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Conserved domains on  [gi|489820032|ref|WP_003723841|]
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MULTISPECIES: zinc-binding alcohol dehydrogenase [Listeria]

Protein Classification

zinc-dependent alcohol dehydrogenase( domain architecture ID 10169599)

zinc-dependent alcohol dehydrogenase belonging to the medium chain dehydrogenase/reductase (MDR) family, similar to Escherichia coli D-guloside 3-dehydrogenase that catalyzes the NAD(+)-dependent oxidation of the hydroxyl group at C3 of D-gulosides leading to 3-dehydro-D-gulosides

CATH:  3.40.50.720|3.90.180.10
EC:  1.1.1.-
Gene Ontology:  GO:0030554|GO:0016616|GO:0008270
PubMed:  19011745|19011751|12199705|7957243|8749365
SCOP:  3000040

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
 75-341 1.66e-86

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: 262.21  E-value: 1.66e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  75 VFGEFQLGNMVVGEVVERGSKVTEYALGDIVCSYGPIMETVIVkavDNYKLRKLPKGANWKNAVCYDPAQFAMSGVRDAH 154
Cdd:cd08255   18 LPLPLPPGYSSVGRVVEVGSGVTGFKPGDRVFCFGPHAERVVV---PANLLVPLPDGLPPERAALTALAATALNGVRDAE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 155 VRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGadaTFDPITTDVGLEvkrlTGKLGADSIIETS 234
Cdd:cd08255   95 PRLGERVAVVGLGLVGLLAAQLAKAAGAREVVGVDPDAARRELAEALG---PADPVAADTADE----IGGRGADVVIEAS 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 235 GNAAALQAALRGIAYGGTISYVAFAKPFPEgfNLGREAHFNNAKIVFSRAASEPNPDYP-RWDRKRIEETCWELLMNGYL 313
Cdd:cd08255  168 GSPSALETALRLLRDRGRVVLVGWYGLKPL--LLGEEFHFKRLPIRSSQVYGIGRYDRPrRWTEARNLEEALDLLAEGRL 245

                        250       260
                 ....*....|....*....|....*...
gi 489820032 314 DcsDIIDPVVPFADSAESYMKYVDQQPD 341
Cdd:cd08255  246 E--ALITHRVPFEDAPEAYRLLFEDPPE 271
 
Name Accession Description Interval E-value
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
 75-341 1.66e-86

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: 262.21  E-value: 1.66e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  75 VFGEFQLGNMVVGEVVERGSKVTEYALGDIVCSYGPIMETVIVkavDNYKLRKLPKGANWKNAVCYDPAQFAMSGVRDAH 154
Cdd:cd08255   18 LPLPLPPGYSSVGRVVEVGSGVTGFKPGDRVFCFGPHAERVVV---PANLLVPLPDGLPPERAALTALAATALNGVRDAE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 155 VRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGadaTFDPITTDVGLEvkrlTGKLGADSIIETS 234
Cdd:cd08255   95 PRLGERVAVVGLGLVGLLAAQLAKAAGAREVVGVDPDAARRELAEALG---PADPVAADTADE----IGGRGADVVIEAS 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 235 GNAAALQAALRGIAYGGTISYVAFAKPFPEgfNLGREAHFNNAKIVFSRAASEPNPDYP-RWDRKRIEETCWELLMNGYL 313
Cdd:cd08255  168 GSPSALETALRLLRDRGRVVLVGWYGLKPL--LLGEEFHFKRLPIRSSQVYGIGRYDRPrRWTEARNLEEALDLLAEGRL 245

                        250       260
                 ....*....|....*....|....*...
gi 489820032 314 DcsDIIDPVVPFADSAESYMKYVDQQPD 341
Cdd:cd08255  246 E--ALITHRVPFEDAPEAYRLLFEDPPE 271
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 1-345 2.91e-49

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: 168.39  E-value: 2.91e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032   1 MKKLVATAPRVAALVEYNDREVLEDEVKIKVQFASPKhGTEVVDFRGISPFIDEefspewnlfvsretnsarGIVFG-EF 79
Cdd:COG1063    1 MKALVLHGPGDLRLEEVPDPEPGPGEVLVRVTAVGIC-GSDLHIYRGGYPFVRP------------------PLVLGhEF 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  80 qlgnmvVGEVVERGSKVTEYALGDIVCSYGPI------------------METVIVK----------AVDNYKLRKLPKG 131
Cdd:COG1063   62 ------VGEVVEVGEGVTGLKVGDRVVVEPNIpcgecrycrrgrynlcenLQFLGIAgrdggfaeyvRVPAANLVKVPDG 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 132 ANWKNAVCYDPAQFAMSGVRDAHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGADATFDPIT 211
Cdd:COG1063  136 LSDEAAALVEPLAVALHAVERAGVKPGDTVLVIGAGPIGLLAALAARLAGAARVIVVDRNPERLELARELGADAVVNPRE 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 212 TDVGLEVKRLTGKLGADSIIETSGNAAALQAALRGIAYGGTISYVAFAKPfPEGFNLGrEAHFNNAKIVFSRAASepnpd 291
Cdd:COG1063  216 EDLVEAVRELTGGRGADVVIEAVGAPAALEQALDLVRPGGTVVLVGVPGG-PVPIDLN-ALVRKELTLRGSRNYT----- 288

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489820032 292 yprwdRKRIEETCwELLMNGYLDCSDIIDPVVPFADSAESYMKYVDQQPDlSIK 345
Cdd:COG1063  289 -----REDFPEAL-ELLASGRIDLEPLITHRFPLDDAPEAFEAAADRADG-AIK 335
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
168-280 6.12e-26

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 100.37  E-value: 6.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  168 AIGQIAIQLAKKAGASVvIGVDPLSHRREIAEKHGADATFDPITTDVGLEVKRLTGKLGADSIIETSGNAAALQAALRGI 247
Cdd:pfam00107   1 GVGLAAIQLAKAAGAKV-IAVDGSEEKLELAKELGADHVINPKETDLVEEIKELTGGKGVDVVFDCVGSPATLEQALKLL 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 489820032  248 AYGGTISYVAFAKPfPEGFNLGReAHFNNAKIV 280
Cdd:pfam00107  80 RPGGRVVVVGLPGG-PLPLPLAP-LLLKELTIL 110
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
 1-254 4.40e-18

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 83.72  E-value: 4.40e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032   1 MKKLVATAPRVAA-LVEYNDREVLEDEVKIKVQFASpKHGTEVvdfrgispFIDEefspeWNLFvsretnSARGI----V 75
Cdd:PRK05396   1 MKALVKLKAEPGLwLTDVPVPEPGPNDVLIKVKKTA-ICGTDV--------HIYN-----WDEW------AQKTIpvpmV 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  76 FG-EFqlgnmvVGEVVERGSKVTEYALGDIVCSYGPI----------------METVIVkAVDnyklR--------KLPK 130
Cdd:PRK05396  61 VGhEF------VGEVVEVGSEVTGFKVGDRVSGEGHIvcghcrncragrrhlcRNTKGV-GVN----RpgafaeylVIPA 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 131 GANWKN--------AVCYDP--------AQFAMSGvRDahvragdyVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHR 194
Cdd:PRK05396 130 FNVWKIpddipddlAAIFDPfgnavhtaLSFDLVG-ED--------VLITGAGPIGIMAAAVAKHVGARHVVITDVNEYR 200

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 195 REIAEKHGADATFDPITTDVGLEVKRLTGKLGADSIIETSGNAAALQAALRGIAYGGTIS 254
Cdd:PRK05396 201 LELARKMGATRAVNVAKEDLRDVMAELGMTEGFDVGLEMSGAPSAFRQMLDNMNHGGRIA 260
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 71-251 7.30e-08

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 53.16  E-value: 7.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032    71 ARGIVFGEFQLGNMVVGEVVERGSKVTEYALGDIVC-----SYGPimeTVIVKAvdnYKLRKLPKGANWKNAVCYdPAQF 145
Cdd:smart00829  16 ALGLYPGEAVLGGECAGVVTRVGPGVTGLAVGDRVMglapgAFAT---RVVTDA---RLVVPIPDGWSFEEAATV-PVVF 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032   146 --AMSGVRD-AHVRAGDYVVV-VGLGAIGQIAIQLAKKAGASV--VIGVDPlshRREIAEKHGADAT--FDPITTDVGLE 217
Cdd:smart00829  89 ltAYYALVDlARLRPGESVLIhAAAGGVGQAAIQLARHLGAEVfaTAGSPE---KRDFLRALGIPDDhiFSSRDLSFADE 165

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 489820032   218 VKRLTGKLGADSIIET-SGnaAALQAALRGIAYGG 251
Cdd:smart00829 166 ILRATGGRGVDVVLNSlSG--EFLDASLRCLAPGG 198
 
Name Accession Description Interval E-value
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
 75-341 1.66e-86

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: 262.21  E-value: 1.66e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  75 VFGEFQLGNMVVGEVVERGSKVTEYALGDIVCSYGPIMETVIVkavDNYKLRKLPKGANWKNAVCYDPAQFAMSGVRDAH 154
Cdd:cd08255   18 LPLPLPPGYSSVGRVVEVGSGVTGFKPGDRVFCFGPHAERVVV---PANLLVPLPDGLPPERAALTALAATALNGVRDAE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 155 VRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGadaTFDPITTDVGLEvkrlTGKLGADSIIETS 234
Cdd:cd08255   95 PRLGERVAVVGLGLVGLLAAQLAKAAGAREVVGVDPDAARRELAEALG---PADPVAADTADE----IGGRGADVVIEAS 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 235 GNAAALQAALRGIAYGGTISYVAFAKPFPEgfNLGREAHFNNAKIVFSRAASEPNPDYP-RWDRKRIEETCWELLMNGYL 313
Cdd:cd08255  168 GSPSALETALRLLRDRGRVVLVGWYGLKPL--LLGEEFHFKRLPIRSSQVYGIGRYDRPrRWTEARNLEEALDLLAEGRL 245

                        250       260
                 ....*....|....*....|....*...
gi 489820032 314 DcsDIIDPVVPFADSAESYMKYVDQQPD 341
Cdd:cd08255  246 E--ALITHRVPFEDAPEAYRLLFEDPPE 271
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 1-345 2.91e-49

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: 168.39  E-value: 2.91e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032   1 MKKLVATAPRVAALVEYNDREVLEDEVKIKVQFASPKhGTEVVDFRGISPFIDEefspewnlfvsretnsarGIVFG-EF 79
Cdd:COG1063    1 MKALVLHGPGDLRLEEVPDPEPGPGEVLVRVTAVGIC-GSDLHIYRGGYPFVRP------------------PLVLGhEF 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  80 qlgnmvVGEVVERGSKVTEYALGDIVCSYGPI------------------METVIVK----------AVDNYKLRKLPKG 131
Cdd:COG1063   62 ------VGEVVEVGEGVTGLKVGDRVVVEPNIpcgecrycrrgrynlcenLQFLGIAgrdggfaeyvRVPAANLVKVPDG 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 132 ANWKNAVCYDPAQFAMSGVRDAHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGADATFDPIT 211
Cdd:COG1063  136 LSDEAAALVEPLAVALHAVERAGVKPGDTVLVIGAGPIGLLAALAARLAGAARVIVVDRNPERLELARELGADAVVNPRE 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 212 TDVGLEVKRLTGKLGADSIIETSGNAAALQAALRGIAYGGTISYVAFAKPfPEGFNLGrEAHFNNAKIVFSRAASepnpd 291
Cdd:COG1063  216 EDLVEAVRELTGGRGADVVIEAVGAPAALEQALDLVRPGGTVVLVGVPGG-PVPIDLN-ALVRKELTLRGSRNYT----- 288

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489820032 292 yprwdRKRIEETCwELLMNGYLDCSDIIDPVVPFADSAESYMKYVDQQPDlSIK 345
Cdd:COG1063  289 -----REDFPEAL-ELLASGRIDLEPLITHRFPLDDAPEAFEAAADRADG-AIK 335
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
 81-349 9.61e-33

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: 124.63  E-value: 9.61e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  81 LGNMVVGEVVERGSKVTEYALGDIV----------CSY--------------------GPIMETVIV--KAVDNYKLRKL 128
Cdd:cd08235   57 LGHEIAGEIVEVGDGVTGFKVGDRVfvaphvpcgeCHYclrgnenmcpnykkfgnlydGGFAEYVRVpaWAVKRGGVLKL 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 129 PKGANWKNAVCYDPAQFAMSGVRDAHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGADATFD 208
Cdd:cd08235  137 PDNVSFEEAALVEPLACCINAQRKAGIKPGDTVLVIGAGPIGLLHAMLAKASGARKVIVSDLNEFRLEFAKKLGADYTID 216

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 209 PITTDVGLEVKRLTGKLGADSIIETSGNAAALQAALRGIAYGGTISYvaFAkPFPEGFNLGREA---HFNNAKIVFSRAA 285
Cdd:cd08235  217 AAEEDLVEKVRELTDGRGADVVIVATGSPEAQAQALELVRKGGRILF--FG-GLPKGSTVNIDPnliHYREITITGSYAA 293

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489820032 286 SepNPDYPRwdrkrieetCWELLMNGYLDCSDIIDPVVPFADSAESYMKYVDQQpdlSIKMGIT 349
Cdd:cd08235  294 S--PEDYKE---------ALELIASGKIDVKDLITHRFPLEDIEEAFELAADGK---SLKIVIT 343
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 1-332 1.33e-31

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: 121.53  E-value: 1.33e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032   1 MKKLVATAPRVAALVEYNDREVLEDEVKIKVQFASpKHGTEVVDFRGISPFideefspewnlfvsretnsargivfgeFQ 80
Cdd:cd08261    1 MKALVCEKPGRLEVVDIPEPVPGAGEVLVRVKRVG-ICGSDLHIYHGRNPF---------------------------AS 52

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  81 ----LGNMVVGEVVERGSKVTEYALGDIVCSYgPI------------------------------METVIVKAVDNYKLr 126
Cdd:cd08261   53 ypriLGHELSGEVVEVGEGVAGLKVGDRVVVD-PYiscgecyacrkgrpnccenlqvlgvhrdggFAEYIVVPADALLV- 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 127 klPKGANWKNAVCYDPAQFAMSGVRDAHVRAGDYVVVVGLGAIGQIAIQLAKKAGAsVVIGVDPLSHRREIAEKHGADAT 206
Cdd:cd08261  131 --PEGLSLDQAALVEPLAIGAHAVRRAGVTAGDTVLVVGAGPIGLGVIQVAKARGA-RVIVVDIDDERLEFARELGADDT 207

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 207 FDPITTDVGLEVKRLTGKLGADSIIETSGNAAALQAALRGIAYGGTISYVAFAKPfPEGFNlGREAHFNNAKIVFSRAAS 286
Cdd:cd08261  208 INVGDEDVAARLRELTDGEGADVVIDATGNPASMEEAVELVAHGGRVVLVGLSKG-PVTFP-DPEFHKKELTILGSRNAT 285

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 489820032 287 epNPDYPrwdrkrieeTCWELLMNGYLDCSDIIDPVVPFADSAESY 332
Cdd:cd08261  286 --REDFP---------DVIDLLESGKVDPEALITHRFPFEDVPEAF 320
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
 1-337 3.59e-31

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: 120.41  E-value: 3.59e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032   1 MKKLVATAPRVAALVEYNDREVLEDEVKIKVQFAspkhgtevvdfrGI--SpfiDeefspewnlfVSRETNSAR---GIV 75
Cdd:cd08236    1 MKALVLTGPGDLRYEDIPKPEPGPGEVLVKVKAC------------GIcgS---D----------IPRYLGTGAyhpPLV 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  76 FG-EFqlgnmvVGEVVERGSKVTEYALGDIV----------CSY--------------------GPIMETVIVKAVDNYK 124
Cdd:cd08236   56 LGhEF------SGTVEEVGSGVDDLAVGDRVavnpllpcgkCEYckkgeyslcsnydyigsrrdGAFAEYVSVPARNLIK 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 125 LrklPKGANWKNAVCYDPAQFAMSGVRDAHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGAD 204
Cdd:cd08236  130 I---PDHVDYEEAAMIEPAAVALHAVRLAGITLGDTVVVIGAGTIGLLAIQWLKILGAKRVIAVDIDDEKLAVARELGAD 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 205 ATFDPITTDVGlEVKRLTGKLGADSIIETSGNAAALQAALRGIAYGGTISYVAfakpFPEGFNLGREAHFNnaKIVF--- 281
Cdd:cd08236  207 DTINPKEEDVE-KVRELTEGRGADLVIEAAGSPATIEQALALARPGGKVVLVG----IPYGDVTLSEEAFE--KILRkel 279

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489820032 282 -------SRAASEPNPDYprwdrkrieETCWELLMNGYLDCSDIIDPVVPFADSAESYMKYVD 337
Cdd:cd08236  280 tiqgswnSYSAPFPGDEW---------RTALDLLASGKIKVEPLITHRLPLEDGPAAFERLAD 333
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 1-253 3.96e-31

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: 119.94  E-value: 3.96e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032   1 MKKLVATAPRVAALVEYNDREVLEDEVKIKVQfASPKHGTEVVDFRGispfideefspewnlfvsrETNSARGIVFG-EF 79
Cdd:cd08234    1 MKALVYEGPGELEVEEVPVPEPGPDEVLIKVA-ACGICGTDLHIYEG-------------------EFGAAPPLVPGhEF 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  80 qlgnmvVGEVVERGSKVTEYALGDIV----------CSY--------------------GPIMETVIVKAVDNYKLrklP 129
Cdd:cd08234   61 ------AGVVVAVGSKVTGFKVGDRVavdpniycgeCFYcrrgrpnlcenltavgvtrnGGFAEYVVVPAKQVYKI---P 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 130 KGANWKNAVCYDPAQFAMSGVRDAHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGADATFDP 209
Cdd:cd08234  132 DNLSFEEAALAEPLSCAVHGLDLLGIKPGDSVLVFGAGPIGLLLAQLLKLNGASRVTVAEPNEEKLELAKKLGATETVDP 211

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 489820032 210 ITTDVglEVKRLTGKLGADSIIETSGNAAALQAALRGIAYGGTI 253
Cdd:cd08234  212 SREDP--EAQKEDNPYGFDVVIEATGVPKTLEQAIEYARRGGTV 253
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 79-294 7.45e-30

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: 115.11  E-value: 7.45e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  79 FQLGNMVVGEVVERGSKVTEYALGDIV----------CSYGPIMETVIVK-------------AVDNYKLRKLPKGANWK 135
Cdd:cd05188   31 LILGHEGAGVVVEVGPGVTGVKVGDRVvvlpnlgcgtCELCRELCPGGGIlgegldggfaeyvVVPADNLVPLPDGLSLE 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 136 NAVC-YDPAQFAMSGVRDA-HVRAGDYVVVVGLGAIGQIAIQLAKKAGAsVVIGVDPLSHRREIAEKHGADATFDPITTD 213
Cdd:cd05188  111 EAALlPEPLATAYHALRRAgVLKPGDTVLVLGAGGVGLLAAQLAKAAGA-RVIVTDRSDEKLELAKELGADHVIDYKEED 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 214 VGLEVKRLTGKlGADSIIETSGNAAALQAALRGIAYGGTISYVAFAKPFPEgFNLGREAHFNNAKIVFSRAASepNPDYP 293
Cdd:cd05188  190 LEEELRLTGGG-GADVVIDAVGGPETLAQALRLLRPGGRIVVVGGTSGGPP-LDDLRRLLFKELTIIGSTGGT--REDFE 265


                 .
gi 489820032 294 R 294
Cdd:cd05188  266 E 266
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
 72-350 8.70e-29

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: 113.91  E-value: 8.70e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  72 RGIVFGE---FQLGNMVVGEVVERGSKVTEYALGDIV----------CSY-----------------------GPIMETV 115
Cdd:cd05278   46 RGGVPGAkhgMILGHEFVGEVVEVGSDVKRLKPGDRVsvpcitfcgrCRFcrrgyhahcenglwgwklgnridGGQAEYV 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 116 IVKAVDnYKLRKLPKGANWKNAVCY-DPAQFAMSGVRDAHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHR 194
Cdd:cd05278  126 RVPYAD-MNLAKIPDGLPDEDALMLsDILPTGFHGAELAGIKPGSTVAVIGAGPVGLCAVAGARLLGAARIIAVDSNPER 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 195 REIAEKHGADATFDPITTDVGLEVKRLTGKLGADSIIETSGNAAALQAALRGIAYGGTISYVA-FAKP---FPEGFNLGR 270
Cdd:cd05278  205 LDLAKEAGATDIINPKNGDIVEQILELTGGRGVDCVIEAVGFEETFEQAVKVVRPGGTIANVGvYGKPdplPLLGEWFGK 284

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 271 EAHFnnakivfsRAASEPNPDYprwdrkrieetCWELL---MNGYLDCSDIIDPVVPFADSAESYMKYvDQQPDLSIKMG 347
Cdd:cd05278  285 NLTF--------KTGLVPVRAR-----------MPELLdliEEGKIDPSKLITHRFPLDDILKAYRLF-DNKPDGCIKVV 344


                 ...
gi 489820032 348 ITL 350
Cdd:cd05278  345 IRP 347
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 81-330 8.89e-29

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: 113.32  E-value: 8.89e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  81 LGNMVVGEVVERGSKVTEYALGDIVCSYGPI---METVIVKAVDnykLRKLPKGANWKNAVCYdPAQF--AMSGVRD-AH 154
Cdd:COG0604   61 PGSDAAGVVVAVGEGVTGFKVGDRVAGLGRGggyAEYVVVPADQ---LVPLPDGLSFEEAAAL-PLAGltAWQALFDrGR 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 155 VRAGDYVVVVG-LGAIGQIAIQLAKKAGASVvIGVDPLSHRREIAEKHGADATFDPITTDVGLEVKRLTGKLGADSIIET 233
Cdd:COG0604  137 LKPGETVLVHGaAGGVGSAAVQLAKALGARV-IATASSPEKAELLRALGADHVIDYREEDFAERVRALTGGRGVDVVLDT 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 234 SGnAAALQAALRGIAYGGTISYVAFAKPFPEGFNLgREAHFNNAKIVFSRAASepnpdYPRWDRKRIEETCWELLMNGYL 313
Cdd:COG0604  216 VG-GDTLARSLRALAPGGRLVSIGAASGAPPPLDL-APLLLKGLTLTGFTLFA-----RDPAERRAALAELARLLAAGKL 288

                        250
                 ....*....|....*..
gi 489820032 314 DCsdIIDPVVPFADSAE 330
Cdd:COG0604  289 RP--VIDRVFPLEEAAE 303
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
 1-261 9.31e-29

(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: 113.79  E-value: 9.31e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032   1 MKKLVATAPRVAALVEYNDREVLEDEVKIKVQFASpKHGTEVVDFRGISPFIDEEFSPEwnlfvsrETNSARGIVFG-EF 79
Cdd:cd08233    1 MKAARYHGRKDIRVEEVPEPPVKPGEVKIKVAWCG-ICGSDLHEYLDGPIFIPTEGHPH-------LTGETAPVTLGhEF 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  80 qlgnmvVGEVVERGSKVTEYALGDIVCSYgPIM--------------------------------ETVIVKAvdnYKLRK 127
Cdd:cd08233   73 ------SGVVVEVGSGVTGFKVGDRVVVE-PTIkcgtcgackrglynlcdslgfiglggggggfaEYVVVPA---YHVHK 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 128 LPKGANWKNAVCYDPAQFAMSGVRDAHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGADATF 207
Cdd:cd08233  143 LPDNVPLEEAALVEPLAVAWHAVRRSGFKPGDTALVLGAGPIGLLTILALKAAGASKIIVSEPSEARRELAEELGATIVL 222

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489820032 208 DPITTDVGLEVKRLTGKLGADSIIETSGNAAALQAALRGIAYGGTISYVA-FAKP 261
Cdd:cd08233  223 DPTEVDVVAEVRKLTGGGGVDVSFDCAGVQATLDTAIDALRPRGTAVNVAiWEKP 277
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 81-349 1.18e-28

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: 112.84  E-value: 1.18e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  81 LGNMVVGEVVERGSKVTEYALGDIVC--SYGPIMETVIVKAVDNYKLRKLPKGanwkNAVCYDPAQFAMSGVRDAHVRAG 158
Cdd:cd08269   55 PGHEGWGRVVALGPGVRGLAVGDRVAglSGGAFAEYDLADADHAVPLPSLLDG----QAFPGEPLGCALNVFRRGWIRAG 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 159 DYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGADATFDPITTDVGLEVKRLTGKLGADSIIETSGNAA 238
Cdd:cd08269  131 KTVAVIGAGFIGLLFLQLAAAAGARRVIAIDRRPARLALARELGATEVVTDDSEAIVERVRELTGGAGADVVIEAVGHQW 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 239 ALQAALRGIAYGGTISYVAFAKPFPEGFNLgREAHFNNAKIVFSRAASepnpdyPRWDRKRIEETCwELLMNGYLDCSDI 318
Cdd:cd08269  211 PLDLAGELVAERGRLVIFGYHQDGPRPVPF-QTWNWKGIDLINAVERD------PRIGLEGMREAV-KLIADGRLDLGSL 282

                        250       260       270
                 ....*....|....*....|....*....|.
gi 489820032 319 IDPVVPFADSAESYmKYVDQQPDLSIKMGIT 349
Cdd:cd08269  283 LTHEFPLEELGDAF-EAARRRPDGFIKGVIV 312
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 85-263 1.64e-27

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 110.20  E-value: 1.64e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  85 VVGEVVERGSKVTEYALGDIV---------------------CSYGPIM---------ETVIVKAvdNYkLRKLPKGanw 134
Cdd:COG1064   62 IVGRVVAVGPGVTGFKVGDRVgvgwvdscgtceycrsgrenlCENGRFTgyttdggyaEYVVVPA--RF-LVKLPDG--- 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 135 knavcYDPAQFA---------MSGVRDAHVRAGDYVVVVGLGAIGQIAIQLAKKAGASvVIGVDPLSHRREIAEKHGADA 205
Cdd:COG1064  136 -----LDPAEAApllcagitaYRALRRAGVGPGDRVAVIGAGGLGHLAVQIAKALGAE-VIAVDRSPEKLELARELGADH 209

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489820032 206 TFDPITTDVGLEVKRLTgklGADSIIETSGNAAALQAALRGIAYGGTISYV-AFAKPFP 263
Cdd:COG1064  210 VVNSSDEDPVEAVRELT---GADVVIDTVGAPATVNAALALLRRGGRLVLVgLPGGPIP 265
Zn_ADH_class_III cd08279
Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, ...
 150-261 1.55e-26

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: 108.01  E-value: 1.55e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 150 VRDAHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGADATFDPITTDVGLEVKRLTGKLGADS 229
Cdd:cd08279  175 VNTARVRPGDTVAVIGCGGVGLNAIQGARIAGASRIIAVDPVPEKLELARRFGATHTVNASEDDAVEAVRDLTDGRGADY 254

                         90       100       110
                 ....*....|....*....|....*....|..
gi 489820032 230 IIETSGNAAALQAALRGIAYGGTISYVAFAKP 261
Cdd:cd08279  255 AFEAVGRAATIRQALAMTRKGGTAVVVGMGPP 286
FrmA COG1062
Zn-dependent alcohol/formaldehyde dehydrogenase [Energy production and conversion];
150-261 1.83e-26

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


Pssm-ID: 440682 [Multi-domain]  Cd Length: 355  Bit Score: 107.86  E-value: 1.83e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 150 VRDAHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGADATFDPITTDVGLEVKRLTGKlGADS 229
Cdd:COG1062  168 LNTAKVRPGDTVAVFGLGGVGLSAVQGARIAGASRIIAVDPVPEKLELARELGATHTVNPADEDAVEAVRELTGG-GVDY 246

                         90       100       110
                 ....*....|....*....|....*....|..
gi 489820032 230 IIETSGNAAALQAALRGIAYGGTISYVAFAKP 261
Cdd:COG1062  247 AFETTGNPAVIRQALEALRKGGTVVVVGLAPP 278
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
 127-345 4.79e-26

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: 106.42  E-value: 4.79e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 127 KLPKGANWKNAVCYDPAQFAMSGVRDAHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGADAT 206
Cdd:cd05285  132 KLPDNVSLEEGALVEPLSVGVHACRRAGVRPGDTVLVFGAGPIGLLTAAVAKAFGATKVVVTDIDPSRLEFAKELGATHT 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 207 FDPITTDVG---LEVKRLTGKLGADSIIETSGNAAALQAALRGIAYGGTISYVAFAKP---FPEGFNLGREAHFnnaKIV 280
Cdd:cd05285  212 VNVRTEDTPesaEKIAELLGGKGPDVVIECTGAESCIQTAIYATRPGGTVVLVGMGKPevtLPLSAASLREIDI---RGV 288

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489820032 281 FsRAASepnpDYPrwdrkrieeTCWELLMNGYLDCSDIIDPVVPFADSAESYmKYVDQQPDLSIK 345
Cdd:cd05285  289 F-RYAN----TYP---------TAIELLASGKVDVKPLITHRFPLEDAVEAF-ETAAKGKKGVIK 338
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
168-280 6.12e-26

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 100.37  E-value: 6.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  168 AIGQIAIQLAKKAGASVvIGVDPLSHRREIAEKHGADATFDPITTDVGLEVKRLTGKLGADSIIETSGNAAALQAALRGI 247
Cdd:pfam00107   1 GVGLAAIQLAKAAGAKV-IAVDGSEEKLELAKELGADHVINPKETDLVEEIKELTGGKGVDVVFDCVGSPATLEQALKLL 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 489820032  248 AYGGTISYVAFAKPfPEGFNLGReAHFNNAKIV 280
Cdd:pfam00107  80 RPGGRVVVVGLPGG-PLPLPLAP-LLLKELTIL 110
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
 1-297 2.84e-25

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: 103.55  E-value: 2.84e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032   1 MKKLVATAPRV--AALVEYNDREVLEDEVKIKVQFASpKHGTEVVDFRGispfideefsPEWNLfvsrETNSArgivfge 78
Cdd:cd08258    1 MKALVKTGPGPgnVELREVPEPEPGPGEVLIKVAAAG-ICGSDLHIYKG----------DYDPV----ETPVV------- 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  79 fqLGNMVVGEVVERGSKVTEYALGDIV-----------CSY--------------------GPIMETVIVKAVdnyKLRK 127
Cdd:cd08258   59 --LGHEFSGTIVEVGPDVEGWKVGDRVvsettfstcgrCPYcrrgdynlcphrkgigtqadGGFAEYVLVPEE---SLHE 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 128 LPKGANWKNAVCYDPAQFAMSGV-RDAHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVI-GVDPLSHRREIAEKHGADA 205
Cdd:cd08258  134 LPENLSLEAAALTEPLAVAVHAVaERSGIRPGDTVVVFGPGPIGLLAAQVAKLQGATVVVvGTEKDEVRLDVAKELGADA 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 206 TfDPITTDVGLEVKRLTGKLGADSIIETSGNAAALQAALRGIAYGGTISYVAFAKPFPEGFNLGREAhFNNAKIVFSRAA 285
Cdd:cd08258  214 V-NGGEEDLAELVNEITDGDGADVVIECSGAVPALEQALELLRKGGRIVQVGIFGPLAASIDVERII-QKELSVIGSRSS 291

                        330
                 ....*....|..
gi 489820032 286 sepnpDYPRWDR 297
Cdd:cd08258  292 -----TPASWET 298
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 1-327 4.28e-25

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: 103.85  E-value: 4.28e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032   1 MKKLVATAP-RVAALVEYNDREVLEDEVKIKVQFASpKHGTEVvdfrgispFIDEefspeWNLFvsretnsARGIVFGEF 79
Cdd:cd05281    1 MKAIVKTKAgPGAELVEVPVPKPGPGEVLIKVLAAS-ICGTDV--------HIYE-----WDEW-------AQSRIKPPL 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  80 QLGNMVVGEVVERGSKVTEYALGD-------IVCSY-----------------------GPIMETVIVKAVDnykLRKLP 129
Cdd:cd05281   60 IFGHEFAGEVVEVGEGVTRVKVGDyvsaethIVCGKcyqcrtgnyhvcqntkilgvdtdGCFAEYVVVPEEN---LWKND 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 130 KGANWKNAVCYDPAQFAMSGVRDAHVRAGDyVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGADATFDP 209
Cdd:cd05281  137 KDIPPEIASIQEPLGNAVHTVLAGDVSGKS-VLITGCGPIGLMAIAVAKAAGASLVIASDPNPYRLELAKKMGADVVINP 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 210 ITTDVgLEVKRLTGKLGADSIIETSGNAAALQAALRGIAYGGTISYVA-FAKPFPegFNLGREAHFNNAKI--VFSRaas 286
Cdd:cd05281  216 REEDV-VEVKSVTDGTGVDVVLEMSGNPKAIEQGLKALTPGGRVSILGlPPGPVD--IDLNNLVIFKGLTVqgITGR--- 289

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 489820032 287 epnpdyprwdrkRIEETcW----ELLMNGYLDCSDIIDPVVPFAD 327
Cdd:cd05281  290 ------------KMFET-WyqvsALLKSGKVDLSPVITHKLPLED 321
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
 79-332 1.58e-24

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


Pssm-ID: 176244 [Multi-domain]  Cd Length: 344  Bit Score: 102.34  E-value: 1.58e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  79 FQLGNMVVGEVVERGSKVTEYALGDIV----------CSY------------------------GPIMETVIVKAVDNyK 124
Cdd:cd08284   55 FVLGHEFVGEVVEVGPEVRTLKVGDRVvspftiacgeCFYcrrgqsgrcakgglfgyagspnldGAQAEYVRVPFADG-T 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 125 LRKLPKGanwknavCYDPAQFAMS--------GVRDAHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRRE 196
Cdd:cd08284  134 LLKLPDG-------LSDEAALLLGdilptgyfGAKRAQVRPGDTVAVIGCGPVGLCAVLSAQVLGAARVFAVDPVPERLE 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 197 IAEKHGADAtFDPITTDVGLEVKRLTGKLGADSIIETSGNAAALQAALRGIAYGGTISYVAF--AKPFPegFNlGREAHF 274
Cdd:cd08284  207 RAAALGAEP-INFEDAEPVERVREATEGRGADVVLEAVGGAAALDLAFDLVRPGGVISSVGVhtAEEFP--FP-GLDAYN 282

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489820032 275 NNAKIVFSRAasepnpDYPRWDRKRIeetcwELLMNGYLDCSDIIDPVVPFADSAESY 332
Cdd:cd08284  283 KNLTLRFGRC------PVRSLFPELL-----PLLESGRLDLEFLIDHRMPLEEAPEAY 329
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
 81-256 2.70e-23

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: 98.85  E-value: 2.70e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  81 LGNMVVGEVVERGSKVTEYALGDIV----------CSY-----------------------GPIMETVIVKAVDNyKLRK 127
Cdd:cd08285   57 LGHEAVGVVEEVGSEVKDFKPGDRVivpaitpdwrSVAaqrgypsqsggmlggwkfsnfkdGVFAEYFHVNDADA-NLAP 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 128 LPKGANWKNAV-CYDPAQFAMSGVRDAHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGADAT 206
Cdd:cd08285  136 LPDGLTDEQAVmLPDMMSTGFHGAELANIKLGDTVAVFGIGPVGLMAVAGARLRGAGRIIAVGSRPNRVELAKEYGATDI 215

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 489820032 207 FDPITTDVGLEVKRLTGKLGADSIIETSGNAAALQAALRGIAYGGTISYV 256
Cdd:cd08285  216 VDYKNGDVVEQILKLTGGKGVDAVIIAGGGQDTFEQALKVLKPGGTISNV 265
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
 1-259 8.02e-23

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: 97.18  E-value: 8.02e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032   1 MKKLVATA---PRVAALVEYNDREVLEDEVKIKVQFAspkhgtevvdfrGISpFIDeefspewNLFVSretnsargivfG 77
Cdd:cd08241    1 MKAVVCKElggPEDLVLEEVPPEPGAPGEVRIRVEAA------------GVN-FPD-------LLMIQ-----------G 49

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  78 EFQ--------LGNMVVGEVVERGSKVTEYALGDIVCSYGPI---METVIVKAvdnYKLRKLPKGANWKNA----VCYDP 142
Cdd:cd08241   50 KYQvkpplpfvPGSEVAGVVEAVGEGVTGFKVGDRVVALTGQggfAEEVVVPA---AAVFPLPDGLSFEEAaalpVTYGT 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 143 AQFAMsgVRDAHVRAGDYVVVVGL-GAIGQIAIQLAKKAGASVVIGVDPlSHRREIAEKHGADATFDPITTDVGLEVKRL 221
Cdd:cd08241  127 AYHAL--VRRARLQPGETVLVLGAaGGVGLAAVQLAKALGARVIAAASS-EEKLALARALGADHVIDYRDPDLRERVKAL 203

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 489820032 222 TGKLGADSIIETSGNAAAlQAALRGIAYGGTISYVAFA 259
Cdd:cd08241  204 TGGRGVDVVYDPVGGDVF-EASLRSLAWGGRLLVIGFA 240
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
 79-256 6.12e-22

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: 94.93  E-value: 6.12e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  79 FQLGNMVVGEVVERGSKVTEYALGDIVCSYGPI------------------------------METVIVKAvdnYKLRKL 128
Cdd:cd05284   59 FTLGHENAGWVEEVGSGVDGLKEGDPVVVHPPWgcgtcrycrrgeenycenarfpgigtdggfAEYLLVPS---RRLVKL 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 129 PKGANWKNAVCY-DPAQFAMSGVRDA--HVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGADA 205
Cdd:cd05284  136 PRGLDPVEAAPLaDAGLTAYHAVKKAlpYLDPGSTVVVIGVGGLGHIAVQILRALTPATVIAVDRSEEALKLAERLGADH 215

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489820032 206 TFDPiTTDVGLEVKRLTGKLGADSIIETSGNAAALQAALRGIAYGGTISYV 256
Cdd:cd05284  216 VLNA-SDDVVEEVRELTGGRGADAVIDFVGSDETLALAAKLLAKGGRYVIV 265
THR_DH_like cd08239
L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as ...
 149-257 8.85e-22

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: 94.31  E-value: 8.85e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 149 GVRDAHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGADATFDPITTDVGlEVKRLTGKLGAD 228
Cdd:cd08239  155 ALRRVGVSGRDTVLVVGAGPVGLGALMLARALGAEDVIGVDPSPERLELAKALGADFVINSGQDDVQ-EIRELTSGAGAD 233

                         90       100
                 ....*....|....*....|....*....
gi 489820032 229 SIIETSGNAAALQAALRGIAYGGTISYVA 257
Cdd:cd08239  234 VAIECSGNTAARRLALEAVRPWGRLVLVG 262
benzyl_alcohol_DH cd08278
Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol ...
 155-264 3.09e-21

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


Pssm-ID: 176239 [Multi-domain]  Cd Length: 365  Bit Score: 93.33  E-value: 3.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 155 VRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGADATFDPITTDVGLEVKRLTGKlGADSIIETS 234
Cdd:cd08278  184 PRPGSSIAVFGAGAVGLAAVMAAKIAGCTTIIAVDIVDSRLELAKELGATHVINPKEEDLVAAIREITGG-GVDYALDTT 262

                         90       100       110
                 ....*....|....*....|....*....|
gi 489820032 235 GNAAALQAALRGIAYGGTISYVAFAKPFPE 264
Cdd:cd08278  263 GVPAVIEQAVDALAPRGTLALVGAPPPGAE 292
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 81-338 1.07e-20

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: 91.12  E-value: 1.07e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  81 LGNMVVGEVVERGSKVTEYALGDIVCS--------YGPIMETVIVKAvdnYKLRKLPKGANWKNAVC----YDPAQFAMs 148
Cdd:cd08268   61 LGYEAAGVVEAVGAGVTGFAVGDRVSVipaadlgqYGTYAEYALVPA---AAVVKLPDGLSFVEAAAlwmqYLTAYGAL- 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 149 gVRDAHVRAGDYVVVVGL-GAIGQIAIQLAKKAGAsVVIGVDPLSHRREIAEKHGADATFDPITTDVGLEVKRLTGKLGA 227
Cdd:cd08268  137 -VELAGLRPGDSVLITAAsSSVGLAAIQIANAAGA-TVIATTRTSEKRDALLALGAAHVIVTDEEDLVAEVLRITGGKGV 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 228 DSIIETSGnAAALQAALRGIAYGGTI-SYVAFAK---PFPEGFNLGREAHFnnakivfsRAASEPNPDYPRWDRKRIEET 303
Cdd:cd08268  215 DVVFDPVG-GPQFAKLADALAPGGTLvVYGALSGeptPFPLKAALKKSLTF--------RGYSLDEITLDPEARRRAIAF 285

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 489820032 304 CWELLMNGYLdcSDIIDPVVPFADSAESYmKYVDQ 338
Cdd:cd08268  286 ILDGLASGAL--KPVVDRVFPFDDIVEAH-RYLES 317
CAD3 cd08297
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
 86-258 5.93e-20

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: 89.13  E-value: 5.93e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  86 VGEVVERGSKVTEYALGDIV-----------CSY--------------------GPIMETVIVKAvdNYkLRKLPKGanw 134
Cdd:cd08297   65 AGVVVAVGPGVSGLKVGDRVgvkwlydacgkCEYcrtgdetlcpnqknsgytvdGTFAEYAIADA--RY-VTPIPDG--- 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 135 knavcYDPAQFA--M-------SGVRDAHVRAGDYVVVVGLGA-IGQIAIQLAKKAGASVvIGVDPLSHRREIAEKHGAD 204
Cdd:cd08297  139 -----LSFEQAAplLcagvtvyKALKKAGLKPGDWVVISGAGGgLGHLGVQYAKAMGLRV-IAIDVGDEKLELAKELGAD 212

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489820032 205 ATFDPITTDVGLEVKRLTGKLGADSIIETSGNAAALQAALRGIAYGGTISYVAF 258
Cdd:cd08297  213 AFVDFKKSDDVEAVKELTGGGGAHAVVVTAVSAAAYEQALDYLRPGGTLVCVGL 266
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 87-339 1.96e-19

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: 87.59  E-value: 1.96e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  87 GEVVERGSKVTEYALGDIVCS-------YGPIMETVIVKAV--------------DNYKLRKLPKGANWKNAVCYDPAQ- 144
Cdd:cd08276   67 GEVVAVGEGVTRFKVGDRVVPtffpnwlDGPPTAEDEASALggpidgvlaeyvvlPEEGLVRAPDHLSFEEAATLPCAGl 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 145 ---FAMSGVRdaHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVI--GVDPlshRREIAEKHGADATFDPITT-DVGLEV 218
Cdd:cd08276  147 tawNALFGLG--PLKPGDTVLVQGTGGVSLFALQFAKAAGARVIAtsSSDE---KLERAKALGADHVINYRTTpDWGEEV 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 219 KRLTGKLGADSIIETsGNAAALQAALRGIAYGGTISYVAFAKPFPEGFNLGrEAHFNNAKI----VFSRAAsepnpdypr 294
Cdd:cd08276  222 LKLTGGRGVDHVVEV-GGPGTLAQSIKAVAPGGVISLIGFLSGFEAPVLLL-PLLTKGATLrgiaVGSRAQ--------- 290

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 489820032 295 wdrkrIEEtcwellMNGYLDCSDI---IDPVVPFADSAESYmKYVDQQ 339
Cdd:cd08276  291 -----FEA------MNRAIEAHRIrpvIDRVFPFEEAKEAY-RYLESG 326
FDH_like_1 cd08283
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified ...
 149-341 7.07e-19

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


Pssm-ID: 176243 [Multi-domain]  Cd Length: 386  Bit Score: 86.82  E-value: 7.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 149 GVRDAHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGADATFDPITTD-VGLEVKRLTGKLGA 227
Cdd:cd08283  176 AAELAEVKPGDTVAVWGCGPVGLFAARSAKLLGAERVIAIDRVPERLEMARSHLGAETINFEEVDdVVEALRELTGGRGP 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 228 DSIIETSGNAA---------------------ALQAALRGIAYGGTISYVAFAKPFPEGFNLGreAHFNnaKIVFSRAAS 286
Cdd:cd08283  256 DVCIDAVGMEAhgsplhkaeqallkletdrpdALREAIQAVRKGGTVSIIGVYGGTVNKFPIG--AAMN--KGLTLRMGQ 331

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489820032 287 EPNPDYprWDRkrieetCWELLMNGYLDCSDIIDPVVPFADSAESYMKYVDQQPD 341
Cdd:cd08283  332 THVQRY--LPR------LLELIESGELDPSFIITHRLPLEDAPEAYKIFDKKEDG 378
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
 81-261 9.47e-19

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: 85.76  E-value: 9.47e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  81 LGNMVVGEVVERGSKVTEYALGDIVC------------------------------SYGPIMETVIVKAVDnykLRKLPK 130
Cdd:cd08254   60 LGHEIAGTVVEVGAGVTNFKVGDRVAvpavipcgacalcrrgrgnlclnqgmpglgIDGGFAEYIVVPARA---LVPVPD 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 131 GAnwknavcyDPAQFAMS----------GVRDAHVRAGDYVVVVGLGAIGQIAIQLAKKAGASvVIGVDPLSHRREIAEK 200
Cdd:cd08254  137 GV--------PFAQAAVAtdavltpyhaVVRAGEVKPGETVLVIGLGGLGLNAVQIAKAMGAA-VIAVDIKEEKLELAKE 207

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489820032 201 HGADATFDPItTDVGLEVKRLTGKLGADSIIETSGNAAALQAALRGIAYGGTISYVAFAKP 261
Cdd:cd08254  208 LGADEVLNSL-DDSPKDKKAAGLGGGFDVIFDFVGTQPTFEDAQKAVKPGGRIVVVGLGRD 267
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
 146-256 1.47e-18

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: 85.39  E-value: 1.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 146 AMSGVRDAH-VRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGADATFDPITTDVGLEVKR---L 221
Cdd:cd08231  165 VLAALDRAGpVGAGDTVVVQGAGPLGLYAVAAAKLAGARRVIVIDGSPERLELAREFGADATIDIDELPDPQRRAIvrdI 244

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489820032 222 TGKLGADSIIETSGNAAALQAALRGIAYGGTisYV 256
Cdd:cd08231  245 TGGRGADVVIEASGHPAAVPEGLELLRRGGT--YV 277
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
 1-254 4.40e-18

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 83.72  E-value: 4.40e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032   1 MKKLVATAPRVAA-LVEYNDREVLEDEVKIKVQFASpKHGTEVvdfrgispFIDEefspeWNLFvsretnSARGI----V 75
Cdd:PRK05396   1 MKALVKLKAEPGLwLTDVPVPEPGPNDVLIKVKKTA-ICGTDV--------HIYN-----WDEW------AQKTIpvpmV 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  76 FG-EFqlgnmvVGEVVERGSKVTEYALGDIVCSYGPI----------------METVIVkAVDnyklR--------KLPK 130
Cdd:PRK05396  61 VGhEF------VGEVVEVGSEVTGFKVGDRVSGEGHIvcghcrncragrrhlcRNTKGV-GVN----RpgafaeylVIPA 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 131 GANWKN--------AVCYDP--------AQFAMSGvRDahvragdyVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHR 194
Cdd:PRK05396 130 FNVWKIpddipddlAAIFDPfgnavhtaLSFDLVG-ED--------VLITGAGPIGIMAAAVAKHVGARHVVITDVNEYR 200

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 195 REIAEKHGADATFDPITTDVGLEVKRLTGKLGADSIIETSGNAAALQAALRGIAYGGTIS 254
Cdd:PRK05396 201 LELARKMGATRAVNVAKEDLRDVMAELGMTEGFDVGLEMSGAPSAFRQMLDNMNHGGRIA 260
liver_ADH_like1 cd08281
Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); ...
 153-261 8.60e-18

Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. This group contains members identified as zinc dependent alcohol dehydrogenases (ADH), and class III ADG (aka formaldehyde dehydrogenase, FDH). 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. 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 know as glutathione-dependent formaldehyde dehydrogenase (FDH), which convert aldehydes to the corresponding carboxylic acid and alcohol. 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: 176241 [Multi-domain]  Cd Length: 371  Bit Score: 83.58  E-value: 8.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 153 AHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGADATFDPITTDVGLEVKRLTGKlGADSIIE 232
Cdd:cd08281  187 AGVRPGQSVAVVGLGGVGLSALLGAVAAGASQVVAVDLNEDKLALARELGATATVNAGDPNAVEQVRELTGG-GVDYAFE 265

                         90       100
                 ....*....|....*....|....*....
gi 489820032 233 TSGNAAALQAALRGIAYGGTISYVAFAKP 261
Cdd:cd08281  266 MAGSVPALETAYEITRRGGTTVTAGLPDP 294
FDH_like_ADH2 cd08286
formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase ...
 81-256 1.97e-17

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: 81.91  E-value: 1.97e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  81 LGNMVVGEVVERGSKVTEYALGDIV----------CSY------------GPIM---------ETVIVKAVDNyKLRKLP 129
Cdd:cd08286   58 LGHEGVGVVEEVGSAVTNFKVGDRVliscisscgtCGYcrkglyshcesgGWILgnlidgtqaEYVRIPHADN-SLYKLP 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 130 KGANWKNAV-CYD--PAQFAMsGVRDAHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGADAT 206
Cdd:cd08286  137 EGVDEEAAVmLSDilPTGYEC-GVLNGKVKPGDTVAIVGAGPVGLAALLTAQLYSPSKIIMVDLDDNRLEVAKKLGATHT 215

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 489820032 207 FDPITTDVGLEVKRLTGKLGADSIIETSGNAAALQAALRGIAYGGTISYV 256
Cdd:cd08286  216 VNSAKGDAIEQVLELTDGRGVDVVIEAVGIPATFELCQELVAPGGHIANV 265
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 81-252 4.77e-17

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: 81.11  E-value: 4.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  81 LGNMVVGEVVERGSKVTEYALGDIV----------CSY--------------------GPIMETVIVKAVDnYKLRKLPK 130
Cdd:cd08260   58 PGHEFAGVVVEVGEDVSRWRVGDRVtvpfvlgcgtCPYcragdsnvcehqvqpgfthpGSFAEYVAVPRAD-VNLVRLPD 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 131 GAnwknavcyDPAQFAMSGVR----------DAHVRAGDYVVVVGLGAIGQIAIQLAKKAGASvVIGVDPLSHRREIAEK 200
Cdd:cd08260  137 DV--------DFVTAAGLGCRfatafralvhQARVKPGEWVAVHGCGGVGLSAVMIASALGAR-VIAVDIDDDKLELARE 207

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489820032 201 HGADATFDP-ITTDVGLEVKRLTGKlGADSIIETSGNAAALQAALRGIAYGGT 252
Cdd:cd08260  208 LGAVATVNAsEVEDVAAAVRDLTGG-GAHVSVDALGIPETCRNSVASLRKRGR 259
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 153-259 8.88e-17

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: 80.49  E-value: 8.88e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 153 AHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGADATFDPITTDVGLEVKRLTGKLGADSIIE 232
Cdd:cd08263  183 ADVRPGETVAVIGVGGVGSSAIQLAKAFGASPIIAVDVRDEKLAKAKELGATHTVNAAKEDAVAAIREITGGRGVDVVVE 262

                         90       100
                 ....*....|....*....|....*..
gi 489820032 233 TSGNAAALQAALRGIAYGGTISYVAFA 259
Cdd:cd08263  263 ALGKPETFKLALDVVRDGGRAVVVGLA 289
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
 81-253 1.38e-16

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: 79.61  E-value: 1.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  81 LGNMVVGEVVERGSKVTEYALGDIV----------CSY--------------------GPIMETVIVKAVDnykLRKLPK 130
Cdd:cd08266   61 LGSDGAGVVEAVGPGVTNVKPGQRVviypgiscgrCEYclagrenlcaqygilgehvdGGYAEYVAVPARN---LLPIPD 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 131 GANWKNAVCYdPAQFAMSG---VRDAHVRAGDYVVVVGLGA-IGQIAIQLAKKAGASVVIGVDPlSHRREIAEKHGADAT 206
Cdd:cd08266  138 NLSFEEAAAA-PLTFLTAWhmlVTRARLRPGETVLVHGAGSgVGSAAIQIAKLFGATVIATAGS-EDKLERAKELGADYV 215

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 489820032 207 FDPITTDVGLEVKRLTGKLGADSIIETSGnAAALQAALRGIAYGGTI 253
Cdd:cd08266  216 IDYRKEDFVREVRELTGKRGVDVVVEHVG-AATWEKSLKSLARGGRL 261
Zn_ADH3 cd08265
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 81-346 1.38e-16

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: 79.87  E-value: 1.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  81 LGNMVVGEVVERGSKVTEYALGDIVCSY------------------------------GPIMETVIVKAVDNYKLRKLPK 130
Cdd:cd08265   91 IGHEFSGVVEKTGKNVKNFEKGDPVTAEemmwcgmcracrsgspnhcknlkelgfsadGAFAEYIAVNARYAWEINELRE 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 131 GANWKNA----VCYDPAQFAMSGV--RDAHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGAD 204
Cdd:cd08265  171 IYSEDKAfeagALVEPTSVAYNGLfiRGGGFRPGAYVVVYGAGPIGLAAIALAKAAGASKVIAFEISEERRNLAKEMGAD 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 205 ATFDPI---TTDVGLEVKRLTGKLGADSIIETSGNAAALQAAL-RGIAYGGTISYVAFAKP----FPEGFNLGReahfnn 276
Cdd:cd08265  251 YVFNPTkmrDCLSGEKVMEVTKGWGADIQVEAAGAPPATIPQMeKSIAINGKIVYIGRAATtvplHLEVLQVRR------ 324

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 277 AKIVFSRAASEpNPDYPRWDRkrieetcweLLMNGYLDCSDIIDPVVPFADSAESyMKYVDQQPDLSIKM 346
Cdd:cd08265  325 AQIVGAQGHSG-HGIFPSVIK---------LMASGKIDMTKIITARFPLEGIMEA-IKAASERTDGKITI 383
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
 79-255 6.58e-16

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: 77.48  E-value: 6.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  79 FQLGNMVVGEVVERGSKVTEYALGDIVCSYGPI---METVIVKAvdnYKLRKLPKGANWKNAvcydpAQFAMSG------ 149
Cdd:cd05286   56 FVLGVEGAGVVEAVGPGVTGFKVGDRVAYAGPPgayAEYRVVPA---SRLVKLPDGISDETA-----AALLLQGltahyl 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 150 VRDAH-VRAGDYVVVVGL-GAIGQIAIQLAKKAGASVvIGVDPLSHRREIAEKHGADATFDPITTDVGLEVKRLTGKLGA 227
Cdd:cd05286  128 LRETYpVKPGDTVLVHAAaGGVGLLLTQWAKALGATV-IGTVSSEEKAELARAAGADHVINYRDEDFVERVREITGGRGV 206

                        170       180
                 ....*....|....*....|....*....
gi 489820032 228 DSIIETSGnAAALQAALRGIAYGGT-ISY 255
Cdd:cd05286  207 DVVYDGVG-KDTFEGSLDSLRPRGTlVSF 234
Zn_ADH8 cd08262
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 70-253 1.68e-15

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: 76.58  E-value: 1.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  70 SARGIVFG-EFqlgnmvVGEVVERGSKV-TEYALGDIVCS---------------YGPIM-----ETVIVKAVdnyKLRK 127
Cdd:cd08262   61 LGADIVLGhEF------CGEVVDYGPGTeRKLKVGTRVTSlplllcgqgascgigLSPEApggyaEYMLLSEA---LLLR 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 128 LPKGANWKNAVCYDPAQFAMSGVRDAHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGADATF 207
Cdd:cd08262  132 VPDGLSMEDAALTEPLAVGLHAVRRARLTPGEVALVIGCGPIGLAVIAALKARGVGPIVASDFSPERRALALAMGADIVV 211

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 489820032 208 DPITTDV----GLEVKRLTGkLGADSIIETSGNAAALQAALRGIAYGGTI 253
Cdd:cd08262  212 DPAADSPfaawAAELARAGG-PKPAVIFECVGAPGLIQQIIEGAPPGGRI 260
Zn_ADH2 cd08256
Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and ...
 127-259 2.21e-15

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


Pssm-ID: 176218 [Multi-domain]  Cd Length: 350  Bit Score: 76.29  E-value: 2.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 127 KLPKGANWKNAVCYDPAQFAMSGVRDAHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGADAT 206
Cdd:cd08256  144 KVPDDIPPEDAILIEPLACALHAVDRANIKFDDVVVLAGAGPLGLGMIGAARLKNPKKLIVLDLKDERLALARKFGADVV 223

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489820032 207 FDPITTDVGLEVKRLTGKLGADSIIETSGNAAALQAALRGIAYGGTisYVAFA 259
Cdd:cd08256  224 LNPPEVDVVEKIKELTGGYGCDIYIEATGHPSAVEQGLNMIRKLGR--FVEFS 274
CAD cd08245
Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases ...
 82-269 9.25e-15

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: 74.28  E-value: 9.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  82 GNMVVGEVVERGSKVTEYALGDIV-----------CSY--------------------GPIMETVIVKAvdNYKLRkLPK 130
Cdd:cd08245   58 GHEIVGEVVEVGAGVEGRKVGDRVgvgwlvgscgrCEYcrrglenlcqkavntgyttqGGYAEYMVADA--EYTVL-LPD 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 131 GanwknavcYDPAQFA---------MSGVRDAHVRAGDYVVVVGLGAIGQIAIQLAKKAGAsVVIGVDPLSHRREIAEKH 201
Cdd:cd08245  135 G--------LPLAQAApllcagitvYSALRDAGPRPGERVAVLGIGGLGHLAVQYARAMGF-ETVAITRSPDKRELARKL 205

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489820032 202 GADATFDpiTTDVGLEVKRLTgklGADSIIETSGNAAALQAALRGIAYGGTISYVA--FAKPF-PEGFNLG 269
Cdd:cd08245  206 GADEVVD--SGAELDEQAAAG---GADVILVTVVSGAAAEAALGGLRRGGRIVLVGlpESPPFsPDIFPLI 271
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
 81-274 5.22e-14

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: 71.88  E-value: 5.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  81 LGNMVVGEVVERGSKVTEYALGDIV----------CSY-------------------------GPIMETVIVKAVdnyKL 125
Cdd:cd08232   57 LGHEVSGVVEAVGPGVTGLAPGQRVavnpsrpcgtCDYcragrpnlclnmrflgsamrfphvqGGFREYLVVDAS---QC 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 126 RKLPKGANWKNAVCYDPAQFAMSGVRDAHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVD----PLshrrEIAEKH 201
Cdd:cd08232  134 VPLPDGLSLRRAALAEPLAVALHAVNRAGDLAGKRVLVTGAGPIGALVVAAARRAGAAEIVATDladaPL----AVARAM 209

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489820032 202 GADATFDPITTDVGLEVKrltGKLGADSIIETSGNAAALQAALRGIAYGGTISYVAF---AKPFPEGFNLGREAHF 274
Cdd:cd08232  210 GADETVNLARDPLAAYAA---DKGDFDVVFEASGAPAALASALRVVRPGGTVVQVGMlggPVPLPLNALVAKELDL 282
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
 82-330 7.16e-14

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: 71.46  E-value: 7.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  82 GNMVVGEVVERGSKVTEYALGDIV--------CSYGPIMETVIVKAvdnYKLRKLPKGANWKNAVC----YDPAQFAMsg 149
Cdd:cd08253   62 GSDGAGVVEAVGEGVDGLKVGDRVwltnlgwgRRQGTAAEYVVVPA---DQLVPLPDGVSFEQGAAlgipALTAYRAL-- 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 150 VRDAHVRAGDYVVVVG-LGAIGQIAIQLAKKAGASVvIGVDPLSHRREIAEKHGADATFDPITTDVGLEVKRLTGKLGAD 228
Cdd:cd08253  137 FHRAGAKAGETVLVHGgSGAVGHAAVQLARWAGARV-IATASSAEGAELVRQAGADAVFNYRAEDLADRILAATAGQGVD 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 229 SIIETSGNaAALQAALRGIAYGGTISYVAFAKPFPEgFNLgREAHFNNAKIVF---SRAASEpnpdyprwDRKRIEETCW 305
Cdd:cd08253  216 VIIEVLAN-VNLAKDLDVLAPGGRIVVYGSGGLRGT-IPI-NPLMAKEASIRGvllYTATPE--------ERAAAAEAIA 284

                        250       260
                 ....*....|....*....|....*
gi 489820032 306 ELLMNGYLDCsdIIDPVVPFADSAE 330
Cdd:cd08253  285 AGLADGALRP--VIAREYPLEEAAA 307
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
 85-330 2.58e-13

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: 69.78  E-value: 2.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  85 VVGEVVERGSKVTEYALGDIVCS------YGpimETVIVKAVdnyKLRKLPKGANWKNAVCYDPAQF-AMSGVRD-AHVR 156
Cdd:cd05276   65 VAGVVVAVGPGVTGWKVGDRVCAllagggYA---EYVVVPAG---QLLPVPEGLSLVEAAALPEVFFtAWQNLFQlGGLK 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 157 AGDYVVVVGlGA--IGQIAIQLAKKAGASVVIGVDPLShRREIAEKHGADATFDPITTDVGLEVKRLTGKLGADSIIETS 234
Cdd:cd05276  139 AGETVLIHG-GAsgVGTAAIQLAKALGARVIATAGSEE-KLEACRALGADVAINYRTEDFAEEVKEATGGRGVDVILDMV 216

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 235 GnAAALQAALRGIAYGGTISYVAFAKpfpegfnlGREAHFNNAKIVFSRAA-------SEPnPDYPRWDRKRIEETCWEL 307
Cdd:cd05276  217 G-GDYLARNLRALAPDGRLVLIGLLG--------GAKAELDLAPLLRKRLTltgstlrSRS-LEEKAALAAAFREHVWPL 286

                        250       260
                 ....*....|....*....|...
gi 489820032 308 LMNGYLDcsDIIDPVVPFADSAE 330
Cdd:cd05276  287 FASGRIR--PVIDKVFPLEEAAE 307
CAD_like cd08296
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 82-257 8.70e-13

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: 68.43  E-value: 8.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  82 GNMVVGEVVERGSKVTEYALGDIV----------------------CSYGPI---------METVIVKAVdnyKLRKLPK 130
Cdd:cd08296   59 GHEVVGRIDAVGEGVSRWKVGDRVgvgwhgghcgtcdacrrgdfvhCENGKVtgvtrdggyAEYMLAPAE---ALARIPD 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 131 GAnwknavcyDPAQFA---------MSGVRDAHVRAGDYVVVVGLGAIGQIAIQLAKKAGAsVVIGVDPLSHRREIAEKH 201
Cdd:cd08296  136 DL--------DAAEAApllcagvttFNALRNSGAKPGDLVAVQGIGGLGHLAVQYAAKMGF-RTVAISRGSDKADLARKL 206

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489820032 202 GADATFDPITTDVGLEVKRLTgklGADSIIETSGNAAALQAALRGIAYGGTISYVA 257
Cdd:cd08296  207 GAHHYIDTSKEDVAEALQELG---GAKLILATAPNAKAISALVGGLAPRGKLLILG 259
PRK09422 PRK09422
ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional
 81-268 2.32e-12

ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional


Pssm-ID: 181842 [Multi-domain]  Cd Length: 338  Bit Score: 66.98  E-value: 2.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  81 LGNMVVGEVVERGSKVTEYALGDIV-----------CSY--------------------GPIMETVIVKAvdNYKLrKLP 129
Cdd:PRK09422  57 LGHEGIGIVKEVGPGVTSLKVGDRVsiawffegcghCEYcttgretlcrsvknagytvdGGMAEQCIVTA--DYAV-KVP 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 130 KGanwknavcYDPAQfAMS----------GVRDAHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAE 199
Cdd:PRK09422 134 EG--------LDPAQ-ASSitcagvttykAIKVSGIKPGQWIAIYGAGGLGNLALQYAKNVFNAKVIAVDINDDKLALAK 204

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 200 KHGADATFDPITT-DVGLEVKRLTGklGADSIIETSGNAAALQAALRGIAYGGTIsyVAFAKPfPEGFNL 268
Cdd:PRK09422 205 EVGADLTINSKRVeDVAKIIQEKTG--GAHAAVVTAVAKAAFNQAVDAVRAGGRV--VAVGLP-PESMDL 269
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
 81-298 2.44e-12

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: 66.84  E-value: 2.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  81 LGNMVVGEVVERGSKVTEYALGDIVCSYGPIMETVIVK--------AVDNYKLRKLPKGANWKNAVC------------Y 140
Cdd:cd08249   58 LGCDFAGTVVEVGSGVTRFKVGDRVAGFVHGGNPNDPRngafqeyvVADADLTAKIPDNISFEEAATlpvglvtaalalF 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 141 DPAQFAMSGVRDAHVRAGDYVVVVGlG--AIGQIAIQLAKKAGASVVIGVDPlsHRREIAEKHGADATFDPITTDVGLEV 218
Cdd:cd08249  138 QKLGLPLPPPKPSPASKGKPVLIWG-GssSVGTLAIQLAKLAGYKVITTASP--KNFDLVKSLGADAVFDYHDPDVVEDI 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 219 KRLTG---KLGADSIIETSGNAAALQAAlrGIAYGGTISYVAfakPFPEGFNLGREAHFnnaKIVFSRAASEPNPDYPRW 295
Cdd:cd08249  215 RAATGgklRYALDCISTPESAQLCAEAL--GRSGGGKLVSLL---PVPEETEPRKGVKV---KFVLGYTVFGEIPEDREF 286


                 ...
gi 489820032 296 DRK 298
Cdd:cd08249  287 GEV 289
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
 71-253 2.69e-12

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: 66.87  E-value: 2.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  71 ARGIVFgEFQLGNMVVGEVVERGSKVTEYALGDIV----------CSY--------------------GPIMETVIVkav 120
Cdd:cd08240   61 DRGVKL-PLVLGHEIVGEVVAVGPDAADVKVGDKVlvypwigcgeCPVclagdenlcakgralgifqdGGYAEYVIV--- 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 121 DNYKLRKLPKGAnwknavcyDPAQFAM---------SGVRDAHVRAGD-YVVVVGLGAIGQIAIQLAKKAGASVVIGVDP 190
Cdd:cd08240  137 PHSRYLVDPGGL--------DPALAATlacsgltaySAVKKLMPLVADePVVIIGAGGLGLMALALLKALGPANIIVVDI 208

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489820032 191 LSHRREIAEKHGADATFDPITTDVGLEVKRLTGKlGADSIIETSGNAAALQAALRGIAYGGTI 253
Cdd:cd08240  209 DEAKLEAAKAAGADVVVNGSDPDAAKRIIKAAGG-GVDAVIDFVNNSATASLAFDILAKGGKL 270
Zn_ADH1 cd05279
Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases; NAD(P)(H) ...
 150-261 3.01e-12

Liver alcohol dehydrogenase and related 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. There are 7 vertebrate ADH 7 classes, 6 of which have been identified in humans. Class III, glutathione-dependent formaldehyde dehydrogenase, has been identified as the primordial form and exists in diverse species, including plants, micro-organisms, vertebrates, and invertebrates. Class I, typified by liver dehydrogenase, is an evolving form. Gene duplication and functional specialization of ADH into ADH classes and subclasses created numerous forms in vertebrates. For example, the A, B and C (formerly alpha, beta, gamma) human class I subunits have high overall structural similarity, but differ in the substrate binding pocket and therefore in substrate specificity. 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. 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: 176182 [Multi-domain]  Cd Length: 365  Bit Score: 67.08  E-value: 3.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 150 VRDAHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGADATFDPITTDVGLE--VKRLTGKlGA 227
Cdd:cd05279  176 VNTAKVTPGSTCAVFGLGGVGLSVIMGCKAAGASRIIAVDINKDKFEKAKQLGATECINPRDQDKPIVevLTEMTDG-GV 254

                         90       100       110
                 ....*....|....*....|....*....|....
gi 489820032 228 DSIIETSGNAAALQAALRGIAYGGTISYVAFAKP 261
Cdd:cd05279  255 DYAFEVIGSADTLKQALDATRLGGGTSVVVGVPP 288
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 85-257 3.87e-12

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: 66.15  E-value: 3.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  85 VVGEVVERGSKVTEYALGDIVCSYGPIME-------TVivkaVDNYKLRKLPKGANWKNAV---CydPAQFAMSGVRD-A 153
Cdd:cd08271   64 GAGVVVAVGAKVTGWKVGDRVAYHASLARggsfaeyTV----VDARAVLPLPDSLSFEEAAalpC--AGLTAYQALFKkL 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 154 HVRAGDYVVVVGL-GAIGQIAIQLAKKAGASVVIGVDPLSHRReiAEKHGADATFDPITTDVGLEVKRLTGKLGADSIIE 232
Cdd:cd08271  138 RIEAGRTILITGGaGGVGSFAVQLAKRAGLRVITTCSKRNFEY--VKSLGADHVIDYNDEDVCERIKEITGGRGVDAVLD 215

                        170       180
                 ....*....|....*....|....*..
gi 489820032 233 TSG--NAAALQAALrgiAYGGTISYVA 257
Cdd:cd08271  216 TVGgeTAAALAPTL---AFNGHLVCIQ 239
liver_alcohol_DH_like cd08277
Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 150-244 4.57e-12

Liver alcohol dehydrogenase; 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. There are 7 vertebrate ADH 7 classes, 6 of which have been identified in humans. Class III, glutathione-dependent formaldehyde dehydrogenase, has been identified as the primordial form and exists in diverse species, including plants, micro-organisms, vertebrates, and invertebrates. Class I, typified by liver dehydrogenase, is an evolving form. Gene duplication and functional specialization of ADH into ADH classes and subclasses created numerous forms in vertebrates. For example, the A, B and C (formerly alpha, beta, gamma) human class I subunits have high overall structural similarity, but differ in the substrate binding pocket and therefore in substrate specificity. 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. 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: 176238 [Multi-domain]  Cd Length: 365  Bit Score: 66.21  E-value: 4.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 150 VRDAHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGADATFDPITTDVGLE--VKRLTGkLGA 227
Cdd:cd08277  177 WNTAKVEPGSTVAVFGLGAVGLSAIMGAKIAGASRIIGVDINEDKFEKAKEFGATDFINPKDSDKPVSevIREMTG-GGV 255

                         90
                 ....*....|....*..
gi 489820032 228 DSIIETSGNAAALQAAL 244
Cdd:cd08277  256 DYSFECTGNADLMNEAL 272
FDH_like_ADH3 cd08287
formaldehyde dehydrogenase (FDH)-like; This group contains proteins identified as alcohol ...
 153-332 9.24e-12

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


Pssm-ID: 176247 [Multi-domain]  Cd Length: 345  Bit Score: 65.41  E-value: 9.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 153 AHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGAdatfdpitTDVGLE--------VKRLTGK 224
Cdd:cd08287  164 AGVRPGSTVVVVGDGAVGLCAVLAAKRLGAERIIAMSRHEDRQALAREFGA--------TDIVAErgeeavarVRELTGG 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 225 LGADSIIETSGNAAALQAALRGIAYGGTISYVAFakPFPEGFNLGREAHFNNAKIvfsraASEPNPdyprwDRKRIEETC 304
Cdd:cd08287  236 VGADAVLECVGTQESMEQAIAIARPGGRVGYVGV--PHGGVELDVRELFFRNVGL-----AGGPAP-----VRRYLPELL 303

                        170       180
                 ....*....|....*....|....*...
gi 489820032 305 wELLMNGYLDCSDIIDPVVPFADSAESY 332
Cdd:cd08287  304 -DDVLAGRINPGRVFDLTLPLDEVAEGY 330
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
 66-253 9.74e-12

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: 64.90  E-value: 9.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  66 RETNSARGIVFG-EFQLGNMVVGEVVERGSKVTEYALGDIVCSYGPI-METVIVkaVDNYKLRKLPKGANWKNA----VC 139
Cdd:cd05195   15 RDVLVALGLLPGdETPLGLECSGIVTRVGSGVTGLKVGDRVMGLAPGaFATHVR--VDARLVVKIPDSLSFEEAatlpVA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 140 YDPAQFAMSGVrdAHVRAGDYVVVV-GLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGADAT-FDPITTDVGLE 217
Cdd:cd05195   93 YLTAYYALVDL--ARLQKGESVLIHaAAGGVGQAAIQLAQHLGAEVFATVGSEEKREFLRELGGPVDHiFSSRDLSFADG 170

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 489820032 218 VKRLTGKLGADSIIeTSGNAAALQAALRGIAYGGTI 253
Cdd:cd05195  171 ILRATGGRGVDVVL-NSLSGELLRASWRCLAPFGRF 205
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 81-269 2.85e-11

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: 63.87  E-value: 2.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  81 LGNMVVGEVVERGSKVTEYALGDIVCSY------------------------------GPIMETVIVKAVDnykLRKLPK 130
Cdd:cd08259   58 LGHEIVGTVEEVGEGVERFKPGDRVILYyyipcgkceyclsgeenlcrnraeygeevdGGFAEYVKVPERS---LVKLPD 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 131 GANWKNAV---CydPAQFAMSGVRDAHVRAGDYVVVVG-LGAIGQIAIQLAKKAGASvVIGVDPLSHRREIAEKHGADAT 206
Cdd:cd08259  135 NVSDESAAlaaC--VVGTAVHALKRAGVKKGDTVLVTGaGGGVGIHAIQLAKALGAR-VIAVTRSPEKLKILKELGADYV 211

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489820032 207 FDpiTTDVGLEVKRLtgkLGADSIIETSGnAAALQAALRGIAYGGTISYVAFAKPFPEGFNLG 269
Cdd:cd08259  212 ID--GSKFSEDVKKL---GGADVVIELVG-SPTIEESLRSLNKGGRLVLIGNVTPDPAPLRPG 268
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 81-283 9.26e-11

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: 62.19  E-value: 9.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  81 LGNMVVGEVVERGSKVTEYALGDIV--C---------SYGPIMetvivkAVDNYKLRKLPKGANWKNAVCYdPAQF--AM 147
Cdd:cd08272   61 LGCDVAGVVEAVGEGVTRFRVGDEVygCagglgglqgSLAEYA------VVDARLLALKPANLSMREAAAL-PLVGitAW 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 148 SG-VRDAHVRAGDYVVVV-GLGAIGQIAIQLAKKAGASVVIGVdpLSHRREIAEKHGADATFDPiTTDVGLEVKRLTGKL 225
Cdd:cd08272  134 EGlVDRAAVQAGQTVLIHgGAGGVGHVAVQLAKAAGARVYATA--SSEKAAFARSLGADPIIYY-RETVVEYVAEHTGGR 210

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489820032 226 GADSIIETSGNaAALQAALRGIA-YGGTISYVAFAKpfpegFNLGrEAHFNNAKI--VFSR 283
Cdd:cd08272  211 GFDVVFDTVGG-ETLDASFEAVAlYGRVVSILGGAT-----HDLA-PLSFRNATYsgVFTL 264
alcohol_DH_class_III cd08300
class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde ...
 153-244 2.24e-10

class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde dehydrogenase(FDH), a member of the zinc dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes or ketones. Like many zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these FDHs form dimers, with 4 zinc ions per dimer. The medium chain alcohol dehydrogenase family (MDR) 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. 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.


Pssm-ID: 176260 [Multi-domain]  Cd Length: 368  Bit Score: 61.09  E-value: 2.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 153 AHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGADATFDPITTDVGL-EVKRLTGKLGADSII 231
Cdd:cd08300  182 AKVEPGSTVAVFGLGAVGLAVIQGAKAAGASRIIGIDINPDKFELAKKFGATDCVNPKDHDKPIqQVLVEMTDGGVDYTF 261

                         90
                 ....*....|...
gi 489820032 232 ETSGNAAALQAAL 244
Cdd:cd08300  262 ECIGNVKVMRAAL 274
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
 79-259 1.92e-09

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: 57.82  E-value: 1.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  79 FQLGNMVVGEVVERGSKVTEYALGD-IVCSYGPIM--ETVIVKAVDNYKLRKlPKGANWKNAvCYDPAQF--AMSGVRDA 153
Cdd:cd08251   39 FTPGFEASGVVRAVGPHVTRLAVGDeVIAGTGESMggHATLVTVPEDQVVRK-PASLSFEEA-CALPVVFltVIDAFARA 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 154 HVRAGDYVVV-VGLGAIGQIAIQLAKKAGAsVVIGVDPLSHRREIAEKHGADATFDPITTDVGLEVKRLTGKLGADSIIE 232
Cdd:cd08251  117 GLAKGEHILIqTATGGTGLMAVQLARLKGA-EIYATASSDDKLEYLKQLGVPHVINYVEEDFEEEIMRLTGGRGVDVVIN 195

                        170       180
                 ....*....|....*....|....*...
gi 489820032 233 T-SGNaaALQAALRGIAYGGtiSYVAFA 259
Cdd:cd08251  196 TlSGE--AIQKGLNCLAPGG--RYVEIA 219
PGDH cd05288
Prostaglandin dehydrogenases; Prostaglandins and related eicosanoids are metabolized by the ...
 79-185 1.99e-09

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: 58.26  E-value: 1.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  79 FQLG----NMVVGEVVErgSKVTEYALGDIVCSYGPIMETVIVKAvdNYKLRKLPKGANWKNA----VCYDPAQFAMSGV 150
Cdd:cd05288   62 VQLGepmrGGGVGEVVE--SRSPDFKVGDLVSGFLGWQEYAVVDG--ASGLRKLDPSLGLPLSaylgVLGMTGLTAYFGL 137

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489820032 151 RD-AHVRAGDYVVVVGL-GAIGQIAIQLAKKAGASVV 185
Cdd:cd05288  138 TEiGKPKPGETVVVSAAaGAVGSVVGQIAKLLGARVV 174
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
 81-274 2.02e-09

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: 57.96  E-value: 2.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  81 LGNMVVGEVVERGSKVTEYALGDIVcsYGPIMET--------VIVKAVDnykLRKLPKGANWKNAvcydpAQFAMSG--- 149
Cdd:cd05289   63 PGHDVAGVVVAVGPGVTGFKVGDEV--FGMTPFTrggayaeyVVVPADE---LALKPANLSFEEA-----AALPLAGlta 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 150 ----VRDAHVRAGDYVVVVG-LGAIGQIAIQLAKKAGASVVIGVDPlsHRREIAEKHGADATFDPITTDvgleVKRLTGK 224
Cdd:cd05289  133 wqalFELGGLKAGQTVLIHGaAGGVGSFAVQLAKARGARVIATASA--ANADFLRSLGADEVIDYTKGD----FERAAAP 206

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489820032 225 LGADSIIETSGnAAALQAALRGIAYGGTI-SYVAFAKPFPEGFNLGREAHF 274
Cdd:cd05289  207 GGVDAVLDTVG-GETLARSLALVKPGGRLvSIAGPPPAEQAAKRRGVRAGF 256
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 85-256 3.56e-09

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: 57.51  E-value: 3.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  85 VVGEVVERGSKVTEYALGDIV--------------CSYGpiMETVIVKAVDNYKLRKLPKGANW----KNAVCydPAQFA 146
Cdd:cd05283   61 IVGIVVAVGSKVTKFKVGDRVgvgcqvdscgtceqCKSG--EEQYCPKGVVTYNGKYPDGTITQggyaDHIVV--DERFV 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 147 M----------------------SGVRDAHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIgvdpLSH---RREIAEKH 201
Cdd:cd05283  137 FkipegldsaaaapllcagitvySPLKRNGVGPGKRVGVVGIGGLGHLAVKFAKALGAEVTA----FSRspsKKEDALKL 212

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489820032 202 GADATfdPITTDVGlEVKRLTGKLgaDSIIETSGNAAALQAALRGIAYGGTISYV 256
Cdd:cd05283  213 GADEF--IATKDPE-AMKKAAGSL--DLIIDTVSASHDLDPYLSLLKPGGTLVLV 262
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
 79-255 3.98e-09

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: 57.29  E-value: 3.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  79 FQLGNMVVGEVVERGSKVTEYALGDIVCSYGPIM---ETVIVKAVDnykLRKLPKGAnwknavcyDPAQFAMSGV----- 150
Cdd:cd05282   58 AVPGNEGVGVVVEVGSGVSGLLVGQRVLPLGGEGtwqEYVVAPADD---LIPVPDSI--------SDEQAAMLYInplta 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 151 -----RDAHVRAGDYVVVVGLG-AIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKhGADATFDPITTDVGLEVKRLTGK 224
Cdd:cd05282  127 wlmltEYLKLPPGDWVIQNAANsAVGRMLIQLAKLLGFKTINVVRRDEQVEELKAL-GADEVIDSSPEDLAQRVKEATGG 205

                        170       180       190
                 ....*....|....*....|....*....|...
gi 489820032 225 LGADSIIE-TSGNAAALQAALrgIAYGGT-ISY 255
Cdd:cd05282  206 AGARLALDaVGGESATRLARS--LRPGGTlVNY 236
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 87-236 4.63e-09

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: 56.84  E-value: 4.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  87 GEVVERGSKVTEYALGDIVCSYGPIM------ETVIVKAvdnYKLRKLPKGANWKNAVCYD-PAQFAMSGVRD-AHVRAG 158
Cdd:cd08267   68 GEVVAVGSGVTRFKVGDEVFGRLPPKgggalaEYVVAPE---SGLAKKPEGVSFEEAAALPvAGLTALQALRDaGKVKPG 144

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489820032 159 DYVVVVGL-GAIGQIAIQLAKKAGASVViGVDPlSHRREIAEKHGADATFDPITTDVGLEVKRlTGKLgaDSIIETSGN 236
Cdd:cd08267  145 QRVLINGAsGGVGTFAVQIAKALGAHVT-GVCS-TRNAELVRSLGADEVIDYTTEDFVALTAG-GEKY--DVIFDAVGN 218
alcohol_DH_plants cd08301
Plant alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 153-244 5.09e-09

Plant alcohol dehydrogenase; 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. There are 7 vertebrate ADH 7 classes, 6 of which have been identified in humans. Class III, glutathione-dependent formaldehyde dehydrogenase, has been identified as the primordial form and exists in diverse species, including plants, micro-organisms, vertebrates, and invertebrates. Class I, typified by liver dehydrogenase, is an evolving form. Gene duplication and functional specialization of ADH into ADH classes and subclasses created numerous forms in vertebrates. For example, the A, B and C (formerly alpha, beta, gamma) human class I subunits have high overall structural similarity, but differ in the substrate binding pocket and therefore in substrate specificity. 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. 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: 176261 [Multi-domain]  Cd Length: 369  Bit Score: 56.92  E-value: 5.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 153 AHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGADATFDPITTDVGLE--VKRLTGKlGADSI 230
Cdd:cd08301  183 AKVKKGSTVAIFGLGAVGLAVAEGARIRGASRIIGVDLNPSKFEQAKKFGVTEFVNPKDHDKPVQevIAEMTGG-GVDYS 261

                         90
                 ....*....|....
gi 489820032 231 IETSGNAAALQAAL 244
Cdd:cd08301  262 FECTGNIDAMISAF 275
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
 81-263 7.07e-09

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 56.58  E-value: 7.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  81 LGNMVVGEVVERGSKVTEYALGDIV----------CSYGPIMETVIVK-----------------AVDNYKLRKLPKGAN 133
Cdd:PRK13771  58 LGHEVVGTVEEVGENVKGFKPGDRVasllyapdgtCEYCRSGEEAYCKnrlgygeeldgffaeyaKVKVTSLVKVPPNVS 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 134 WKNAVcYDPAQFAM--SGVRDAHVRAGDYVVVVGL-GAIGQIAIQLAKKAGASvVIGVDPLSHRREIAEKHgADATFDpi 210
Cdd:PRK13771 138 DEGAV-IVPCVTGMvyRGLRRAGVKKGETVLVTGAgGGVGIHAIQVAKALGAK-VIAVTSSESKAKIVSKY-ADYVIV-- 212

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489820032 211 TTDVGLEVKRLTgklGADSIIETSGnAAALQAALRGIAYGGTISYVAFAKPFP 263
Cdd:PRK13771 213 GSKFSEEVKKIG---GADIVIETVG-TPTLEESLRSLNMGGKIIQIGNVDPSP 261
MDR_like cd08242
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-253 3.32e-08

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


Pssm-ID: 176204 [Multi-domain]  Cd Length: 319  Bit Score: 54.17  E-value: 3.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032   1 MKKLVATAPRVAALVEYNDREVLEDEVKIKVQFASpKHGTEVVDFRGISPFideefspewnlfvsretnsaRGIvfgefq 80
Cdd:cd08242    1 MKALVLDGGLDLRVEDLPKPEPPPGEALVRVLLAG-ICNTDLEIYKGYYPF--------------------PGV------ 53

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  81 LGNMVVGEVVE------RGSKVT-EYALGDIVCSYG--------PIMETV------------IVKAVDNykLRKLPKGAN 133
Cdd:cd08242   54 PGHEFVGIVEEgpeaelVGKRVVgEINIACGRCEYCrrglythcPNRTVLgivdrdgafaeyLTLPLEN--LHVVPDLVP 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 134 WKNAVCYDPAQFAMSGVRDAHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIgVDPLSHRREIAEKHGADATfdpittd 213
Cdd:cd08242  132 DEQAVFAEPLAAALEILEQVPITPGDKVAVLGDGKLGLLIAQVLALTGPDVVL-VGRHSEKLALARRLGVETV------- 203

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 489820032 214 vgLEVKRLTGKLGADSIIETSGNAAALQAALRGIAYGGTI 253
Cdd:cd08242  204 --LPDEAESEGGGFDVVVEATGSPSGLELALRLVRPRGTV 241
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 85-330 3.42e-08

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: 54.19  E-value: 3.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  85 VVGEVVERGSKVTEYALGDIVCS---YGPIMETVIvkaVDNYKLRKLPKGANWKNAVC----YDPAQFAMSgvRDAHVRA 157
Cdd:cd08273   65 LVGRVDALGSGVTGFEVGDRVAAltrVGGNAEYIN---LDAKYLVPVPEGVDAAEAVClvlnYVTAYQMLH--RAAKVLT 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 158 GDYVVVVGL-GAIGQIAIQLAKKAGASvVIGVDPLSHRREIAEkhgADATFDPITTDVGLEVKRLTGklGADSIIETSGN 236
Cdd:cd08273  140 GQRVLIHGAsGGVGQALLELALLAGAE-VYGTASERNHAALRE---LGATPIDYRTKDWLPAMLTPG--GVDVVFDGVGG 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 237 ---AAALQAALRG---IAYGGTISYVAFAKPFPEGFNLGREAHFNNAKIVFSRAASEPNPDYPRWDRKRIEETCWELLmn 310
Cdd:cd08273  214 esyEESYAALAPGgtlVCYGGNSSLLQGRRSLAALGSLLARLAKLKLLPTGRRATFYYVWRDRAEDPKLFRQDLTELL-- 291

                        250       260
                 ....*....|....*....|...
gi 489820032 311 GYLDCSDI---IDPVVPFADSAE 330
Cdd:cd08273  292 DLLAKGKIrpkIAKRLPLSEVAE 314
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 71-251 7.30e-08

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 53.16  E-value: 7.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032    71 ARGIVFGEFQLGNMVVGEVVERGSKVTEYALGDIVC-----SYGPimeTVIVKAvdnYKLRKLPKGANWKNAVCYdPAQF 145
Cdd:smart00829  16 ALGLYPGEAVLGGECAGVVTRVGPGVTGLAVGDRVMglapgAFAT---RVVTDA---RLVVPIPDGWSFEEAATV-PVVF 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032   146 --AMSGVRD-AHVRAGDYVVV-VGLGAIGQIAIQLAKKAGASV--VIGVDPlshRREIAEKHGADAT--FDPITTDVGLE 217
Cdd:smart00829  89 ltAYYALVDlARLRPGESVLIhAAAGGVGQAAIQLARHLGAEVfaTAGSPE---KRDFLRALGIPDDhiFSSRDLSFADE 165

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 489820032   218 VKRLTGKLGADSIIET-SGnaAALQAALRGIAYGG 251
Cdd:smart00829 166 ILRATGGRGVDVVLNSlSG--EFLDASLRCLAPGG 198
Zn_ADH_like2 cd08264
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 14-235 1.21e-07

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: 52.74  E-value: 1.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  14 LVEYNDREVLEDEVKIKVQFAspkhgtevvdfrGISPfIDeefspeWNLFVSRETNSARGIVFGEFqlgnmvVGEVVERG 93
Cdd:cd08264   16 VEDVKDPKPGPGEVLIRVKMA------------GVNP-VD------YNVINAVKVKPMPHIPGAEF------AGVVEEVG 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  94 SKVTEYALGDIVCSYGPI-----------METVIVK----------------AVDNYKLRKLPKGANWKNAVCYDPAQF- 145
Cdd:cd08264   71 DHVKGVKKGDRVVVYNRVfdgtcdmclsgNEMLCRNggiigvvsnggyaeyiVVPEKNLFKIPDSISDELAASLPVAALt 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 146 AMSGVRDAHVRAGDYVVVVGL-GAIGQIAIQLAKKAGASvVIGVDplshRREIAEKHGADATFDPitTDVGLEVKRLTGK 224
Cdd:cd08264  151 AYHALKTAGLGPGETVVVFGAsGNTGIFAVQLAKMMGAE-VIAVS----RKDWLKEFGADEVVDY--DEVEEKVKEITKM 223

                        250
                 ....*....|.
gi 489820032 225 lgADSIIETSG 235
Cdd:cd08264  224 --ADVVINSLG 232
PRK09880 PRK09880
L-idonate 5-dehydrogenase; Provisional
 118-269 1.69e-07

L-idonate 5-dehydrogenase; Provisional


Pssm-ID: 182130 [Multi-domain]  Cd Length: 343  Bit Score: 52.38  E-value: 1.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 118 KAVDNYKLRKLPKGANWKNAVCYDPAQFAMSGVRDAHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREI 197
Cdd:PRK09880 130 KVVDTAQCIPYPEKADEKVMAFAEPLAVAIHAAHQAGDLQGKRVFVSGVGPIGCLIVAAVKTLGAAEIVCADVSPRSLSL 209

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489820032 198 AEKHGADATFDPITTDVGlEVKRLTGKLgaDSIIETSGNAAALQAALRGIAYGGTISYVAFAKPFPEgFNLG 269
Cdd:PRK09880 210 AREMGADKLVNPQNDDLD-HYKAEKGYF--DVSFEVSGHPSSINTCLEVTRAKGVMVQVGMGGAPPE-FPMM 277
CAD2 cd08298
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
 82-253 2.37e-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: 51.80  E-value: 2.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  82 GNMVVGEVVERGSKVTEYALGDIV-----------CSY--------------------GPIMETVIVKAVDNYKLrklPK 130
Cdd:cd08298   63 GHEIVGRVEAVGPGVTRFSVGDRVgvpwlgstcgeCRYcrsgrenlcdnarftgytvdGGYAEYMVADERFAYPI---PE 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 131 GanwknavcYDPAQFA---MSG------VRDAHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHrREIAEKH 201
Cdd:cd08298  140 D--------YDDEEAApllCAGiigyraLKLAGLKPGQRLGLYGFGASAHLALQIARYQGAEVFAFTRSGEH-QELAREL 210

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489820032 202 GADATFDPittDVGLEVKrltgklgADSIIETSGNAAALQAALRGIAYGGTI 253
Cdd:cd08298  211 GADWAGDS---DDLPPEP-------LDAAIIFAPVGALVPAALRAVKKGGRV 252
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 79-330 3.71e-07

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: 51.05  E-value: 3.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  79 FQLGNMVVGEVVERGSKVTEYALGD---IVCSYGPIMETVIVKAvdnYKLRKLPKGANWKNAVCYdPAQFA---MSGVRD 152
Cdd:cd08275   58 FVPGFECAGTVEAVGEGVKDFKVGDrvmGLTRFGGYAEVVNVPA---DQVFPLPDGMSFEEAAAF-PVNYLtayYALFEL 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 153 AHVRAGDYVVV-VGLGAIGQIAIQLAKKAGASVVIGV-DPLSHrrEIAEKHGADATFDPITTDVGLEVKRLTGKlGADSI 230
Cdd:cd08275  134 GNLRPGQSVLVhSAAGGVGLAAGQLCKTVPNVTVVGTaSASKH--EALKENGVTHVIDYRTQDYVEEVKKISPE-GVDIV 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 231 IE------TSGNAAALQAALRGIAYG-------GTISYVAFAKPFPE-----------------GFNLGReahfnnakiv 280
Cdd:cd08275  211 LDalggedTRKSYDLLKPMGRLVVYGaanlvtgEKRSWFKLAKKWWNrpkvdpmklisenksvlGFNLGW---------- 280

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489820032 281 fsraasepnpdypRWDRKRIEETCW----ELLMNGYLDCsdIIDPVVPFADSAE 330
Cdd:cd08275  281 -------------LFEERELLTEVMdkllKLYEEGKIKP--KIDSVFPFEEVGE 319
PLN02702 PLN02702
L-idonate 5-dehydrogenase
 127-259 5.60e-07

L-idonate 5-dehydrogenase


Pssm-ID: 215378 [Multi-domain]  Cd Length: 364  Bit Score: 50.93  E-value: 5.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 127 KLPKGANWKNAVCYDPAQFAMSGVRDAHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGADAT 206
Cdd:PLN02702 151 KLPENVSLEEGAMCEPLSVGVHACRRANIGPETNVLVMGAGPIGLVTMLAARAFGAPRIVIVDVDDERLSVAKQLGADEI 230

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489820032 207 FDPITT--DVGLEVKRLTGKLGA--DSIIETSGNAAALQAALRGIAYGGTISYVAFA 259
Cdd:PLN02702 231 VLVSTNieDVESEVEEIQKAMGGgiDVSFDCVGFNKTMSTALEATRAGGKVCLVGMG 287
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
 82-252 1.66e-06

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: 49.14  E-value: 1.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  82 GNMVVGEVVERGSKVTEYALGDIVCSYGPIMET----VIVKAVDnykLRKLPKGAnwknavcyDPAQFAMSGV------- 150
Cdd:cd08290   68 GNEGVGEVVKVGSGVKSLKPGDWVIPLRPGLGTwrthAVVPADD---LIKVPNDV--------DPEQAATLSVnpctayr 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 151 -RDAHV--RAGDYVVV-VGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAE---KHGADATF------DPITTDVGLE 217
Cdd:cd08290  137 lLEDFVklQPGDWVIQnGANSAVGQAVIQLAKLLGIKTINVVRDRPDLEELKErlkALGADHVLteeelrSLLATELLKS 216

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 489820032 218 VKRLTGKLGADSIietSGNAAALQAALrgIAYGGT 252
Cdd:cd08290  217 APGGRPKLALNCV---GGKSATELARL--LSPGGT 246
PRK10309 PRK10309
galactitol-1-phosphate 5-dehydrogenase;
71-208 3.69e-06

galactitol-1-phosphate 5-dehydrogenase;


Pssm-ID: 182371 [Multi-domain]  Cd Length: 347  Bit Score: 48.29  E-value: 3.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  71 ARGIVFGEFQLGNMVVGEVVERGSKVTEYALGDIV---------------------C---------SYGPIMETVIVKAV 120
Cdd:PRK10309  47 KNGAHYYPITLGHEFSGYVEAVGSGVDDLHPGDAVacvpllpcftcpeclrgfyslCakydfigsrRDGGNAEYIVVKRK 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 121 DnykLRKLPKGANWKNAVCYDPAQFAMSGVRDAHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEK 200
Cdd:PRK10309 127 N---LFALPTDMPIEDGAFIEPITVGLHAFHLAQGCEGKNVIIIGAGTIGLLAIQCAVALGAKSVTAIDINSEKLALAKS 203


                 ....*...
gi 489820032 201 HGADATFD 208
Cdd:PRK10309 204 LGAMQTFN 211
PLN02827 PLN02827
Alcohol dehydrogenase-like
 153-261 7.38e-06

Alcohol dehydrogenase-like


Pssm-ID: 215442 [Multi-domain]  Cd Length: 378  Bit Score: 47.20  E-value: 7.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 153 AHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGADATFDP--ITTDVGLEVKRLTGKlGADSI 230
Cdd:PLN02827 189 ADVSKGSSVVIFGLGTVGLSVAQGAKLRGASQIIGVDINPEKAEKAKTFGVTDFINPndLSEPIQQVIKRMTGG-GADYS 267

                         90       100       110
                 ....*....|....*....|....*....|....
gi 489820032 231 IETSGNAAALQAALRGIA--YGGTISY-VAFAKP 261
Cdd:PLN02827 268 FECVGDTGIATTALQSCSdgWGLTVTLgVPKAKP 301
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
 153-338 1.76e-05

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 46.18  E-value: 1.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 153 AHVRAGDYVVV-VGLGAIGQIAIQLAKKAGASVVIGVDPlSHRREIAEKHGADA-TFDPITTDVGLEVKRLTGKLGADSI 230
Cdd:PTZ00354 136 GDVKKGQSVLIhAGASGVGTAAAQLAEKYGAATIITTSS-EEKVDFCKKLAAIIlIRYPDEEGFAPKVKKLTGEKGVNLV 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 231 IETSGnAAALQAALRGIAYGGTISYVAF-AKPFPEGFNLG---REahfnNAKIVFSRAASEPNpDYPRWDRKRIEETCWE 306
Cdd:PTZ00354 215 LDCVG-GSYLSETAEVLAVDGKWIVYGFmGGAKVEKFNLLpllRK----RASIIFSTLRSRSD-EYKADLVASFEREVLP 288

                        170       180       190
                 ....*....|....*....|....*....|..
gi 489820032 307 LLMNGYLDCsdIIDPVVPFADSAESYmKYVDQ 338
Cdd:PTZ00354 289 YMEEGEIKP--IVDRTYPLEEVAEAH-TFLEQ 317
PFDH_like cd08282
Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde ...
 153-260 6.16e-05

Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. Unlike typical FDH, Pseudomonas putida aldehyde-dismutating FDH (PFDH) is glutathione-independent. PFDH converts 2 molecules of aldehydes to corresponding carboxylic acid and alcohol. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like the zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these tetrameric FDHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains and a structural zinc in a lobe of the catalytic domain. 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 an 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: 176242 [Multi-domain]  Cd Length: 375  Bit Score: 44.51  E-value: 6.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 153 AHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGAdATFDPITTDVGLEVKRLTGKlGADSIIE 232
Cdd:cd08282  172 AGVQPGDTVAVFGAGPVGLMAAYSAILRGASRVYVVDHVPERLDLAESIGA-IPIDFSDGDPVEQILGLEPG-GVDRAVD 249

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489820032 233 TSG-----------NAAALQAALRGIAYGGTIS----YVAFAK 260
Cdd:cd08282  250 CVGyeardrggeaqPNLVLNQLIRVTRPGGGIGivgvYVAEDP 292
alcohol_DH_class_I_II_IV cd08299
class I, II, IV alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major ...
 148-244 7.05e-05

class I, II, IV alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. This group includes alcohol dehydrogenases corresponding to mammalian classes I, II, IV. 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: 176259 [Multi-domain]  Cd Length: 373  Bit Score: 44.23  E-value: 7.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 148 SGVRDAHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGADATFDPITTDVGL-EV-KRLTGkL 225
Cdd:cd08299  181 AAVNTAKVTPGSTCAVFGLGGVGLSAIMGCKAAGASRIIAVDINKDKFAKAKELGATECINPQDYKKPIqEVlTEMTD-G 259

                         90
                 ....*....|....*....
gi 489820032 226 GADSIIETSGNAAALQAAL 244
Cdd:cd08299  260 GVDFSFEVIGRLDTMKAAL 278
PLN02514 PLN02514
cinnamyl-alcohol dehydrogenase
 82-233 1.53e-04

cinnamyl-alcohol dehydrogenase


Pssm-ID: 166155 [Multi-domain]  Cd Length: 357  Bit Score: 43.25  E-value: 1.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  82 GNMVVGEVVERGSKVTEYALGDIV--------C-------------------SY-----------GPIMETVIvkaVDNY 123
Cdd:PLN02514  68 GHEVVGEVVEVGSDVSKFTVGDIVgvgvivgcCgecspcksdleqycnkriwSYndvytdgkptqGGFASAMV---VDQK 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 124 KLRKLPKGANWKNA---VC-----YDP-AQFamsGVRDAHVRAGdyvvVVGLGAIGQIAIQLAKKAGASVVIgVDPLSHR 194
Cdd:PLN02514 145 FVVKIPEGMAPEQAaplLCagvtvYSPlSHF---GLKQSGLRGG----ILGLGGVGHMGVKIAKAMGHHVTV-ISSSDKK 216

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 489820032 195 REIAEKH-GADATFdpITTDVGlEVKRLTGKLgaDSIIET 233
Cdd:PLN02514 217 REEALEHlGADDYL--VSSDAA-EMQEAADSL--DYIIDT 251
PLN02740 PLN02740
Alcohol dehydrogenase-like
 153-243 1.54e-04

Alcohol dehydrogenase-like


Pssm-ID: 178341 [Multi-domain]  Cd Length: 381  Bit Score: 43.25  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 153 AHVRAGDYVVVVGLGAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGADATFDPITTD--VGLEVKRLTGKlGADSI 230
Cdd:PLN02740 194 ANVQAGSSVAIFGLGAVGLAVAEGARARGASKIIGVDINPEKFEKGKEMGITDFINPKDSDkpVHERIREMTGG-GVDYS 272

                         90
                 ....*....|...
gi 489820032 231 IETSGNAAALQAA 243
Cdd:PLN02740 273 FECAGNVEVLREA 285
MDR_enoyl_red cd08244
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. ...
 146-259 2.75e-04

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: 42.36  E-value: 2.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 146 AMSGVRDAHVRAGDYVVVVGL-GAIGQIAIQLAKKAGASVViGVDPLSHRREIAEKHGADATFDPITTDVGLEVKRLTGK 224
Cdd:cd08244  131 ALGLLDLATLTPGDVVLVTAAaGGLGSLLVQLAKAAGATVV-GAAGGPAKTALVRALGADVAVDYTRPDWPDQVREALGG 209

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489820032 225 LGADSIIETSGNAAAlQAALRGIAYGGTISYVAFA 259
Cdd:cd08244  210 GGVTVVLDGVGGAIG-RAALALLAPGGRFLTYGWA 243
PTGR2 cd08293
Prostaglandin reductase; Prostaglandins and related eicosanoids are metabolized by the ...
 86-188 2.29e-03

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: 39.29  E-value: 2.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032  86 VGEVVErgSKVTEYALGDIVCSYGPIMETVIVkaVDNYKLRKL-PKGANWKNAV----CYDPAQFAMSGVRD-AHVRAG- 158
Cdd:cd08293   79 VGVVEE--SKHQKFAVGDIVTSFNWPWQTYAV--LDGSSLEKVdPQLVDGHLSYflgaVGLPGLTALIGIQEkGHITPGa 154

                         90       100       110
                 ....*....|....*....|....*....|..
gi 489820032 159 --DYVVVVGLGAIGQIAIQLAKKAGASVVIGV 188
Cdd:cd08293  155 nqTMVVSGAAGACGSLAGQIGRLLGCSRVVGI 186
MDR4 cd08270
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 157-269 2.43e-03

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: 39.28  E-value: 2.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 157 AGDYVVVVGL-GAIGQIAIQLAKKAGASVVIGVDPLSHRREIAEKHGADATFDPItTDVGLEVkrltgklgaDSIIETSG 235
Cdd:cd08270  132 LGRRVLVTGAsGGVGRFAVQLAALAGAHVVAVVGSPARAEGLRELGAAEVVVGGS-ELSGAPV---------DLVVDSVG 201

                         90       100       110
                 ....*....|....*....|....*....|....
gi 489820032 236 nAAALQAALRGIAYGGTISYVAFAKPFPEGFNLG 269
Cdd:cd08270  202 -GPQLARALELLAPGGTVVSVGSSSGEPAVFNPA 234
crotonyl_coA_red cd08246
crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase ...
 120-208 2.86e-03

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: 39.32  E-value: 2.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820032 120 VDNYKLRKLPKGANWKNAVCY---DPAQFAM-SGVRDAHVRAGDYVVVVG-LGAIGQIAIQLAKKAGASVVIGV-DPlsH 193
Cdd:cd08246  152 VQATQLMPKPKHLSWEEAAAYmlvGATAYRMlFGWNPNTVKPGDNVLIWGaSGGLGSMAIQLARAAGANPVAVVsSE--E 229

                         90
                 ....*....|....*
gi 489820032 194 RREIAEKHGADATFD 208
Cdd:cd08246  230 KAEYCRALGAEGVIN 244
 
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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