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Conserved domains on  [gi|682443620|gb|KFZ05228|]
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hypothetical protein V501_08582 [Pseudogymnoascus sp. VKM F-4519 (FW-2642)]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1519-1788 1.51e-62

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: 214.88  E-value: 1.51e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1519 EIQVSILTAALNHRDLFIRQSLYPA-ISFTTPLLADGCGVVT---SGSSKLN-GKRVILTPAHGWESQVSGPET-FIGIL 1592
Cdd:cd05188     1 EVLVRVEAAGLCGTDLHIRRGGYPPpPKLPLILGHEGAGVVVevgPGVTGVKvGDRVVVLPNLGCGTCELCRELcPGGGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1593 GGTTMNevGTAQEVVVIPETEVELAPEHLSDAQAAALPLTGLTAWRALVTkSGEAIEGRNILVTGiGGGVALNALQFAVA 1672
Cdd:cd05188    81 LGEGLD--GGFAEYVVVPADNLVPLPDGLSLEEAALLPEPLATAYHALRR-AGVLKPGDTVLVLG-AGGVGLLAAQLAKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1673 KGCNVWVTSGDEGKIKKAVALGAKGGVSYKGAAWDKELLAMlpeERKWIDAIIDGAGG-DIMKRSVRLVKQGGVVVSYG- 1750
Cdd:cd05188   157 AGARVIVTDRSDEKLELAKELGADHVIDYKEEDLEEELRLT---GGGGADVVIDAVGGpETLAQALRLLRPGGRIVVVGg 233

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 682443620 1751 MTLGPKIDFPMSAVLKNIDLKGSTMGSRVEFREMVRFV 1788
Cdd:cd05188   234 TSGGPPLDDLRRLLFKELTIIGSTGGTREDFEEALDLL 271
GYF pfam02213
GYF domain; The GYF domain is named because of the presence of Gly-Tyr-Phe residues. The GYF ...
 730-774 3.77e-19

GYF domain; The GYF domain is named because of the presence of Gly-Tyr-Phe residues. The GYF domain is a proline-binding domain in CD2-binding protein Swiss:O95400.


:

Pssm-ID: 460496  Cd Length: 45  Bit Score: 82.24  E-value: 3.77e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 682443620   730 WVYLDPQGQTQGPWSGLEMHDWYKASFFTPDLSVKKLEDVEFEPL 774
Cdd:pfam02213    1 WEYKDPQGEVQGPFSSAEMQEWYKAGYFPDDLPVRRVGDTEFYPL 45
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 909-1236 6.57e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.40  E-value: 6.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620  909 PIMPQQQIPTSgssffdastRPAPTtgsnlPPDFFREDEVARLSLQDRQQTFGAPTGATQAPRSQLPAifsqqsqaqAAA 988
Cdd:PHA03247 2561 PAAPDRSVPPP---------RPAPR-----PSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPP---------SPL 2617

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620  989 SQHQAHSENDPQGFRARLQEFEQLRAQHDMEQAEHAPAPATTEPIRPPQNRQQSRTETVTTETEVLVERKDQEEILSLTE 1068
Cdd:PHA03247 2618 PPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTS 2697

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1069 QIQKAASAKqTPQPESPWAKVSSGLPMPFPPPPQSTTPLPAPAAQRGRSNLPETlhAGTRSRSETPDTSAAPPSIAPwak 1148
Cdd:PHA03247 2698 LADPPPPPP-TPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPAT--PGGPARPARPPTTAGPPAPAP--- 2771

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1149 ePVDAPKGPSLKEIQEAEAKKAAKLEESAAAARRAlleqelrAQPAAVAHGLPTTSTWASSASPVGPAVTATSTWSKATT 1228
Cdd:PHA03247 2772 -PAAPAAGPPRRLTRPAVASLSESRESLPSPWDPA-------DPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP 2843


                  ....*...
gi 682443620 1229 TKVQNPAP 1236
Cdd:PHA03247 2844 GPPPPSLP 2851
 
Name Accession Description Interval E-value
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1519-1788 1.51e-62

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: 214.88  E-value: 1.51e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1519 EIQVSILTAALNHRDLFIRQSLYPA-ISFTTPLLADGCGVVT---SGSSKLN-GKRVILTPAHGWESQVSGPET-FIGIL 1592
Cdd:cd05188     1 EVLVRVEAAGLCGTDLHIRRGGYPPpPKLPLILGHEGAGVVVevgPGVTGVKvGDRVVVLPNLGCGTCELCRELcPGGGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1593 GGTTMNevGTAQEVVVIPETEVELAPEHLSDAQAAALPLTGLTAWRALVTkSGEAIEGRNILVTGiGGGVALNALQFAVA 1672
Cdd:cd05188    81 LGEGLD--GGFAEYVVVPADNLVPLPDGLSLEEAALLPEPLATAYHALRR-AGVLKPGDTVLVLG-AGGVGLLAAQLAKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1673 KGCNVWVTSGDEGKIKKAVALGAKGGVSYKGAAWDKELLAMlpeERKWIDAIIDGAGG-DIMKRSVRLVKQGGVVVSYG- 1750
Cdd:cd05188   157 AGARVIVTDRSDEKLELAKELGADHVIDYKEEDLEEELRLT---GGGGADVVIDAVGGpETLAQALRLLRPGGRIVVVGg 233

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 682443620 1751 MTLGPKIDFPMSAVLKNIDLKGSTMGSRVEFREMVRFV 1788
Cdd:cd05188   234 TSGGPPLDDLRRLLFKELTIIGSTGGTREDFEEALDLL 271
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 1488-1830 9.98e-62

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: 214.63  E-value: 9.98e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1488 ALSITKAeGKPGVvyhpLKLANVEKRTPAQGEIQVSILTAALNHRDLFIRQSLYP-AISFTTPLLADGCGVVT---SGSS 1563
Cdd:COG0604     3 AIVITEF-GGPEV----LELEEVPVPEPGPGEVLVRVKAAGVNPADLLIRRGLYPlPPGLPFIPGSDAAGVVVavgEGVT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1564 KLN-GKRVILTPAHGwesqvsgpetfigilggttmnevgTAQEVVVIPETEVELAPEHLSDAQAAALPLTGLTAWRALVT 1642
Cdd:COG0604    78 GFKvGDRVAGLGRGG------------------------GYAEYVVVPADQLVPLPDGLSFEEAAALPLAGLTAWQALFD 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1643 KsGEAIEGRNILVTGIGGGVALNALQFAVAKGCNVWVTSGDEGKIKKAVALGAKGGVSYKGAAWDKELLAMLPEERkwID 1722
Cdd:COG0604   134 R-GRLKPGETVLVHGAAGGVGSAAVQLAKALGARVIATASSPEKAELLRALGADHVIDYREEDFAERVRALTGGRG--VD 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1723 AIIDGAGGDIMKRSVRLVKQGGVVVSYGMTLGPKIDFPMSAVL-KNIDLKGSTMGSRV------EFREMVRFVNEKKIVP 1795
Cdd:COG0604   211 VVLDTVGGDTLARSLRALAPGGRLVSIGAASGAPPPLDLAPLLlKGLTLTGFTLFARDpaerraALAELARLLAAGKLRP 290

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 682443620 1796 VVSRVVDgldnLEGVEELFQEMKQGKQFGKLIIRI 1830
Cdd:COG0604   291 VIDRVFP----LEEAAEAHRLLESGKHRGKVVLTV 321
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
 1505-1835 9.33e-28

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 116.28  E-value: 9.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1505 LKLANVEKRTPAQGEIQVSILTAALNHRDLFIRQSLYPAISFTTPLLA-DGCGVVTSGSSKL----NGKRVIltpahgwe 1579
Cdd:PTZ00354   16 LKIGESPKPAPKRNDVLIKVSAAGVNRADTLQRQGKYPPPPGSSEILGlEVAGYVEDVGSDVkrfkEGDRVM-------- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1580 sqvsgpetfiGILGGttmnevGTAQEVVVIPETEVELAPEHLSDAQAAALPLTGLTAWRALvTKSGEAIEGRNILVTGIG 1659
Cdd:PTZ00354   88 ----------ALLPG------GGYAEYAVAHKGHVMHIPQGYTFEEAAAIPEAFLTAWQLL-KKHGDVKKGQSVLIHAGA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1660 GGVALNALQFAVAKGCNVWVTSGDEGKIKKAVALGAKGGVSYK-GAAWDKELLAMLPEERkwIDAIIDGAGGDIMKRSVR 1738
Cdd:PTZ00354  151 SGVGTAAAQLAEKYGAATIITTSSEEKVDFCKKLAAIILIRYPdEEGFAPKVKKLTGEKG--VNLVLDCVGGSYLSETAE 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1739 LVKQGGVVVSYGMTLGPKIDFP--MSAVLKNIDLKGSTMGSR-VEF---------REMVRFVNEKKIVPVVSRVVdgldN 1806
Cdd:PTZ00354  229 VLAVDGKWIVYGFMGGAKVEKFnlLPLLRKRASIIFSTLRSRsDEYkadlvasfeREVLPYMEEGEIKPIVDRTY----P 304

                         330       340
                  ....*....|....*....|....*....
gi 682443620 1807 LEGVEELFQEMKQGKQFGKLIIRIKKDTG 1835
Cdd:PTZ00354  305 LEEVAEAHTFLEQNKNIGKVVLTVNEPLS 333
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
1661-1790 1.82e-21

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 91.90  E-value: 1.82e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620  1661 GVALNALQFAVAKGCNVWVTSGDEGKIKKAVALGAKGGVSYKGAAWDKELLAMLPEERkwIDAIIDGAG-GDIMKRSVRL 1739
Cdd:pfam00107    1 GVGLAAIQLAKAAGAKVIAVDGSEEKLELAKELGADHVINPKETDLVEEIKELTGGKG--VDVVFDCVGsPATLEQALKL 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 682443620  1740 VKQGGVVVSYGMTLGPKIDFPMSAVLKNIDLKGSTMGSRVEFREMVRFVNE 1790
Cdd:pfam00107   79 LRPGGRVVVVGLPGGPLPLPLAPLLLKELTILGSFLGSPEEFPEALDLLAS 129
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 1527-1828 2.35e-19

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 90.53  E-value: 2.35e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620   1527 AALNHRDLFIRQSLYPAisfTTPLLADGCGVVT---SGSSKLN-GKRVIltpahgwesqvsgpetfiGILGGTTmnevGT 1602
Cdd:smart00829    6 AGLNFRDVLIALGLYPG---EAVLGGECAGVVTrvgPGVTGLAvGDRVM------------------GLAPGAF----AT 60

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620   1603 aqeVVVIPETEVELAPEHLSDAQAAALPLTGLTAWRALVT----KSGEaiegrNILVTGIGGGVALNALQFAVAKGCNVW 1678
Cdd:smart00829   61 ---RVVTDARLVVPIPDGWSFEEAATVPVVFLTAYYALVDlarlRPGE-----SVLIHAAAGGVGQAAIQLARHLGAEVF 132

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620   1679 VTSGDEGKIKKAVALGakggvsykgaawdkellamLPEER----------KWIDAIIDGAG---------GDIMKRSVRL 1739
Cdd:smart00829  133 ATAGSPEKRDFLRALG-------------------IPDDHifssrdlsfaDEILRATGGRGvdvvlnslsGEFLDASLRC 193

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620   1740 VKQGGVVVSYGmtlgpKIDF------PMSAVLKN-----IDL----KGSTMGSRVeFREMVRFVNEKKIVPVVSRVVDgl 1804
Cdd:smart00829  194 LAPGGRFVEIG-----KRDIrdnsqlAMAPFRPNvsyhaVDLdaleEGPDRIREL-LAEVLELFAEGVLRPLPVTVFP-- 265

                           330       340
                    ....*....|....*....|....
gi 682443620   1805 dnLEGVEELFQEMKQGKQFGKLII 1828
Cdd:smart00829  266 --ISDAEDAFRYMQQGKHIGKVVL 287
GYF pfam02213
GYF domain; The GYF domain is named because of the presence of Gly-Tyr-Phe residues. The GYF ...
 730-774 3.77e-19

GYF domain; The GYF domain is named because of the presence of Gly-Tyr-Phe residues. The GYF domain is a proline-binding domain in CD2-binding protein Swiss:O95400.


Pssm-ID: 460496  Cd Length: 45  Bit Score: 82.24  E-value: 3.77e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 682443620   730 WVYLDPQGQTQGPWSGLEMHDWYKASFFTPDLSVKKLEDVEFEPL 774
Cdd:pfam02213    1 WEYKDPQGEVQGPFSSAEMQEWYKAGYFPDDLPVRRVGDTEFYPL 45
GYF smart00444
Contains conserved Gly-Tyr-Phe residues; Proline-binding domain in CD2-binding protein. ...
 728-783 6.55e-14

Contains conserved Gly-Tyr-Phe residues; Proline-binding domain in CD2-binding protein. Contains conserved Gly-Tyr-Phe residues.


Pssm-ID: 214666  Cd Length: 56  Bit Score: 67.74  E-value: 6.55e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 682443620    728 MRWVYLDPQGQTQGPWSGLEMHDWYKASFFTPDLSVKKLEDVEFEPLGQLIRRIGN 783
Cdd:smart00444    1 VLWLYKDPDGEIQGPFTASQMSQWYQAGYFPDSLQIKRLNEPPYETLGDLDRLLGL 56
GYF cd00072
GYF domain: contains conserved Gly-Tyr-Phe residues; Proline-binding domain in CD2-binding and ...
 730-782 2.51e-12

GYF domain: contains conserved Gly-Tyr-Phe residues; Proline-binding domain in CD2-binding and other proteins. Involved in signaling lymphocyte activity. Also present in other unrelated proteins (mainly unknown) derived from diverse eukaryotic species.


Pssm-ID: 238027  Cd Length: 57  Bit Score: 63.09  E-value: 2.51e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 682443620  730 WVYLDPQGQTQGPWSGLEMHDWYKASFFTPDLSVKKL-EDVEFEPLGQLIRRIG 782
Cdd:cd00072     4 WFYKDPQGEIQGPFSASQMLQWYQAGYFPDGLQVRRLdNGGEFYTLGDILFDLG 57
adh_fam_1 TIGR02817
zinc-binding alcohol dehydrogenase family protein; Members of this model form a distinct ...
 1497-1673 4.50e-08

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


Pssm-ID: 274313 [Multi-domain]  Cd Length: 336  Bit Score: 57.06  E-value: 4.50e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620  1497 KPGVVYHPLKLANVE--KRTPAQGEIQVSILTAALNHRDLFIRQSLYPAISFTTPLLADGCGVVTSGSSKLNGKRViltp 1574
Cdd:TIGR02817    7 KPLPITDPDALVDIDlpKPKPGGRDLLVEVKAISVNPVDTKVRARMAPEAGQPKILGWDAAGVVVAVGDEVTLFKP---- 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620  1575 ahgwesqvsGPETFIGilggTTMNEVGTAQEVVVIPETEVELAPEHLSDAQAAALPLTGLTAWRALVTK----SGEAIEG 1650
Cdd:TIGR02817   83 ---------GDEVWYA----GDIDRPGSNAEFHLVDERIVGHKPKSLSFAEAAALPLTSITAWELLFDRlginDPVAGDK 149

                          170       180
                   ....*....|....*....|...
gi 682443620  1651 RNILVTGIGGGVALNALQFAVAK 1673
Cdd:TIGR02817  150 RALLIIGGAGGVGSILIQLARQL 172
PHA03247 PHA03247
large tegument protein UL36; Provisional
 909-1236 6.57e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.40  E-value: 6.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620  909 PIMPQQQIPTSgssffdastRPAPTtgsnlPPDFFREDEVARLSLQDRQQTFGAPTGATQAPRSQLPAifsqqsqaqAAA 988
Cdd:PHA03247 2561 PAAPDRSVPPP---------RPAPR-----PSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPP---------SPL 2617

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620  989 SQHQAHSENDPQGFRARLQEFEQLRAQHDMEQAEHAPAPATTEPIRPPQNRQQSRTETVTTETEVLVERKDQEEILSLTE 1068
Cdd:PHA03247 2618 PPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTS 2697

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1069 QIQKAASAKqTPQPESPWAKVSSGLPMPFPPPPQSTTPLPAPAAQRGRSNLPETlhAGTRSRSETPDTSAAPPSIAPwak 1148
Cdd:PHA03247 2698 LADPPPPPP-TPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPAT--PGGPARPARPPTTAGPPAPAP--- 2771

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1149 ePVDAPKGPSLKEIQEAEAKKAAKLEESAAAARRAlleqelrAQPAAVAHGLPTTSTWASSASPVGPAVTATSTWSKATT 1228
Cdd:PHA03247 2772 -PAAPAAGPPRRLTRPAVASLSESRESLPSPWDPA-------DPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP 2843


                  ....*...
gi 682443620 1229 TKVQNPAP 1236
Cdd:PHA03247 2844 GPPPPSLP 2851
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 1074-1371 3.73e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 45.68  E-value: 3.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620  1074 ASAKQTPQPESPWAKVSSGLPMPFPPPPQSTTPLPAPAAQRGRSNLPETLHAGTRSRSETPDTSAAPPSI---APWAKEP 1150
Cdd:pfam05109  526 AVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSAVTTPTPNATSPTVgetSPQANTT 605

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620  1151 VDAPKGPSLKEIQEAEAKKAAKLEESAAAARRALLEQELRAQPAAVAHGL-PTTSTWASSASP---------------VG 1214
Cdd:pfam05109  606 NHTLGGTSSTPVVTSPPKNATSAVTTGQHNITSSSTSSMSLRPSSISETLsPSTSDNSTSHMPlltsahptggenitqVT 685

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620  1215 PAVTAT---STWSKA----TTTKVQNPAPAATASKKTLADIQR----EEELRKQKLAAAAVAAAPALPSGGKRYAELASK 1283
Cdd:pfam05109  686 PASTSThhvSTSSPAprpgTTSQASGPGNSSTSTKPGEVNVTKgtppKNATSPQAPSGQKTAVPTVTSTGGKANSTTGGK 765

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620  1284 PTAGQPAMNSAWSTVGAGGKVKMPGGPIVAapSPVMRPASSTAGPTLAKVARPAVIENRAnTSSAALSSQGGVSTAQQEF 1363
Cdd:pfam05109  766 HTTGHGARTSTEPTTDYGGDSTTPRTRYNA--TTYLPPSTSSKLRPRWTFTSPPVTTAQA-TVPVPPTSQPRFSNLSMLV 842


                   ....*...
gi 682443620  1364 TKWANAAL 1371
Cdd:pfam05109  843 LQWASLAV 850
 
Name Accession Description Interval E-value
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1519-1788 1.51e-62

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: 214.88  E-value: 1.51e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1519 EIQVSILTAALNHRDLFIRQSLYPA-ISFTTPLLADGCGVVT---SGSSKLN-GKRVILTPAHGWESQVSGPET-FIGIL 1592
Cdd:cd05188     1 EVLVRVEAAGLCGTDLHIRRGGYPPpPKLPLILGHEGAGVVVevgPGVTGVKvGDRVVVLPNLGCGTCELCRELcPGGGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1593 GGTTMNevGTAQEVVVIPETEVELAPEHLSDAQAAALPLTGLTAWRALVTkSGEAIEGRNILVTGiGGGVALNALQFAVA 1672
Cdd:cd05188    81 LGEGLD--GGFAEYVVVPADNLVPLPDGLSLEEAALLPEPLATAYHALRR-AGVLKPGDTVLVLG-AGGVGLLAAQLAKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1673 KGCNVWVTSGDEGKIKKAVALGAKGGVSYKGAAWDKELLAMlpeERKWIDAIIDGAGG-DIMKRSVRLVKQGGVVVSYG- 1750
Cdd:cd05188   157 AGARVIVTDRSDEKLELAKELGADHVIDYKEEDLEEELRLT---GGGGADVVIDAVGGpETLAQALRLLRPGGRIVVVGg 233

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 682443620 1751 MTLGPKIDFPMSAVLKNIDLKGSTMGSRVEFREMVRFV 1788
Cdd:cd05188   234 TSGGPPLDDLRRLLFKELTIIGSTGGTREDFEEALDLL 271
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 1488-1830 9.98e-62

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: 214.63  E-value: 9.98e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1488 ALSITKAeGKPGVvyhpLKLANVEKRTPAQGEIQVSILTAALNHRDLFIRQSLYP-AISFTTPLLADGCGVVT---SGSS 1563
Cdd:COG0604     3 AIVITEF-GGPEV----LELEEVPVPEPGPGEVLVRVKAAGVNPADLLIRRGLYPlPPGLPFIPGSDAAGVVVavgEGVT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1564 KLN-GKRVILTPAHGwesqvsgpetfigilggttmnevgTAQEVVVIPETEVELAPEHLSDAQAAALPLTGLTAWRALVT 1642
Cdd:COG0604    78 GFKvGDRVAGLGRGG------------------------GYAEYVVVPADQLVPLPDGLSFEEAAALPLAGLTAWQALFD 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1643 KsGEAIEGRNILVTGIGGGVALNALQFAVAKGCNVWVTSGDEGKIKKAVALGAKGGVSYKGAAWDKELLAMLPEERkwID 1722
Cdd:COG0604   134 R-GRLKPGETVLVHGAAGGVGSAAVQLAKALGARVIATASSPEKAELLRALGADHVIDYREEDFAERVRALTGGRG--VD 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1723 AIIDGAGGDIMKRSVRLVKQGGVVVSYGMTLGPKIDFPMSAVL-KNIDLKGSTMGSRV------EFREMVRFVNEKKIVP 1795
Cdd:COG0604   211 VVLDTVGGDTLARSLRALAPGGRLVSIGAASGAPPPLDLAPLLlKGLTLTGFTLFARDpaerraALAELARLLAAGKLRP 290

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 682443620 1796 VVSRVVDgldnLEGVEELFQEMKQGKQFGKLIIRI 1830
Cdd:COG0604   291 VIDRVFP----LEEAAEAHRLLESGKHRGKVVLTV 321
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1502-1830 6.39e-60

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: 210.08  E-value: 6.39e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1502 YHPLKLANVEKRTPAQGEIQVSILTAALNHRDLFIRQSLYPAiSFTTPL--LADGCGVVT---SGSSKLN-GKRVILTPA 1575
Cdd:cd08276    12 LDNLKLVEEPVPEPGPGEVLVRVHAVSLNYRDLLILNGRYPP-PVKDPLipLSDGAGEVVavgEGVTRFKvGDRVVPTFF 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1576 HGWESQVSGPETFIGILGGTTMnevGTAQEVVVIPETEVELAPEHLSDAQAAALPLTGLTAWRALVTkSGEAIEGRNILV 1655
Cdd:cd08276    91 PNWLDGPPTAEDEASALGGPID---GVLAEYVVLPEEGLVRAPDHLSFEEAATLPCAGLTAWNALFG-LGPLKPGDTVLV 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1656 TGIgGGVALNALQFAVAKGCNVWVTSGDEGKIKKAVALGAKGGVSYKG-AAWDKELLAMLPeeRKWIDAIIDGAGGDIMK 1734
Cdd:cd08276   167 QGT-GGVSLFALQFAKAAGARVIATSSSDEKLERAKALGADHVINYRTtPDWGEEVLKLTG--GRGVDHVVEVGGPGTLA 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1735 RSVRLVKQGGVVVSYGMTLGPKIDFPMSAVL-KNIDLKGSTMGSRVEFREMVRFVNEKKIVPVVSRVVDgldnLEGVEEL 1813
Cdd:cd08276   244 QSIKAVAPGGVISLIGFLSGFEAPVLLLPLLtKGATLRGIAVGSRAQFEAMNRAIEAHRIRPVIDRVFP----FEEAKEA 319

                         330
                  ....*....|....*..
gi 682443620 1814 FQEMKQGKQFGKLIIRI 1830
Cdd:cd08276   320 YRYLESGSHFGKVVIRV 336
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
 1488-1830 9.67e-57

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: 200.95  E-value: 9.67e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1488 ALSITKAEGkPGVvyhpLKLANVEKRTPAQGEIQVSILTAALNHRDLFIRQSLYPA-ISFTTPLLADGCGVVT---SGSS 1563
Cdd:cd08266     3 AVVIRGHGG-PEV----LEYGDLPEPEPGPDEVLVRVKAAALNHLDLWVRRGMPGIkLPLPHILGSDGAGVVEavgPGVT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1564 KLN-GKRVILTPAHG---WESQVSGPETF---IGILGgttMNEVGTAQEVVVIPETEVELAPEHLSDAQAAALPLTGLTA 1636
Cdd:cd08266    78 NVKpGQRVVIYPGIScgrCEYCLAGRENLcaqYGILG---EHVDGGYAEYVAVPARNLLPIPDNLSFEEAAAAPLTFLTA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1637 WRALVTKsGEAIEGRNILVTGIGGGVALNALQFAVAKGCNVWVTSGDEGKIKKAVALGAKGGVSYKGAAWDKELLAMLpe 1716
Cdd:cd08266   155 WHMLVTR-ARLRPGETVLVHGAGSGVGSAAIQIAKLFGATVIATAGSEDKLERAKELGADYVIDYRKEDFVREVRELT-- 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1717 ERKWIDAIIDGAGGDIMKRSVRLVKQGGVVVSYGMTLGPKIDFPMSAVL-KNIDLKGSTMGSRVEFREMVRFVNEKKIVP 1795
Cdd:cd08266   232 GKRGVDVVVEHVGAATWEKSLKSLARGGRLVTCGATTGYEAPIDLRHVFwRQLSILGSTMGTKAELDEALRLVFRGKLKP 311

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 682443620 1796 VVSRVVDgldnLEGVEELFQEMKQGKQFGKLIIRI 1830
Cdd:cd08266   312 VIDSVFP----LEEAAEAHRRLESREQFGKIVLTP 342
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 1503-1828 1.14e-42

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 159.89  E-value: 1.14e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1503 HPLKLANVEKRTPAQGEIQVSILTAALNHRDLFIRQSLYPAISFttPLLA--DGCGVVT---SGSSKLN-GKRVILTPAH 1576
Cdd:COG1064    11 GPLELEEVPRPEPGPGEVLVKVEACGVCHSDLHVAEGEWPVPKL--PLVPghEIVGRVVavgPGVTGFKvGDRVGVGWVD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1577 ----------GWEsQV--SGPETFIGILGGTtmnevgtAQEVVViPETEVELAPEHLSDAQAAALPLTGLTAWRALvtKS 1644
Cdd:COG1064    89 scgtceycrsGRE-NLceNGRFTGYTTDGGY-------AEYVVV-PARFLVKLPDGLDPAEAAPLLCAGITAYRAL--RR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1645 GEAIEGRNILVTGIGGgVALNALQFAVAKGCNVWVTSGDEGKIKKAVALGAKGGVSYKGAAWDKELLAMLPeerkwIDAI 1724
Cdd:COG1064   158 AGVGPGDRVAVIGAGG-LGHLAVQIAKALGAEVIAVDRSPEKLELARELGADHVVNSSDEDPVEAVRELTG-----ADVV 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1725 ID--GAGGDiMKRSVRLVKQGGVVVSYGMTLGPkIDFPMSA-VLKNIDLKGSTMGSRVEFREMVRFVNEKKIVPVVSRVv 1801
Cdd:COG1064   232 IDtvGAPAT-VNAALALLRRGGRLVLVGLPGGP-IPLPPFDlILKERSIRGSLIGTRADLQEMLDLAAEGKIKPEVETI- 308

                         330       340
                  ....*....|....*....|....*..
gi 682443620 1802 dgldNLEGVEELFQEMKQGKQFGKLII 1828
Cdd:COG1064   309 ----PLEEANEALERLRAGKVRGRAVL 331
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
 1493-1828 9.50e-42

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: 156.83  E-value: 9.50e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1493 KAEGKPGVvyhpLKLANVEKRTPAQGEIQVSILTAALNHRDLFIRQSLYPAISFTTPLLadG---CGVVT---SGSSKLN 1566
Cdd:cd05276     7 KEPGGPEV----LELGEVPKPAPGPGEVLIRVAAAGVNRADLLQRQGLYPPPPGASDIL--GlevAGVVVavgPGVTGWK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1567 -GKRVIltpahgwesqvsgpetfiGILGGTtmnevGTAQEVVViPETEVELAPEHLSDAQAAALPLTGLTAWRALVTkSG 1645
Cdd:cd05276    81 vGDRVC------------------ALLAGG-----GYAEYVVV-PAGQLLPVPEGLSLVEAAALPEVFFTAWQNLFQ-LG 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1646 EAIEGRNILVTGIGGGVALNALQFAVAKGCNVWVTSGDEGKIKKAVALGAKGGVSYKGAAWDKELLAMLPEERkwIDAII 1725
Cdd:cd05276   136 GLKAGETVLIHGGASGVGTAAIQLAKALGARVIATAGSEEKLEACRALGADVAINYRTEDFAEEVKEATGGRG--VDVIL 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1726 DGAGGDIMKRSVRLVKQGGVVVSYGMTLGPKIDFPMSAVL-KNIDLKGSTMGSR-VEFR-EMVRFVNEK--------KIV 1794
Cdd:cd05276   214 DMVGGDYLARNLRALAPDGRLVLIGLLGGAKAELDLAPLLrKRLTLTGSTLRSRsLEEKaALAAAFREHvwplfasgRIR 293

                         330       340       350
                  ....*....|....*....|....*....|....
gi 682443620 1795 PVVSRVVDgldnLEGVEELFQEMKQGKQFGKLII 1828
Cdd:cd05276   294 PVIDKVFP----LEEAAEAHRRMESNEHIGKIVL 323
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
 1496-1828 1.04e-37

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: 144.63  E-value: 1.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1496 GKPGVvyhpLKLANVEKRTPAQGEIQVSILTAALNHRDLFIRQSLY-PAISFTTPLLA--DGCGVVT---SGSSKLN-GK 1568
Cdd:cd05289    10 GGPEV----LELADVPTPEPGPGEVLVKVHAAGVNPVDLKIREGLLkAAFPLTLPLIPghDVAGVVVavgPGVTGFKvGD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1569 RVIltpahgwesqvsgpetfigilGGTTMNEVGTAQEVVVIPETEVELAPEHLSDAQAAALPLTGLTAWRALVTKsGEAI 1648
Cdd:cd05289    86 EVF---------------------GMTPFTRGGAYAEYVVVPADELALKPANLSFEEAAALPLAGLTAWQALFEL-GGLK 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1649 EGRNILVTGIGGGVALNALQFAVAKGCNVWVT--SGDEGKIKkavALGAKGGVSYKGAAWDKEllamlpEERKWIDAIID 1726
Cdd:cd05289   144 AGQTVLIHGAAGGVGSFAVQLAKARGARVIATasAANADFLR---SLGADEVIDYTKGDFERA------AAPGGVDAVLD 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1727 GAGGDIMKRSVRLVKQGGVVVSygmtLGPKIDFPMSAVLKNIDLKGSTM-GSRVEFREMVRFVNEKKIVPVVSRVVDgld 1805
Cdd:cd05289   215 TVGGETLARSLALVKPGGRLVS----IAGPPPAEQAAKRRGVRAGFVFVePDGEQLAELAELVEAGKLRPVVDRVFP--- 287

                         330       340
                  ....*....|....*....|...
gi 682443620 1806 nLEGVEELFQEMKQGKQFGKLII 1828
Cdd:cd05289   288 -LEDAAEAHERLESGHARGKVVL 309
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
 1493-1829 2.50e-32

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: 129.54  E-value: 2.50e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1493 KAEGKPGVvyhpLKLANVEKRTPAQGEIQVSILTAALNHRDLFIRQSLY---PAISFTtpLLADGCGVVTS----GSSKL 1565
Cdd:cd08241     7 KELGGPED----LVLEEVPPEPGAPGEVRIRVEAAGVNFPDLLMIQGKYqvkPPLPFV--PGSEVAGVVEAvgegVTGFK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1566 NGKRVILTPAHGwesqvsgpetfigilggttmnevGTAQEVVViPETEVELAPEHLSDAQAAALPLTGLTAWRALVTKsG 1645
Cdd:cd08241    81 VGDRVVALTGQG-----------------------GFAEEVVV-PAAAVFPLPDGLSFEEAAALPVTYGTAYHALVRR-A 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1646 EAIEGRNILVTGIGGGVALNALQFAVAKGCNVWVTSGDEGKIKKAVALGAKGGVSYKGAAWDKELLAMLPeeRKWIDAII 1725
Cdd:cd08241   136 RLQPGETVLVLGAAGGVGLAAVQLAKALGARVIAAASSEEKLALARALGADHVIDYRDPDLRERVKALTG--GRGVDVVY 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1726 DGAGGDIMKRSVRLVKQGGVVVSYGMTLG--PKIdfPMSAVL-KNIDLKGSTMGS---------RVEFREMVRFVNEKKI 1793
Cdd:cd08241   214 DPVGGDVFEASLRSLAWGGRLLVIGFASGeiPQI--PANLLLlKNISVVGVYWGAyarrepellRANLAELFDLLAEGKI 291

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 682443620 1794 VPVVSRVVDgldnLEGVEELFQEMKQGKQFGKLIIR 1829
Cdd:cd08241   292 RPHVSAVFP----LEQAAEALRALADRKATGKVVLT 323
CAD3 cd08297
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
 1503-1830 5.58e-30

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


Pssm-ID: 176257 [Multi-domain]  Cd Length: 341  Bit Score: 123.03  E-value: 5.58e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1503 HPLKLANVEKRTPAQGEIQVSILTAALNHRDLFIRQSLYPAISFTTPLLA-DGCGVVT---SGSSKLN-GKRVILTPAHG 1577
Cdd:cd08297    12 KPYEVKDVPVPEPGPGEVLVKLEASGVCHTDLHAALGDWPVKPKLPLIGGhEGAGVVVavgPGVSGLKvGDRVGVKWLYD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1578 W----ESQVSGPETFIG--ILGGTTMNevGTAQEVVVIPETEVELAPEHLSDAQAAalPLT--GLTAWRALvtKSGEAIE 1649
Cdd:cd08297    92 AcgkcEYCRTGDETLCPnqKNSGYTVD--GTFAEYAIADARYVTPIPDGLSFEQAA--PLLcaGVTVYKAL--KKAGLKP 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1650 GRNILVTGIGGGVALNALQFAVAKGCNVWVTSGDEGKIKKAVALGAKGGVSYKGAAWDKELLamlpEERKWI--DAIIDG 1727
Cdd:cd08297   166 GDWVVISGAGGGLGHLGVQYAKAMGLRVIAIDVGDEKLELAKELGADAFVDFKKSDDVEAVK----ELTGGGgaHAVVVT 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1728 AGGDI-MKRSVRLVKQGGVVVSYGMTLGPKIDF-PMSAVLKNIDLKGSTMGSRVEFREMVRFVNEKKIVPVVSRVvdgld 1805
Cdd:cd08297   242 AVSAAaYEQALDYLRPGGTLVCVGLPPGGFIPLdPFDLVLRGITIVGSLVGTRQDLQEALEFAARGKVKPHIQVV----- 316

                         330       340
                  ....*....|....*....|....*
gi 682443620 1806 NLEGVEELFQEMKQGKQFGKLIIRI 1830
Cdd:cd08297   317 PLEDLNEVFEKMEEGKIAGRVVVDF 341
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1514-1828 1.33e-29

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


Pssm-ID: 176235 [Multi-domain]  Cd Length: 350  Bit Score: 122.02  E-value: 1.33e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1514 TPAQGEIQVSILTAALNHRDLFIRQSLY------PAISFTT------------PLL--ADGCG-VVTSG---SSKLNGKR 1569
Cdd:cd08274    25 TPAPGEVLIRVGACGVNNTDINTREGWYstevdgATDSTGAgeagwwggtlsfPRIqgADIVGrVVAVGegvDTARIGER 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1570 VILTPahgWESQVSGPETFIGILGGTTMNevGTAQEVVVIPETEVELAPEHLSDAQAAALPLTGLTAWRALVtkSGEAIE 1649
Cdd:cd08274   105 VLVDP---SIRDPPEDDPADIDYIGSERD--GGFAEYTVVPAENAYPVNSPLSDVELATFPCSYSTAENMLE--RAGVGA 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1650 GRNILVTGIGGGVALNALQFAVAKGCNVWVTSGDeGKIKKAVALGAKGgVSYKGAAwDKELLAMLPEERkwIDAIIDGAG 1729
Cdd:cd08274   178 GETVLVTGASGGVGSALVQLAKRRGAIVIAVAGA-AKEEAVRALGADT-VILRDAP-LLADAKALGGEP--VDVVADVVG 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1730 GDIMKRSVRLVKQGGVVVSYGMTLGPKIDFPMSAV-LKNIDLKGSTMGSRVEFREMVRFVNEKKIVPVVSRVVDgldnLE 1808
Cdd:cd08274   253 GPLFPDLLRLLRPGGRYVTAGAIAGPVVELDLRTLyLKDLTLFGSTLGTREVFRRLVRYIEEGEIRPVVAKTFP----LS 328

                         330       340
                  ....*....|....*....|
gi 682443620 1809 GVEELFQEMKQGKQFGKLII 1828
Cdd:cd08274   329 EIREAQAEFLEKRHVGKLVL 348
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1505-1830 3.01e-29

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: 120.40  E-value: 3.01e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1505 LKLANVEKRTPAQGEIQVSILTAALNHRDLFIRQSLYPAI-SFTTPLLADGCGVVTS---GSSKLN-GKRVILTPAHgwe 1579
Cdd:cd08268    15 LRIEELPVPAPGAGEVLIRVEAIGLNRADAMFRRGAYIEPpPLPARLGYEAAGVVEAvgaGVTGFAvGDRVSVIPAA--- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1580 sqvsgpetfigilggtTMNEVGTAQEVVVIPETEVELAPEHLSDAQAAALPLTGLTAWRALVTKSGeAIEGRNILVTGIG 1659
Cdd:cd08268    92 ----------------DLGQYGTYAEYALVPAAAVVKLPDGLSFVEAAALWMQYLTAYGALVELAG-LRPGDSVLITAAS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1660 GGVALNALQFAVAKGCNVWVTSGDEGKIKKAVALGAKGGVSYKGAAWDKELLAMLpeERKWIDAIIDGAGGDIMKRSVRL 1739
Cdd:cd08268   155 SSVGLAAIQIANAAGATVIATTRTSEKRDALLALGAAHVIVTDEEDLVAEVLRIT--GGKGVDVVFDPVGGPQFAKLADA 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1740 VKQGGVVVSYGMTLGPKIDFPMSAVL-KNIDLKG----STMGSRVEFREMVRFVNE----KKIVPVVSRVVdgldNLEGV 1810
Cdd:cd08268   233 LAPGGTLVVYGALSGEPTPFPLKAALkKSLTFRGysldEITLDPEARRRAIAFILDglasGALKPVVDRVF----PFDDI 308

                         330       340
                  ....*....|....*....|
gi 682443620 1811 EELFQEMKQGKQFGKLIIRI 1830
Cdd:cd08268   309 VEAHRYLESGQQIGKIVVTP 328
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 1500-1829 4.75e-29

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: 120.11  E-value: 4.75e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1500 VVYH----PLKLANVEKRTPAQGEIQVSILTAALNHRDLFIRQSLYPAIsfTTPLLA--DGCGVV----TSGSSKLNGKR 1569
Cdd:cd08259     4 AILHkpnkPLQIEEVPDPEPGPGEVLIKVKAAGVCYRDLLFWKGFFPRG--KYPLILghEIVGTVeevgEGVERFKPGDR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1570 VILTPAHG-WESQ--VSGPETF---IGILGGTTMnevGTAQEVVVIPETEVELAPEHLSDAQAAALPLTGLTAWRALvtK 1643
Cdd:cd08259    82 VILYYYIPcGKCEycLSGEENLcrnRAEYGEEVD---GGFAEYVKVPERSLVKLPDNVSDESAALAACVVGTAVHAL--K 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1644 SGEAIEGRNILVTGIGGGVALNALQFAVAKGCNVWVTSGDEGKIKKAVALGAkgGVSYKGAAWDKELLAMLPeerkwIDA 1723
Cdd:cd08259   157 RAGVKKGDTVLVTGAGGGVGIHAIQLAKALGARVIAVTRSPEKLKILKELGA--DYVIDGSKFSEDVKKLGG-----ADV 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1724 IIDGAGGDIMKRSVRLVKQGGVVVSYGMTLGPKIDF-PMSAVLKNIDLKGSTMGSRVEFREMVRFVNEKKIVPVVSRVVD 1802
Cdd:cd08259   230 VIELVGSPTIEESLRSLNKGGRLVLIGNVTPDPAPLrPGLLILKEIRIIGSISATKADVEEALKLVKEGKIKPVIDRVVS 309

                         330       340
                  ....*....|....*....|....*..
gi 682443620 1803 gldnLEGVEELFQEMKQGKQFGKLIIR 1829
Cdd:cd08259   310 ----LEDINEALEDLKSGKVVGRIVLK 332
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
 1504-1829 1.38e-28

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: 118.89  E-value: 1.38e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1504 PLKLANVEKRTPAQGEIQVSILTAALNHRDLFIrqsLYPAISFTTPL-LADG---CGVVTSGSSKL----NGKRVIL--- 1572
Cdd:cd08254    13 LLVLEEVPVPEPGPGEVLVKVKAAGVCHSDLHI---LDGGVPTLTKLpLTLGheiAGTVVEVGAGVtnfkVGDRVAVpav 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1573 TPAHGWESQVSGPETFIGILGGTTMNEVGTAQEVVVIPETEVELAPEHLSDAQAAALPLTGLTAWRALVTKsGEAIEGRN 1652
Cdd:cd08254    90 IPCGACALCRRGRGNLCLNQGMPGLGIDGGFAEYIVVPARALVPVPDGVPFAQAAVATDAVLTPYHAVVRA-GEVKPGET 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1653 ILVTGIGGgVALNALQFAVAKGCNVWVTSGDEGKIKKAVALGAKGGVSYKGaawDKELLAMLPEERKWIDAIIDGAG-GD 1731
Cdd:cd08254   169 VLVIGLGG-LGLNAVQIAKAMGAAVIAVDIKEEKLELAKELGADEVLNSLD---DSPKDKKAAGLGGGFDVIFDFVGtQP 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1732 IMKRSVRLVKQGGVVVSYGMTlGPKIDFPMS-AVLKNIDLKGSTMGSRVEFREMVRFVNEKKIVPVVSRVvdGLDNLEGV 1810
Cdd:cd08254   245 TFEDAQKAVKPGGRIVVVGLG-RDKLTVDLSdLIARELRIIGSFGGTPEDLPEVLDLIAKGKLDPQVETR--PLDEIPEV 321

                         330
                  ....*....|....*....
gi 682443620 1811 eelFQEMKQGKQFGKLIIR 1829
Cdd:cd08254   322 ---LERLHKGKVKGRVVLV 337
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
 1505-1835 9.33e-28

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 116.28  E-value: 9.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1505 LKLANVEKRTPAQGEIQVSILTAALNHRDLFIRQSLYPAISFTTPLLA-DGCGVVTSGSSKL----NGKRVIltpahgwe 1579
Cdd:PTZ00354   16 LKIGESPKPAPKRNDVLIKVSAAGVNRADTLQRQGKYPPPPGSSEILGlEVAGYVEDVGSDVkrfkEGDRVM-------- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1580 sqvsgpetfiGILGGttmnevGTAQEVVVIPETEVELAPEHLSDAQAAALPLTGLTAWRALvTKSGEAIEGRNILVTGIG 1659
Cdd:PTZ00354   88 ----------ALLPG------GGYAEYAVAHKGHVMHIPQGYTFEEAAAIPEAFLTAWQLL-KKHGDVKKGQSVLIHAGA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1660 GGVALNALQFAVAKGCNVWVTSGDEGKIKKAVALGAKGGVSYK-GAAWDKELLAMLPEERkwIDAIIDGAGGDIMKRSVR 1738
Cdd:PTZ00354  151 SGVGTAAAQLAEKYGAATIITTSSEEKVDFCKKLAAIILIRYPdEEGFAPKVKKLTGEKG--VNLVLDCVGGSYLSETAE 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1739 LVKQGGVVVSYGMTLGPKIDFP--MSAVLKNIDLKGSTMGSR-VEF---------REMVRFVNEKKIVPVVSRVVdgldN 1806
Cdd:PTZ00354  229 VLAVDGKWIVYGFMGGAKVEKFnlLPLLRKRASIIFSTLRSRsDEYkadlvasfeREVLPYMEEGEIKPIVDRTY----P 304

                         330       340
                  ....*....|....*....|....*....
gi 682443620 1807 LEGVEELFQEMKQGKQFGKLIIRIKKDTG 1835
Cdd:PTZ00354  305 LEEVAEAHTFLEQNKNIGKVVLTVNEPLS 333
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1505-1828 1.34e-27

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


Pssm-ID: 176228 [Multi-domain]  Cd Length: 319  Bit Score: 115.39  E-value: 1.34e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1505 LKLANVEKRTPAQGEIQVSILTAALNHRDLFIRQ-SLYPAISFTTP--LLADGCGVVTSGSSKLNGKRViltpahgwesq 1581
Cdd:cd08267    14 LLEVEVPIPTPKPGEVLVKVHAASVNPVDWKLRRgPPKLLLGRPFPpiPGMDFAGEVVAVGSGVTRFKV----------- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1582 vsGPETFiGILGGTTMnevGTAQEVVVIPETEVELAPEHLSDAQAAALPLTGLTAWRALVTKsGEAIEGRNILVTGIGGG 1661
Cdd:cd08267    83 --GDEVF-GRLPPKGG---GALAEYVVAPESGLAKKPEGVSFEEAAALPVAGLTALQALRDA-GKVKPGQRVLINGASGG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1662 VALNALQFAVAKGCNVWVTSGdEGKIKKAVALGAKGGVSYKgaawDKELLAMLPEERKWiDAIIDGAGGD--IMKRSVRL 1739
Cdd:cd08267   156 VGTFAVQIAKALGAHVTGVCS-TRNAELVRSLGADEVIDYT----TEDFVALTAGGEKY-DVIFDAVGNSpfSLYRASLA 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1740 VKQGGVVVSYGMTLGPKIDFPMSAVLKNIDLK-----GSTMGSRVEFREMVRFVNEKKIVPVVSRVVDgldnLEGVEELF 1814
Cdd:cd08267   230 LKPGGRYVSVGGGPSGLLLVLLLLPLTLGGGGrrlkfFLAKPNAEDLEQLAELVEEGKLKPVIDSVYP----LEDAPEAY 305

                         330
                  ....*....|....
gi 682443620 1815 QEMKQGKQFGKLII 1828
Cdd:cd08267   306 RRLKSGRARGKVVI 319
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
 1505-1830 1.80e-27

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: 115.37  E-value: 1.80e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1505 LKLANVEKRTPAQGEIQVSILTAALNHRDLFIRQSLYPaisfTTPLL-----ADGCGVVTSGSSKLN----GKRVILtpa 1575
Cdd:cd08253    15 LRLGDLPVPTPGPGEVLVRVHASGVNPVDTYIRAGAYP----GLPPLpyvpgSDGAGVVEAVGEGVDglkvGDRVWL--- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1576 hgWESQVSGPEtfigilggttmnevGTAQEVVVIPETEVELAPEHLSDAQAAALPLTGLTAWRALVTKsGEAIEGRNILV 1655
Cdd:cd08253    88 --TNLGWGRRQ--------------GTAAEYVVVPADQLVPLPDGVSFEQGAALGIPALTAYRALFHR-AGAKAGETVLV 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1656 TGIGGGVALNALQFAVAKGCNVWVTSGDEGKIKKAVALGAKGGVSYKGAAWDKELLAMLPeeRKWIDAIIDGAGGDIMKR 1735
Cdd:cd08253   151 HGGSGAVGHAAVQLARWAGARVIATASSAEGAELVRQAGADAVFNYRAEDLADRILAATA--GQGVDVIIEVLANVNLAK 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1736 SVRLVKQGGVVVSYGmTLGPKIDFPMSAVL-KNIDLKGSTMG--SRVEFREMVRFVNE----KKIVPVVSRVVDgldnLE 1808
Cdd:cd08253   229 DLDVLAPGGRIVVYG-SGGLRGTIPINPLMaKEASIRGVLLYtaTPEERAAAAEAIAAgladGALRPVIAREYP----LE 303

                         330       340
                  ....*....|....*....|..
gi 682443620 1809 GVEELFQEMKQGKQFGKLIIRI 1830
Cdd:cd08253   304 EAAAAHEAVESGGAIGKVVLDP 325
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
 1599-1828 8.30e-26

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


Pssm-ID: 176210 [Multi-domain]  Cd Length: 350  Bit Score: 111.16  E-value: 8.30e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1599 EVGTAQEVVVIPETEVELAPEHLSDAQAAALPLTGLTAWRALVTKSG---EAIEGRNILVTGIGGGVALNALQFAVAKGC 1675
Cdd:cd08248   109 SQGTHAEYVVVPENEVSKKPKNLSHEEAASLPYAGLTAWSALVNVGGlnpKNAAGKRVLILGGSGGVGTFAIQLLKAWGA 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1676 NVWVTSGdegkiKKAV----ALGAKGGVSYKGAAWDKELlamlpEERKWIDAIIDGAGGDIMKRSVRLVKQGGVVVSYGM 1751
Cdd:cd08248   189 HVTTTCS-----TDAIplvkSLGADDVIDYNNEDFEEEL-----TERGKFDVILDTVGGDTEKWALKLLKKGGTYVTLVS 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1752 TLGPKIDFP----------MSAVLKNID--LKGST------MGSRVEFREMVRFVNEKKIVPVVSRVVdgldNLEGVEEL 1813
Cdd:cd08248   259 PLLKNTDKLglvggmlksaVDLLKKNVKslLKGSHyrwgffSPSGSALDELAKLVEDGKIKPVIDKVF----PFEEVPEA 334

                         250
                  ....*....|....*
gi 682443620 1814 FQEMKQGKQFGKLII 1828
Cdd:cd08248   335 YEKVESGHARGKTVI 349
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 1500-1830 8.76e-25

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: 107.92  E-value: 8.76e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1500 VVYH---PLKLANVEKRTPAQGEIQVSILTAALNHRDLFIRQSLYPAISFTTPLladG---CGVVT---SGSSKLN-GKR 1569
Cdd:COG1063     4 LVLHgpgDLRLEEVPDPEPGPGEVLVRVTAVGICGSDLHIYRGGYPFVRPPLVL---GhefVGEVVevgEGVTGLKvGDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1570 VILTPA----------HGWESQvSGPETFIGILGGTtmnevGTAQEVVVIPETEVELAPEHLSDAQAAAL-PLTglTAWR 1638
Cdd:COG1063    81 VVVEPNipcgecrycrRGRYNL-CENLQFLGIAGRD-----GGFAEYVRVPAANLVKVPDGLSDEAAALVePLA--VALH 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1639 ALvtKSGEAIEGRNILVTGiGGGVALNALQFAVAKGC-NVWVTSGDEGKIKKAVALGAKGGVSYKGAAWDKELLAMLPEE 1717
Cdd:COG1063   153 AV--ERAGVKPGDTVLVIG-AGPIGLLAALAARLAGAaRVIVVDRNPERLELARELGADAVVNPREEDLVEAVRELTGGR 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1718 RkwIDAIIDGAG-GDIMKRSVRLVKQGGVVVSYGMTlGPKIDFPMSA-VLKNIDLKGSTMGSRVEFREMVRFVNEKKIVP 1795
Cdd:COG1063   230 G--ADVVIEAVGaPAALEQALDLVRPGGTVVLVGVP-GGPVPIDLNAlVRKELTLRGSRNYTREDFPEALELLASGRIDL 306

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 682443620 1796 --VVSRVVDgldnLEGVEELFQEMKQGK-QFGKLIIRI 1830
Cdd:COG1063   307 epLITHRFP----LDDAPEAFEAAADRAdGAIKVVLDP 340
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
 1515-1828 1.21e-24

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: 106.36  E-value: 1.21e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1515 PAQGEIQVSILTAALNHRDLFIRQSLYPAIS---FTTPLLADGcgVVTSGSSKLNGKRViltpahgwesqvsGPETFIGI 1591
Cdd:cd08251     5 PGPGEVRIQVRAFSLNFGDLLCVRGLYPTMPpypFTPGFEASG--VVRAVGPHVTRLAV-------------GDEVIAGT 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1592 lgGTTMnevGTAQEVVVIPETEVELAPEHLSDAQAAALPLTGLTAWRALvtKSGEAIEGRNILVTGIGGGVALNALQFAV 1671
Cdd:cd08251    70 --GESM---GGHATLVTVPEDQVVRKPASLSFEEACALPVVFLTVIDAF--ARAGLAKGEHILIQTATGGTGLMAVQLAR 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1672 AKGCNVWVTSGDEGKIKKAVALGAKGGVSYKGAAWDKELLAMlpEERKWIDAIIDGAGGDIMKRSVRLVKQGGVVVSYGM 1751
Cdd:cd08251   143 LKGAEIYATASSDDKLEYLKQLGVPHVINYVEEDFEEEIMRL--TGGRGVDVVINTLSGEAIQKGLNCLAPGGRYVEIAM 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1752 T---LGPKIDFpmsAVLKN------IDLKGSTMGS--RV--EFREMVRFVNEKKIVPVVSRVVDgldnLEGVEELFQEMK 1818
Cdd:cd08251   221 TalkSAPSVDL---SVLSNnqsfhsVDLRKLLLLDpeFIadYQAEMVSLVEEGELRPTVSRIFP----FDDIGEAYRYLS 293

                         330
                  ....*....|
gi 682443620 1819 QGKQFGKLII 1828
Cdd:cd08251   294 DRENIGKVVV 303
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
 1488-1830 2.25e-24

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: 105.99  E-value: 2.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1488 ALSITKAEGkPGVvyhpLKLANVEKRTPAQGEIQVSILTAALNHRDLFIRQSLYPAiSFTTPLLADGCGVVT---SGSSK 1564
Cdd:cd05286     2 AVRIHKTGG-PEV----LEYEDVPVPEPGPGEVLVRNTAIGVNFIDTYFRSGLYPL-PLPFVLGVEGAGVVEavgPGVTG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1565 LN-GKRViltpahGWesqvsgpetfigilggttMNEVGTAQEVVVIPETEVELAPEHLSDAQAAALPLTGLTAWrALVTK 1643
Cdd:cd05286    76 FKvGDRV------AY------------------AGPPGAYAEYRVVPASRLVKLPDGISDETAAALLLQGLTAH-YLLRE 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1644 SGEAIEGRNILVTGIGGGVALNALQFAVAKGCNVWVTSGDEGKIKKAVALGAKGGVSYKGAAWDKELLAmLPEERKwIDA 1723
Cdd:cd05286   131 TYPVKPGDTVLVHAAAGGVGLLLTQWAKALGATVIGTVSSEEKAELARAAGADHVINYRDEDFVERVRE-ITGGRG-VDV 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1724 IIDGAGGDIMKRSVRLVKQGGVVVSYGMTLGPKIDFPMSAVL-KNIDLKGSTMG----SRVEFREMVR----FVNEKKIV 1794
Cdd:cd05286   209 VYDGVGKDTFEGSLDSLRPRGTLVSFGNASGPVPPFDLLRLSkGSLFLTRPSLFhyiaTREELLARAAelfdAVASGKLK 288

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 682443620 1795 PVVSRVVDgldnLEGVEELFQEMKQGKQFGKLIIRI 1830
Cdd:cd05286   289 VEIGKRYP----LADAAQAHRDLESRKTTGKLLLIP 320
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1488-1828 1.45e-23

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


Pssm-ID: 176236 [Multi-domain]  Cd Length: 337  Bit Score: 104.20  E-value: 1.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1488 ALSITKAEGkpgvvYHPLKLANVEKRTPAQGEIQVSILTAALNHRDLFIRQSLYPAisftTPLLA-----DGCGVVTS-G 1561
Cdd:cd08275     2 AVVLTGFGG-----LDKLKVEKEALPEPSSGEVRVRVEACGLNFADLMARQGLYDS----APKPPfvpgfECAGTVEAvG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1562 SSKLN---GKRVI-LTPAHGWesqvsgpetfigilggttmnevgtaQEVVVIPETEVELAPEHLSDAQAAALPLTGLTAW 1637
Cdd:cd08275    73 EGVKDfkvGDRVMgLTRFGGY-------------------------AEVVNVPADQVFPLPDGMSFEEAAAFPVNYLTAY 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1638 RALVTkSGEAIEGRNILVTGIGGGVALNALQFavAKGCNVWVTSGD--EGKIKKAVALGAKGGVSYKGAAWDKELLAMLP 1715
Cdd:cd08275   128 YALFE-LGNLRPGQSVLVHSAAGGVGLAAGQL--CKTVPNVTVVGTasASKHEALKENGVTHVIDYRTQDYVEEVKKISP 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1716 EErkwIDAIIDGAGGDIMKRSVRLVKQGGVVVSYG---MTLG---------------PKIDfPMSAVLKNIDLKGSTMGS 1777
Cdd:cd08275   205 EG---VDIVLDALGGEDTRKSYDLLKPMGRLVVYGaanLVTGekrswfklakkwwnrPKVD-PMKLISENKSVLGFNLGW 280

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 682443620 1778 --------RVEFREMVRFVNEKKIVPVVSRVVDgldnLEGVEELFQEMKQGKQFGKLII 1828
Cdd:cd08275   281 lfeerellTEVMDKLLKLYEEGKIKPKIDSVFP----FEEVGEAMRRLQSRKNIGKVVL 335
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
 1504-1830 3.97e-23

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 102.81  E-value: 3.97e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1504 PLKLANVEKRTPAQGEIQVSILTAALNHRDLFIRQSLYPAISFTTPLLADGCGVVT---SGSSKLN-GKRVI-LTPAHGW 1578
Cdd:PRK13771   12 GYRIEEVPDPKPGKDEVVIKVNYAGLCYRDLLQLQGFYPRMKYPVILGHEVVGTVEevgENVKGFKpGDRVAsLLYAPDG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1579 ESQV--SGPETFigilggtTMNEVGTAQEV-------VVIPETEVELAPEHLSDAQAAALPLTGLTAWRALvtKSGEAIE 1649
Cdd:PRK13771   92 TCEYcrSGEEAY-------CKNRLGYGEELdgffaeyAKVKVTSLVKVPPNVSDEGAVIVPCVTGMVYRGL--RRAGVKK 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1650 GRNILVTGIGGGVALNALQFAVAKGCNV-WVTSGDEgkikKAVALGAKGGVSYKGAAWDKELlamlpeeRKW--IDAIID 1726
Cdd:PRK13771  163 GETVLVTGAGGGVGIHAIQVAKALGAKViAVTSSES----KAKIVSKYADYVIVGSKFSEEV-------KKIggADIVIE 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1727 GAGGDIMKRSVRLVKQGGVVVSYGmTLGPKIDFPMS---AVLKNIDLKGSTMGSRVEFREMVRFVNEKKIVPVVSRVVdg 1803
Cdd:PRK13771  232 TVGTPTLEESLRSLNMGGKIIQIG-NVDPSPTYSLRlgyIILKDIEIIGHISATKRDVEEALKLVAEGKIKPVIGAEV-- 308

                         330       340
                  ....*....|....*....|....*..
gi 682443620 1804 ldNLEGVEELFQEMKQGKQFGKLIIRI 1830
Cdd:PRK13771  309 --SLSEIDKALEELKDKSRIGKILVKP 333
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1504-1830 9.18e-23

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


Pssm-ID: 176233 [Multi-domain]  Cd Length: 326  Bit Score: 101.48  E-value: 9.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1504 PLKLANVEKRTPAQGEIQVSILTAALNHRDLFIRQSLY------PAIsfttpLLADGCGVVT---SGSSKLN-GKRVILT 1573
Cdd:cd08272    14 VFELREVPRPQPGPGQVLVRVHASGVNPLDTKIRRGGAaarpplPAI-----LGCDVAGVVEavgEGVTRFRvGDEVYGC 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1574 PahgwesqvsgpetfiGILGGTTmnevGTAQEVVVIPETEVELAPEHLSDAQAAALPLTGLTAWRALVTKSgeAIE-GRN 1652
Cdd:cd08272    89 A---------------GGLGGLQ----GSLAEYAVVDARLLALKPANLSMREAAALPLVGITAWEGLVDRA--AVQaGQT 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1653 ILVTGIGGGVALNALQFAVAKGCNVWVTSGDEgKIKKAVALGAKgGVSYKGAAWDKELLAMLpeERKWIDAIIDGAGGDI 1732
Cdd:cd08272   148 VLIHGGAGGVGHVAVQLAKAAGARVYATASSE-KAAFARSLGAD-PIIYYRETVVEYVAEHT--GGRGFDVVFDTVGGET 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1733 MKRSVRLVKQGGVVVSygMTLGPKIDF-PMSAvlKNIDLKGSTM------GSRVE-----FREMVRFVNEKKIVPVVSRV 1800
Cdd:cd08272   224 LDASFEAVALYGRVVS--ILGGATHDLaPLSF--RNATYSGVFTllplltGEGRAhhgeiLREAARLVERGQLRPLLDPR 299

                         330       340       350
                  ....*....|....*....|....*....|
gi 682443620 1801 VDGLDNlegVEELFQEMKQGKQFGKLIIRI 1830
Cdd:cd08272   300 TFPLEE---AAAAHARLESGSARGKIVIDV 326
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
 1518-1828 1.22e-22

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: 100.34  E-value: 1.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1518 GEIQVSILTAALNHRDLFIRQSLYPaiSFTTPLLADGCGVVT---SGSSKL-NGKRVIltpahgwesqvsgpetfiGILG 1593
Cdd:cd05195     1 DEVEVEVKAAGLNFRDVLVALGLLP--GDETPLGLECSGIVTrvgSGVTGLkVGDRVM------------------GLAP 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1594 GTtmneVGTaqeVVVIPETEVELAPEHLSDAQAAALPLTGLTAWRALVT----KSGEaiegrNILVTGIGGGVALNALQF 1669
Cdd:cd05195    61 GA----FAT---HVRVDARLVVKIPDSLSFEEAATLPVAYLTAYYALVDlarlQKGE-----SVLIHAAAGGVGQAAIQL 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1670 AVAKGCNVWVTSGDEGKIKKAVALGAKG-GVSY-KGAAWDKELLAMLPEERkwIDAIIDGAGGDIMKRSVRLVKQGGVVV 1747
Cdd:cd05195   129 AQHLGAEVFATVGSEEKREFLRELGGPVdHIFSsRDLSFADGILRATGGRG--VDVVLNSLSGELLRASWRCLAPFGRFV 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1748 ---SYGMTLGPKIDfpMSAVLKN-----IDL------KGSTMGSRveFREMVRFVNEKKIVPVVSRVVDGLDnlegVEEL 1813
Cdd:cd05195   207 eigKRDILSNSKLG--MRPFLRNvsfssVDLdqlareRPELLREL--LREVLELLEAGVLKPLPPTVVPSAS----EIDA 278

                         330
                  ....*....|....*
gi 682443620 1814 FQEMKQGKQFGKLII 1828
Cdd:cd05195   279 FRLMQSGKHIGKVVL 293
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
 1504-1828 1.30e-22

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: 101.54  E-value: 1.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1504 PLKLANVEKRTPAQGEIQVSILTAALNHRDLFIRQSLYPAISFTTPLLADG------------CGVVTS-GSSKLN---G 1567
Cdd:cd08240    12 PLEEVEIDTPKPPGTEVLVKVTACGVCHSDLHIWDGGYDLGGGKTMSLDDRgvklplvlgheiVGEVVAvGPDAADvkvG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1568 KRVILTP----------AHGWESQVSGPETFIGILGGttmnevGTAqEVVVIPETEVELAPEHLSDAQAAALPLTGLTAW 1637
Cdd:cd08240    92 DKVLVYPwigcgecpvcLAGDENLCAKGRALGIFQDG------GYA-EYVIVPHSRYLVDPGGLDPALAATLACSGLTAY 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1638 RAlVTKSGEAIEGRNILVTGiGGGVALNALQFAVAKG-CNVWVTSGDEGKIKKAVALGAKGGVSYKGAAWDKELLAMLPe 1716
Cdd:cd08240   165 SA-VKKLMPLVADEPVVIIG-AGGLGLMALALLKALGpANIIVVDIDEAKLEAAKAAGADVVVNGSDPDAAKRIIKAAG- 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1717 erKWIDAIIDGAG-GDIMKRSVRLVKQGGVVVSYGMtLGPKIDFPMS-AVLKNIDLKGSTMGSRVEFREMVRFVNEKKIV 1794
Cdd:cd08240   242 --GGVDAVIDFVNnSATASLAFDILAKGGKLVLVGL-FGGEATLPLPlLPLRALTIQGSYVGSLEELRELVALAKAGKLK 318

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 682443620 1795 PV-VSRVvdgldNLEGVEELFQEMKQGKQFGKLII 1828
Cdd:cd08240   319 PIpLTER-----PLSDVNDALDDLKAGKVVGRAVL 348
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1505-1829 3.21e-22

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


Pssm-ID: 176234 [Multi-domain]  Cd Length: 331  Bit Score: 100.03  E-value: 3.21e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1505 LKLANVEKRTPAQGEIQVSILTAALNHRDLFIRQSLYPAIS---FTTPLlaDGCGVV---TSGSSKL-NGKRVI-LTPAH 1576
Cdd:cd08273    15 LKVVEADLPEPAAGEVVVKVEASGVSFADVQMRRGLYPDQPplpFTPGY--DLVGRVdalGSGVTGFeVGDRVAaLTRVG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1577 GWesqvsgpetfigilggttmnevgtaQEVVVIPETEVELAPEHLSDAQAAALPLTGLTAWRAL--VTKSgeaIEGRNIL 1654
Cdd:cd08273    93 GN-------------------------AEYINLDAKYLVPVPEGVDAAEAVCLVLNYVTAYQMLhrAAKV---LTGQRVL 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1655 VTGIGGGVALNALQFAVAKGCNVWVT--SGDEGKIKkavALGAKgGVSYKGAAWdkELLAMLPEERkwiDAIIDGAGGDI 1732
Cdd:cd08273   145 IHGASGGVGQALLELALLAGAEVYGTasERNHAALR---ELGAT-PIDYRTKDW--LPAMLTPGGV---DVVFDGVGGES 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1733 MKRSVRLVKQGGVVVSYGMT-------LGPKIDFPMSAVLKNIDLKGSTMGSRV----------------EFREMVRFVN 1789
Cdd:cd08273   216 YEESYAALAPGGTLVCYGGNssllqgrRSLAALGSLLARLAKLKLLPTGRRATFyyvwrdraedpklfrqDLTELLDLLA 295

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 682443620 1790 EKKIVPVVSRVVDgldnLEGVEELFQEMKQGKQFGKLIIR 1829
Cdd:cd08273   296 KGKIRPKIAKRLP----LSEVAEAHRLLESGKVVGKIVLL 331
quinone_oxidoreductase_like_1 cd08243
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 1500-1828 1.67e-21

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


Pssm-ID: 176205 [Multi-domain]  Cd Length: 320  Bit Score: 97.68  E-value: 1.67e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1500 VVYHP-----LKLANVEKRTPAQGEIQVSILTAALNHRDLFIRQSLYPAISFTTPLLADGCGVV--TSGSSKLNGKRVIl 1572
Cdd:cd08243     5 VIEQPggpevLKLREIPIPEPKPGWVLIRVKAFGLNRSEIFTRQGHSPSVKFPRVLGIEAVGEVeeAPGGTFTPGQRVA- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1573 tpahgwesqvsgpetfigilggTTMNEVGTA-----QEVVVIPETEVELAPEHLSDAQAAALPLTGLTAWRALvTKSGEA 1647
Cdd:cd08243    84 ----------------------TAMGGMGRTfdgsyAEYTLVPNEQVYAIDSDLSWAELAALPETYYTAWGSL-FRSLGL 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1648 IEGRNILVTGIGGGVALNALQFAVAKGCNVWVTSGDEGKIKKAVALGAKGGVSYKGaawdkELLAMLPEERKWIDAIIDG 1727
Cdd:cd08243   141 QPGDTLLIRGGTSSVGLAALKLAKALGATVTATTRSPERAALLKELGADEVVIDDG-----AIAEQLRAAPGGFDKVLEL 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1728 AGGDIMKRSVRLVKQGGVVVSYGMTLGPKI--DF-PMSAVLK--NIDLKGSTMG--SRVEFREMVRFVNEKKIVPVVSRV 1800
Cdd:cd08243   216 VGTATLKDSLRHLRPGGIVCMTGLLGGQWTleDFnPMDDIPSgvNLTLTGSSSGdvPQTPLQELFDFVAAGHLDIPPSKV 295

                         330       340
                  ....*....|....*....|....*...
gi 682443620 1801 VdgldNLEGVEELFQEMKQGKQFGKLII 1828
Cdd:cd08243   296 F----TFDEIVEAHAYMESNRAFGKVVV 319
MDR4 cd08270
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1505-1763 1.72e-21

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


Pssm-ID: 176231 [Multi-domain]  Cd Length: 305  Bit Score: 97.06  E-value: 1.72e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1505 LKLANVEKRTPAQGEIQVSILTAALNHRDlfirqslypaISFTTPLLA------DGCGVV----TSGSSKLNGKRVI-LT 1573
Cdd:cd08270    14 LRLGEVPDPQPAPHEALVRVAAISLNRGE----------LKFAAERPDgavpgwDAAGVVeraaADGSGPAVGARVVgLG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1574 PAHGWESQVSGPETFIGILggttmnevgtaqevvvipetevelaPEHLSDAQAAALPLTGLTAWRALvtKSGEAIEGRNI 1653
Cdd:cd08270    84 AMGAWAELVAVPTGWLAVL-------------------------PDGVSFAQAATLPVAGVTALRAL--RRGGPLLGRRV 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1654 LVTGIGGGVALNALQFAVAKGCNVWVTSGDEGKIKKAVALGAKggvsykgaawdKELLAMLPEERKWIDAIIDGAGGDIM 1733
Cdd:cd08270   137 LVTGASGGVGRFAVQLAALAGAHVVAVVGSPARAEGLRELGAA-----------EVVVGGSELSGAPVDLVVDSVGGPQL 205

                         250       260       270
                  ....*....|....*....|....*....|
gi 682443620 1734 KRSVRLVKQGGVVVSYGMTLGPKIDFPMSA 1763
Cdd:cd08270   206 ARALELLAPGGTVVSVGSSSGEPAVFNPAA 235
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
1661-1790 1.82e-21

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 91.90  E-value: 1.82e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620  1661 GVALNALQFAVAKGCNVWVTSGDEGKIKKAVALGAKGGVSYKGAAWDKELLAMLPEERkwIDAIIDGAG-GDIMKRSVRL 1739
Cdd:pfam00107    1 GVGLAAIQLAKAAGAKVIAVDGSEEKLELAKELGADHVINPKETDLVEEIKELTGGKG--VDVVFDCVGsPATLEQALKL 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 682443620  1740 VKQGGVVVSYGMTLGPKIDFPMSAVLKNIDLKGSTMGSRVEFREMVRFVNE 1790
Cdd:pfam00107   79 LRPGGRVVVVGLPGGPLPLPLAPLLLKELTILGSFLGSPEEFPEALDLLAS 129
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1505-1830 3.25e-21

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: 96.96  E-value: 3.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1505 LKLANVEKRTPAQGEIQVSILTAALNHRDLFIRQSLYPAISFTTPLLADGCGVVTSGSSKLNGKRVILTpahgwesqvsg 1584
Cdd:cd08271    15 LTLEEIEIPGPGAGEVLVKVHAAGLNPVDWKVIAWGPPAWSYPHVPGVDGAGVVVAVGAKVTGWKVGDR----------- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1585 petfigILGGTTMNEVGTAQEVVVIPETEVELAPEHLSDAQAAALPLTGLTAWRALVTKSgeAIE-GRNILVTGIGGGVA 1663
Cdd:cd08271    84 ------VAYHASLARGGSFAEYTVVDARAVLPLPDSLSFEEAAALPCAGLTAYQALFKKL--RIEaGRTILITGGAGGVG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1664 LNALQFAVAKGCNVWVTSGDEgKIKKAVALGAKGGVSYKGAAWDKELLAMLPEERkwIDAIIDGAGGDIMKRSVRLVKQG 1743
Cdd:cd08271   156 SFAVQLAKRAGLRVITTCSKR-NFEYVKSLGADHVIDYNDEDVCERIKEITGGRG--VDAVLDTVGGETAAALAPTLAFN 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1744 G--VVVSYGMTLGPKIDFPMSAVLKNIDLKGS-TMGSRVEFR-------EMVRFVNEKKIVPVVSRVVDGLDNLEGVEEL 1813
Cdd:cd08271   233 GhlVCIQGRPDASPDPPFTRALSVHEVALGAAhDHGDPAAWQdlryageELLELLAAGKLEPLVIEVLPFEQLPEALRAL 312

                         330
                  ....*....|....*..
gi 682443620 1814 fqemKQGKQFGKLIIRI 1830
Cdd:cd08271   313 ----KDRHTRGKIVVTI 325
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
 1505-1821 8.14e-21

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: 95.42  E-value: 8.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1505 LKLANVEKRTPAQGEIQVSILTAALNHRDLFIRQSLYPaisFTTPLLA----DGCGVVT---SGSSKLN-GKRVIltPAH 1576
Cdd:cd05282    14 LELVSLPIPPPGPGEVLVRMLAAPINPSDLITISGAYG---SRPPLPAvpgnEGVGVVVevgSGVSGLLvGQRVL--PLG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1577 GwesqvsgpetfigilggttmneVGTAQEVVVIPETEVELAPEHLSDAQAAALPLTGLTAWrALVTKSGEAIEGRNILVT 1656
Cdd:cd05282    89 G----------------------EGTWQEYVVAPADDLIPVPDSISDEQAAMLYINPLTAW-LMLTEYLKLPPGDWVIQN 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1657 GIGGGVALNALQFAVAKGCNVWVTSGDEGKIKKAVALGAKGGVSYKGAAWDKELLAMLPEERkwIDAIIDGAGGDIMKRS 1736
Cdd:cd05282   146 AANSAVGRMLIQLAKLLGFKTINVVRRDEQVEELKALGADEVIDSSPEDLAQRVKEATGGAG--ARLALDAVGGESATRL 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1737 VRLVKQGGVVVSYGMTLGPKIDFPMSA-VLKNIDLKG---------STMGSRVE-FREMVRFVNEKKIVPVVSRVVDgLD 1805
Cdd:cd05282   224 ARSLRPGGTLVNYGLLSGEPVPFPRSVfIFKDITVRGfwlrqwlhsATKEAKQEtFAEVIKLVEAGVLTTPVGAKFP-LE 302

                         330
                  ....*....|....*..
gi 682443620 1806 NL-EGVEELFQEMKQGK 1821
Cdd:cd05282   303 DFeEAVAAAEQPGRGGK 319
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 1618-1821 5.27e-20

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: 93.33  E-value: 5.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1618 PEHLSDAQAAALPLTGLTAWRALV---TKSGEAIeGrnilVTGIGGgvaLN--ALQFAVAKGCNVWVTSGDEGKIKKAVA 1692
Cdd:cd05283   140 PEGLDSAAAAPLLCAGITVYSPLKrngVGPGKRV-G----VVGIGG---LGhlAVKFAKALGAEVTAFSRSPSKKEDALK 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1693 LGAKGGVSYKGAAWdkellaMLPEERKwIDAIIDGAGGDI-MKRSVRLVKQGGVVVSYGMTLGPKIDFPMSAVLKNIDLK 1771
Cdd:cd05283   212 LGADEFIATKDPEA------MKKAAGS-LDLIIDTVSASHdLDPYLSLLKPGGTLVLVGAPEEPLPVPPFPLIFGRKSVA 284

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 682443620 1772 GSTMGSRVEFREMVRFVNEKKIVPVVsRVVDgldnLEGVEELFQEMKQGK 1821
Cdd:cd05283   285 GSLIGGRKETQEMLDFAAEHGIKPWV-EVIP----MDGINEALERLEKGD 329
Zn_ADH_like2 cd08264
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 1505-1821 9.27e-20

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


Pssm-ID: 176225 [Multi-domain]  Cd Length: 325  Bit Score: 92.41  E-value: 9.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1505 LKLANVEKRTPAQGEIQVSILTAALNHRDLFIRQSL-------YPAISFTTPLLADGCGVvtSGSSKlnGKRVILTPA-- 1575
Cdd:cd08264    14 LKVEDVKDPKPGPGEVLIRVKMAGVNPVDYNVINAVkvkpmphIPGAEFAGVVEEVGDHV--KGVKK--GDRVVVYNRvf 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1576 HGWESQ-VSGPETFI---GILGGTTMnevGTAQEVVVIPETEVELAPEHLSDAQAAALPLTGLTAWRALvtKSGEAIEGR 1651
Cdd:cd08264    90 DGTCDMcLSGNEMLCrngGIIGVVSN---GGYAEYIVVPEKNLFKIPDSISDELAASLPVAALTAYHAL--KTAGLGPGE 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1652 NILVTGIGGGVALNALQFAVAKGCNVWVTSGdegkiKKAVA-LGAKGGVSYKGAAWD-KELLAMlpeerkwIDAIIDGAG 1729
Cdd:cd08264   165 TVVVFGASGNTGIFAVQLAKMMGAEVIAVSR-----KDWLKeFGADEVVDYDEVEEKvKEITKM-------ADVVINSLG 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1730 GDIMKRSVRLVKQGGVVVSYGMTLGPKIDFPMSAVL-KNIDLKGSTMGSRVEFREMVRFVNEKKIvpVVSRVVDGLDNLE 1808
Cdd:cd08264   233 SSFWDLSLSVLGRGGRLVTFGTLTGGEVKLDLSDLYsKQISIIGSTGGTRKELLELVKIAKDLKV--KVWKTFKLEEAKE 310

                         330
                  ....*....|...
gi 682443620 1809 GVEELFQEMKQGK 1821
Cdd:cd08264   311 ALKELFSKERDGR 323
CAD cd08245
Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases ...
 1504-1828 2.24e-19

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: 91.61  E-value: 2.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1504 PLKLANVEKRTPAQGEIQVSILTAALNHRDLFIRQSLYPAISFttPLLA--DGCGVVTSGSSKLNGKRV---ILTPAH-- 1576
Cdd:cd08245    11 PLEPEEVPVPEPGPGEVLIKIEACGVCHTDLHAAEGDWGGSKY--PLVPghEIVGEVVEVGAGVEGRKVgdrVGVGWLvg 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1577 ----------GWEsqVSGPETfigILGGTTMNevGTAQEVVVIPETEVELAPEHLSDAQAAALPLTGLTAWRALvtKSGE 1646
Cdd:cd08245    89 scgrceycrrGLE--NLCQKA---VNTGYTTQ--GGYAEYMVADAEYTVLLPDGLPLAQAAPLLCAGITVYSAL--RDAG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1647 AIEGRNILVTGIGGGVALnALQFAVAKGCNVWVTSGDEGKIKKAVALGAKGGVSyKGAAWDKELLAmlpeerKWIDAIID 1726
Cdd:cd08245   160 PRPGERVAVLGIGGLGHL-AVQYARAMGFETVAITRSPDKRELARKLGADEVVD-SGAELDEQAAA------GGADVILV 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1727 -GAGGDIMKRSVRLVKQGGVVVSYGMTLGPKIDFPM-SAVLKNIDLKGSTMGSRVEFREMVRFVNEKKIVPVVSRVvdgl 1804
Cdd:cd08245   232 tVVSGAAAEAALGGLRRGGRIVLVGLPESPPFSPDIfPLIMKRQSIAGSTHGGRADLQEALDFAAEGKVKPMIETF---- 307

                         330       340
                  ....*....|....*....|....
gi 682443620 1805 dNLEGVEELFQEMKQGKQFGKLII 1828
Cdd:cd08245   308 -PLDQANEAYERMEKGDVRFRFVL 330
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 1527-1828 2.35e-19

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 90.53  E-value: 2.35e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620   1527 AALNHRDLFIRQSLYPAisfTTPLLADGCGVVT---SGSSKLN-GKRVIltpahgwesqvsgpetfiGILGGTTmnevGT 1602
Cdd:smart00829    6 AGLNFRDVLIALGLYPG---EAVLGGECAGVVTrvgPGVTGLAvGDRVM------------------GLAPGAF----AT 60

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620   1603 aqeVVVIPETEVELAPEHLSDAQAAALPLTGLTAWRALVT----KSGEaiegrNILVTGIGGGVALNALQFAVAKGCNVW 1678
Cdd:smart00829   61 ---RVVTDARLVVPIPDGWSFEEAATVPVVFLTAYYALVDlarlRPGE-----SVLIHAAAGGVGQAAIQLARHLGAEVF 132

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620   1679 VTSGDEGKIKKAVALGakggvsykgaawdkellamLPEER----------KWIDAIIDGAG---------GDIMKRSVRL 1739
Cdd:smart00829  133 ATAGSPEKRDFLRALG-------------------IPDDHifssrdlsfaDEILRATGGRGvdvvlnslsGEFLDASLRC 193

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620   1740 VKQGGVVVSYGmtlgpKIDF------PMSAVLKN-----IDL----KGSTMGSRVeFREMVRFVNEKKIVPVVSRVVDgl 1804
Cdd:smart00829  194 LAPGGRFVEIG-----KRDIrdnsqlAMAPFRPNvsyhaVDLdaleEGPDRIREL-LAEVLELFAEGVLRPLPVTVFP-- 265

                           330       340
                    ....*....|....*....|....
gi 682443620   1805 dnLEGVEELFQEMKQGKQFGKLII 1828
Cdd:smart00829  266 --ISDAEDAFRYMQQGKHIGKVVL 287
GYF pfam02213
GYF domain; The GYF domain is named because of the presence of Gly-Tyr-Phe residues. The GYF ...
 730-774 3.77e-19

GYF domain; The GYF domain is named because of the presence of Gly-Tyr-Phe residues. The GYF domain is a proline-binding domain in CD2-binding protein Swiss:O95400.


Pssm-ID: 460496  Cd Length: 45  Bit Score: 82.24  E-value: 3.77e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 682443620   730 WVYLDPQGQTQGPWSGLEMHDWYKASFFTPDLSVKKLEDVEFEPL 774
Cdd:pfam02213    1 WEYKDPQGEVQGPFSSAEMQEWYKAGYFPDDLPVRRVGDTEFYPL 45
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
 1498-1830 8.75e-18

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: 86.87  E-value: 8.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1498 PGVVYHPLKLANVEKRTPAQGEIQVSILTAALN-----HRDLFIRQSlYPAIsfttpLLADGCGVVT---SGSSKLN-GK 1568
Cdd:cd08249     7 TGPGGGLLVVVDVPVPKPGPDEVLVKVKAVALNpvdwkHQDYGFIPS-YPAI-----LGCDFAGTVVevgSGVTRFKvGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1569 RViLTPAHGwesqvsgpetfigilGGTTMNEVGTAQEVVVIPETEVELAPEHLSDAQAAALPLTGLTAWRALVTKSG--- 1645
Cdd:cd08249    81 RV-AGFVHG---------------GNPNDPRNGAFQEYVVADADLTAKIPDNISFEEAATLPVGLVTAALALFQKLGlpl 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1646 ------EAIEGRNILVTGIGGGVALNALQFAVAKGCNVWVTSG--DEGKIKKavaLGAKGGVSYKGAAW-DKELLAMLPE 1716
Cdd:cd08249   145 pppkpsPASKGKPVLIWGGSSSVGTLAIQLAKLAGYKVITTASpkNFDLVKS---LGADAVFDYHDPDVvEDIRAATGGK 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1717 ERKWIDAIIDGAGG----DIMKRSvrlvkQGGVVVSygmTLGPKIDFPMSAVLKNIDLKGSTMGSRVE---------FRE 1783
Cdd:cd08249   222 LRYALDCISTPESAqlcaEALGRS-----GGGKLVS---LLPVPEETEPRKGVKVKFVLGYTVFGEIPedrefgevfWKY 293

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 682443620 1784 MVRFVNEKKIVPVVSRVVDGLdnLEGVEELFQEMKQGKQ-FGKLIIRI 1830
Cdd:cd08249   294 LPELLEEGKLKPHPVRVVEGG--LEGVQEGLDLLRKGKVsGEKLVVRL 339
crotonyl_coA_red cd08246
crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase ...
 1555-1830 1.08e-17

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: 87.47  E-value: 1.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1555 CGVVTSGSSKLNGKRVILTPahgwESQVSGPETFIGILGgttmnevgtaqEVVVIPETEVELAPEHLSDAQAAALPLTGL 1634
Cdd:cd08246   113 CSVWDGNDPERAGGDPMFDP----SQRIWGYETNYGSFA-----------QFALVQATQLMPKPKHLSWEEAAAYMLVGA 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1635 TAWRALVTKSGEAI-EGRNILVTGIGGGVALNALQFAVAKGCN-VWVTSGDEgKIKKAVALGAKG----------GV--- 1699
Cdd:cd08246   178 TAYRMLFGWNPNTVkPGDNVLIWGASGGLGSMAIQLARAAGANpVAVVSSEE-KAEYCRALGAEGvinrrdfdhwGVlpd 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1700 --SYKGAAWDKELLA------MLPEERKWIDAIIDGAGGDIMKRSVRLVKQGGVVVSYGMTLGPKIDFPMSAV---LKNI 1768
Cdd:cd08246   257 vnSEAYTAWTKEARRfgkaiwDILGGREDPDIVFEHPGRATFPTSVFVCDRGGMVVICAGTTGYNHTYDNRYLwmrQKRI 336

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 682443620 1769 dlKGSTMGSRVEFREMVRFVNEKKIVPVVSRVVDgldnLEGVEELFQEMKQGKQ-FGKLIIRI 1830
Cdd:cd08246   337 --QGSHFANDREAAEANRLVMKGRIDPCLSKVFS----LDETPDAHQLMHRNQHhVGNMAVLV 393
PGDH cd05288
Prostaglandin dehydrogenases; Prostaglandins and related eicosanoids are metabolized by the ...
 1604-1828 2.01e-16

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: 82.53  E-value: 2.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1604 QEVVVIPETEV--ELAPEHLSDAQAA--ALPLTGLTAWRALvTKSGEAIEGRNILVTGIGGGVALNALQFAVAKGCNVWV 1679
Cdd:cd05288    97 QEYAVVDGASGlrKLDPSLGLPLSAYlgVLGMTGLTAYFGL-TEIGKPKPGETVVVSAAAGAVGSVVGQIAKLLGARVVG 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1680 TSGDEGKIKKAV-ALGAKGGVSYKGAAWDKELLAMLPEErkwIDAIIDGAGGDIMKRSVRLVKQGGVVV------SYGMT 1752
Cdd:cd05288   176 IAGSDEKCRWLVeELGFDAAINYKTPDLAEALKEAAPDG---IDVYFDNVGGEILDAALTLLNKGGRIAlcgaisQYNAT 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1753 LGPKIDFPMSAVLKNIDLKG----STMGSRVEF-REMVRFVNEKKIVPVVSrVVDGLDNlegVEELFQEMKQGKQFGKLI 1827
Cdd:cd05288   253 EPPGPKNLGNIITKRLTMQGfivsDYADRFPEAlAELAKWLAEGKLKYRED-VVEGLEN---APEAFLGLFTGKNTGKLV 328


                  .
gi 682443620 1828 I 1828
Cdd:cd05288   329 V 329
PRK10754 PRK10754
NADPH:quinone reductase;
1494-1755 5.11e-16

NADPH:quinone reductase;


Pssm-ID: 182701 [Multi-domain]  Cd Length: 327  Bit Score: 81.32  E-value: 5.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1494 AEGKPGVvyhpLKLANVEKRTPAQGEIQVSILTAALNHRDLFIRQSLYPAISFTTPLLADGCGVVT---SGSSKLN-GKR 1569
Cdd:PRK10754    9 KHGGPEV----LQAVEFTPADPAENEVQVENKAIGINYIDTYIRSGLYPPPSLPSGLGTEAAGVVSkvgSGVKHIKvGDR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1570 VILTPAhgwesqvsgpetfigilggttmnEVGTAQEVVVIPETEVELAPEHLSDAQAAALPLTGLTAWRaLVTKSGEAIE 1649
Cdd:PRK10754   85 VVYAQS-----------------------ALGAYSSVHNVPADKAAILPDAISFEQAAASFLKGLTVYY-LLRKTYEIKP 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1650 GRNILVTGIGGGVALNALQFAVAKGCNVWVTSGDEGKIKKAVALGAKGGVSYKGAAWDKELLAMLPEERkwIDAIIDGAG 1729
Cdd:PRK10754  141 DEQFLFHAAAGGVGLIACQWAKALGAKLIGTVGSAQKAQRAKKAGAWQVINYREENIVERVKEITGGKK--VRVVYDSVG 218

                         250       260
                  ....*....|....*....|....*.
gi 682443620 1730 GDIMKRSVRLVKQGGVVVSYGMTLGP 1755
Cdd:PRK10754  219 KDTWEASLDCLQRRGLMVSFGNASGP 244
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 1601-1819 4.90e-14

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: 75.30  E-value: 4.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1601 GTAQEVVVIPETEVeLAPEHLSDAQAAAL-PLT-GLTA-WRALVTKsgeaieGRNILVTGiGGGVALNALQFAVAKGCNV 1677
Cdd:cd08261   115 GGFAEYIVVPADAL-LVPEGLSLDQAALVePLAiGAHAvRRAGVTA------GDTVLVVG-AGPIGLGVIQVAKARGARV 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1678 WVTSGDEGKIKKAVALGAKGGVsykgAAWDKELLAMLPE--ERKWIDAIIDGAGG-DIMKRSVRLVKQGGVVVSYGMTLG 1754
Cdd:cd08261   187 IVVDIDDERLEFARELGADDTI----NVGDEDVAARLREltDGEGADVVIDATGNpASMEEAVELVAHGGRVVLVGLSKG 262

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 682443620 1755 PkIDFPMSA-VLKNIDLKGSTMGSRVEFREMVRFVNEKKI--VPVVSRVVDgldnLEGVEELFQEMKQ 1819
Cdd:cd08261   263 P-VTFPDPEfHKKELTILGSRNATREDFPDVIDLLESGKVdpEALITHRFP----FEDVPEAFDLWEA 325
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
 1605-1828 5.13e-14

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: 75.34  E-value: 5.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1605 EVVVIPETEVELAPEHLSDAQAAAL-PLTglTAWRAlVTKSGeAIEGRNILVtgIGGG-VALNALQFAVAKGC-NVWVTS 1681
Cdd:cd08236   118 EYVSVPARNLIKIPDHVDYEEAAMIePAA--VALHA-VRLAG-ITLGDTVVV--IGAGtIGLLAIQWLKILGAkRVIAVD 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1682 GDEGKIKKAVALGAKGGV--SYKGAAWDKELLamlpeERKWIDAIIDGAGGDI-MKRSVRLVKQGGVVVSYG-----MTL 1753
Cdd:cd08236   192 IDDEKLAVARELGADDTInpKEEDVEKVRELT-----EGRGADLVIEAAGSPAtIEQALALARPGGKVVLVGipygdVTL 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1754 gPKIDFpMSAVLKNIDLKGSTMGS-----RVEFREMVRFVNEKKIV--PVVSRVVDgldnLEGVEELFQEMKQGKQ-FGK 1825
Cdd:cd08236   267 -SEEAF-EKILRKELTIQGSWNSYsapfpGDEWRTALDLLASGKIKvePLITHRLP----LEDGPAAFERLADREEfSGK 340


                  ...
gi 682443620 1826 LII 1828
Cdd:cd08236   341 VLL 343
GYF smart00444
Contains conserved Gly-Tyr-Phe residues; Proline-binding domain in CD2-binding protein. ...
 728-783 6.55e-14

Contains conserved Gly-Tyr-Phe residues; Proline-binding domain in CD2-binding protein. Contains conserved Gly-Tyr-Phe residues.


Pssm-ID: 214666  Cd Length: 56  Bit Score: 67.74  E-value: 6.55e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 682443620    728 MRWVYLDPQGQTQGPWSGLEMHDWYKASFFTPDLSVKKLEDVEFEPLGQLIRRIGN 783
Cdd:smart00444    1 VLWLYKDPDGEIQGPFTASQMSQWYQAGYFPDSLQIKRLNEPPYETLGDLDRLLGL 56
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 1504-1829 7.02e-14

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. 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: 75.48  E-value: 7.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1504 PLKLANVEKRTPAQGEIQVSILTAALNHRDLFIrqsLYPAISFTTPLLA--DGCGVV------TSGSSKLN-GKRVI--- 1571
Cdd:cd08263    12 PLTIEEIPVPRPKEGEILIRVAACGVCHSDLHV---LKGELPFPPPFVLghEISGEVvevgpnVENPYGLSvGDRVVgsf 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1572 LTPAHGWESQVSGPETF-----------IGILGGTT-----------MNEVGTAQEVVVIPETEVELAPEHLSDAQAAAL 1629
Cdd:cd08263    89 IMPCGKCRYCARGKENLcedffaynrlkGTLYDGTTrlfrldggpvyMYSMGGLAEYAVVPATALAPLPESLDYTESAVL 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1630 PLTGLTAWRALVTkSGEAIEGRNILVTGIgGGVALNALQFAVAKGCNVWVTSG-DEGKIKKAVALGAKGGV-SYKGAAWD 1707
Cdd:cd08263   169 GCAGFTAYGALKH-AADVRPGETVAVIGV-GGVGSSAIQLAKAFGASPIIAVDvRDEKLAKAKELGATHTVnAAKEDAVA 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1708 KellamlpeerkwIDAIIDGAGGDI----------MKRSVRLVKQGGVVVSYG-MTLGPKIDFPMSAVLKN-IDLKGSTM 1775
Cdd:cd08263   247 A------------IREITGGRGVDVvvealgkpetFKLALDVVRDGGRAVVVGlAPGGATAEIPITRLVRRgIKIIGSYG 314

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 682443620 1776 G-SRVEFREMVRFVNEKKIVPvvSRVVDGLDNLEGVEELFQEMKQGKQFGKLIIR 1829
Cdd:cd08263   315 ArPRQDLPELVGLAASGKLDP--EALVTHKYKLEEINEAYENLRKGLIHGRAIVE 367
CAD2 cd08298
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
 1605-1821 1.18e-13

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: 74.14  E-value: 1.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1605 EVVVIPETEVELAPEHLSDAQAAALPLTGLTAWRALvtKSGEAIEGRNILVTGIgGGVALNALQFAVAKGCNVWVTSGDE 1684
Cdd:cd08298   125 EYMVADERFAYPIPEDYDDEEAAPLLCAGIIGYRAL--KLAGLKPGQRLGLYGF-GASAHLALQIARYQGAEVFAFTRSG 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1685 GKIKKAVALGAKGGVSYKgaawdkellAMLPEErkwIDAIIDGAG-GDIMKRSVRLVKQGGVVVSYGMTLGPKIDFPMSA 1763
Cdd:cd08298   202 EHQELARELGADWAGDSD---------DLPPEP---LDAAIIFAPvGALVPAALRAVKKGGRVVLAGIHMSDIPAFDYEL 269

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 682443620 1764 VLKNIDLKGSTMGSRVEFREMVRFVNEKKIVPVVSRVvdgldNLEGVEELFQEMKQGK 1821
Cdd:cd08298   270 LWGEKTIRSVANLTRQDGEEFLKLAAEIPIKPEVETY-----PLEEANEALQDLKEGR 322
PRK09422 PRK09422
ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional
 1601-1832 1.41e-13

ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional


Pssm-ID: 181842 [Multi-domain]  Cd Length: 338  Bit Score: 74.30  E-value: 1.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1601 GTAQEVVVIPETEVELaPEHLSDAQAAALPLTGLTAWRALvtKSGEAIEGRNILVTGIGGGVALnALQFAvaK---GCNV 1677
Cdd:PRK09422  117 GMAEQCIVTADYAVKV-PEGLDPAQASSITCAGVTTYKAI--KVSGIKPGQWIAIYGAGGLGNL-ALQYA--KnvfNAKV 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1678 WVTSGDEGKIKKAVALGAKGGVSYKGaawDKELLAMLPEERKWIDAIIDGAGGDI-MKRSVRLVKQGGVVVSYG-----M 1751
Cdd:PRK09422  191 IAVDINDDKLALAKEVGADLTINSKR---VEDVAKIIQEKTGGAHAAVVTAVAKAaFNQAVDAVRAGGRVVAVGlppesM 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1752 TLG-PKIdfpmsaVLKNIDLKGSTMGSRVEFREMVRFVNEKKIVPVVSRVvdgldNLEGVEELFQEMKQGKQFGKLIIRI 1830
Cdd:PRK09422  268 DLSiPRL------VLDGIEVVGSLVGTRQDLEEAFQFGAEGKVVPKVQLR-----PLEDINDIFDEMEQGKIQGRMVIDF 336


                  ..
gi 682443620 1831 KK 1832
Cdd:PRK09422  337 TH 338
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
 1504-1828 1.03e-12

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: 71.44  E-value: 1.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1504 PLKLANVEKRTPAQGEIQVSILTAALNHRDLFIRQSLYPAIS-FTTPLL----------ADGCGVvtSGSSKlnGKRVIL 1572
Cdd:cd05284    12 PLRLEDVPVPEPGPGQVLVRVGGAGVCHSDLHVIDGVWGGILpYKLPFTlghenagwveEVGSGV--DGLKE--GDPVVV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1573 TP----------AHGWESQVSGPeTFIGIlggttmNEVGTAQEVVVIPETEVELAPEHLSDAQAAALPLTGLTAWRALVT 1642
Cdd:cd05284    88 HPpwgcgtcrycRRGEENYCENA-RFPGI------GTDGGFAEYLLVPSRRLVKLPRGLDPVEAAPLADAGLTAYHAVKK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1643 KSGEAIEGRNILVTGIgGGVALNALQFAVA-KGCNVWVTSGDEGKIKKAVALGAKGGVSyKGAAWDKELLAMlpEERKWI 1721
Cdd:cd05284   161 ALPYLDPGSTVVVIGV-GGLGHIAVQILRAlTPATVIAVDRSEEALKLAERLGADHVLN-ASDDVVEEVREL--TGGRGA 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1722 DAIIDGAGGDI-MKRSVRLVKQGGVVVSYGMtlGPKIDFPMSA-VLKNIDLKGSTMGSRVEFREMVRFVNEKKIVPVVSR 1799
Cdd:cd05284   237 DAVIDFVGSDEtLALAAKLLAKGGRYVIVGY--GGHGRLPTSDlVPTEISVIGSLWGTRAELVEVVALAESGKVKVEITK 314

                         330       340
                  ....*....|....*....|....*....
gi 682443620 1800 VvdgldNLEGVEELFQEMKQGKQFGKLII 1828
Cdd:cd05284   315 F-----PLEDANEALDRLREGRVTGRAVL 338
GYF cd00072
GYF domain: contains conserved Gly-Tyr-Phe residues; Proline-binding domain in CD2-binding and ...
 730-782 2.51e-12

GYF domain: contains conserved Gly-Tyr-Phe residues; Proline-binding domain in CD2-binding and other proteins. Involved in signaling lymphocyte activity. Also present in other unrelated proteins (mainly unknown) derived from diverse eukaryotic species.


Pssm-ID: 238027  Cd Length: 57  Bit Score: 63.09  E-value: 2.51e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 682443620  730 WVYLDPQGQTQGPWSGLEMHDWYKASFFTPDLSVKKL-EDVEFEPLGQLIRRIG 782
Cdd:cd00072     4 WFYKDPQGEIQGPFSASQMLQWYQAGYFPDGLQVRRLdNGGEFYTLGDILFDLG 57
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 1601-1829 3.25e-12

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


Pssm-ID: 176221 [Multi-domain]  Cd Length: 345  Bit Score: 69.94  E-value: 3.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1601 GTAQEVVVIPETEVELA--PEHLSDAQAAALPLTGLTAWRALVTKsGEAIEGRNILVTGiGGGVALNALQFAVAKGCNVW 1678
Cdd:cd08260   116 GSFAEYVAVPRADVNLVrlPDDVDFVTAAGLGCRFATAFRALVHQ-ARVKPGEWVAVHG-CGGVGLSAVMIASALGARVI 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1679 VTSGDEGKIKKAVALGAKGGVSYKGAawDKELLAMLPEERKWIDAIIDgAGG--DIMKRSVRLVKQGGVVVSYGMTLGPK 1756
Cdd:cd08260   194 AVDIDDDKLELARELGAVATVNASEV--EDVAAAVRDLTGGGAHVSVD-ALGipETCRNSVASLRKRGRHVQVGLTLGEE 270

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 682443620 1757 IDFPMSA---VLKNIDLKGSTMGSRVEFREMVRFVNEKKIVP--VVSRVVDgldnLEGVEELFQEMKQGKQFGKLIIR 1829
Cdd:cd08260   271 AGVALPMdrvVARELEIVGSHGMPAHRYDAMLALIASGKLDPepLVGRTIS----LDEAPDALAAMDDYATAGITVIT 344
MDR_yhdh_yhfp cd05280
Yhdh and yhfp-like putative quinone oxidoreductases; Yhdh and yhfp-like putative quinone ...
 1488-1830 3.78e-12

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


Pssm-ID: 176183 [Multi-domain]  Cd Length: 325  Bit Score: 69.49  E-value: 3.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1488 ALSITKAEGKPGVVYHPLKLANVEKrtpaqGEIQVSILTAALNHRDLF--------IRQslYPAIsfttpLLADGCG-VV 1558
Cdd:cd05280     3 ALVVEEQDGGVSLFLRTLPLDDLPE-----GDVLIRVHYSSLNYKDALaatgnggvTRN--YPHT-----PGIDAAGtVV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1559 TSGSSKLN-GKRVILTpahGWesqvsgpetfigilgGTTMNEVGTAQEVVVIPETEVELAPEHLSDAQAAALPLTGLTAW 1637
Cdd:cd05280    71 SSDDPRFReGDEVLVT---GY---------------DLGMNTDGGFAEYVRVPADWVVPLPEGLSLREAMILGTAGFTAA 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1638 RAL--VTKSGEAIEGRNILVTGIGGGVALNALQFAVAKGCNVWVTSGDEGKIKKAVALGAKGgVSYKGAAWDKELLAMLP 1715
Cdd:cd05280   133 LSVhrLEDNGQTPEDGPVLVTGATGGVGSIAVAILAKLGYTVVALTGKEEQADYLKSLGASE-VLDREDLLDESKKPLLK 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1716 EerKWiDAIIDGAGGDIMKRSVRLVKQGGVVVSYGMTLGPKID---FPMsaVLKNIDLKG--STMGSRvEFREMV--RFV 1788
Cdd:cd05280   212 A--RW-AGAIDTVGGDVLANLLKQTKYGGVVASCGNAAGPELTttvLPF--ILRGVSLLGidSVNCPM-ELRKQVwqKLA 285

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 682443620 1789 NEKKI--VPVVSRVVDgldnLEGVEELFQEMKQGKQFGKLIIRI 1830
Cdd:cd05280   286 TEWKPdlLEIVVREIS----LEELPEAIDRLLAGKHRGRTVVKI 325
MDR_enoyl_red cd08244
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. ...
 1584-1755 8.37e-11

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: 65.47  E-value: 8.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1584 GPETFIG--ILGGTTMNEVGTAqEVVVIPETEVELAPEHLSDAQAAALPLTGLTAWRALvtKSGEAIEGRNILVTGIGGG 1661
Cdd:cd08244    78 VDPAWLGrrVVAHTGRAGGGYA-ELAVADVDSLHPVPDGLDLEAAVAVVHDGRTALGLL--DLATLTPGDVVLVTAAAGG 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1662 VALNALQFAVAKGCNVWVTSGDEGKIKKAVALGAKGGVSYKGAAWDKELLAMLPEERkwIDAIIDGAGGDIMKRSVRLVK 1741
Cdd:cd08244   155 LGSLLVQLAKAAGATVVGAAGGPAKTALVRALGADVAVDYTRPDWPDQVREALGGGG--VTVVLDGVGGAIGRAALALLA 232

                         170
                  ....*....|....
gi 682443620 1742 QGGVVVSYGMTLGP 1755
Cdd:cd08244   233 PGGRFLTYGWASGE 246
ADH_zinc_N_2 pfam13602
Zinc-binding dehydrogenase;
1721-1828 1.11e-10

Zinc-binding dehydrogenase;


Pssm-ID: 433341 [Multi-domain]  Cd Length: 131  Bit Score: 61.19  E-value: 1.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620  1721 IDAIIDGAGGDIMKRSVRLVKQGGVVVSYGMTLGPKIDFPMSAVLKNIDLKGSTMGSRV-----EFREMVRFVNEKKIVP 1795
Cdd:pfam13602   23 VDVVLDTVGGEAFEASLRVLPGGGRLVTIGGPPLSAGLLLPARKRGGRGVKYLFLFVRPnlgadILQELADLIEEGKLRP 102

                           90       100       110
                   ....*....|....*....|....*....|...
gi 682443620  1796 VVSRVVDgldnLEGVEELFQEMKQGKQFGKLII 1828
Cdd:pfam13602  103 VIDRVFP----LEEAAEAHRYLESGRARGKIVL 131
AL_MDR cd08252
Arginate lyase and other MDR family members; This group contains a structure identified as an ...
 1601-1670 1.33e-10

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


Pssm-ID: 176214 [Multi-domain]  Cd Length: 336  Bit Score: 64.85  E-value: 1.33e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 682443620 1601 GTAQEVVVIPETEVELAPEHLSDAQAAALPLTGLTAWRAL-----VTKSGEAiEGRNILVTGIGGGVALNALQFA 1670
Cdd:cd08252    97 GSNAEYQLVDERIVGHKPKSLSFAEAAALPLTSLTAWEALfdrlgISEDAEN-EGKTLLIIGGAGGVGSIAIQLA 170
ETR_like_2 cd08292
2-enoyl thioester reductase (ETR) like proteins, child 2; 2-enoyl thioester reductase (ETR) ...
 1496-1829 1.41e-10

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


Pssm-ID: 176252 [Multi-domain]  Cd Length: 324  Bit Score: 64.66  E-value: 1.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1496 GKPGVVyhpLKLANVEKRTPAQGEIQVSILTAALNHRDLFIRQSLY------PAISFTtpllaDGCGVVT---SGSSKLN 1566
Cdd:cd08292    10 GDPADV---LEIGEVPKPTPGAGEVLVRTTLSPIHNHDLWTIRGTYgykpelPAIGGS-----EAVGVVDavgEGVKGLQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1567 -GKRVILTPAHGwesqvsgpetfigilggttmnevgTAQEVVVIPETEVELAPEHLSD---AQAAALPLTGLTAWRALVT 1642
Cdd:cd08292    82 vGQRVAVAPVHG------------------------TWAEYFVAPADGLVPLPDGISDevaAQLIAMPLSALMLLDFLGV 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1643 KSGEAIegrniLVTGIGGGVALNALQFAVAKGCNVW-VTSGDEGkIKKAVALGAKGGVSYKGAAWDKELLAMLPEERkwI 1721
Cdd:cd08292   138 KPGQWL-----IQNAAGGAVGKLVAMLAAARGINVInLVRRDAG-VAELRALGIGPVVSTEQPGWQDKVREAAGGAP--I 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1722 DAIIDGAGGDIMKRSVRLVKQGGVVVSYGMTLGPKIDFPMSAVL-KNIDLKGSTmGSRVeFREMVRFVNEKKIVPVVSRV 1800
Cdd:cd08292   210 SVALDSVGGKLAGELLSLLGEGGTLVSFGSMSGEPMQISSGDLIfKQATVRGFW-GGRW-SQEMSVEYRKRMIAELLTLA 287

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 682443620 1801 VDGLDNL--EGVEELFQ-------EMKQGKQfGKLIIR 1829
Cdd:cd08292   288 LKGQLLLpvEAVFDLGDaakaaaaSMRPGRA-GKVLLR 324
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
 1505-1822 6.03e-10

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: 63.01  E-value: 6.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1505 LKLANVEKRTP-AQGEIQVSILTAALNHRDLFIRQSLYP-AISFTTPLLA----DGCGVVT---SGSSKLN-GKRVI-LT 1573
Cdd:cd08290    16 LQLESYEIPPPgPPNEVLVKMLAAPINPADINQIQGVYPiKPPTTPEPPAvggnEGVGEVVkvgSGVKSLKpGDWVIpLR 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1574 PAHG-WESQVsgpetfigilggttmneVGTAQEVVVIPETevelapehLSDAQAAALPLTGLTAWRaLVTKSGEAIEGRN 1652
Cdd:cd08290    96 PGLGtWRTHA-----------------VVPADDLIKVPND--------VDPEQAATLSVNPCTAYR-LLEDFVKLQPGDW 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1653 ILVTGIGGGVALNALQFAVAKGCNVWVTSGDEGKIKKAV----ALGAKGGVSYKGAAW--DKELLAMLPEERkwIDAIID 1726
Cdd:cd08290   150 VIQNGANSAVGQAVIQLAKLLGIKTINVVRDRPDLEELKerlkALGADHVLTEEELRSllATELLKSAPGGR--PKLALN 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1727 GAGGDIMKRSVRLVKQGGVVVSYGMTLGPKIDFPMSAVL-KNIDLKG------STMGSRVEFREMV----RFVNEKKIVP 1795
Cdd:cd08290   228 CVGGKSATELARLLSPGGTMVTYGGMSGQPVTVPTSLLIfKDITLRGfwltrwLKRANPEEKEDMLeelaELIREGKLKA 307

                         330       340       350
                  ....*....|....*....|....*....|
gi 682443620 1796 VVSRVVDGL---DNLEGVEELFQEMKQGKQ 1822
Cdd:cd08290   308 PPVEKVTDDpleEFKDALANALKGGGGGKQ 337
Zn_ADH_class_III cd08279
Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, ...
 1504-1821 7.88e-10

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


Pssm-ID: 176240 [Multi-domain]  Cd Length: 363  Bit Score: 62.94  E-value: 7.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1504 PLKLANVEKRTPAQGEIQVSILTAALNHRDLFIRQSLYPaisFTTPLLA--DGCGVVT---SGSSKLN-GKRVILT---- 1573
Cdd:cd08279    12 PLEIEEVELDDPGPGEVLVRIAAAGLCHSDLHVVTGDLP---APLPAVLghEGAGVVEevgPGVTGVKpGDHVVLSwipa 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1574 -----------------PAHGWESQVSGPETFIGiLGGTTMNE---VGTAQEVVVIPETEVELAPEHLSDAQAAALP--- 1630
Cdd:cd08279    89 cgtcrycsrgqpnlcdlGAGILGGQLPDGTRRFT-ADGEPVGAmcgLGTFAEYTVVPEASVVKIDDDIPLDRAALLGcgv 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1631 LTGLTAwralVTKSGEAIEGRNILVTGIGGgVALNALQFAVAKGCNVwVTSGD--EGKIKKAVALGAKGGVsykgAAWDK 1708
Cdd:cd08279   168 TTGVGA----VVNTARVRPGDTVAVIGCGG-VGLNAIQGARIAGASR-IIAVDpvPEKLELARRFGATHTV----NASED 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1709 ELLAMLPE--ERKWIDAIIDGAG-GDIMKRSVRLVKQGGVVVSYGMT-LGPKIDFPMSAVL---KNIdlKGSTMGS---R 1778
Cdd:cd08279   238 DAVEAVRDltDGRGADYAFEAVGrAATIRQALAMTRKGGTAVVVGMGpPGETVSLPALELFlseKRL--QGSLYGSanpR 315

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 682443620 1779 VEFREMVRFVNEKKIV--PVVSRVVDgldnLEGVEELFQEMKQGK 1821
Cdd:cd08279   316 RDIPRLLDLYRAGRLKldELVTRRYS----LDEINEAFADMLAGE 356
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
 1588-1821 1.60e-09

(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: 61.79  E-value: 1.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1588 FIGI--LGGttmnevGTAQEVVViPETEVELAPEHLSDAQAAAL-PLTglTAWRALvtKSGEAIEGRNILVTGiGGGVAL 1664
Cdd:cd08233   119 FIGLggGGG------GFAEYVVV-PAYHVHKLPDNVPLEEAALVePLA--VAWHAV--RRSGFKPGDTALVLG-AGPIGL 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1665 NALQFAVAKGC-NVWVTSGDEGKIKKAVALGA-------KGGVSykgaawdKELLAMLPEerKWIDAIIDGAG-GDIMKR 1735
Cdd:cd08233   187 LTILALKAAGAsKIIVSEPSEARRELAEELGAtivldptEVDVV-------AEVRKLTGG--GGVDVSFDCAGvQATLDT 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1736 SVRLVKQGGVVVSYGMTLGPkIDF-PMSAVLKNIDLKGSTMGSRVEFREMVRFVNEKKIVP---VVSRVvdGLDNleGVE 1811
Cdd:cd08233   258 AIDALRPRGTAVNVAIWEKP-ISFnPNDLVLKEKTLTGSICYTREDFEEVIDLLASGKIDAeplITSRI--PLED--IVE 332

                         250
                  ....*....|
gi 682443620 1812 ELFQEMKQGK 1821
Cdd:cd08233   333 KGFEELINDK 342
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
 1601-1752 7.42e-09

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: 58.82  E-value: 7.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1601 GTAQEVVVIPETEVELAPEHLSDAQAAALPL--TGLTA-WRAlvtksgEAIEGRNILVTGiGGGVALNALQFAVAKGC-N 1676
Cdd:cd08255    52 GPHAERVVVPANLLVPLPDGLPPERAALTALaaTALNGvRDA------EPRLGERVAVVG-LGLVGLLAAQLAKAAGArE 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1677 VWVTSGDEGKIKKAVALGAKGGVSYKGAAWDKELLAmlpeerkwiDAIIDGAG-GDIMKRSVRLVKQGGVVV---SYGMT 1752
Cdd:cd08255   125 VVGVDPDAARRELAEALGPADPVAADTADEIGGRGA---------DVVIEASGsPSALETALRLLRDRGRVVlvgWYGLK 195
liver_ADH_like1 cd08281
Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); ...
 1504-1789 1.29e-08

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: 58.93  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1504 PLKLANVEKRTPAQGEIQVSILTAALNHRDLFIRQSLYPaisftTPL-LADG---CGVVTS---GSSKLN-GKRVILT-- 1573
Cdd:cd08281    20 PLVIEEVELDPPGPGEVLVKIAAAGLCHSDLSVINGDRP-----RPLpMALGheaAGVVVEvgeGVTDLEvGDHVVLVfv 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1574 -------------PA---HGWESQVSGpETFIGIL-----GGTTMNEVGT---AQEVVVIPETEVELAPEhLSDAQAAAL 1629
Cdd:cd08281    95 pscghcrpcaegrPAlcePGAAANGAG-TLLSGGRrlrlrGGEINHHLGVsafAEYAVVSRRSVVKIDKD-VPLEIAALF 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1630 P---LTGLTAwralVTKSGEAIEGRNILVTGIGGgVALNALQFAVAKGCN-VWVTSGDEGKIKKAVALGAKGGVSykgaA 1705
Cdd:cd08281   173 GcavLTGVGA----VVNTAGVRPGQSVAVVGLGG-VGLSALLGAVAAGASqVVAVDLNEDKLALARELGATATVN----A 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1706 WDKELLAMLPEERK-WIDAIIDGAG-GDIMKRSVRLVKQGGVVVSYGMTlGPKIDFPMSA---VLKNIDLKGSTMGSRVE 1780
Cdd:cd08281   244 GDPNAVEQVRELTGgGVDYAFEMAGsVPALETAYEITRRGGTTVTAGLP-DPEARLSVPAlslVAEERTLKGSYMGSCVP 322


                  ....*....
gi 682443620 1781 FREMVRFVN 1789
Cdd:cd08281   323 RRDIPRYLA 331
adh_fam_1 TIGR02817
zinc-binding alcohol dehydrogenase family protein; Members of this model form a distinct ...
 1497-1673 4.50e-08

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


Pssm-ID: 274313 [Multi-domain]  Cd Length: 336  Bit Score: 57.06  E-value: 4.50e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620  1497 KPGVVYHPLKLANVE--KRTPAQGEIQVSILTAALNHRDLFIRQSLYPAISFTTPLLADGCGVVTSGSSKLNGKRViltp 1574
Cdd:TIGR02817    7 KPLPITDPDALVDIDlpKPKPGGRDLLVEVKAISVNPVDTKVRARMAPEAGQPKILGWDAAGVVVAVGDEVTLFKP---- 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620  1575 ahgwesqvsGPETFIGilggTTMNEVGTAQEVVVIPETEVELAPEHLSDAQAAALPLTGLTAWRALVTK----SGEAIEG 1650
Cdd:TIGR02817   83 ---------GDEVWYA----GDIDRPGSNAEFHLVDERIVGHKPKSLSFAEAAALPLTSITAWELLFDRlginDPVAGDK 149

                          170       180
                   ....*....|....*....|...
gi 682443620  1651 RNILVTGIGGGVALNALQFAVAK 1673
Cdd:TIGR02817  150 RALLIIGGAGGVGSILIQLARQL 172
AST1_like cd08247
AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast; This group ...
 1518-1830 5.22e-08

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


Pssm-ID: 176209 [Multi-domain]  Cd Length: 352  Bit Score: 56.89  E-value: 5.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1518 GEIQVSILTAALNHRDLFIRQSlYPAISFTTP--LLADGCGVVTSGSSKLngkrviltpAHGWE--SQVSGpeTFIGILG 1593
Cdd:cd08247    29 NEIVVKVHAAALNPVDLKLYNS-YTFHFKVKEkgLGRDYSGVIVKVGSNV---------ASEWKvgDEVCG--IYPHPYG 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1594 GttmneVGTAQEVVVI-PET---EVELAPEHLSDAQAAALPLTGLTAWRALVTKSGEAIEGRNILVTGIGGGVALNALQF 1669
Cdd:cd08247    97 G-----QGTLSQYLLVdPKKdkkSITRKPENISLEEAAAWPLVLGTAYQILEDLGQKLGPDSKVLVLGGSTSVGRFAIQL 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1670 A--VAKGCNVWVTSGDEGkIKKAVALGAKGGVSYKGAAWDKELLAMLpEERKW---IDAIIDGAGG-DIMKRSVRLVKQ- 1742
Cdd:cd08247   172 AknHYNIGTVVGTCSSRS-AELNKKLGADHFIDYDAHSGVKLLKPVL-ENVKGqgkFDLILDCVGGyDLFPHINSILKPk 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1743 ----------GGVVVSYGMTLGPKIDFP---MSAVLKNIDLKG--------STMGSRVE-FREMVRfvnEKKIVPVVSRV 1800
Cdd:cd08247   250 sknghyvtivGDYKANYKKDTFNSWDNPsanARKLFGSLGLWSynyqffllDPNADWIEkCAELIA---DGKVKPPIDSV 326

                         330       340       350
                  ....*....|....*....|....*....|
gi 682443620 1801 VDgldnLEGVEELFQEMKQGKQFGKLIIRI 1830
Cdd:cd08247   327 YP----FEDYKEAFERLKSNRAKGKVVIKV 352
oxido_YhdH TIGR02823
putative quinone oxidoreductase, YhdH/YhfP family; This model represents a subfamily of ...
 1557-1830 8.19e-08

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


Pssm-ID: 274315 [Multi-domain]  Cd Length: 323  Bit Score: 56.03  E-value: 8.19e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620  1557 VVTSGSSKLN-GKRVILTpahGWEsqvsgpetfigiLGGTTMNevGTAQEVVVIPETEVELaPEHLSDAQAAALPLTGLT 1635
Cdd:TIGR02823   68 VVSSEDPRFReGDEVIVT---GYG------------LGVSHDG--GYSQYARVPADWLVPL-PEGLSLREAMALGTAGFT 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620  1636 AwrAL----VTKSGEAIEGRNILVTGIGGGVALNALQFAVAKGCNVWVTSGDEGKIKKAVALGAK-----GGVSYKGAAW 1706
Cdd:TIGR02823  130 A--ALsvmaLERNGLTPEDGPVLVTGATGGVGSLAVAILSKLGYEVVASTGKAEEEDYLKELGASevidrEDLSPPGKPL 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620  1707 DKEllamlpeerKWiDAIIDGAGGDIMKRSVRLVKQGGVVVSYGMTLGPkiDFPMSA---VLKNIDLKG--STMGSRVEf 1781
Cdd:TIGR02823  208 EKE---------RW-AGAVDTVGGHTLANVLAQLKYGGAVAACGLAGGP--DLPTTVlpfILRGVSLLGidSVYCPMAL- 274

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 682443620  1782 REMV--RFVNEKKI--VPVVSRVVDgldnLEGVEELFQEMKQGKQFGKLIIRI 1830
Cdd:TIGR02823  275 REAAwqRLATDLKPrnLESITREIT----LEELPEALEQILAGQHRGRTVVDV 323
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
 1594-1773 3.40e-07

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: 54.24  E-value: 3.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1594 GTTMNevGTAQEVVVIPETEVELAPEHLSdAQAAALPLTGLTAWRALVTKSGeaIE-GRNILVTGiGGGVALNALQFAVA 1672
Cdd:cd08258   113 GTQAD--GGFAEYVLVPEESLHELPENLS-LEAAALTEPLAVAVHAVAERSG--IRpGDTVVVFG-PGPIGLLAAQVAKL 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1673 KGCNVWV--TSGDEGKIKKAVALGAkggvsyKGAAWDKELLAMLPEE---RKWIDAIIDGAGGDI-MKRSVRLVKQGG-- 1744
Cdd:cd08258   187 QGATVVVvgTEKDEVRLDVAKELGA------DAVNGGEEDLAELVNEitdGDGADVVIECSGAVPaLEQALELLRKGGri 260

                         170       180
                  ....*....|....*....|....*....
gi 682443620 1745 VVVSYGMTLGPKIDFPmSAVLKNIDLKGS 1773
Cdd:cd08258   261 VQVGIFGPLAASIDVE-RIIQKELSVIGS 288
leukotriene_B4_DH_like cd08294
13-PGR is a bifunctional enzyme with delta-13 15-prostaglandin reductase and leukotriene B4 12 ...
 1628-1830 5.68e-07

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


Pssm-ID: 176254 [Multi-domain]  Cd Length: 329  Bit Score: 53.81  E-value: 5.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1628 ALPLTGLTAWRALVtKSGEAIEGRNILVTGIGGGVALNALQFAVAKGCNVWVTSGDEGKIKKAVALGAKGGVSYKGAAWD 1707
Cdd:cd08294   123 VLGMPGLTAYFGLL-EICKPKAGETVVVNGAAGAVGSLVGQIAKIKGCKVIGCAGSDDKVAWLKELGFDAVFNYKTVSLE 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1708 KELLAMLPEErkwIDAIIDGAGGDIMKRSVRLVKQGGVVV------SYGMTLGPKID-FPMSAVLKNIDLKGsTMGSRVE 1780
Cdd:cd08294   202 EALKEAAPDG---IDCYFDNVGGEFSSTVLSHMNDFGRVAvcgsisTYNDKEPKKGPyVQETIIFKQLKMEG-FIVYRWQ 277

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 682443620 1781 ------FREMVRFVNEKKIvPVVSRVVDGLDNLegvEELFQEMKQGKQFGKLIIRI 1830
Cdd:cd08294   278 drwpeaLKQLLKWIKEGKL-KYREHVTEGFENM---PQAFIGMLKGENTGKAIVKV 329
THR_DH_like cd08239
L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as ...
 1601-1828 7.10e-07

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: 53.48  E-value: 7.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1601 GTAQEVVVIPETEVELAPEHLSDAQAAALPLTGLTAWRALvtKSGEAIEGRNILVTGIgGGVALNALQFAVAKGC-NVWV 1679
Cdd:cd08239   117 GGHAEYMLVPEKTLIPLPDDLSFADGALLLCGIGTAYHAL--RRVGVSGRDTVLVVGA-GPVGLGALMLARALGAeDVIG 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1680 TSGDEGKIKKAVALGAKggvsyKGAAWDKELLAMLPE--ERKWIDAIIDGAGGDIMKR-SVRLVKQGGVVVSYGmtLGPK 1756
Cdd:cd08239   194 VDPSPERLELAKALGAD-----FVINSGQDDVQEIREltSGAGADVAIECSGNTAARRlALEAVRPWGRLVLVG--EGGE 266

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 682443620 1757 IDFPMSAVL--KNIDLKGSTMGSRVEFREMVRFVNEKKIVPvvSRVVDGLDNLEGVEELFQEMKQGKQfGKLII 1828
Cdd:cd08239   267 LTIEVSNDLirKQRTLIGSWYFSVPDMEECAEFLARHKLEV--DRLVTHRFGLDQAPEAYALFAQGES-GKVVF 337
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
 1601-1788 8.90e-07

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: 53.03  E-value: 8.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1601 GTAQEVVVIPETEVELAPEHLSDAQAA----ALPlTGLTAWRALvtksGEAIEGRNILVTGiGGGVALNALQFAVAKGC- 1675
Cdd:cd08231   130 GYAEHIYLPPGTAIVRVPDNVPDEVAApancALA-TVLAALDRA----GPVGAGDTVVVQG-AGPLGLYAVAAAKLAGAr 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1676 NVWVTSGDEGKIKKAVALGAKGGVSYKGAAwdkellamLPEERKWIDAIIDGAGGDI----------MKRSVRLVKQGGV 1745
Cdd:cd08231   204 RVIVIDGSPERLELAREFGADATIDIDELP--------DPQRRAIVRDITGGRGADVvieasghpaaVPEGLELLRRGGT 275

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 682443620 1746 VVSYGM-TLGPKIDF-PMSAVLKNIDLKGSTMGSRVEFREMVRFV 1788
Cdd:cd08231   276 YVLVGSvAPAGTVPLdPERIVRKNLTIIGVHNYDPSHLYRAVRFL 320
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
 1588-1821 9.14e-07

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: 53.03  E-value: 9.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1588 FIGILGGTTMNevGTAQEVVVIPETEVEL--APEHLSDAQAAALPLTGLTAWRALvtKSGEAIEGRNILVTGiGGGVALN 1665
Cdd:cd08284   108 LFGYAGSPNLD--GAQAEYVRVPFADGTLlkLPDGLSDEAALLLGDILPTGYFGA--KRAQVRPGDTVAVIG-CGPVGLC 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1666 ALQFA-VAKGCNVWVTSGDEGKIKKAVALGAKGGVSykGAAWDKELLAMLPEERKwIDAIIDGAGGD-IMKRSVRLVKQG 1743
Cdd:cd08284   183 AVLSAqVLGAARVFAVDPVPERLERAAALGAEPINF--EDAEPVERVREATEGRG-ADVVLEAVGGAaALDLAFDLVRPG 259

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1744 GVVVSYGMTLGPKIDFP-MSAVLKNIDLKGSTMGSRVEFREMVRFVNEKKIVP--VVSRVVdGLDnlEGVE--ELFQEMK 1818
Cdd:cd08284   260 GVISSVGVHTAEEFPFPgLDAYNKNLTLRFGRCPVRSLFPELLPLLESGRLDLefLIDHRM-PLE--EAPEayRLFDKRK 336


                  ...
gi 682443620 1819 QGK 1821
Cdd:cd08284   337 VLK 339
MDR_yhfp_like cd08289
Yhfp putative quinone oxidoreductases; yhfp putative quinone oxidoreductases (QOR). QOR ...
 1618-1830 1.37e-06

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


Pssm-ID: 176249 [Multi-domain]  Cd Length: 326  Bit Score: 52.33  E-value: 1.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1618 PEHLSDAQAAALPLTGLTAWRAL--VTKSGEAIEGRNILVTGIGGGVALNALQFAVAKGCNVWVTSGDEGKIKKAVALGA 1695
Cdd:cd08289   113 PKGLTLKEAMILGTAGFTAALSIhrLEENGLTPEQGPVLVTGATGGVGSLAVSILAKLGYEVVASTGKADAADYLKKLGA 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1696 KGGVSYKGAAWDKellAMLPEERKWiDAIIDGAGGDIMKRSVRLVKQGGVVVSYGMTLGPKID---FPMsaVLKNIDLKG 1772
Cdd:cd08289   193 KEVIPREELQEES---IKPLEKQRW-AGAVDPVGGKTLAYLLSTLQYGGSVAVSGLTGGGEVEttvFPF--ILRGVNLLG 266

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 682443620 1773 -STMGSRVEFREMV--RFVNEKKIVPVVSRVVDGLdNLEGVEELFQEMKQGKQFGKLIIRI 1830
Cdd:cd08289   267 iDSVECPMELRRRIwrRLATDLKPTQLLNEIKQEI-TLDELPEALKQILQGRVTGRTVVKL 326
CAD_like cd08296
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 1488-1695 5.20e-06

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: 50.71  E-value: 5.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1488 ALSITKAEGkpgvvyhPLKLANVEKRTPAQGEIQVSILTAALNHRDLFIRQSLYPAISF-TTP-------LLADGCGVvt 1559
Cdd:cd08296     3 AVQVTEPGG-------PLELVERDVPLPGPGEVLIKVEACGVCHSDAFVKEGAMPGLSYpRVPghevvgrIDAVGEGV-- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1560 sgSSKLNGKRViltpAHGW--------------------ESQVSGpETFIGilggttmnevGTAqEVVVIPETEVELAPE 1619
Cdd:cd08296    74 --SRWKVGDRV----GVGWhgghcgtcdacrrgdfvhceNGKVTG-VTRDG----------GYA-EYMLAPAEALARIPD 135

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 682443620 1620 HLSDAQAAALPLTGLTAWRALvTKSGeAIEGRNILVTGIGGGVALnALQFAVAKGCNVWVTSGDEGKIKKAVALGA 1695
Cdd:cd08296   136 DLDAAEAAPLLCAGVTTFNAL-RNSG-AKPGDLVAVQGIGGLGHL-AVQYAAKMGFRTVAISRGSDKADLARKLGA 208
MDR_yhdh cd08288
Yhdh putative quinone oxidoreductases; Yhdh putative quinone oxidoreductases (QOR). QOR ...
 1488-1772 6.18e-06

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


Pssm-ID: 176248 [Multi-domain]  Cd Length: 324  Bit Score: 50.23  E-value: 6.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1488 ALSITKAEGKPGVVYHPLKLANVEkrtpaQGEIQVSILTAALNHRD-LFIRQSlyPAISFTTPLLA--DGCGVVTSGSSK 1564
Cdd:cd08288     3 ALVLEKDDGGTSAELRELDESDLP-----EGDVTVEVHYSTLNYKDgLAITGK--GGIVRTFPLVPgiDLAGTVVESSSP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1565 L--NGKRVILTpahGWesQVSgpETFIGilggttmnevGTAQEVVVIPETEVELaPEHLSDAQAAALPLTGLTAwrAL-- 1640
Cdd:cd08288    76 RfkPGDRVVLT---GW--GVG--ERHWG----------GYAQRARVKADWLVPL-PEGLSARQAMAIGTAGFTA--MLcv 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1641 --VTKSGEAIEGRNILVTGIGGGVALNALQFAVAKGCNVWVTSGDEGKIKKAVALGAKGGV-----SYKGAAWDKELLAm 1713
Cdd:cd08288   136 maLEDHGVTPGDGPVLVTGAAGGVGSVAVALLARLGYEVVASTGRPEEADYLRSLGASEIIdraelSEPGRPLQKERWA- 214

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 682443620 1714 lpeerkwidAIIDGAGGDIMKRSVRLVKQGGVVVSYGMTLGPkiDFP---MSAVLKNIDLKG 1772
Cdd:cd08288   215 ---------GAVDTVGGHTLANVLAQTRYGGAVAACGLAGGA--DLPttvMPFILRGVTLLG 265
Mgc45594_like cd08250
Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of ...
 1600-1829 3.87e-05

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


Pssm-ID: 176212 [Multi-domain]  Cd Length: 329  Bit Score: 48.02  E-value: 3.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1600 VGTAQEVVVIPEteveLAPEHLSdaqaaaLPLTGLTAWRALvTKSGEAIEGRNILVTGIGGGVALNALQFAVAKGCNVWV 1679
Cdd:cd08250   101 VVPARHAVPVPE----LKPEVLP------LLVSGLTASIAL-EEVGEMKSGETVLVTAAAGGTGQFAVQLAKLAGCHVIG 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1680 TSGDEGKIKKAVALGAKGGVSYKGAAWDKELLAMLPeerKWIDAIIDGAGGDIMKRSV-------RLV---------KQG 1743
Cdd:cd08250   170 TCSSDEKAEFLKSLGCDRPINYKTEDLGEVLKKEYP---KGVDVVYESVGGEMFDTCVdnlalkgRLIvigfisgyqSGT 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1744 GVVVSYGMTLGPKIdFPMSAVLKNIDLKGSTMGSRVEFREMVRFVNEKKIVPVVSRVVdgLDNLEGVEELFQEMKQGKQF 1823
Cdd:cd08250   247 GPSPVKGATLPPKL-LAKSASVRGFFLPHYAKLIPQHLDRLLQLYQRGKLVCEVDPTR--FRGLESVADAVDYLYSGKNI 323


                  ....*.
gi 682443620 1824 GKLIIR 1829
Cdd:cd08250   324 GKVVVE 329
PHA03247 PHA03247
large tegument protein UL36; Provisional
 909-1236 6.57e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.40  E-value: 6.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620  909 PIMPQQQIPTSgssffdastRPAPTtgsnlPPDFFREDEVARLSLQDRQQTFGAPTGATQAPRSQLPAifsqqsqaqAAA 988
Cdd:PHA03247 2561 PAAPDRSVPPP---------RPAPR-----PSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPP---------SPL 2617

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620  989 SQHQAHSENDPQGFRARLQEFEQLRAQHDMEQAEHAPAPATTEPIRPPQNRQQSRTETVTTETEVLVERKDQEEILSLTE 1068
Cdd:PHA03247 2618 PPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTS 2697

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1069 QIQKAASAKqTPQPESPWAKVSSGLPMPFPPPPQSTTPLPAPAAQRGRSNLPETlhAGTRSRSETPDTSAAPPSIAPwak 1148
Cdd:PHA03247 2698 LADPPPPPP-TPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPAT--PGGPARPARPPTTAGPPAPAP--- 2771

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1149 ePVDAPKGPSLKEIQEAEAKKAAKLEESAAAARRAlleqelrAQPAAVAHGLPTTSTWASSASPVGPAVTATSTWSKATT 1228
Cdd:PHA03247 2772 -PAAPAAGPPRRLTRPAVASLSESRESLPSPWDPA-------DPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP 2843


                  ....*...
gi 682443620 1229 TKVQNPAP 1236
Cdd:PHA03247 2844 GPPPPSLP 2851
Zn_ADH8 cd08262
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 1584-1829 7.81e-05

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: 46.92  E-value: 7.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1584 GPETFIGIlggTTMNEVGTAQEVVVIPETEVELaPEHLSDAQAA-ALPLTglTAWRAlVTKSGEAIEGRNiLVTG---IG 1659
Cdd:cd08262   103 GASCGIGL---SPEAPGGYAEYMLLSEALLLRV-PDGLSMEDAAlTEPLA--VGLHA-VRRARLTPGEVA-LVIGcgpIG 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1660 GGVALNALQFAVAkgcNVWVTSGDEGKIKKAVALGAKGGVSYK----GAAWDKELLAMLPEERkwiDAIID--GAGGdIM 1733
Cdd:cd08262   175 LAVIAALKARGVG---PIVASDFSPERRALALAMGADIVVDPAadspFAAWAAELARAGGPKP---AVIFEcvGAPG-LI 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1734 KRSVRLVKQGGVVVSYGMTLGPKIDFPMSAVLKNIDLKGSTMGSRVEFREMVRFVNEKKI--VPVVSRVVdGLDnleGVE 1811
Cdd:cd08262   248 QQIIEGAPPGGRIVVVGVCMESDNIEPALAIRKELTLQFSLGYTPEEFADALDALAEGKVdvAPMVTGTV-GLD---GVP 323

                         250
                  ....*....|....*...
gi 682443620 1812 ELFQEMKQGKQFGKLIIR 1829
Cdd:cd08262   324 DAFEALRDPEHHCKILVD 341
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
 1567-1816 8.98e-05

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: 46.85  E-value: 8.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1567 GKRVIL---TPA-HGWESQVSGPETFIGILGGTTMNEV--GTAQEVVVIPETEVELA--PEHLSDAQAAALP---LTGLT 1635
Cdd:cd08285    78 GDRVIVpaiTPDwRSVAAQRGYPSQSGGMLGGWKFSNFkdGVFAEYFHVNDADANLAplPDGLTDEQAVMLPdmmSTGFH 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1636 AWRALVTKSGEAIegrniLVTGIGGgVALNALQFAVAKGCN-VWVTSGDEGKIKKAVALGAKGGVSYKGAAWDKELLAMl 1714
Cdd:cd08285   158 GAELANIKLGDTV-----AVFGIGP-VGLMAVAGARLRGAGrIIAVGSRPNRVELAKEYGATDIVDYKNGDVVEQILKL- 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1715 pEERKWIDAIIDGAGG-DIMKRSVRLVKQGGVVVSYGMTLGP-KIDFP---MSAVLKNIDLKGSTM-GSRVEFREMVRFV 1788
Cdd:cd08285   231 -TGGKGVDAVIIAGGGqDTFEQALKVLKPGGTISNVNYYGEDdYLPIPreeWGVGMGHKTINGGLCpGGRLRMERLASLI 309

                         250       260       270
                  ....*....|....*....|....*....|
gi 682443620 1789 NEKKIVP--VVSRVVDGLDNLEGVEELFQE 1816
Cdd:cd08285   310 EYGRVDPskLLTHHFFGFDDIEEALMLMKD 339
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1024-1338 1.43e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1024 APAPATTEPI-------RPPQNRQQSRTETVTTETEVLVERKDQEEILSLTEQIQKAASAKQTPQPESPWAKVSSGLPMP 1096
Cdd:PHA03247 2559 APPAAPDRSVppprpapRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEP 2638

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1097 FPPPPQSTTPLPAP--AAQRGRSNLPETLHAGTR-----SRSETPDTSAAPPSIAPWAkEPVDAPKGPSLKEIQEAEAKK 1169
Cdd:PHA03247 2639 DPHPPPTVPPPERPrdDPAPGRVSRPRRARRLGRaaqasSPPQRPRRRAARPTVGSLT-SLADPPPPPPTPEPAPHALVS 2717

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1170 AAKLEESAAAARRALLEQELRAQPAAVAHGlptTSTWASSASPVGPAVTATSTWSKATTTKVQNPAPAATASKKTLADIQ 1249
Cdd:PHA03247 2718 ATPLPPGPAAARQASPALPAAPAPPAVPAG---PATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSES 2794

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1250 REE--ELRKQKLAAAAVAAAPALPSGGKRYAELASKPTAGQPAMNSAWS-----TVGAGGKVkMPGGPIVAAP---SPVM 1319
Cdd:PHA03247 2795 RESlpSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPgppppSLPLGGSV-APGGDVRRRPpsrSPAA 2873

                         330
                  ....*....|....*....
gi 682443620 1320 RPASSTAgPTLAKVARPAV 1338
Cdd:PHA03247 2874 KPAAPAR-PPVRRLARPAV 2891
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 1074-1371 3.73e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 45.68  E-value: 3.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620  1074 ASAKQTPQPESPWAKVSSGLPMPFPPPPQSTTPLPAPAAQRGRSNLPETLHAGTRSRSETPDTSAAPPSI---APWAKEP 1150
Cdd:pfam05109  526 AVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSAVTTPTPNATSPTVgetSPQANTT 605

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620  1151 VDAPKGPSLKEIQEAEAKKAAKLEESAAAARRALLEQELRAQPAAVAHGL-PTTSTWASSASP---------------VG 1214
Cdd:pfam05109  606 NHTLGGTSSTPVVTSPPKNATSAVTTGQHNITSSSTSSMSLRPSSISETLsPSTSDNSTSHMPlltsahptggenitqVT 685

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620  1215 PAVTAT---STWSKA----TTTKVQNPAPAATASKKTLADIQR----EEELRKQKLAAAAVAAAPALPSGGKRYAELASK 1283
Cdd:pfam05109  686 PASTSThhvSTSSPAprpgTTSQASGPGNSSTSTKPGEVNVTKgtppKNATSPQAPSGQKTAVPTVTSTGGKANSTTGGK 765

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620  1284 PTAGQPAMNSAWSTVGAGGKVKMPGGPIVAapSPVMRPASSTAGPTLAKVARPAVIENRAnTSSAALSSQGGVSTAQQEF 1363
Cdd:pfam05109  766 HTTGHGARTSTEPTTDYGGDSTTPRTRYNA--TTYLPPSTSSKLRPRWTFTSPPVTTAQA-TVPVPPTSQPRFSNLSMLV 842


                   ....*...
gi 682443620  1364 TKWANAAL 1371
Cdd:pfam05109  843 LQWASLAV 850
PHA03269 PHA03269
envelope glycoprotein C; Provisional
 1064-1246 1.15e-03

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 43.56  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1064 LSLTEQIQKAASAKQTPQPESpwakvssglpmpfpPPPQSTTPLPAPAAQRGRSNLPETLHAGTRSRSETPDTSAAPPSI 1143
Cdd:PHA03269   26 IPIPELHTSAATQKPDPAPAP--------------HQAASRAPDPAVAPTSAASRKPDLAQAPTPAASEKFDPAPAPHQA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443620 1144 APWAKEPVDAPkgpslkeiqeaeakkaakleesaaaarralleqELRAQPAAVAHGLPTTSTWASSASPVGPAVTATSTW 1223
Cdd:PHA03269   92 ASRAPDPAVAP---------------------------------QLAAAPKPDAAEAFTSAAQAHEAPADAGTSAASKKP 138

                         170       180
                  ....*....|....*....|...
gi 682443620 1224 SKATTTKVQNPAPAATASKKTLA 1246
Cdd:PHA03269  139 DPAAHTQHSPPPFAYTRSMEHIA 161
 
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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