPLLCAGITVYSPLkrNGVG-------PGKRVGVVGI-GGLGHLAVKFAKALGAEVTAF-SRSP 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 141 S--ELVRKLGADDVIDykSGSVEEQLKSLKPFDFILDNVGGSTEtWAPdFLKK-WSGATYVTL--------VTPFLLNMD 209
Cdd:cd05283  204 SkkEDALKLGADEFIA--TKDPEAMKKAAGSLDLIIDTVSASHD-LDP-YLSLlKPGGTLVLVgapeeplpVPPFPLIFG 279
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 210 RLGIAdgmlqtGVTVGSKAlkhfwkgvhyrwaffmasgpcldDIAELVD-AGK--IRPVIEqTFPFSKVPEAFLKVERGH 286
Cdd:cd05283  280 RKSVA------GSLIGGRK-----------------------ETQEMLDfAAEhgIKPWVE-VIPMDGINEALERLEKGD 329

                 ....*..
gi 974005217 287 ARGKTVI 293
Cdd:cd05283  330 VRYRFVL 336
oxido_YhdH TIGR02823
putative quinone oxidoreductase, YhdH/YhfP family; This model represents a subfamily of ...
14-295 6.40e-19

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: 84.92  E-value: 6.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217   14 EFPLTLGRDVSGVVMECglDVKYFKPGDEVwaAVPPWKQGT-----LSEFVVVSGNEVSHKPKSLTHTQAASLPYVALTA 88
Cdd:TIGR02823  55 SYPMIPGIDAAGTVVSS--EDPRFREGDEV--IVTGYGLGVshdggYSQYARVPADWLVPLPEGLSLREAMALGTAGFTA 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217   89 WSAINKvggLNDKNCTGKR--VLILGASGGVGTFAIQVMKAWDAHVTAVCS-QDASELVRKLGADDVIDyksgsVEEQLK 165
Cdd:TIGR02823 131 ALSVMA---LERNGLTPEDgpVLVTGATGGVGSLAVAILSKLGYEVVASTGkAEEEDYLKELGASEVID-----REDLSP 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  166 SLKP-----FDFILDNVGGSTETWAPDFLKKW---------SGATYVTLVTPFLL-NMDRLGIadgmlqTGVTVGSKALK 230
Cdd:TIGR02823 203 PGKPlekerWAGAVDTVGGHTLANVLAQLKYGgavaacglaGGPDLPTTVLPFILrGVSLLGI------DSVYCPMALRE 276
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 974005217  231 HFWKGVHYRWaffmasgpcldDIAELVDagkirpvIEQTFPFSKVPEAFLKVERGHARGKTVINV 295
Cdd:TIGR02823 277 AAWQRLATDL-----------KPRNLES-------ITREITLEELPEALEQILAGQHRGRTVVDV 323
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
25-293 2.93e-18

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: 83.42  E-value: 2.93e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  25 GVVMECGLDVKYFKPGDEVWAAVPPWkqGTLSEFVVVSGNEVsHK-PKSLTHTQAASLPYVALTAWSAINKVGGLNdknc 103
Cdd:cd08290   73 GEVVKVGSGVKSLKPGDWVIPLRPGL--GTWRTHAVVPADDL-IKvPNDVDPEQAATLSVNPCTAYRLLEDFVKLQ---- 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 104 tGKRVLIL-GASGGVGTFAIQVMKAWDAHVTAVC-----SQDASELVRKLGADDVI---DYKSGSVEEQLKSLKPFDFIL 174
Cdd:cd08290  146 -PGDWVIQnGANSAVGQAVIQLAKLLGIKTINVVrdrpdLEELKERLKALGADHVLteeELRSLLATELLKSAPGGRPKL 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 175 --DNVGGSTetwAPDFLKKWS-GATYVTlvtpfllnmdrlgiADGMLQTGVTVGSKALkhFWKGVHYRwAFFM----ASG 247
Cdd:cd08290  225 alNCVGGKS---ATELARLLSpGGTMVT--------------YGGMSGQPVTVPTSLL--IFKDITLR-GFWLtrwlKRA 284
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 974005217 248 P------CLDDIAELVDAGKIRPV---IEQTFPFSKVPEAFLKVERGHARGKTVI 293
Cdd:cd08290  285 NpeekedMLEELAELIREGKLKAPpveKVTDDPLEEFKDALANALKGGGGGKQVL 339
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
12-293 3.77e-16

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: 77.66  E-value: 3.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  12 GEEFPLTLGRDVSGVVMECGLDVKYFKPGDEVwaAVPPW--------------------------KQGTLSEFVVVSGNE 65
Cdd:cd08240   63 GVKLPLVLGHEIVGEVVAVGPDAADVKVGDKV--LVYPWigcgecpvclagdenlcakgralgifQDGGYAEYVIVPHSR 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  66 VSHKPKSLTHTQAASLPYVALTAWSAINKVGGLNDKNctgkRVLILGAsGGVGTFAIQVMKAWdAHVTAVC---SQDASE 142
Cdd:cd08240  141 YLVDPGGLDPALAATLACSGLTAYSAVKKLMPLVADE----PVVIIGA-GGLGLMALALLKAL-GPANIIVvdiDEAKLE 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 143 LVRKLGADDVIDYKSGSVEEQLKSL--KPFDFILDNVG-GSTETWAPDFLKKwsGATYV---------TLVTPfLLNMDR 210
Cdd:cd08240  215 AAKAAGADVVVNGSDPDAAKRIIKAagGGVDAVIDFVNnSATASLAFDILAK--GGKLVlvglfggeaTLPLP-LLPLRA 291
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 211 LGIAdgmlqtGVTVGSKalkhfwkgvhyrwaffmasgPCLDDIAELVDAGKIRPVIEQTFPFSKVPEAFLKVERGHARGK 290
Cdd:cd08240  292 LTIQ------GSYVGSL--------------------EELRELVALAKAGKLKPIPLTERPLSDVNDALDDLKAGKVVGR 345

                 ...
gi 974005217 291 TVI 293
Cdd:cd08240  346 AVL 348
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
7-178 2.38e-15

(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: 75.27  E-value: 2.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217   7 HVKIKGEEFPLTLGRDVSGVVMECGLDVKYFKPGDEVwAAVPPWKQGT--------------------------LSEFVV 60
Cdd:cd08233   56 HPHLTGETAPVTLGHEFSGVVVEVGSGVTGFKVGDRV-VVEPTIKCGTcgackrglynlcdslgfiglggggggFAEYVV 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  61 VSGNEVSHKPKSLTHTQAASLPYVAlTAWSAInKVGGLNdkncTGKRVLILGAsGGVGTFAIQVMKAWDAHvTAVCSQDA 140
Cdd:cd08233  135 VPAYHVHKLPDNVPLEEAALVEPLA-VAWHAV-RRSGFK----PGDTALVLGA-GPIGLLTILALKAAGAS-KIIVSEPS 206
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 974005217 141 S---ELVRKLGADDVIDYKSGSVEEQLKSL---KPFDFILDNVG 178
Cdd:cd08233  207 EarrELAEELGATIVLDPTEVDVVAEVRKLtggGGVDVSFDCAG 250
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
15-293 5.32e-15

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: 74.19  E-value: 5.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  15 FPLTLGRDVSGVVMECGLDVKYFKPGDEVwaAVPPWK--------------------------QGTLSEFVVVSGNEVSH 68
Cdd:cd08236   52 PPLVLGHEFSGTVEEVGSGVDDLAVGDRV--AVNPLLpcgkceyckkgeyslcsnydyigsrrDGAFAEYVSVPARNLIK 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  69 KPKSLTHTQAASLPYVAlTAWSAINKVGGlndknCTGKRVLILGAsGGVGTFAIQVMKAWDAH-VTAVC-SQDASELVRK 146
Cdd:cd08236  130 IPDHVDYEEAAMIEPAA-VALHAVRLAGI-----TLGDTVVVIGA-GTIGLLAIQWLKILGAKrVIAVDiDDEKLAVARE 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 147 LGADDVIDYKSGSVEEQLKSL--KPFDFILDNVG-GSTETWAPDFLKKwsGATyVTLVtpfllnmdrlGIADGmlqtGVT 223
Cdd:cd08236  203 LGADDTINPKEEDVEKVRELTegRGADLVIEAAGsPATIEQALALARP--GGK-VVLV----------GIPYG----DVT 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 224 VGSKAlkhFWK------GVHYRWAFFMASGPCLD--DIAELVDAGKIR--PVIEQTFPFSKVPEAFLKV-ERGHARGKTV 292
Cdd:cd08236  266 LSEEA---FEKilrkelTIQGSWNSYSAPFPGDEwrTALDLLASGKIKvePLITHRLPLEDGPAAFERLaDREEFSGKVL 342

                 .
gi 974005217 293 I 293
Cdd:cd08236  343 L 343
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
5-296 1.03e-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: 70.38  E-value: 1.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217   5 PLHVKIKGEEFPLTLGRDVSGVVMECGLDVKYFKPGDEVW--AAVPPW-------------------------KQGTLSE 57
Cdd:cd05278   44 IYRGGVPGAKHGMILGHEFVGEVVEVGSDVKRLKPGDRVSvpCITFCGrcrfcrrgyhahcenglwgwklgnrIDGGQAE 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  58 FVVVSGNEVS--HKPKSLTHTQAASLPYVALTAWSAiNKVGGLNDknctGKRVLILGAsGGVGTFAIQVMKAWDAHVTAV 135
Cdd:cd05278  124 YVRVPYADMNlaKIPDGLPDEDALMLSDILPTGFHG-AELAGIKP----GSTVAVIGA-GPVGLCAVAGARLLGAARIIA 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 136 CSQDAS--ELVRKLGADDVIDYKSGSVEEQLKSL---KPFDFILDNVGGSTetwapdflkkwSGATYVTLVTPfllnMDR 210
Cdd:cd05278  198 VDSNPErlDLAKEAGATDIINPKNGDIVEQILELtggRGVDCVIEAVGFEE-----------TFEQAVKVVRP----GGT 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 211 LGIAdGMLQTGVTVGSKALkhfWKGVHYRWAFFMASGPC-LDDIAELVDAGKIRP--VIEQTFPFSKVPEAFLKVErghA 287
Cdd:cd05278  263 IANV-GVYGKPDPLPLLGE---WFGKNLTFKTGLVPVRArMPELLDLIEEGKIDPskLITHRFPLDDILKAYRLFD---N 335

                 ....*....
gi 974005217 288 RGKTVINVV 296
Cdd:cd05278  336 KPDGCIKVV 344
MDR_yhfp_like cd08289
Yhfp putative quinone oxidoreductases; yhfp putative quinone oxidoreductases (QOR). QOR ...
13-295 1.14e-13

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: 70.05  E-value: 1.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  13 EEFPLTLGRDVSGVVMECglDVKYFKPGDEVWAA---VPPWKQGTLSEFVVVSGNEVSHKPKSLTHTQAASLPYVALTAW 89
Cdd:cd08289   55 KRYPFIPGIDLAGTVVES--NDPRFKPGDEVIVTsydLGVSHHGGYSEYARVPAEWVVPLPKGLTLKEAMILGTAGFTAA 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  90 SAINKvggLNDKNCT--GKRVLILGASGGVGTFAIQVMKAWDAHVTAVCSQ-DASELVRKLGADDVIdyksGSVEEQLKS 166
Cdd:cd08289  133 LSIHR---LEENGLTpeQGPVLVTGATGGVGSLAVSILAKLGYEVVASTGKaDAADYLKKLGAKEVI----PREELQEES 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 167 LKPFD-----FILDNVGGSTetwAPDFLKKW------------SGATYVTLVTPFLL-NMDRLGIadgmlqTGVTVGSKA 228
Cdd:cd08289  206 IKPLEkqrwaGAVDPVGGKT---LAYLLSTLqyggsvavsgltGGGEVETTVFPFILrGVNLLGI------DSVECPMEL 276
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 974005217 229 LKHFWKgvhyRWAFFMASGPCLDDIAelvdagkirpvieQTFPFSKVPEAFLKVERGHARGKTVINV 295
Cdd:cd08289  277 RRRIWR----RLATDLKPTQLLNEIK-------------QEITLDELPEALKQILQGRVTGRTVVKL 326
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
16-294 2.39e-13

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: 69.17  E-value: 2.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  16 PLTLGRDVSGVVMECGLDVKYFKPGDEVwaAVP----------------------------PWkqGTLSEFVVVSGNEVS 67
Cdd:cd08260   55 PHVPGHEFAGVVVEVGEDVSRWRVGDRV--TVPfvlgcgtcpycragdsnvcehqvqpgftHP--GSFAEYVAVPRADVN 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  68 --HKPKSLTHTQAASLPYVALTAWSAINKVGGLndknCTGKRVLILGAsGGVGTFAIQVMKAWDAHVTAV-CSQDASELV 144
Cdd:cd08260  131 lvRLPDDVDFVTAAGLGCRFATAFRALVHQARV----KPGEWVAVHGC-GGVGLSAVMIASALGARVIAVdIDDDKLELA 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 145 RKLGADDVIDykSGSVEEQLKSLKPF-----DFILDNVgGSTETwapdflkkwsgatyvtlVTPFLLNMDRLGiadGMLQ 219
Cdd:cd08260  206 RELGAVATVN--ASEVEDVAAAVRDLtgggaHVSVDAL-GIPET-----------------CRNSVASLRKRG---RHVQ 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 220 TGVTVGSKALKHFWKGVHYRW------AFFMASgPCLDDIAELVDAGKIRP--VIEQTFPFSKVPEAFLKVERGHARGKT 291
Cdd:cd08260  263 VGLTLGEEAGVALPMDRVVAReleivgSHGMPA-HRYDAMLALIASGKLDPepLVGRTISLDEAPDALAAMDDYATAGIT 341

                 ...
gi 974005217 292 VIN 294
Cdd:cd08260  342 VIT 344
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
13-296 2.89e-13

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: 68.92  E-value: 2.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  13 EEFPLTLGRDVSGVVMECGLDVKYFKPGDEVWAavppWKQGTLSEFVVVSGNEVSHKPkSLTHTQAASLPYVAlTAWSAI 92
Cdd:cd08269   49 PAEPGGPGHEGWGRVVALGPGVRGLAVGDRVAG----LSGGAFAEYDLADADHAVPLP-SLLDGQAFPGEPLG-CALNVF 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  93 NKVgglndKNCTGKRVLILGAsGGVGTFAIQVMKAWDAH-VTAVCSQDAS-ELVRKLGADDVIDYKSGSVEEQLKSLKP- 169
Cdd:cd08269  123 RRG-----WIRAGKTVAVIGA-GFIGLLFLQLAAAAGARrVIAIDRRPARlALARELGATEVVTDDSEAIVERVRELTGg 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 170 --FDFILDNVGgstetwapdflKKWSGATYVTLVTPfllnMDRLGIA----DGMLQtgVTVGSkalkHFWKGVHYRWAFF 243
Cdd:cd08269  197 agADVVIEAVG-----------HQWPLDLAGELVAE----RGRLVIFgyhqDGPRP--VPFQT----WNWKGIDLINAVE 255
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 974005217 244 MASGPCLDDI---AELVDAGKIRP--VIEQTFPFSKVPEAFLKVERghaRGKTVINVV 296
Cdd:cd08269  256 RDPRIGLEGMreaVKLIADGRLDLgsLLTHEFPLEELGDAFEAARR---RPDGFIKGV 310
CAD_like cd08296
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
11-294 1.31e-12

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: 66.88  E-value: 1.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  11 KGEEFPLTLGRDVSGVVMECGLDVKYFKPGDEV---W---------------------AAVPPW-KQGTLSEFVVVSGNE 65
Cdd:cd08296   50 PGLSYPRVPGHEVVGRIDAVGEGVSRWKVGDRVgvgWhgghcgtcdacrrgdfvhcenGKVTGVtRDGGYAEYMLAPAEA 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  66 VSHKPKSLTHTQAASLPYVALTAWSAINKVGGLndkncTGKRVLILGAsGGVGTFAIQVMKAWDAHVTAVCSQ-DASELV 144
Cdd:cd08296  130 LARIPDDLDAAEAAPLLCAGVTTFNALRNSGAK-----PGDLVAVQGI-GGLGHLAVQYAAKMGFRTVAISRGsDKADLA 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 145 RKLGADDVIDYKSGSVEEQLKSLKPFDFILdnvggSTetwAPDflkkwsgATYVTLVTPFLLNMDRLGIAdGMLQTGVTV 224
Cdd:cd08296  204 RKLGAHHYIDTSKEDVAEALQELGGAKLIL-----AT---APN-------AKAISALVGGLAPRGKLLIL-GAAGEPVAV 267
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 974005217 225 GSKALKHFWKGVHyRWaffmASGPCLD-----DIAELVDagkIRPVIEqTFPFSKVPEAFLKVERGHARGKTVIN 294
Cdd:cd08296  268 SPLQLIMGRKSIH-GW----PSGTALDsedtlKFSALHG---VRPMVE-TFPLEKANEAYDRMMSGKARFRVVLT 333
PRK10754 PRK10754
NADPH:quinone reductase;
15-191 1.73e-12

NADPH:quinone reductase;


Pssm-ID: 182701 [Multi-domain]  Cd Length: 327  Bit Score: 66.68  E-value: 1.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  15 FPLTLGRDVSGVVMECGLDVKYFKPGDEVWAAVPPWkqGTLSEFVVVSGNEVSHKPKSLTHTQAASLPYVALTAWSAINK 94
Cdd:PRK10754  57 LPSGLGTEAAGVVSKVGSGVKHIKVGDRVVYAQSAL--GAYSSVHNVPADKAAILPDAISFEQAAASFLKGLTVYYLLRK 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  95 VGGLNdkncTGKRVLILGASGGVGTFAIQVMKAWDAH-VTAVCSQDASELVRKLGADDVIDYKSGSVEEQLKSL---KPF 170
Cdd:PRK10754 135 TYEIK----PDEQFLFHAAAGGVGLIACQWAKALGAKlIGTVGSAQKAQRAKKAGAWQVINYREENIVERVKEItggKKV 210
                        170       180
                 ....*....|....*....|.
gi 974005217 171 DFILDNVGGSTETWAPDFLKK 191
Cdd:PRK10754 211 RVVYDSVGKDTWEASLDCLQR 231
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
14-279 2.15e-12

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: 66.44  E-value: 2.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  14 EFPLTLGRDVSGVVMECGLDVKYFKPGDEVwaAVPPW--------------------------KQGTLSEFVVVSgNEVS 67
Cdd:cd08261   52 SYPRILGHELSGEVVEVGEGVAGLKVGDRV--VVDPYiscgecyacrkgrpnccenlqvlgvhRDGGFAEYIVVP-ADAL 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  68 HKPKSLTHTQAASL-PY-VALTAwsaiNKVGGLNDknctGKRVLILGAsGGVGTFAIQVMKAWDAHVTAV-CSQDASELV 144
Cdd:cd08261  129 LVPEGLSLDQAALVePLaIGAHA----VRRAGVTA----GDTVLVVGA-GPIGLGVIQVAKARGARVIVVdIDDERLEFA 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 145 RKLGADDVIDYKSGSVEEQLKSL---KPFDFILDNVGG-STETWAPDFLKkwSGATYVTlvtpfllnmdrLGIADGML-- 218
Cdd:cd08261  200 RELGADDTINVGDEDVAARLRELtdgEGADVVIDATGNpASMEEAVELVA--HGGRVVL-----------VGLSKGPVtf 266
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 219 -QTGVT------VGSKAlkhfwkgvhyrwaffmASGPCLDDIAELVDAGKIRP--VIEQTFPFSKVPEAF 279
Cdd:cd08261  267 pDPEFHkkeltiLGSRN----------------ATREDFPDVIDLLESGKVDPeaLITHRFPFEDVPEAF 320
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
116-178 2.92e-12

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 62.62  E-value: 2.92e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 974005217  116 GVGTFAIQVMKAWDAHVTAVCSQDAS-ELVRKLGADDVIDYKSGSVEEQLKSL---KPFDFILDNVG 178
Cdd:pfam00107   1 GVGLAAIQLAKAAGAKVIAVDGSEEKlELAKELGADHVINPKETDLVEEIKELtggKGVDVVFDCVG 67
PLN02514 PLN02514
cinnamyl-alcohol dehydrogenase
6-177 4.26e-12

cinnamyl-alcohol dehydrogenase


Pssm-ID: 166155 [Multi-domain]  Cd Length: 357  Bit Score: 65.59  E-value: 4.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217   6 LHvKIKGE----EFPLTLGRDVSGVVMECGLDVKYFKPGDEVWAAV--------PPWK---------------------- 51
Cdd:PLN02514  51 LH-QIKNDlgmsNYPMVPGHEVVGEVVEVGSDVSKFTVGDIVGVGVivgccgecSPCKsdleqycnkriwsyndvytdgk 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  52 --QGTLSEFVVVSGNEVSHKPKSLTHTQAASLPYVALTAWSAINKVGGLNdkncTGKRVLILGAsGGVGTFAIQVMKAWD 129
Cdd:PLN02514 130 ptQGGFASAMVVDQKFVVKIPEGMAPEQAAPLLCAGVTVYSPLSHFGLKQ----SGLRGGILGL-GGVGHMGVKIAKAMG 204
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 974005217 130 AHVTAVCSQDAS--ELVRKLGADD-VIDYKSGSVEEQLKSLkpfDFILDNV 177
Cdd:PLN02514 205 HHVTVISSSDKKreEALEHLGADDyLVSSDAAEMQEAADSL---DYIIDTV 252
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
11-294 5.14e-12

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: 65.24  E-value: 5.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  11 KGEEFPLTLGRDVSGVVMECGLDVKYFKPGDEV------------------------WAAVPPWKQGTLSEFVVVSGNEV 66
Cdd:cd08234   48 FGAAPPLVPGHEFAGVVVAVGSKVTGFKVGDRVavdpniycgecfycrrgrpnlcenLTAVGVTRNGGFAEYVVVPAKQV 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  67 SHKPKSLTHTQAASLPYVAltawSAINKVGGLNDKncTGKRVLILGAsGGVGTFAIQVMKAWDAHVTAVCSQDAS--ELV 144
Cdd:cd08234  128 YKIPDNLSFEEAALAEPLS----CAVHGLDLLGIK--PGDSVLVFGA-GPIGLLLAQLLKLNGASRVTVAEPNEEklELA 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 145 RKLGADDVIDYKSGSVEEQlKSLKP--FDFILDNVgGSTETW--APDFLKKwsGATYVTL----------VTPFLLNMDR 210
Cdd:cd08234  201 KKLGATETVDPSREDPEAQ-KEDNPygFDVVIEAT-GVPKTLeqAIEYARR--GGTVLVFgvyapdarvsISPFEIFQKE 276
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 211 LGIadgmlqtgvtVGSKALKHfwkgvhyrwaffmasgpCLDDIAELVDAGKIR--PVIEQTFPFSKVPEAFLKVERGHAr 288
Cdd:cd08234  277 LTI----------IGSFINPY-----------------TFPRAIALLESGKIDvkGLVSHRLPLEEVPEALEGMRSGGA- 328

                 ....*.
gi 974005217 289 GKTVIN 294
Cdd:cd08234  329 LKVVVV 334
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
16-296 1.82e-11

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: 63.67  E-value: 1.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  16 PLTLGRDVSGVVMECGLDVKYFKPGDEV--------------------------WAAVPPWkQGTLSEFVVVSGNEVSHK 69
Cdd:cd05285   55 PMVLGHESAGTVVAVGSGVTHLKVGDRVaiepgvpcrtcefcksgrynlcpdmrFAATPPV-DGTLCRYVNHPADFCHKL 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  70 PKSLTHTQAASLPYVALTAWSAinKVGGLNDknctGKRVLILGAsGGVGTFAIQVMKAWDAHVTAVC--SQDASELVRKL 147
Cdd:cd05285  134 PDNVSLEEGALVEPLSVGVHAC--RRAGVRP----GDTVLVFGA-GPIGLLTAAVAKAFGATKVVVTdiDPSRLEFAKEL 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 148 GADDVIDYKSGSVEEQLKSLKP------FDFILDNVG--GSTETwAPDFLKkwSGATYVtLVtpfllnmdrlgiadGMLQ 219
Cdd:cd05285  207 GATHTVNVRTEDTPESAEKIAEllggkgPDVVIECTGaeSCIQT-AIYATR--PGGTVV-LV--------------GMGK 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 220 TGVT--VGSKALKHFW-KGVhYRWAffmasgPCLDDIAELVDAGKI--RPVIEQTFPFSKVPEAFlkvERGHARGKTVIN 294
Cdd:cd05285  269 PEVTlpLSAASLREIDiRGV-FRYA------NTYPTAIELLASGKVdvKPLITHRFPLEDAVEAF---ETAAKGKKGVIK 338

                 ..
gi 974005217 295 VV 296
Cdd:cd05285  339 VV 340
PRK10309 PRK10309
galactitol-1-phosphate 5-dehydrogenase;
15-178 8.07e-11

galactitol-1-phosphate 5-dehydrogenase;


Pssm-ID: 182371 [Multi-domain]  Cd Length: 347  Bit Score: 61.77  E-value: 8.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  15 FPLTLGRDVSGVVMECGLDVKYFKPGDEVwAAVP-------------------------PWKQGTLSEFVVVSGNEVSHK 69
Cdd:PRK10309  53 YPITLGHEFSGYVEAVGSGVDDLHPGDAV-ACVPllpcftcpeclrgfyslcakydfigSRRDGGNAEYIVVKRKNLFAL 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  70 PKSLTHTQAASLPYVALtAWSAINKVGGlndknCTGKRVLILGAsGGVGTFAIQVMKAWDAH-VTAV-CSQDASELVRKL 147
Cdd:PRK10309 132 PTDMPIEDGAFIEPITV-GLHAFHLAQG-----CEGKNVIIIGA-GTIGLLAIQCAVALGAKsVTAIdINSEKLALAKSL 204
                        170       180       190
                 ....*....|....*....|....*....|....
gi 974005217 148 GADDVIDYKSGSVEEQLKSLKPFDF---ILDNVG 178
Cdd:PRK10309 205 GAMQTFNSREMSAPQIQSVLRELRFdqlILETAG 238
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
16-293 2.08e-10

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: 60.71  E-value: 2.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  16 PLTLGRDVSGVVMECGLDVKYFKPGDEVW-----------------------------AAVPPWKQGTLSEFVVVSGNEV 66
Cdd:cd08232   54 PMVLGHEVSGVVEAVGPGVTGLAPGQRVAvnpsrpcgtcdycragrpnlclnmrflgsAMRFPHVQGGFREYLVVDASQC 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  67 SHKPKSLTHTQAA-SLPY-VALtawSAINKVGGLndkncTGKRVLILGAsGGVGTFAIQVMK-AWDAHVTAVCSQDAS-E 142
Cdd:cd08232  134 VPLPDGLSLRRAAlAEPLaVAL---HAVNRAGDL-----AGKRVLVTGA-GPIGALVVAAARrAGAAEIVATDLADAPlA 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 143 LVRKLGADDVIDYKSGSVE--EQLKSlkPFDFILD------NVGGSTETWAPdflkkwsGATYVTLvtpfllnmdrlgia 214
Cdd:cd08232  205 VARAMGADETVNLARDPLAayAADKG--DFDVVFEasgapaALASALRVVRP-------GGTVVQV-------------- 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 215 dGMLQTGVTVGSKALkhFWKGVHYRWAF-FmasGPCLDDIAELVDAGKI--RPVIEQTFPFSKVPEAF-LKVERGHArGK 290
Cdd:cd08232  262 -GMLGGPVPLPLNAL--VAKELDLRGSFrF---DDEFAEAVRLLAAGRIdvRPLITAVFPLEEAAEAFaLAADRTRS-VK 334

                 ...
gi 974005217 291 TVI 293
Cdd:cd08232  335 VQL 337
MDR_yhdh cd08288
Yhdh putative quinone oxidoreductases; Yhdh putative quinone oxidoreductases (QOR). QOR ...
14-154 2.83e-10

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: 60.24  E-value: 2.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  14 EFPLTLGRDVSGVVMECglDVKYFKPGDEVwaAVPPWKQGT-----LSEFVVVSGNEVSHKPKSLTHTQAASLPYVALTA 88
Cdd:cd08288   56 TFPLVPGIDLAGTVVES--SSPRFKPGDRV--VLTGWGVGErhwggYAQRARVKADWLVPLPEGLSARQAMAIGTAGFTA 131
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 974005217  89 WSAINKV--GGLNDKnctGKRVLILGASGGVGTFAIQVMKAWDAHVTAVC-SQDASELVRKLGADDVID 154
Cdd:cd08288  132 MLCVMALedHGVTPG---DGPVLVTGAAGGVGSVAVALLARLGYEVVASTgRPEEADYLRSLGASEIID 197
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
17-279 1.06e-09

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: 58.41  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  17 LTLGRDVSGVVMECGLDVKYFKPGDEVW--AAVPPW-------------------------KQGTLSEFVVVS---GNeV 66
Cdd:cd08285   55 MILGHEAVGVVEEVGSEVKDFKPGDRVIvpAITPDWrsvaaqrgypsqsggmlggwkfsnfKDGVFAEYFHVNdadAN-L 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  67 SHKPKSLTHTQAASLPYVALTAWSainkvGGLNDKNCTGKRVLILGAsGGVGTFAI---QVMKAwdAHVTAVCSQDAS-E 142
Cdd:cd08285  134 APLPDGLTDEQAVMLPDMMSTGFH-----GAELANIKLGDTVAVFGI-GPVGLMAVagaRLRGA--GRIIAVGSRPNRvE 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 143 LVRKLGADDVIDYKSGSVEEQLKSL---KPFDFILDnVGGSTETWAPDF--LK---KWSGATYvtLVTPFLLNMDRLGIA 214
Cdd:cd08285  206 LAKEYGATDIVDYKNGDVVEQILKLtggKGVDAVII-AGGGQDTFEQALkvLKpggTISNVNY--YGEDDYLPIPREEWG 282
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 974005217 215 DGM----LQTGVTVGSKAlkhfwkgvhyRwaffmasgpcLDDIAELVDAGKI---RPVIEQTFPFSKVPEAF 279
Cdd:cd08285  283 VGMghktINGGLCPGGRL----------R----------MERLASLIEYGRVdpsKLLTHHFFGFDDIEEAL 334
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
6-152 4.83e-08

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: 53.09  E-value: 4.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217   6 LHVKIKGEEFPLTLGRDVSGVVMECGLDVKYFKPGDEVWAAV--------PPWKQ-----------------GTLSEFVV 60
Cdd:cd08258   46 YKGDYDPVETPVVLGHEFSGTIVEVGPDVEGWKVGDRVVSETtfstcgrcPYCRRgdynlcphrkgigtqadGGFAEYVL 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  61 VSGNEVSHKPKSLthtqaaSLPYVALT-----AWSAINKVGGLNdkncTGKRVLILGaSGGVGTFAIQVMKAWDAHVTAV 135
Cdd:cd08258  126 VPEESLHELPENL------SLEAAALTeplavAVHAVAERSGIR----PGDTVVVFG-PGPIGLLAAQVAKLQGATVVVV 194
                        170       180
                 ....*....|....*....|
gi 974005217 136 -CSQDASEL--VRKLGADDV 152
Cdd:cd08258  195 gTEKDEVRLdvAKELGADAV 214
THR_DH_like cd08239
L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as ...
53-294 9.30e-08

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: 52.71  E-value: 9.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  53 GTLSEFVVVSGNEVSHKPKSLTHTQAASLPYVALTAWSAINKVGGLNDKNctgkrVLILGAsGGVGTFAIQVMKAWDAHV 132
Cdd:cd08239  117 GGHAEYMLVPEKTLIPLPDDLSFADGALLLCGIGTAYHALRRVGVSGRDT-----VLVVGA-GPVGLGALMLARALGAED 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 133 TAVC--SQDASELVRKLGADDVIDYKSGSVEE--QLKSLKPFDFILDNVGG-STETWAPDFLKKWSGATYVtlvtpflln 207
Cdd:cd08239  191 VIGVdpSPERLELAKALGADFVINSGQDDVQEirELTSGAGADVAIECSGNtAARRLALEAVRPWGRLVLV--------- 261
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 208 mdrlgiadGMLQTGVTVGSKALKHFWKGVHYRWAFfmaSGPCLDDIAELVDAGKIRP--VIEQTFPFSKVPEAFLKVERG 285
Cdd:cd08239  262 --------GEGGELTIEVSNDLIRKQRTLIGSWYF---SVPDMEECAEFLARHKLEVdrLVTHRFGLDQAPEAYALFAQG 330

                 ....*....
gi 974005217 286 hARGKTVIN 294
Cdd:cd08239  331 -ESGKVVFV 338
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
16-153 1.43e-07

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: 51.50  E-value: 1.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  16 PLTLGRDVSGVVMECGLDVKYFKPGDEVWAAvppwkqGTLSEFVVVSGNEVSHKPKSLTHTQAASLPYVALtawsAINKV 95
Cdd:cd08255   21 PLPPGYSSVGRVVEVGSGVTGFKPGDRVFCF------GPHAERVVVPANLLVPLPDGLPPERAALTALAAT----ALNGV 90
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 974005217  96 GGLNDKncTGKRVLILGAsGGVGTFAIQVMKA-WDAHVTAVcsqDAS----ELVRKLGADDVI 153
Cdd:cd08255   91 RDAEPR--LGERVAVVGL-GLVGLLAAQLAKAaGAREVVGV---DPDaarrELAEALGPADPV 147
B4_12hDH TIGR02825
leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 ...
39-293 1.59e-07

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: 51.92  E-value: 1.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217   39 PGDEVWAAVPPWKQGTLSEfvvvsGNEVSHKPKSLTHTQAASLP-----YVALTAWSAINKVGGLNdkncTGKRVLILGA 113
Cdd:TIGR02825  77 PKGTIVLASPGWTSHSISD-----GKDLEKLLTEWPDTLPLSLAlgtvgMPGLTAYFGLLEICGVK----GGETVMVNAA 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  114 SGGVGTFAIQVMKAWDAHVT-AVCSQDASELVRKLGADDVIDYKS-GSVEEQLKSLKP--FDFILDNVGGSTETWAPDFL 189
Cdd:TIGR02825 148 AGAVGSVVGQIAKLKGCKVVgAAGSDEKVAYLKKLGFDVAFNYKTvKSLEETLKKASPdgYDCYFDNVGGEFSNTVIGQM 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  190 KKWSGATYVTLVTPFllnmDRLG-IADGMLQTGVTVGSKALKHFwkgVHYRWAfFMASGPCLDDIAELVDAGKIRPVIEQ 268
Cdd:TIGR02825 228 KKFGRIAICGAISTY----NRTGpLPPGPPPEIVIYQELRMEGF---IVNRWQ-GEVRQKALKELLKWVLEGKIQYKEYV 299
                         250       260
                  ....*....|....*....|....*
gi 974005217  269 TFPFSKVPEAFLKVERGHARGKTVI 293
Cdd:TIGR02825 300 IEGFENMPAAFMGMLKGENLGKTIV 324
CAD2 cd08298
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
6-157 2.51e-07

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: 51.03  E-value: 2.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217   6 LHVkIKGE----EFPLTLGRDVSGVVMECGLDVKYFKPGDEVwaAVPPWKQ---------------------------GT 54
Cdd:cd08298   46 LHI-VEGDlpppKLPLIPGHEIVGRVEAVGPGVTRFSVGDRV--GVPWLGStcgecrycrsgrenlcdnarftgytvdGG 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  55 LSEFVVVSGNEVSHKPKSLTHTQAASLPYVALTAWSAINKVGGLNdknctGKRVLILGAsGGVGTFAIQVMKAWDAHVTA 134
Cdd:cd08298  123 YAEYMVADERFAYPIPEDYDDEEAAPLLCAGIIGYRALKLAGLKP-----GQRLGLYGF-GASAHLALQIARYQGAEVFA 196
                        170       180
                 ....*....|....*....|....
gi 974005217 135 VC-SQDASELVRKLGADDVIDYKS 157
Cdd:cd08298  197 FTrSGEHQELARELGADWAGDSDD 220
Zn_ADH_class_III cd08279
Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, ...
6-293 4.49e-07

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: 50.62  E-value: 4.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217   6 LHVkIKGE---EFPLTLGRDVSGVVMECGLDVKYFKPGDEVWAAVPP------WKQ------------------------ 52
Cdd:cd08279   42 LHV-VTGDlpaPLPAVLGHEGAGVVEEVGPGVTGVKPGDHVVLSWIPacgtcrYCSrgqpnlcdlgagilggqlpdgtrr 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  53 --------------GTLSEFVVVSGNEVSHKPKSLTHTQAASLPYVALTAW-SAIN--KVGGlndknctGKRVLILGAsG 115
Cdd:cd08279  121 ftadgepvgamcglGTFAEYTVVPEASVVKIDDDIPLDRAALLGCGVTTGVgAVVNtaRVRP-------GDTVAVIGC-G 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 116 GVGTFAIQVMK-AWDAHVTAVCSQDAS-ELVRKLGADDVIDYKSGSVEEQLKSLKP---FDFILDNVgGSTETW--APDF 188
Cdd:cd08279  193 GVGLNAIQGARiAGASRIIAVDPVPEKlELARRFGATHTVNASEDDAVEAVRDLTDgrgADYAFEAV-GRAATIrqALAM 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 189 LKKwSGATYVTlvtpfllnmdrlgiadGMLQTGVTVGSKALKHFWKGVHYRWAFFMASGPcLDDIAELVD---AGKIR-- 263
Cdd:cd08279  272 TRK-GGTAVVV----------------GMGPPGETVSLPALELFLSEKRLQGSLYGSANP-RRDIPRLLDlyrAGRLKld 333
                        330       340       350
                 ....*....|....*....|....*....|
gi 974005217 264 PVIEQTFPFSKVPEAFLKVERGHArGKTVI 293
Cdd:cd08279  334 ELVTRRYSLDEINEAFADMLAGEN-ARGVI 362
PTGR2 cd08293
Prostaglandin reductase; Prostaglandins and related eicosanoids are metabolized by the ...
78-179 1.08e-06

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: 49.31  E-value: 1.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  78 AASLPyvALTAWSAINKVG----GLNdknctgKRVLILGASGGVGTFAIQVMKAWD-AHVTAVCSQD--ASELVRKLGAD 150
Cdd:cd08293  132 AVGLP--GLTALIGIQEKGhitpGAN------QTMVVSGAAGACGSLAGQIGRLLGcSRVVGICGSDekCQLLKSELGFD 203
                         90       100       110
                 ....*....|....*....|....*....|.
gi 974005217 151 DVIDYKSGSVEEQLKSLKP--FDFILDNVGG 179
Cdd:cd08293  204 AAINYKTDNVAERLRELCPegVDVYFDNVGG 234
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
6-165 1.12e-06

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: 49.29  E-value: 1.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217   6 LHVkIKGE---EFPLTLGRDVSGVVMECGLDVK---YFKPGD------------------------EVWAAVPPWKQ--- 52
Cdd:cd08263   42 LHV-LKGElpfPPPFVLGHEISGEVVEVGPNVEnpyGLSVGDrvvgsfimpcgkcrycargkenlcEDFFAYNRLKGtly 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  53 -------------------GTLSEFVVVSGNEVSHKPKSLTHTQAASLPYVALTAWSAINKVGGLNdkncTGKRVLILGA 113
Cdd:cd08263  121 dgttrlfrldggpvymysmGGLAEYAVVPATALAPLPESLDYTESAVLGCAGFTAYGALKHAADVR----PGETVAVIGV 196
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 974005217 114 sGGVGTFAIQVMKAWDAH-VTAVCSQDAS-ELVRKLGADDVIDYKSGSVEEQLK 165
Cdd:cd08263  197 -GGVGSSAIQLAKAFGASpIIAVDVRDEKlAKAKELGATHTVNAAKEDAVAAIR 249
double_bond_reductase_like cd08295
Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase; This ...
37-295 1.83e-06

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: 48.47  E-value: 1.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  37 FKPGDEVWAAVPpWkqgtlSEFVVVSGNE----VSHKPKSLT-HTQAASLPyvALTAWSAINKVGglndKNCTGKRVLIL 111
Cdd:cd08295   91 FKVGDLVWGFTG-W-----EEYSLIPRGQdlrkIDHTDVPLSyYLGLLGMP--GLTAYAGFYEVC----KPKKGETVFVS 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 112 GASGGVGTFAIQVMKAWDAHVtaVCSQDASELVR----KLGADDVIDYKSgsvEEQLKS-LKPF-----DFILDNVGGST 181
Cdd:cd08295  159 AASGAVGQLVGQLAKLKGCYV--VGSAGSDEKVDllknKLGFDDAFNYKE---EPDLDAaLKRYfpngiDIYFDNVGGKM 233
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 182 ETWApdflkkwsgatyvtlvtpfLLNMDRLG-IAD-GMLQTGVTVGSKALKHFWKGVHYR--------WAFFMASGPCLD 251
Cdd:cd08295  234 LDAV-------------------LLNMNLHGrIAAcGMISQYNLEWPEGVRNLLNIIYKRvkiqgflvGDYLHRYPEFLE 294
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 974005217 252 DIAELVDAGKIRPVIEQTFPFSKVPEAFLKVERGHARGKTVINV 295
Cdd:cd08295  295 EMSGYIKEGKLKYVEDIADGLESAPEAFVGLFTGSNIGKQVVKV 338
leukotriene_B4_DH_like cd08294
13-PGR is a bifunctional enzyme with delta-13 15-prostaglandin reductase and leukotriene B4 12 ...
105-179 2.54e-06

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: 48.03  E-value: 2.54e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 974005217 105 GKRVLILGASGGVGTFAIQVMKAWDAHVTAVCSQDAS-ELVRKLGADDVIDYKSGSVEEQLKSLKP--FDFILDNVGG 179
Cdd:cd08294  144 GETVVVNGAAGAVGSLVGQIAKIKGCKVIGCAGSDDKvAWLKELGFDAVFNYKTVSLEEALKEAAPdgIDCYFDNVGG 221
PLN02586 PLN02586
probable cinnamyl alcohol dehydrogenase
15-177 4.28e-06

probable cinnamyl alcohol dehydrogenase


Pssm-ID: 166227 [Multi-domain]  Cd Length: 360  Bit Score: 47.57  E-value: 4.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  15 FPLTLGRDVSGVVMECGLDVKYFKPGDEVWAAV--------PPWKQ------------------------GTLSEFVVVS 62
Cdd:PLN02586  66 YPIVPGHEIVGIVTKLGKNVKKFKEGDRVGVGVivgsckscESCDQdlenycpkmiftynsighdgtknyGGYSDMIVVD 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  63 GNEVSHKPKSLTHTQAASLPYVALTAWSAInKVGGLNDkncTGKRVLILGAsGGVGTFAIQVMKAWDAHVTAVCS--QDA 140
Cdd:PLN02586 146 QHFVLRFPDNLPLDAGAPLLCAGITVYSPM-KYYGMTE---PGKHLGVAGL-GGLGHVAVKIGKAFGLKVTVISSssNKE 220
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 974005217 141 SELVRKLGADDVIdyKSGSVEEQLKSLKPFDFILDNV 177
Cdd:PLN02586 221 DEAINRLGADSFL--VSTDPEKMKAAIGTMDYIIDTV 255
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
37-293 8.51e-06

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: 46.48  E-value: 8.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  37 FKPGDEVWAAVPP-WkqGTLSEFVVV-SGNEVSHKPKSLThTQAASLPYVAL-TAWSAINKVGglndKNCTGKRVLILGA 113
Cdd:cd08231  114 KKYGHEASCDDPHlS--GGYAEHIYLpPGTAIVRVPDNVP-DEVAAPANCALaTVLAALDRAG----PVGAGDTVVVQGA 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 114 sGGVGTFAIQVMKAWDA-HVTAVcsqDAS----ELVRKLGADDVIDYKSGSVEEQLKSLK------PFDFILDNVGGST- 181
Cdd:cd08231  187 -GPLGLYAVAAAKLAGArRVIVI---DGSperlELAREFGADATIDIDELPDPQRRAIVRditggrGADVVIEASGHPAa 262
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 182 --EtwAPDFLKKwsGATYVTL----------VTPFLLNMDRLGIadgmlqTGVTVGSkaLKHFWKGVHyrwafFMASGPC 249
Cdd:cd08231  263 vpE--GLELLRR--GGTYVLVgsvapagtvpLDPERIVRKNLTI------IGVHNYD--PSHLYRAVR-----FLERTQD 325
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 974005217 250 LDDIAELVDagkirpvieQTFPFSKVPEAFLKVERGHArGKTVI 293
Cdd:cd08231  326 RFPFAELVT---------HRYPLEDINEALELAESGTA-LKVVI 359
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
16-154 8.91e-06

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: 46.46  E-value: 8.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  16 PLTLGRDVSGVVMECGLDVKYFKPGDEVWA-------AVPPWK-----------------QGTLSEFVVVSGNEVSHKPK 71
Cdd:cd05281   58 PLIFGHEFAGEVVEVGEGVTRVKVGDYVSAethivcgKCYQCRtgnyhvcqntkilgvdtDGCFAEYVVVPEENLWKNDK 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  72 SLthtqaaslPYvaltAWSAI-----NKVGGLNDKNCTGKRVLILGAsGGVGTFAIQVMKAWDAhvTAVCSQDAS----E 142
Cdd:cd05281  138 DI--------PP----EIASIqeplgNAVHTVLAGDVSGKSVLITGC-GPIGLMAIAVAKAAGA--SLVIASDPNpyrlE 202
                        170
                 ....*....|..
gi 974005217 143 LVRKLGADDVID 154
Cdd:cd05281  203 LAKKMGADVVIN 214
PLN02178 PLN02178
cinnamyl-alcohol dehydrogenase
15-177 5.96e-05

cinnamyl-alcohol dehydrogenase


Pssm-ID: 177834 [Multi-domain]  Cd Length: 375  Bit Score: 44.24  E-value: 5.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  15 FPLTLGRDVSGVVMECGLDVKYFKPGDEVWAAV--------------------------------PPWKQGTLSEFVVVS 62
Cdd:PLN02178  60 YPIIPGHEIVGIATKVGKNVTKFKEGDRVGVGViigscqscescnqdlenycpkvvftynsrssdGTRNQGGYSDVIVVD 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  63 GNEVSHKPKSLTHTQAASLPYVALTAWSAINKVGGLNDkncTGKRVLILGAsGGVGTFAIQVMKAWDAHVTAV--CSQDA 140
Cdd:PLN02178 140 HRFVLSIPDGLPSDSGAPLLCAGITVYSPMKYYGMTKE---SGKRLGVNGL-GGLGHIAVKIGKAFGLRVTVIsrSSEKE 215
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 974005217 141 SELVRKLGADD-VIDYKSGSVEEQLKSLkpfDFILDNV 177
Cdd:PLN02178 216 REAIDRLGADSfLVTTDSQKMKEAVGTM---DFIIDTV 250
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
12-294 6.55e-05

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: 43.74  E-value: 6.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  12 GEEFPLTLGRDVSGVVMECGLDVKYFKPGDEVWAA------------------VPPWKQGT------LSEFVVVSGNEVS 67
Cdd:cd08235   50 DLKPPRILGHEIAGEIVEVGDGVTGFKVGDRVFVAphvpcgechyclrgnenmCPNYKKFGnlydggFAEYVRVPAWAVK 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  68 HK-----PKSLTHTQAASLPYVA--LTAWSAINkVGglndkncTGKRVLILGAsGGVGTFAIQVMKAWDAHVTAVC--SQ 138
Cdd:cd08235  130 RGgvlklPDNVSFEEAALVEPLAccINAQRKAG-IK-------PGDTVLVIGA-GPIGLLHAMLAKASGARKVIVSdlNE 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 139 DASELVRKLGADDVIDYKSGSVEEQLKSL---KPFDFILDNVGG-STETWAPDFLKK-----WSGATYVTLVTPFLLNmd 209
Cdd:cd08235  201 FRLEFAKKLGADYTIDAAEEDLVEKVRELtdgRGADVVIVATGSpEAQAQALELVRKggrilFFGGLPKGSTVNIDPN-- 278
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 210 rlgiadgmlqtgvtvgskalkhfwkGVHYR-WAFFMASGPCLDDIAE---LVDAGKIR--PVIEQTFPFSKVPEAFLKVE 283
Cdd:cd08235  279 -------------------------LIHYReITITGSYAASPEDYKEaleLIASGKIDvkDLITHRFPLEDIEEAFELAA 333
                        330
                 ....*....|.
gi 974005217 284 RGHARgKTVIN 294
Cdd:cd08235  334 DGKSL-KIVIT 343
Zn_ADH3 cd08265
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
14-195 9.01e-05

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: 43.66  E-value: 9.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  14 EFPLTLGRDVSGVVMECGLDVKYFKPGDEVWAAVPPW------------------------KQGTLSEFVVVSG------ 63
Cdd:cd08265   86 EFPVVIGHEFSGVVEKTGKNVKNFEKGDPVTAEEMMWcgmcracrsgspnhcknlkelgfsADGAFAEYIAVNAryawei 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  64 NEVSHKPKSLTHTQAASLPYVALTAWSAINKVGGLNDKnctGKRVLILGAsGGVGTFAIQVMKAWDA-HVTAV-CSQDAS 141
Cdd:cd08265  166 NELREIYSEDKAFEAGALVEPTSVAYNGLFIRGGGFRP---GAYVVVYGA-GPIGLAAIALAKAAGAsKVIAFeISEERR 241
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 974005217 142 ELVRKLGADDVIDyksgsvEEQLKSLKPFDFILDNVGGstetWAPDFLKKWSGA 195
Cdd:cd08265  242 NLAKEMGADYVFN------PTKMRDCLSGEKVMEVTKG----WGADIQVEAAGA 285
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
98-174 1.14e-04

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 41.16  E-value: 1.14e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 974005217  98 LNDKNCTGKRVLILGAsgGVGTFAIQvMKAWDAHVTAV-CSQDASELVRKLGADDVIDYKSGSVEEQLKSLKPFDFIL 174
Cdd:COG2227   18 LARLLPAGGRVLDVGC--GTGRLALA-LARRGADVTGVdISPEALEIARERAAELNVDFVQGDLEDLPLEDGSFDLVI 92
PLN03154 PLN03154
putative allyl alcohol dehydrogenase; Provisional
37-295 1.19e-04

putative allyl alcohol dehydrogenase; Provisional


Pssm-ID: 215606 [Multi-domain]  Cd Length: 348  Bit Score: 42.91  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  37 FKPGDEVwAAVPPWKqgtlsEFVVVSGNEvsHKPKSLTHTQAASLPY-VALTAWSAINKVGGLNDKNC--TGKRVLILGA 113
Cdd:PLN03154  96 FKPGDLI-SGITGWE-----EYSLIRSSD--NQLRKIQLQDDIPLSYhLGLLGMAGFTAYAGFYEVCSpkKGDSVFVSAA 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 114 SGGVGTFAIQVMKAWDAHV--TAVCSQDASELVRKLGADDVIDYK-SGSVEEQLKSLKP--FDFILDNVGGStetwapdf 188
Cdd:PLN03154 168 SGAVGQLVGQLAKLHGCYVvgSAGSSQKVDLLKNKLGFDEAFNYKeEPDLDAALKRYFPegIDIYFDNVGGD-------- 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 189 lkkwsgatyvtLVTPFLLNMD---RLGIAdGMLQTGVTVGSKALKHFWKGVHYRWAF--FMASG------PCLDDIAELV 257
Cdd:PLN03154 240 -----------MLDAALLNMKihgRIAVC-GMVSLNSLSASQGIHNLYNLISKRIRMqgFLQSDylhlfpQFLENVSRYY 307
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 974005217 258 DAGKIRPVIEQTFPFSKVPEAFLKVERGHARGKTVINV 295
Cdd:PLN03154 308 KQGKIVYIEDMSEGLESAPAALVGLFSGKNVGKQVIRV 345
Zn_ADH8 cd08262
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
16-162 1.44e-04

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: 42.68  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  16 PLTLGRDVSGVVMECGLDV-KYFKPGDEVwAAVP---------------PWKQGTLSEFVVVSGNEVSHKPKSLTHTQAA 79
Cdd:cd08262   64 DIVLGHEFCGEVVDYGPGTeRKLKVGTRV-TSLPlllcgqgascgiglsPEAPGGYAEYMLLSEALLLRVPDGLSMEDAA 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  80 SLPYVALtAWSAINKVGGLndkncTGKRVLILGAsGGVGTFAIQVMKAWDAH--VTAVCSQDASELVRKLGADDVIDYKS 157
Cdd:cd08262  143 LTEPLAV-GLHAVRRARLT-----PGEVALVIGC-GPIGLAVIAALKARGVGpiVASDFSPERRALALAMGADIVVDPAA 215

                 ....*
gi 974005217 158 GSVEE 162
Cdd:cd08262  216 DSPFA 220
FDH_like_ADH2 cd08286
formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase ...
6-178 2.09e-04

formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase (FDH), which is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. This family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Another member is identified as a dihydroxyacetone reductase. Like the zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), 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. Unlike ADH, where NAD(P)(H) acts as a cofactor, NADH in FDH is a tightly bound redox cofactor (similar to nicotinamide proteins). 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: 176246 [Multi-domain]  Cd Length: 345  Bit Score: 42.24  E-value: 2.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217   6 LHVkIKGE----EFPLTLGRDVSGVVMECGLDVKYFKPGDEVW-AAVPP-------------------WK-----QGTLS 56
Cdd:cd08286   42 LHI-LKGDvptvTPGRILGHEGVGVVEEVGSAVTNFKVGDRVLiSCISScgtcgycrkglyshcesggWIlgnliDGTQA 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  57 EFVvvsgnEVSHKPKSLtHTQAASLPYVALTAWSAIN----KVGGLNDKNCTGKRVLILGAsGGVGTFAIQVMKAWDAHV 132
Cdd:cd08286  121 EYV-----RIPHADNSL-YKLPEGVDEEAAVMLSDILptgyECGVLNGKVKPGDTVAIVGA-GPVGLAALLTAQLYSPSK 193
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 974005217 133 TAVCSQDAS--ELVRKLGADDVIDYKSGSVEEQLKSL---KPFDFILDNVG 178
Cdd:cd08286  194 IIMVDLDDNrlEVAKKLGATHTVNSAKGDAIEQVLELtdgRGVDVVIEAVG 244
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
6-49 6.79e-04

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: 38.36  E-value: 6.79e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 974005217    6 LHVkIKGE----EFPLTLGRDVSGVVMECGLDVKYFKPGDEVwaAVPP 49
Cdd:pfam08240  17 LHI-YKGGnppvKLPLILGHEFAGEVVEVGPGVTGLKVGDRV--VVEP 61
PRK07060 PRK07060
short chain dehydrogenase; Provisional
104-178 8.57e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 40.08  E-value: 8.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 104 TGKRVLILGASGGVGTFAIQVMKAWDAHVTAVcSQDASELVR---KLGAD----DVIDykSGSVEEQLKSLKPFDFILDN 176
Cdd:PRK07060   8 SGKSVLVTGASSGIGRACAVALAQRGARVVAA-ARNAAALDRlagETGCEplrlDVGD--DAAIRAALAAAGAFDGLVNC 84

                 ..
gi 974005217 177 VG 178
Cdd:PRK07060  85 AG 86
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
16-167 1.39e-03

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 39.81  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  16 PLTLGRDVSGVVMECGLDVKYFKPGDEVWA------------------------AVPPWKQGTLSEFVVVSGNEVSHKPK 71
Cdd:PRK05396  58 PMVVGHEFVGEVVEVGSEVTGFKVGDRVSGeghivcghcrncragrrhlcrntkGVGVNRPGAFAEYLVIPAFNVWKIPD 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217  72 SLTHTQAASL-PY--VALTAWSAinkvgglndkNCTGKRVLILGAsGGVGTFAIQVMKAWDAH---VTAVcSQDASELVR 145
Cdd:PRK05396 138 DIPDDLAAIFdPFgnAVHTALSF----------DLVGEDVLITGA-GPIGIMAAAVAKHVGARhvvITDV-NEYRLELAR 205
                        170       180
                 ....*....|....*....|..
gi 974005217 146 KLGADDVIDYKSGSVEEQLKSL 167
Cdd:PRK05396 206 KMGATRAVNVAKEDLRDVMAEL 227
PRK05866 PRK05866
SDR family oxidoreductase;
104-221 5.26e-03

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 37.80  E-value: 5.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005217 104 TGKRVLILGASGGVGTFAIQVMKAWDAHVTAVC-SQDASELVR----KLGAD-----------DVIDyksGSVEEQLKSL 167
Cdd:PRK05866  39 TGKRILLTGASSGIGEAAAEQFARRGATVVAVArREDLLDAVAdritRAGGDamavpcdlsdlDAVD---ALVADVEKRI 115
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 974005217 168 KPFDFILDNVGGSTETWAPDFLKKWSGATYVTLVTPFLLNMDRLGIADGMLQTG 221
Cdd:PRK05866 116 GGVDILINNAGRSIRRPLAESLDRWHDVERTMVLNYYAPLRLIRGLAPGMLERG 169
 
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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