NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1700447654|ref|NP_001358254|]
View 

prostaglandin reductase 2 isoform 1 [Homo sapiens]

Protein Classification

MDR/zinc-dependent alcohol dehydrogenase-like family protein; zinc-binding alcohol dehydrogenase family protein( domain architecture ID 10169693)

medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family protein may catalyze the reversible NAD(P)(H)-dependent conversion of an alcohol to its corresponding aldehyde; zinc-binding alcohol dehydrogenase family protein similar to Escherichia coli L-galactonate-5-dehydrogenase that catalyzes the oxidation of L-galactonate to D-tagaturonate

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PTGR2 cd08293
Prostaglandin reductase; Prostaglandins and related eicosanoids are metabolized by the ...
 1-345 0e+00

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


:

Pssm-ID: 176253 [Multi-domain]  Cd Length: 345  Bit Score: 717.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654   1 MIVQRVVLNSRPGKNGNPVAENFRMEEVYLPDNINEGQVQVRTLYLSVDPYMRCRMNEDTGTDYITPWQLSQVVDGGGIG 80
Cdd:cd08293     1 MINKRVVLNSRPGKNGNPVAENFRVEECTLPDELNEGQVLVRTLYLSVDPYMRCRMNEDTGTDYLAPWQLSQVLDGGGVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654  81 IIEESKHTNLTKGDFVTSFYWPWQTKVILDGNSLEKVDPQLVDGHLSYFLGAIGMPGLTSLIGIQEKGHITAGSNKTMVV 160
Cdd:cd08293    81 VVEESKHQKFAVGDIVTSFNWPWQTYAVLDGSSLEKVDPQLVDGHLSYFLGAVGLPGLTALIGIQEKGHITPGANQTMVV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 161 SGAAGACGSVAGQIGHFLGCSRVVGICGTHEKCILLTSELGFDAAINYKKDNVAEQLRESCPAGVDVYFDNVGGNISDTV 240
Cdd:cd08293   161 SGAAGACGSLAGQIGRLLGCSRVVGICGSDEKCQLLKSELGFDAAINYKTDNVAERLRELCPEGVDVYFDNVGGEISDTV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 241 ISQMNENSHIILCGQISQYNKDVPYPPPLSPAIEAIQKERNITRERFLVLNYKDKFEPGILQLSQWFKEGKLKIKETVIN 320
Cdd:cd08293   241 ISQMNENSHIILCGQISQYNKDVPYPPPLPEATEAILKERNITRERFLVLNYKDKFEEAIAQLSQWVKEGKLKVKETVYE 320

                         330       340
                  ....*....|....*....|....*
gi 1700447654 321 GLENMGAAFQSMMTGGNIGKQIVCI 345
Cdd:cd08293   321 GLENAGEAFQSMMNGGNIGKQIVKV 345
 
Name Accession Description Interval E-value
PTGR2 cd08293
Prostaglandin reductase; Prostaglandins and related eicosanoids are metabolized by the ...
 1-345 0e+00

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


Pssm-ID: 176253 [Multi-domain]  Cd Length: 345  Bit Score: 717.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654   1 MIVQRVVLNSRPGKNGNPVAENFRMEEVYLPDNINEGQVQVRTLYLSVDPYMRCRMNEDTGTDYITPWQLSQVVDGGGIG 80
Cdd:cd08293     1 MINKRVVLNSRPGKNGNPVAENFRVEECTLPDELNEGQVLVRTLYLSVDPYMRCRMNEDTGTDYLAPWQLSQVLDGGGVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654  81 IIEESKHTNLTKGDFVTSFYWPWQTKVILDGNSLEKVDPQLVDGHLSYFLGAIGMPGLTSLIGIQEKGHITAGSNKTMVV 160
Cdd:cd08293    81 VVEESKHQKFAVGDIVTSFNWPWQTYAVLDGSSLEKVDPQLVDGHLSYFLGAVGLPGLTALIGIQEKGHITPGANQTMVV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 161 SGAAGACGSVAGQIGHFLGCSRVVGICGTHEKCILLTSELGFDAAINYKKDNVAEQLRESCPAGVDVYFDNVGGNISDTV 240
Cdd:cd08293   161 SGAAGACGSLAGQIGRLLGCSRVVGICGSDEKCQLLKSELGFDAAINYKTDNVAERLRELCPEGVDVYFDNVGGEISDTV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 241 ISQMNENSHIILCGQISQYNKDVPYPPPLSPAIEAIQKERNITRERFLVLNYKDKFEPGILQLSQWFKEGKLKIKETVIN 320
Cdd:cd08293   241 ISQMNENSHIILCGQISQYNKDVPYPPPLPEATEAILKERNITRERFLVLNYKDKFEEAIAQLSQWVKEGKLKVKETVYE 320

                         330       340
                  ....*....|....*....|....*
gi 1700447654 321 GLENMGAAFQSMMTGGNIGKQIVCI 345
Cdd:cd08293   321 GLENAGEAFQSMMNGGNIGKQIVKV 345
CurA COG2130
NADPH-dependent curcumin reductase CurA [Secondary metabolites biosynthesis, transport and ...
 1-343 2.31e-150

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


Pssm-ID: 441733 [Multi-domain]  Cd Length: 333  Bit Score: 426.40  E-value: 2.31e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654   1 MIVQRVVLNSRPgkNGNPVAENFRMEEVYLPDnINEGQVQVRTLYLSVDPYMRCRMNEdtGTDYITPWQLSQVVDGGGIG 80
Cdd:COG2130     3 TTNRQIVLASRP--EGEPTPEDFRLEEVPVPE-PGDGEVLVRNLYLSVDPYMRGRMSD--AKSYAPPVELGEVMRGGAVG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654  81 IIEESKHTNLTKGDFVTSFyWPWQTKVILDGNSLEKVDPQLVdgHLSYFLGAIGMPGLTSLIGIQEKGHITAGsnKTMVV 160
Cdd:COG2130    78 EVVESRHPDFAVGDLVLGM-LGWQDYAVSDGAGLRKVDPSLA--PLSAYLGVLGMPGLTAYFGLLDIGKPKAG--ETVVV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 161 SGAAGACGSVAGQIGHFLGCsRVVGICGTHEKCILLTSELGFDAAINYKKDNVAEQLRESCPAGVDVYFDNVGGNISDTV 240
Cdd:COG2130   153 SAAAGAVGSVVGQIAKLKGC-RVVGIAGGAEKCRYLVEELGFDAAIDYKAGDLAAALAAACPDGIDVYFDNVGGEILDAV 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 241 ISQMNENSHIILCGQISQYNKDvpyPPPLSPAIEAIQKERNITRERFLVLNYKDKFEPGILQLSQWFKEGKLKIKETVIN 320
Cdd:COG2130   232 LPLLNTFARIAVCGAISQYNAT---EPPPGPRNLGQLLVKRLRMQGFIVFDHADRFPEFLAELAGWVAEGKLKYRETVVE 308

                         330       340
                  ....*....|....*....|...
gi 1700447654 321 GLENMGAAFQSMMTGGNIGKQIV 343
Cdd:COG2130   309 GLENAPEAFLGLFEGENFGKLLV 331
B4_12hDH TIGR02825
leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 ...
 16-343 2.56e-73

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


Pssm-ID: 131872 [Multi-domain]  Cd Length: 325  Bit Score: 230.27  E-value: 2.56e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654  16 GNPVAENFRMEEVYLPDnINEGQVQVRTLYLSVDPYMRCRMNEDTGTDYITPWQLSQVVdgggigiieESKHTNLTKGDF 95
Cdd:TIGR02825  12 GYPTDSDFELKTVELPP-LNNGEVLLEALFLSVDPYMRVAAKRLKEGDTMMGQQVARVV---------ESKNVALPKGTI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654  96 VTSfYWPWQTKVILDGNSLEKVDPQLVDG-HLSYFLGAIGMPGLTSLIGIQEKGHITAGsnKTMVVSGAAGACGSVAGQI 174
Cdd:TIGR02825  82 VLA-SPGWTSHSISDGKDLEKLLTEWPDTlPLSLALGTVGMPGLTAYFGLLEICGVKGG--ETVMVNAAAGAVGSVVGQI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 175 GHFLGCsRVVGICGTHEKCILLtSELGFDAAINYKK-DNVAEQLRESCPAGVDVYFDNVGGNISDTVISQMNENSHIILC 253
Cdd:TIGR02825 159 AKLKGC-KVVGAAGSDEKVAYL-KKLGFDVAFNYKTvKSLEETLKKASPDGYDCYFDNVGGEFSNTVIGQMKKFGRIAIC 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 254 GQISQYNKDVPYPPPLSPAIEAIQKERnitRERFLVLNYK-DKFEPGILQLSQWFKEGKLKIKETVINGLENMGAAFQSM 332
Cdd:TIGR02825 237 GAISTYNRTGPLPPGPPPEIVIYQELR---MEGFIVNRWQgEVRQKALKELLKWVLEGKIQYKEYVIEGFENMPAAFMGM 313

                         330
                  ....*....|.
gi 1700447654 333 MTGGNIGKQIV 343
Cdd:TIGR02825 314 LKGENLGKTIV 324
PLN03154 PLN03154
putative allyl alcohol dehydrogenase; Provisional
 41-348 1.81e-53

putative allyl alcohol dehydrogenase; Provisional


Pssm-ID: 215606 [Multi-domain]  Cd Length: 348  Bit Score: 179.65  E-value: 1.81e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654  41 VRTLYLSVDPYMRCRMNEDTGTdYITPWQLSQVVDGGGIGIIEESKHTNLTKGDFVTSFYwPWQTKVILDGNSLEKVDPQ 120
Cdd:PLN03154   48 VKNLYLSCDPYMRGRMRDFHDS-YLPPFVPGQRIEGFGVSKVVDSDDPNFKPGDLISGIT-GWEEYSLIRSSDNQLRKIQ 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 121 LVDG-HLSYFLGAIGMPGLTSLIGIQEKGHITAGSNktMVVSGAAGACGSVAGQIGHFLGCSrVVGICGTHEKCILLTSE 199
Cdd:PLN03154  126 LQDDiPLSYHLGLLGMAGFTAYAGFYEVCSPKKGDS--VFVSAASGAVGQLVGQLAKLHGCY-VVGSAGSSQKVDLLKNK 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 200 LGFDAAINYKKD-NVAEQLRESCPAGVDVYFDNVGGNISDTVISQMNENSHIILCGQISQynKDVPYPPPLSPAIEAIQK 278
Cdd:PLN03154  203 LGFDEAFNYKEEpDLDAALKRYFPEGIDIYFDNVGGDMLDAALLNMKIHGRIAVCGMVSL--NSLSASQGIHNLYNLISK 280

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 279 ErnITRERFLVLNYKDKFEPGILQLSQWFKEGKLKIKETVINGLENMGAAFQSMMTGGNIGKQIVCISEE 348
Cdd:PLN03154  281 R--IRMQGFLQSDYLHLFPQFLENVSRYYKQGKIVYIEDMSEGLESAPAALVGLFSGKNVGKQVIRVAKE 348
ADH_N_2 pfam16884
N-terminal domain of oxidoreductase; N-terminal region of oxidoreductase and prostaglandin ...
 5-117 4.54e-35

N-terminal domain of oxidoreductase; N-terminal region of oxidoreductase and prostaglandin reductase and alcohol dehydrogenase.


Pssm-ID: 465297 [Multi-domain]  Cd Length: 108  Bit Score: 123.85  E-value: 4.54e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654   5 RVVLNSRPgkNGNPVAENFRMEEVYLPDnINEGQVQVRTLYLSVDPYMRCRMNEDTGtdYITPWQLSQVVDGGGIGIIEE 84
Cdd:pfam16884   2 QWLLAKRP--EGVPTPSDFELVEAELPE-LGDGEVLVRTLYLSVDPYMRGRMNDAKS--YVPPVELGDVMRGGAVGEVVE 76

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1700447654  85 SKHTNLTKGDFVTSFyWPWQTKVILDGNSLEKV 117
Cdd:pfam16884  77 SNNPDFPVGDLVLGM-LGWQDYAVSDGKGLTKV 108
 
Name Accession Description Interval E-value
PTGR2 cd08293
Prostaglandin reductase; Prostaglandins and related eicosanoids are metabolized by the ...
 1-345 0e+00

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


Pssm-ID: 176253 [Multi-domain]  Cd Length: 345  Bit Score: 717.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654   1 MIVQRVVLNSRPGKNGNPVAENFRMEEVYLPDNINEGQVQVRTLYLSVDPYMRCRMNEDTGTDYITPWQLSQVVDGGGIG 80
Cdd:cd08293     1 MINKRVVLNSRPGKNGNPVAENFRVEECTLPDELNEGQVLVRTLYLSVDPYMRCRMNEDTGTDYLAPWQLSQVLDGGGVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654  81 IIEESKHTNLTKGDFVTSFYWPWQTKVILDGNSLEKVDPQLVDGHLSYFLGAIGMPGLTSLIGIQEKGHITAGSNKTMVV 160
Cdd:cd08293    81 VVEESKHQKFAVGDIVTSFNWPWQTYAVLDGSSLEKVDPQLVDGHLSYFLGAVGLPGLTALIGIQEKGHITPGANQTMVV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 161 SGAAGACGSVAGQIGHFLGCSRVVGICGTHEKCILLTSELGFDAAINYKKDNVAEQLRESCPAGVDVYFDNVGGNISDTV 240
Cdd:cd08293   161 SGAAGACGSLAGQIGRLLGCSRVVGICGSDEKCQLLKSELGFDAAINYKTDNVAERLRELCPEGVDVYFDNVGGEISDTV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 241 ISQMNENSHIILCGQISQYNKDVPYPPPLSPAIEAIQKERNITRERFLVLNYKDKFEPGILQLSQWFKEGKLKIKETVIN 320
Cdd:cd08293   241 ISQMNENSHIILCGQISQYNKDVPYPPPLPEATEAILKERNITRERFLVLNYKDKFEEAIAQLSQWVKEGKLKVKETVYE 320

                         330       340
                  ....*....|....*....|....*
gi 1700447654 321 GLENMGAAFQSMMTGGNIGKQIVCI 345
Cdd:cd08293   321 GLENAGEAFQSMMNGGNIGKQIVKV 345
PGDH cd05288
Prostaglandin dehydrogenases; Prostaglandins and related eicosanoids are metabolized by the ...
 4-343 6.86e-153

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: 432.68  E-value: 6.86e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654   4 QRVVLNSRPGknGNPVAENFRMEEVYLPDnINEGQVQVRTLYLSVDPYMRCRMNEdtGTDYITPWQLSQVVDGGGIGIIE 83
Cdd:cd05288     3 RQVVLAKRPE--GPPPPDDFELVEVPLPE-LKDGEVLVRTLYLSVDPYMRGWMSD--AKSYSPPVQLGEPMRGGGVGEVV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654  84 ESKHTNLTKGDFVTSFyWPWQTKVILDGNS-LEKVDPQLVdGHLSYFLGAIGMPGLTSLIGIQEKGHITAGsnKTMVVSG 162
Cdd:cd05288    78 ESRSPDFKVGDLVSGF-LGWQEYAVVDGASgLRKLDPSLG-LPLSAYLGVLGMTGLTAYFGLTEIGKPKPG--ETVVVSA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 163 AAGACGSVAGQIGHFLGCsRVVGICGTHEKCILLTSELGFDAAINYKKDNVAEQLRESCPAGVDVYFDNVGGNISDTVIS 242
Cdd:cd05288   154 AAGAVGSVVGQIAKLLGA-RVVGIAGSDEKCRWLVEELGFDAAINYKTPDLAEALKEAAPDGIDVYFDNVGGEILDAALT 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 243 QMNENSHIILCGQISQYNKDVPYPPPLSPAIeaiqKERNITRERFLVLNYKDKFEPGILQLSQWFKEGKLKIKETVINGL 322
Cdd:cd05288   233 LLNKGGRIALCGAISQYNATEPPGPKNLGNI----ITKRLTMQGFIVSDYADRFPEALAELAKWLAEGKLKYREDVVEGL 308

                         330       340
                  ....*....|....*....|.
gi 1700447654 323 ENMGAAFQSMMTGGNIGKQIV 343
Cdd:cd05288   309 ENAPEAFLGLFTGKNTGKLVV 329
CurA COG2130
NADPH-dependent curcumin reductase CurA [Secondary metabolites biosynthesis, transport and ...
 1-343 2.31e-150

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


Pssm-ID: 441733 [Multi-domain]  Cd Length: 333  Bit Score: 426.40  E-value: 2.31e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654   1 MIVQRVVLNSRPgkNGNPVAENFRMEEVYLPDnINEGQVQVRTLYLSVDPYMRCRMNEdtGTDYITPWQLSQVVDGGGIG 80
Cdd:COG2130     3 TTNRQIVLASRP--EGEPTPEDFRLEEVPVPE-PGDGEVLVRNLYLSVDPYMRGRMSD--AKSYAPPVELGEVMRGGAVG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654  81 IIEESKHTNLTKGDFVTSFyWPWQTKVILDGNSLEKVDPQLVdgHLSYFLGAIGMPGLTSLIGIQEKGHITAGsnKTMVV 160
Cdd:COG2130    78 EVVESRHPDFAVGDLVLGM-LGWQDYAVSDGAGLRKVDPSLA--PLSAYLGVLGMPGLTAYFGLLDIGKPKAG--ETVVV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 161 SGAAGACGSVAGQIGHFLGCsRVVGICGTHEKCILLTSELGFDAAINYKKDNVAEQLRESCPAGVDVYFDNVGGNISDTV 240
Cdd:COG2130   153 SAAAGAVGSVVGQIAKLKGC-RVVGIAGGAEKCRYLVEELGFDAAIDYKAGDLAAALAAACPDGIDVYFDNVGGEILDAV 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 241 ISQMNENSHIILCGQISQYNKDvpyPPPLSPAIEAIQKERNITRERFLVLNYKDKFEPGILQLSQWFKEGKLKIKETVIN 320
Cdd:COG2130   232 LPLLNTFARIAVCGAISQYNAT---EPPPGPRNLGQLLVKRLRMQGFIVFDHADRFPEFLAELAGWVAEGKLKYRETVVE 308

                         330       340
                  ....*....|....*....|...
gi 1700447654 321 GLENMGAAFQSMMTGGNIGKQIV 343
Cdd:COG2130   309 GLENAPEAFLGLFEGENFGKLLV 331
leukotriene_B4_DH_like cd08294
13-PGR is a bifunctional enzyme with delta-13 15-prostaglandin reductase and leukotriene B4 12 ...
 15-343 4.79e-98

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: 293.40  E-value: 4.79e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654  15 NGNPVAENFRMEEVYLPdNINEGQVQVRTLYLSVDPYMRCrmnedtgtdYITPWQLSQVVDGGGIGIIEESKHTNLTKGD 94
Cdd:cd08294    13 DGKPKESDFELVEEELP-PLKDGEVLCEALFLSVDPYMRP---------YSKRLNEGDTMIGTQVAKVIESKNSKFPVGT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654  95 FVTSFYwPWQTKVILDG---NSLEKVDPQLVDG-HLSYFLGAIGMPGLTSLIGIQEKGHITAGsnKTMVVSGAAGACGSV 170
Cdd:cd08294    83 IVVASF-GWRTHTVSDGkdqPDLYKLPADLPDDlPPSLALGVLGMPGLTAYFGLLEICKPKAG--ETVVVNGAAGAVGSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 171 AGQIGHFLGCsRVVGICGTHEKCILLtSELGFDAAINYKKDNVAEQLRESCPAGVDVYFDNVGGNISDTVISQMNENSHI 250
Cdd:cd08294   160 VGQIAKIKGC-KVIGCAGSDDKVAWL-KELGFDAVFNYKTVSLEEALKEAAPDGIDCYFDNVGGEFSSTVLSHMNDFGRV 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 251 ILCGQISQYN-KDVPYPPPLSPAIeaIQKErnITRERFLVLNYKDKFEPGILQLSQWFKEGKLKIKETVINGLENMGAAF 329
Cdd:cd08294   238 AVCGSISTYNdKEPKKGPYVQETI--IFKQ--LKMEGFIVYRWQDRWPEALKQLLKWIKEGKLKYREHVTEGFENMPQAF 313

                         330
                  ....*....|....
gi 1700447654 330 QSMMTGGNIGKQIV 343
Cdd:cd08294   314 IGMLKGENTGKAIV 327
double_bond_reductase_like cd08295
Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase; This ...
 15-343 2.93e-84

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


Pssm-ID: 176255 [Multi-domain]  Cd Length: 338  Bit Score: 258.40  E-value: 2.93e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654  15 NGNPVAENFRMEEVYLP---DNINEGQVQVRTLYLSVDPYMRCRMNEDTGTDYITPWQLSQVVDGGGIGIIEESKHTNLT 91
Cdd:cd08295    13 TGFPKESDLELRTTKLTlkvPPGGSGDVLVKNLYLSCDPYMRGRMKGHDDSLYLPPFKPGEVITGYGVAKVVDSGNPDFK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654  92 KGDFVTSFYwPWQTKVILD-GNSLEKVDPQLVDghLSYFLGAIGMPGLTSLIGIQEKGHITAGSnkTMVVSGAAGACGSV 170
Cdd:cd08295    93 VGDLVWGFT-GWEEYSLIPrGQDLRKIDHTDVP--LSYYLGLLGMPGLTAYAGFYEVCKPKKGE--TVFVSAASGAVGQL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 171 AGQIGHFLGCsRVVGICGTHEKCILLTSELGFDAAINYKKD-NVAEQLRESCPAGVDVYFDNVGGNISDTVISQMNENSH 249
Cdd:cd08295   168 VGQLAKLKGC-YVVGSAGSDEKVDLLKNKLGFDDAFNYKEEpDLDAALKRYFPNGIDIYFDNVGGKMLDAVLLNMNLHGR 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 250 IILCGQISQYNKDVPYPPPlsPAIEAIQKErnITRERFLVLNYKDKFEPGILQLSQWFKEGKLKIKETVINGLENMGAAF 329
Cdd:cd08295   247 IAACGMISQYNLEWPEGVR--NLLNIIYKR--VKIQGFLVGDYLHRYPEFLEEMSGYIKEGKLKYVEDIADGLESAPEAF 322

                         330
                  ....*....|....
gi 1700447654 330 QSMMTGGNIGKQIV 343
Cdd:cd08295   323 VGLFTGSNIGKQVV 336
B4_12hDH TIGR02825
leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 ...
 16-343 2.56e-73

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


Pssm-ID: 131872 [Multi-domain]  Cd Length: 325  Bit Score: 230.27  E-value: 2.56e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654  16 GNPVAENFRMEEVYLPDnINEGQVQVRTLYLSVDPYMRCRMNEDTGTDYITPWQLSQVVdgggigiieESKHTNLTKGDF 95
Cdd:TIGR02825  12 GYPTDSDFELKTVELPP-LNNGEVLLEALFLSVDPYMRVAAKRLKEGDTMMGQQVARVV---------ESKNVALPKGTI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654  96 VTSfYWPWQTKVILDGNSLEKVDPQLVDG-HLSYFLGAIGMPGLTSLIGIQEKGHITAGsnKTMVVSGAAGACGSVAGQI 174
Cdd:TIGR02825  82 VLA-SPGWTSHSISDGKDLEKLLTEWPDTlPLSLALGTVGMPGLTAYFGLLEICGVKGG--ETVMVNAAAGAVGSVVGQI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 175 GHFLGCsRVVGICGTHEKCILLtSELGFDAAINYKK-DNVAEQLRESCPAGVDVYFDNVGGNISDTVISQMNENSHIILC 253
Cdd:TIGR02825 159 AKLKGC-KVVGAAGSDEKVAYL-KKLGFDVAFNYKTvKSLEETLKKASPDGYDCYFDNVGGEFSNTVIGQMKKFGRIAIC 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 254 GQISQYNKDVPYPPPLSPAIEAIQKERnitRERFLVLNYK-DKFEPGILQLSQWFKEGKLKIKETVINGLENMGAAFQSM 332
Cdd:TIGR02825 237 GAISTYNRTGPLPPGPPPEIVIYQELR---MEGFIVNRWQgEVRQKALKELLKWVLEGKIQYKEYVIEGFENMPAAFMGM 313

                         330
                  ....*....|.
gi 1700447654 333 MTGGNIGKQIV 343
Cdd:TIGR02825 314 LKGENLGKTIV 324
PLN03154 PLN03154
putative allyl alcohol dehydrogenase; Provisional
 41-348 1.81e-53

putative allyl alcohol dehydrogenase; Provisional


Pssm-ID: 215606 [Multi-domain]  Cd Length: 348  Bit Score: 179.65  E-value: 1.81e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654  41 VRTLYLSVDPYMRCRMNEDTGTdYITPWQLSQVVDGGGIGIIEESKHTNLTKGDFVTSFYwPWQTKVILDGNSLEKVDPQ 120
Cdd:PLN03154   48 VKNLYLSCDPYMRGRMRDFHDS-YLPPFVPGQRIEGFGVSKVVDSDDPNFKPGDLISGIT-GWEEYSLIRSSDNQLRKIQ 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 121 LVDG-HLSYFLGAIGMPGLTSLIGIQEKGHITAGSNktMVVSGAAGACGSVAGQIGHFLGCSrVVGICGTHEKCILLTSE 199
Cdd:PLN03154  126 LQDDiPLSYHLGLLGMAGFTAYAGFYEVCSPKKGDS--VFVSAASGAVGQLVGQLAKLHGCY-VVGSAGSSQKVDLLKNK 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 200 LGFDAAINYKKD-NVAEQLRESCPAGVDVYFDNVGGNISDTVISQMNENSHIILCGQISQynKDVPYPPPLSPAIEAIQK 278
Cdd:PLN03154  203 LGFDEAFNYKEEpDLDAALKRYFPEGIDIYFDNVGGDMLDAALLNMKIHGRIAVCGMVSL--NSLSASQGIHNLYNLISK 280

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 279 ErnITRERFLVLNYKDKFEPGILQLSQWFKEGKLKIKETVINGLENMGAAFQSMMTGGNIGKQIVCISEE 348
Cdd:PLN03154  281 R--IRMQGFLQSDYLHLFPQFLENVSRYYKQGKIVYIEDMSEGLESAPAALVGLFSGKNVGKQVIRVAKE 348
Mgc45594_like cd08250
Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of ...
 137-344 2.87e-35

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: 131.23  E-value: 2.87e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 137 GLTSLIGIQEKGHITagSNKTMVVSGAAGACGSVAGQIGHFLGCsRVVGICGTHEKCILLTSeLGFDAAINYKKDNVAEQ 216
Cdd:cd08250   124 GLTASIALEEVGEMK--SGETVLVTAAAGGTGQFAVQLAKLAGC-HVIGTCSSDEKAEFLKS-LGCDRPINYKTEDLGEV 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 217 LRESCPAGVDVYFDNVGGNISDTVISQMNENSHIILCGQISQYNKDVPYPPPLSPAIEAIQKERNITRERFLVLNYKDKF 296
Cdd:cd08250   200 LKKEYPKGVDVVYESVGGEMFDTCVDNLALKGRLIVIGFISGYQSGTGPSPVKGATLPPKLLAKSASVRGFFLPHYAKLI 279

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1700447654 297 EPGILQLSQWFKEGKLKIK--ETVINGLENMGAAFQSMMTGGNIGKQIVC 344
Cdd:cd08250   280 PQHLDRLLQLYQRGKLVCEvdPTRFRGLESVADAVDYLYSGKNIGKVVVE 329
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 14-345 3.43e-35

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: 130.65  E-value: 3.43e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654  14 KNGNPvaENFRMEEVYLPDnINEGQVQVRTLYLSVDP---YMRcrmnedTGTdYITPWQLSQVVdggGI---GIIEESKH 87
Cdd:COG0604     8 EFGGP--EVLELEEVPVPE-PGPGEVLVRVKAAGVNPadlLIR------RGL-YPLPPGLPFIP---GSdaaGVVVAVGE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654  88 --TNLTKGDFVtsFYWP----WQTKVILDGNSLEKVdPQlvdgHLSYFLGA-IGMPGLTSLIGIQEKGHITAGsnKTMVV 160
Cdd:COG0604    75 gvTGFKVGDRV--AGLGrgggYAEYVVVPADQLVPL-PD----GLSFEEAAaLPLAGLTAWQALFDRGRLKPG--ETVLV 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 161 SGAAGACGSVAGQIGHFLGCsRVVGICGTHEKCILLTsELGFDAAINYKKDNVAEQLRE-SCPAGVDVYFDNVGGNISDT 239
Cdd:COG0604   146 HGAAGGVGSAAVQLAKALGA-RVIATASSPEKAELLR-ALGADHVIDYREEDFAERVRAlTGGRGVDVVLDTVGGDTLAR 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 240 VISQMNENSHIILCGQISqynkdvPYPPPLSPAiEAIQKERNITRErFLVLNYKDKFEPGILQLSQWFKEGKLKIKETVI 319
Cdd:COG0604   224 SLRALAPGGRLVSIGAAS------GAPPPLDLA-PLLLKGLTLTGF-TLFARDPAERRAALAELARLLAAGKLRPVIDRV 295

                         330       340
                  ....*....|....*....|....*.
gi 1700447654 320 NGLENMGAAFQSMMTGGNIGKQIVCI 345
Cdd:COG0604   296 FPLEEAAEAHRLLESGKHRGKVVLTV 321
ADH_N_2 pfam16884
N-terminal domain of oxidoreductase; N-terminal region of oxidoreductase and prostaglandin ...
 5-117 4.54e-35

N-terminal domain of oxidoreductase; N-terminal region of oxidoreductase and prostaglandin reductase and alcohol dehydrogenase.


Pssm-ID: 465297 [Multi-domain]  Cd Length: 108  Bit Score: 123.85  E-value: 4.54e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654   5 RVVLNSRPgkNGNPVAENFRMEEVYLPDnINEGQVQVRTLYLSVDPYMRCRMNEDTGtdYITPWQLSQVVDGGGIGIIEE 84
Cdd:pfam16884   2 QWLLAKRP--EGVPTPSDFELVEAELPE-LGDGEVLVRTLYLSVDPYMRGRMNDAKS--YVPPVELGDVMRGGAVGEVVE 76

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1700447654  85 SKHTNLTKGDFVTSFyWPWQTKVILDGNSLEKV 117
Cdd:pfam16884  77 SNNPDFPVGDLVLGM-LGWQDYAVSDGKGLTKV 108
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
 80-344 2.45e-22

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: 95.64  E-value: 2.45e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654  80 GIIEE--SKHTNLTKGDFVTSFYWP--WQTKVILDGNSLEKVdPQLVDghlsyFLGAIGMP--GLTSLIGIQEKGHITAG 153
Cdd:cd08241    67 GVVEAvgEGVTGFKVGDRVVALTGQggFAEEVVVPAAAVFPL-PDGLS-----FEEAAALPvtYGTAYHALVRRARLQPG 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 154 snKTMVVSGAAGACGSVAGQIGHFLGCsRVVGICGTHEKCILLtSELGFDAAINYKKDNVAEQLRESC-PAGVDVYFDNV 232
Cdd:cd08241   141 --ETVLVLGAAGGVGLAAVQLAKALGA-RVIAAASSEEKLALA-RALGADHVIDYRDPDLRERVKALTgGRGVDVVYDPV 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 233 GGNISDTVISQMNENSHIILCGQISqynKDVPYPPPLSPAIeaiqkeRNIT----RERFLVLNYKDKFEPGILQLSQWFK 308
Cdd:cd08241   217 GGDVFEASLRSLAWGGRLLVIGFAS---GEIPQIPANLLLL------KNISvvgvYWGAYARREPELLRANLAELFDLLA 287

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1700447654 309 EGKLKIKETVINGLENMGAAFQSMMTGGNIGKQIVC 344
Cdd:cd08241   288 EGKIRPHVSAVFPLEQAAEALRALADRKATGKVVLT 323
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 16-343 1.54e-19

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


Pssm-ID: 176228 [Multi-domain]  Cd Length: 319  Bit Score: 87.66  E-value: 1.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654  16 GNPVAENFRMEEVYLPDnINEGQVQVRTLYLSVDP------------YMRCRMNEDTGTDyitpwqLS-QVVDGGgigii 82
Cdd:cd08267     7 GSPEVLLLLEVEVPIPT-PKPGEVLVKVHAASVNPvdwklrrgppklLLGRPFPPIPGMD------FAgEVVAVG----- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654  83 eeSKHTNLTKGDFVTSFYWPWQTK-----VILDGNSLEKVDPQLvdghlSYFLGA-IGMPGLTSLIGIQEKGHITAGSNk 156
Cdd:cd08267    75 --SGVTRFKVGDEVFGRLPPKGGGalaeyVVAPESGLAKKPEGV-----SFEEAAaLPVAGLTALQALRDAGKVKPGQR- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 157 tMVVSGAAGACGSVAGQIGHFLGCsRVVGICGTH--EkciLLTSeLGFDAAINYKKDNVAEqlrESCPAGV-DVYFDNVG 233
Cdd:cd08267   147 -VLINGASGGVGTFAVQIAKALGA-HVTGVCSTRnaE---LVRS-LGADEVIDYTTEDFVA---LTAGGEKyDVIFDAVG 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 234 GNISDTVISQMNENSH---IILCGQIS---QYNKDVPYPPPLSPaieaiQKernitRERFLVLNYKDKFEpgilQLSQWF 307
Cdd:cd08267   218 NSPFSLYRASLALKPGgryVSVGGGPSgllLVLLLLPLTLGGGG-----RR-----LKFFLAKPNAEDLE----QLAELV 283

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1700447654 308 KEGKLKikeTVIN---GLENMGAAFQSMMTGGNIGKQIV 343
Cdd:cd08267   284 EEGKLK---PVIDsvyPLEDAPEAYRRLKSGRARGKVVI 319
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
 20-343 1.21e-17

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: 82.22  E-value: 1.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654  20 AENFRMEEVYLPDnINEGQVQVRTLYLSVDPY---MRcrmneDTGTDYITPWQLSQVVDGGGIGIIEE--SKHTNLTKGD 94
Cdd:cd05289    12 PEVLELADVPTPE-PGPGEVLVKVHAAGVNPVdlkIR-----EGLLKAAFPLTLPLIPGHDVAGVVVAvgPGVTGFKVGD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654  95 --FVTSFYWPWQT---KVILDGNSLEKVDPqlvdgHLSyFL--GAIGMPGLTSLIGIQEKGHITAGsnKTMVVSGAAGAC 167
Cdd:cd05289    86 evFGMTPFTRGGAyaeYVVVPADELALKPA-----NLS-FEeaAALPLAGLTAWQALFELGGLKAG--QTVLIHGAAGGV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 168 GSVAGQIGHFLGCsRVVGICGT--HEkciLLTSeLGFDAAINYKKDNVAEQLRescPAGVDVYFDNVGGNISDTVISQMN 245
Cdd:cd05289   158 GSFAVQLAKARGA-RVIATASAanAD---FLRS-LGADEVIDYTKGDFERAAA---PGGVDAVLDTVGGETLARSLALVK 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 246 ENSHIIlcgqisqynkDVPYPPPlspaIEAIQKERNITRERFLVLNYKDKFEpgilQLSQWFKEGKLKIKETVINGLENM 325
Cdd:cd05289   230 PGGRLV----------SIAGPPP----AEQAAKRRGVRAGFVFVEPDGEQLA----ELAELVEAGKLRPVVDRVFPLEDA 291

                         330
                  ....*....|....*...
gi 1700447654 326 GAAFQSMMTGGNIGKQIV 343
Cdd:cd05289   292 AEAHERLESGHARGKVVL 309
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
 20-343 1.98e-17

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: 81.86  E-value: 1.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654  20 AENFRMEEVYLPDnINEGQVQVRTLYLSVDP---YMRcrmnedTGTdYITPWQLSQVVDGGGIGIIEESKH--TNLTKGD 94
Cdd:cd08253    12 PDVLRLGDLPVPT-PGPGEVLVRVHASGVNPvdtYIR------AGA-YPGLPPLPYVPGSDGAGVVEAVGEgvDGLKVGD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654  95 --FVTSFYWPWQTkvildGNSLEKV---DPQLV---DGhLSYFLGA-IGMPGLTSLIGIQEKGHITAGsnKTMVVSGAAG 165
Cdd:cd08253    84 rvWLTNLGWGRRQ-----GTAAEYVvvpADQLVplpDG-VSFEQGAaLGIPALTAYRALFHRAGAKAG--ETVLVHGGSG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 166 ACGSVAGQIGHFLGCsRVVGICGTHEKcILLTSELGFDAAINYKKDNVAEQLRESC-PAGVDVYFDNVGGNISDTVISQM 244
Cdd:cd08253   156 AVGHAAVQLARWAGA-RVIATASSAEG-AELVRQAGADAVFNYRAEDLADRILAATaGQGVDVIIEVLANVNLAKDLDVL 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 245 NENSHIILCGqisqyNKDVPYPPPLSPaieAIQKERNItreRFLVLnY---KDKFEPGILQLSQWFKEGKLKIKETVING 321
Cdd:cd08253   234 APGGRIVVYG-----SGGLRGTIPINP---LMAKEASI---RGVLL-YtatPEERAAAAEAIAAGLADGALRPVIAREYP 301

                         330       340
                  ....*....|....*....|..
gi 1700447654 322 LENMGAAFQSMMTGGNIGKQIV 343
Cdd:cd08253   302 LEEAAAAHEAVESGGAIGKVVL 323
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 78-283 1.10e-14

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: 73.12  E-value: 1.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654  78 GIGIIEE--SKHTNLTKGDFVTSFYWP-------------------------WQTKVILDGNSLEKVDPqlvdgHLSYFL 130
Cdd:cd05188    37 GAGVVVEvgPGVTGVKVGDRVVVLPNLgcgtcelcrelcpgggilgegldggFAEYVVVPADNLVPLPD-----GLSLEE 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 131 GA-IGMPGLTSLIGIQEKGHITAGSnkTMVVSGAaGACGSVAGQIGHFLGCsRVVGICGTHEKcILLTSELGFDAAINYK 209
Cdd:cd05188   112 AAlLPEPLATAYHALRRAGVLKPGD--TVLVLGA-GGVGLLAAQLAKAAGA-RVIVTDRSDEK-LELAKELGADHVIDYK 186

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1700447654 210 KDNVAEQLRESCPAGVDVYFDNVGGNIS-DTVISQMNENSHIILCGQISQynkdvpyPPPLSPAIEAIQKERNIT 283
Cdd:cd05188   187 EEDLEEELRLTGGGGADVVIDAVGGPETlAQALRLLRPGGRIVVVGGTSG-------GPPLDDLRRLLFKELTII 254
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 131-345 2.92e-14

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: 72.59  E-value: 2.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 131 GAIGMPGLTSLIGIQEKGHITAGsnKTMVVSGAAGACGSVAGQIGHFLGCsRVVGICGTHEKCILltSELGFDAAINYKK 210
Cdd:cd08272   123 AALPLVGITAWEGLVDRAAVQAG--QTVLIHGGAGGVGHVAVQLAKAAGA-RVYATASSEKAAFA--RSLGADPIIYYRE 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 211 DNVAEQLRESCPAGVDVYFDNVGGNISDTVISQMNENSHIILCGQISQYNkdvpypppLSPAieaiqKERNITRE----- 285
Cdd:cd08272   198 TVVEYVAEHTGGRGFDVVFDTVGGETLDASFEAVALYGRVVSILGGATHD--------LAPL-----SFRNATYSgvftl 264

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1700447654 286 RFLVLNYKDKFEPGIL-QLSQWFKEGKLK--IKETVInGLENMGAAFQSMMTGGNIGKQIVCI 345
Cdd:cd08272   265 LPLLTGEGRAHHGEILrEAARLVERGQLRplLDPRTF-PLEEAAAAHARLESGSARGKIVIDV 326
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
 37-342 6.86e-14

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: 71.54  E-value: 6.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654  37 GQVQVRTLYLSVDPymrcrmnedtgTDYIT-------PWQLSQVVDGGGIGIIEE--SKHTNLTKGDFVTSFYWP--WQT 105
Cdd:cd05282    27 GEVLVRMLAAPINP-----------SDLITisgaygsRPPLPAVPGNEGVGVVVEvgSGVSGLLVGQRVLPLGGEgtWQE 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 106 KVILDGNSLEKVDPQLVDGHLSYF----LGAIGMpgLTSLIGIQEKGHItagsnktmVVSGAAGACGSVAGQIGHFLGCs 181
Cdd:cd05282    96 YVVAPADDLIPVPDSISDEQAAMLyinpLTAWLM--LTEYLKLPPGDWV--------IQNAANSAVGRMLIQLAKLLGF- 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 182 RVVGIcGTHEKCILLTSELGFDAAINYKKDNVAEQLRE-SCPAGVDVYFDNVGGNISDTVISQMNENSHIILCGQISqyN 260
Cdd:cd05282   165 KTINV-VRRDEQVEELKALGADEVIDSSPEDLAQRVKEaTGGAGARLALDAVGGESATRLARSLRPGGTLVNYGLLS--G 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 261 KDVPYPPplspaieAIQKERNITRERFLVLNYKDKFEPGILQ-----LSQWFKEGKLKIKETVINGLENMGAAFQSMMTG 335
Cdd:cd05282   242 EPVPFPR-------SVFIFKDITVRGFWLRQWLHSATKEAKQetfaeVIKLVEAGVLTTPVGAKFPLEDFEEAVAAAEQP 314


                  ....*..
gi 1700447654 336 GNIGKQI 342
Cdd:cd05282   315 GRGGKVL 321
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
 14-234 1.23e-13

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: 70.55  E-value: 1.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654  14 KNGNPvaENFRMEEVYLPDnINEGQVQVRTLYLSV---DPYMRcrmnedTGTdYitPWQLSQVVDGGGIGIIEE--SKHT 88
Cdd:cd05286     7 KTGGP--EVLEYEDVPVPE-PGPGEVLVRNTAIGVnfiDTYFR------SGL-Y--PLPLPFVLGVEGAGVVEAvgPGVT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654  89 NLTKGDFVTSFYWP--WQTKVILDGNSLEKVdPQLVDGHLSyflGAIGMPGLTSLIGIQEKGHITAGSnkTMVVSGAAGA 166
Cdd:cd05286    75 GFKVGDRVAYAGPPgaYAEYRVVPASRLVKL-PDGISDETA---AALLLQGLTAHYLLRETYPVKPGD--TVLVHAAAGG 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1700447654 167 CGSVAGQIGHFLGCsRVVGICGTHEKCILLTsELGFDAAINYKKDNVAEQLRE-SCPAGVDVYFDNVGG 234
Cdd:cd05286   149 VGLLLTQWAKALGA-TVIGTVSSEEKAELAR-AAGADHVINYRDEDFVERVREiTGGRGVDVVYDGVGK 215
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 132-271 1.36e-12

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


Pssm-ID: 176232 [Multi-domain]  Cd Length: 325  Bit Score: 67.69  E-value: 1.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 132 AIGMPGLTSLIGIQEKGHITAGsnKTMVVSGAAGACGSVAGQIGHFLGcSRVVGICGT--HEKcillTSELGFDAAINYK 209
Cdd:cd08271   121 ALPCAGLTAYQALFKKLRIEAG--RTILITGGAGGVGSFAVQLAKRAG-LRVITTCSKrnFEY----VKSLGADHVIDYN 193

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1700447654 210 KDNVAEQLRESC-PAGVDVYFDNVGGNISDTVISQMNENSHIIlCGQisqynkDVPYPPPLSP 271
Cdd:cd08271   194 DEDVCERIKEITgGRGVDAVLDTVGGETAAALAPTLAFNGHLV-CIQ------GRPDASPDPP 249
ADH_zinc_N_2 pfam13602
Zinc-binding dehydrogenase;
200-343 1.03e-11

Zinc-binding dehydrogenase;


Pssm-ID: 433341 [Multi-domain]  Cd Length: 131  Bit Score: 61.58  E-value: 1.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 200 LGFDAAINYKKDNVAEQLresCPAGVDVYFDNVGGNISDTVISQMNENSHIILCGQisqynkdvpypPPLSPAIEAIQKE 279
Cdd:pfam13602   1 LGADEVIDYRTTDFVQAT---GGEGVDVVLDTVGGEAFEASLRVLPGGGRLVTIGG-----------PPLSAGLLLPARK 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1700447654 280 RNITRERFLVLNYKDKFEPGIL-QLSQWFKEGKLKIketVIN---GLENMGAAFQSMMTGGNIGKqIV 343
Cdd:pfam13602  67 RGGRGVKYLFLFVRPNLGADILqELADLIEEGKLRP---VIDrvfPLEEAAEAHRYLESGRARGK-IV 130
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
 148-234 3.96e-11

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: 63.23  E-value: 3.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 148 GHITAGsnKTMVVSGAAGACGSVAGQIGHFLGCsRVVGICGTHEKCILLTsELGFDAAINYKKDNVAEQLRE-SCPAGVD 226
Cdd:cd05276   135 GGLKAG--ETVLIHGGASGVGTAAIQLAKALGA-RVIATAGSEEKLEACR-ALGADVAINYRTEDFAEEVKEaTGGRGVD 210


                  ....*...
gi 1700447654 227 VYFDNVGG 234
Cdd:cd05276   211 VILDMVGG 218
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 80-343 4.66e-11

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


Pssm-ID: 176236 [Multi-domain]  Cd Length: 337  Bit Score: 62.99  E-value: 4.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654  80 GIIEE--SKHTNLTKGDFVTSFYW--PWQTKVILDGNSLEKVdPQlvdgHLSYFLGA-IGMPGLTSLIGIQEKGHITAGs 154
Cdd:cd08275    66 GTVEAvgEGVKDFKVGDRVMGLTRfgGYAEVVNVPADQVFPL-PD----GMSFEEAAaFPVNYLTAYYALFELGNLRPG- 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 155 nKTMVVSGAAGACGSVAGQIGHFLgcsRVVGICGT-----HEKcillTSELGFDAAINYKKDNVAEQLRESCPAGVDVYF 229
Cdd:cd08275   140 -QSVLVHSAAGGVGLAAGQLCKTV---PNVTVVGTasaskHEA----LKENGVTHVIDYRTQDYVEEVKKISPEGVDIVL 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 230 DNVGGniSDTVISQmnenSHIILCGQISQYN----------------KDVPYPPPLSPaIEAIqkERNITRERF---LVL 290
Cdd:cd08275   212 DALGG--EDTRKSY----DLLKPMGRLVVYGaanlvtgekrswfklaKKWWNRPKVDP-MKLI--SENKSVLGFnlgWLF 282

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1700447654 291 NYKDKFEPGILQLSQWFKEGKLKIKETVINGLENMGAAFQSMMTGGNIGKQIV 343
Cdd:cd08275   283 EERELLTEVMDKLLKLYEEGKIKPKIDSVFPFEEVGEAMRRLQSRKNIGKVVL 335
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
168-254 3.72e-10

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 57.23  E-value: 3.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 168 GSVAGQIGHFLGCsRVVGICGTHEKCILLtSELGFDAAINYKKDNVAEQLRESC-PAGVDVYFDNVGGNIS-DTVISQMN 245
Cdd:pfam00107   3 GLAAIQLAKAAGA-KVIAVDGSEEKLELA-KELGADHVINPKETDLVEEIKELTgGKGVDVVFDCVGSPATlEQALKLLR 80


                  ....*....
gi 1700447654 246 ENSHIILCG 254
Cdd:pfam00107  81 PGGRVVVVG 89
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 132-343 8.09e-10

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: 59.15  E-value: 8.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 132 AIGMPGLTSLIGIQEKGHITAGsnKTMVVSGAAGACGSVAGQIGHFLGcSRVVGICGTHEKCILLtSELGFDAAINYKKD 211
Cdd:cd08268   124 ALWMQYLTAYGALVELAGLRPG--DSVLITAASSSVGLAAIQIANAAG-ATVIATTRTSEKRDAL-LALGAAHVIVTDEE 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 212 NVAEQLRE-SCPAGVDVYFDNVGGNISDTVISQMNENSHIILCGQISqynkdvPYPPPLsPAIEAIQKerNITRERFLVL 290
Cdd:cd08268   200 DLVAEVLRiTGGKGVDVVFDPVGGPQFAKLADALAPGGTLVVYGALS------GEPTPF-PLKAALKK--SLTFRGYSLD 270

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1700447654 291 NYK---DKFEPGILQLSQWFKEGKLKIKETVINGLENMGAAFQSMMTGGNIGKQIV 343
Cdd:cd08268   271 EITldpEARRRAIAFILDGLASGALKPVVDRVFPFDDIVEAHRYLESGQQIGKIVV 326
MDR_enoyl_red cd08244
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. ...
 132-236 2.65e-09

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: 57.76  E-value: 2.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 132 AIGMPGLTSLiGIQEKGHITAGSnkTMVVSGAAGACGSVAGQIGHFLGcSRVVGICGTHEKCILLTsELGFDAAINYKKD 211
Cdd:cd08244   123 AVVHDGRTAL-GLLDLATLTPGD--VVLVTAAAGGLGSLLVQLAKAAG-ATVVGAAGGPAKTALVR-ALGADVAVDYTRP 197

                          90       100
                  ....*....|....*....|....*.
gi 1700447654 212 NVAEQLRESCPA-GVDVYFDNVGGNI 236
Cdd:cd08244   198 DWPDQVREALGGgGVTVVLDGVGGAI 223
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
 125-343 6.51e-09

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: 56.85  E-value: 6.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 125 HLSyFLGAIGMP--GLTSLIGIQEKGHI--TAGSNKTMVVSGAAGACGSVAGQIGHFLGCsRVVGICgtHEKCILLTSEL 200
Cdd:cd08248   130 NLS-HEEAASLPyaGLTAWSALVNVGGLnpKNAAGKRVLILGGSGGVGTFAIQLLKAWGA-HVTTTC--STDAIPLVKSL 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 201 GFDAAINYKKDNVAEQLRESCPagVDVYFDNVGGNISDTVISQMNENSHIILCGQISQYNKDvPYPPPLSPAIEAIQKER 280
Cdd:cd08248   206 GADDVIDYNNEDFEEELTERGK--FDVILDTVGGDTEKWALKLLKKGGTYVTLVSPLLKNTD-KLGLVGGMLKSAVDLLK 282

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 281 NITRERFLVLNYKDKF----EPGILQLSQWFKEGKLKikeTVIN---GLENMGAAFQSMMTGGNIGKQIV 343
Cdd:cd08248   283 KNVKSLLKGSHYRWGFfspsGSALDELAKLVEDGKIK---PVIDkvfPFEEVPEAYEKVESGHARGKTVI 349
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
 157-343 8.40e-08

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: 53.03  E-value: 8.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 157 TMVVSGAAGACGSVAGQIGHFLGCsRVVGICGTHEKcILLTSELGFDAAINYKKDNVAEQLRESCPA-GVDVYFDNVGGN 235
Cdd:cd08266   169 TVLVHGAGSGVGSAAIQIAKLFGA-TVIATAGSEDK-LERAKELGADYVIDYRKEDFVREVRELTGKrGVDVVVEHVGAA 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 236 ISDTVISQMNENSHIILCGQISQY--NKDVPYppplspaieAIQKERNI------TRERFlvlnykdkfepgiLQLSQWF 307
Cdd:cd08266   247 TWEKSLKSLARGGRLVTCGATTGYeaPIDLRH---------VFWRQLSIlgstmgTKAEL-------------DEALRLV 304

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1700447654 308 KEGKLKikeTVIN---GLENMGAAFQSMMTGGNIGKQIV 343
Cdd:cd08266   305 FRGKLK---PVIDsvfPLEEAAEAHRRLESREQFGKIVL 340
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
 125-338 9.93e-07

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: 49.92  E-value: 9.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 125 HLSYFLGAIGMPGLTSLIGIqEKGHITAGsnKTMVVSGAaGACGSVAGQIGHFLGCSRVVGICGTHEKCILLTsELGFDA 204
Cdd:cd08236   133 HVDYEEAAMIEPAAVALHAV-RLAGITLG--DTVVVIGA-GTIGLLAIQWLKILGAKRVIAVDIDDEKLAVAR-ELGADD 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 205 AINYKKDNVaEQLRESCPA-GVDVYFDNVGGNIS-DTVISQMNENSHIILCGqisqynkdVPYPPPLSPAIEAiqkeRNI 282
Cdd:cd08236   208 TINPKEEDV-EKVRELTEGrGADLVIEAAGSPATiEQALALARPGGKVVLVG--------IPYGDVTLSEEAF----EKI 274

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1700447654 283 TRERFLVL---NYKDKFEPGilqlSQW------FKEGKLKIKE--TVINGLENMGAAFQsMMTGGNI 338
Cdd:cd08236   275 LRKELTIQgswNSYSAPFPG----DEWrtaldlLASGKIKVEPliTHRLPLEDGPAAFE-RLADREE 336
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 146-256 1.03e-05

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: 46.91  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 146 EKGHITAGsnKTMVVSGAAGACGSVAGQIGHFLGcSRVVGICGTHEKCILLtsELGFDAAInYKKDNVAEQLRESCPAGV 225
Cdd:cd08274   171 ERAGVGAG--ETVLVTGASGGVGSALVQLAKRRG-AIVIAVAGAAKEEAVR--ALGADTVI-LRDAPLLADAKALGGEPV 244

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1700447654 226 DVYFDNVGGNISDTVISQMNENSHIILCGQI 256
Cdd:cd08274   245 DVVADVVGGPLFPDLLRLLRPGGRYVTAGAI 275
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 155-344 3.17e-05

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: 45.39  E-value: 3.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 155 NKTMVVSGAAGACGSVAGQIGHFLGCsRVVGICGTHEKCILLtSELGFDAAINYKKDNvaEQLREScpAGVDVYFDNVGG 234
Cdd:cd08259   163 GDTVLVTGAGGGVGIHAIQLAKALGA-RVIAVTRSPEKLKIL-KELGADYVIDGSKFS--EDVKKL--GGADVVIELVGS 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 235 NISDTVISQMNENSHIILCGQISqynkdvPYPPPLSPAIeAIQKERNIT-------RERFLVLNYkdkfepgilqlsqwF 307
Cdd:cd08259   237 PTIEESLRSLNKGGRLVLIGNVT------PDPAPLRPGL-LILKEIRIIgsisatkADVEEALKL--------------V 295

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1700447654 308 KEGKLKIKETVINGLENMGAAFQSMMTGGNIGKqIVC 344
Cdd:cd08259   296 KEGKIKPVIDRVVSLEDINEALEDLKSGKVVGR-IVL 331
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
 155-343 5.55e-05

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: 44.34  E-value: 5.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 155 NKTMVVSGAAGACGSVAGQIGHFLGCSrVVGICGTHEKCILLTSeLGFDAAINYKKDNVAEQL-RESCPAGVDVYFDNVG 233
Cdd:cd08251   121 GEHILIQTATGGTGLMAVQLARLKGAE-IYATASSDDKLEYLKQ-LGVPHVINYVEEDFEEEImRLTGGRGVDVVINTLS 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 234 GnisdTVIsQMNENShiilcgqisqynkdvpypppLSP-------AIEAIQKERNITRERF-------------LVLNYK 293
Cdd:cd08251   199 G----EAI-QKGLNC--------------------LAPggryveiAMTALKSAPSVDLSVLsnnqsfhsvdlrkLLLLDP 253

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1700447654 294 DKFEPGILQLSQWFKEGKLKIKETVINGLENMGAAFQSMMTGGNIGKQIV 343
Cdd:cd08251   254 EFIADYQAEMVSLVEEGELRPTVSRIFPFDDIGEAYRYLSDRENIGKVVV 303
oxido_YhdH TIGR02823
putative quinone oxidoreductase, YhdH/YhfP family; This model represents a subfamily of ...
 132-254 9.71e-05

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: 43.70  E-value: 9.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 132 AIGMPGLTSLIGIQ--EKGHITAgSNKTMVVSGAAGACGSVAGQIGHFLGCSrVVGICGTHEKCILLTsELGFDAAINyk 209
Cdd:TIGR02823 122 ALGTAGFTAALSVMalERNGLTP-EDGPVLVTGATGGVGSLAVAILSKLGYE-VVASTGKAEEEDYLK-ELGASEVID-- 196

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1700447654 210 KDNVAEQLR---ESCPAGVdvyFDNVGGNISDTVISQMNENSHIILCG 254
Cdd:TIGR02823 197 REDLSPPGKpleKERWAGA---VDTVGGHTLANVLAQLKYGGAVAACG 241
liver_ADH_like1 cd08281
Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); ...
 112-233 1.28e-04

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: 43.52  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 112 NSLEKVDPQLVDGHLSYFLGAIgmpgLTSLIGIQEKGHITAGSNKTMVVSGAAGAC---GSVAGqighflGCSRVVGIcG 188
Cdd:cd08281   155 RSVVKIDKDVPLEIAALFGCAV----LTGVGAVVNTAGVRPGQSVAVVGLGGVGLSallGAVAA------GASQVVAV-D 223

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1700447654 189 THEKCILLTSELGFDAAINYKKDNVAEQLRESCPAGVDVYFDNVG 233
Cdd:cd08281   224 LNEDKLALARELGATATVNAGDPNAVEQVRELTGGGVDYAFEMAG 268
MDR_yhdh_yhfp cd05280
Yhdh and yhfp-like putative quinone oxidoreductases; Yhdh and yhfp-like putative quinone ...
 132-254 1.33e-04

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: 43.30  E-value: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 132 AIGMPGLT---SLIGIQEKGHITAGSNktMVVSGAAGACGSVAGQIGHFLGCSrVVGICGTHEKCILLTSeLGFDAAINY 208
Cdd:cd05280   123 ILGTAGFTaalSVHRLEDNGQTPEDGP--VLVTGATGGVGSIAVAILAKLGYT-VVALTGKEEQADYLKS-LGASEVLDR 198

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1700447654 209 KK--DNVAEQLRESCPAGVdvyFDNVGGNISDTVISQMNENSHIILCG 254
Cdd:cd05280   199 EDllDESKKPLLKARWAGA---IDTVGGDVLANLLKQTKYGGVVASCG 243
benzyl_alcohol_DH cd08278
Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol ...
 151-244 2.50e-04

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


Pssm-ID: 176239 [Multi-domain]  Cd Length: 365  Bit Score: 42.49  E-value: 2.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 151 TAGSnkTMVVSGAaGACGSVAGQIGHFLGCSRVVGIcGTHEKCILLTSELGFDAAINYKKDNVAEQLRESCPAGVDVYFD 230
Cdd:cd08278   185 RPGS--SIAVFGA-GAVGLAAVMAAKIAGCTTIIAV-DIVDSRLELAKELGATHVINPKEEDLVAAIREITGGGVDYALD 260

                          90
                  ....*....|....
gi 1700447654 231 NVGgniSDTVISQM 244
Cdd:cd08278   261 TTG---VPAVIEQA 271
AL_MDR cd08252
Arginate lyase and other MDR family members; This group contains a structure identified as an ...
 120-226 6.43e-04

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: 40.97  E-value: 6.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 120 QLVD----GH----LSyFLGAIGMPgLTSLI---GIQEKGHIT---AGSNKTMVVSGAAGACGSVAGQIGHFLGCSRVVG 185
Cdd:cd08252   103 QLVDerivGHkpksLS-FAEAAALP-LTSLTaweALFDRLGISedaENEGKTLLIIGGAGGVGSIAIQLAKQLTGLTVIA 180

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1700447654 186 ICG---THEKCIlltsELGFDAAINYKKDnVAEQLRESCPAGVD 226
Cdd:cd08252   181 TASrpeSIAWVK----ELGADHVINHHQD-LAEQLEALGIEPVD 219
AST1_like cd08247
AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast; This group ...
 153-343 6.53e-04

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: 41.10  E-value: 6.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 153 GSNKTMVVSGAAGACGSVAGQIGHF-LGCSRVVGICGthEKCILLTSELGFDAAINYKKDNVAEQLRESCPAG-----VD 226
Cdd:cd08247   150 GPDSKVLVLGGSTSVGRFAIQLAKNhYNIGTVVGTCS--SRSAELNKKLGADHFIDYDAHSGVKLLKPVLENVkgqgkFD 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 227 VYFDNVGGN----ISDTVISQMNENSH-IILCGQ-ISQYNKDVpYPPPLSPAIEAIQKERNItreRFLVLNYK-DKFEPG 299
Cdd:cd08247   228 LILDCVGGYdlfpHINSILKPKSKNGHyVTIVGDyKANYKKDT-FNSWDNPSANARKLFGSL---GLWSYNYQfFLLDPN 303

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1700447654 300 ---ILQLSQWFKEGKLKIKETVINGLENMGAAFQSMMTGGNIGKQIV 343
Cdd:cd08247   304 adwIEKCAELIADGKVKPPIDSVYPFEDYKEAFERLKSNRAKGKVVI 350
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
 137-235 6.62e-04

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: 41.01  E-value: 6.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 137 GLTSLIGIQEK-GHITAGSnkTMVVSGAAGaCGSVAGQIGHFLGCSRVVGICGTHEKcILLTSELGFDAAINyKKDNVAE 215
Cdd:cd05284   151 GLTAYHAVKKAlPYLDPGS--TVVVIGVGG-LGHIAVQILRALTPATVIAVDRSEEA-LKLAERLGADHVLN-ASDDVVE 225

                          90       100
                  ....*....|....*....|.
gi 1700447654 216 QLRES-CPAGVDVYFDNVGGN 235
Cdd:cd05284   226 EVRELtGGRGADAVIDFVGSD 246
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 139-245 9.52e-04

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: 40.66  E-value: 9.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 139 TSLIGIQEKGHITAGsnKTMVVSGAAGAcGSVAGQIGHFLGcSRVVGICGTHEKcILLTSELGFDAAINYKK-DNVAEQL 217
Cdd:cd08260   152 TAFRALVHQARVKPG--EWVAVHGCGGV-GLSAVMIASALG-ARVIAVDIDDDK-LELARELGAVATVNASEvEDVAAAV 226

                          90       100
                  ....*....|....*....|....*...
gi 1700447654 218 RESCPAGVDVYFDNVGgnISDTVISQMN 245
Cdd:cd08260   227 RDLTGGGAHVSVDALG--IPETCRNSVA 252
MDR_yhdh cd08288
Yhdh putative quinone oxidoreductases; Yhdh putative quinone oxidoreductases (QOR). QOR ...
 132-254 2.30e-03

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: 39.44  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700447654 132 AIGMPGLTSLIGIQ--EKGHITAGSNKtMVVSGAAGACGSVAGQIGHFLGcSRVVGICGTHEKCILLTSeLGFDAAINyk 209
Cdd:cd08288   123 AIGTAGFTAMLCVMalEDHGVTPGDGP-VLVTGAAGGVGSVAVALLARLG-YEVVASTGRPEEADYLRS-LGASEIID-- 197

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1700447654 210 KDNVAEQLRescP------AGVdvyFDNVGGNISDTVISQMNENSHIILCG 254
Cdd:cd08288   198 RAELSEPGR---PlqkerwAGA---VDTVGGHTLANVLAQTRYGGAVAACG 242
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH