|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
5-303 |
3.71e-180 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381380 [Multi-domain] Cd Length: 303 Bit Score: 499.63 E-value: 3.71e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 5 VPIFTLSNGVLMPSIGLGTWQMTGEEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAELFAEGILKREDIFITTKAFC 84
Cdd:cd19154 1 SASITLSNGVKMPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLWT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 85 HEVAPDVVEEALRNSLKRLRLDYVDLYLAHIPASTKDD----------GSFRSDVKVEDIWRGFEKVYGLGLTKAIGVSN 154
Cdd:cd19154 81 HEHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDegesgtmengMSIHDAVDVEDVWRGMEKVYDEGLTKAIGVSN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 155 FNESQIVRIMNIQKVPIHASQLELHLYLPQKAHRELCKKHNILITAYATLGSPGRMSVVGSNGrplfesTQNSENEMNDK 234
Cdd:cd19154 161 FNNDQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSPGRANFTKSTG------VSPAPNLLQDP 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17566692 235 HVKALAQKYSKTPAQILLRATVEMGIIVIPKTTNPERMKENINIFDFNISNAEVNLLEAHERTKQERLF 303
Cdd:cd19154 235 IVKAIAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLRLFLF 303
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
13-303 |
5.13e-113 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381337 [Multi-domain] Cd Length: 286 Bit Score: 328.69 E-value: 5.13e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 13 GVLMPSIGLGTWQMTGEEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAELFAEGILKREDIFITTKAFCHEVAPDVV 92
Cdd:cd19111 1 GFPMPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLEFKDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 93 EEALRNSLKRLRLDYVDLYLAHIPA--STKDDGSFRSDVK--VEDIWRGFEKVYGLGLTKAIGVSNFNESQIVRIMNIQK 168
Cdd:cd19111 81 EKSLEKSLENLKLPYVDLYLIHHPCgfVNKKDKGERELASsdVTSVWRAMEALVSEGKVKSIGLSNFNPRQINKILAYAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 169 VPIHASQLELHLYLPQKAHRELCKKHNILITAYATLGSPGRMSVVGSNGRPlfestqnseNEMNDKHVKALAQKYSKTPA 248
Cdd:cd19111 161 VKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSPGRANQSLWPDQP---------DLLEDPTVLAIAKELDKTPA 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 17566692 249 QILLRATVEMGIIVIPKTTNPERMKENINIFDFNISNAEVNLLEAHERTKQERLF 303
Cdd:cd19111 232 QVLLRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMKYFDF 286
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
16-292 |
7.25e-112 |
|
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. The family includes AKR1A/B/C/D/E/G/I, AKR2A/B/C/D/E, AKR3A/B/C/D/E/G, AKR4A/B/C, AKR5A/B/C/D/E/F/G/H, and similar proteins.
Pssm-ID: 381297 [Multi-domain] Cd Length: 251 Bit Score: 324.43 E-value: 7.25e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 16 MPSIGLGTWQMTGEEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAELFaegiLKREDIFITTKAFCHEVAPDVVEEA 95
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESG----VPREELFITTKLWPTDHGYERVREA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 96 LRNSLKRLRLDYVDLYLAHIPASTKDDGSfrsDVKVEDIWRGFEKVYGLGLTKAIGVSNFNESQIVRIMNIQKVPIHASQ 175
Cdd:cd19071 77 LEESLKDLGLDYLDLYLIHWPVPGKEGGS---KEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAARIKPAVNQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 176 LELHLYLPQKAHRELCKKHNILITAYATLGSPGRMsvvgsngrplfestqnsenEMNDKHVKALAQKYSKTPAQILLRAT 255
Cdd:cd19071 154 IELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRRP-------------------LLDDPVLKEIAKKYGKTPAQVLLRWA 214
|
250 260 270
....*....|....*....|....*....|....*..
gi 17566692 256 VEMGIIVIPKTTNPERMKENINIFDFNISNAEVNLLE 292
Cdd:cd19071 215 LQRGVVVIPKSSNPERIKENLDVFDFELSEEDMAAID 251
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
6-293 |
2.71e-111 |
|
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a founding member of aldo-keto reductase family 2 member E4 (AKR2E4). It is a NADP-dependent oxidoreductase with high 3-dehydroecdysone reductase activity. It may play a role in the regulation of molting and has lower activity with phenylglyoxal and isatin (in vitro). This family also includes 3-dehydroecdysone 3b-reductase from Spodoptera littoralis and Trichoplusia ni, DL-glyceraldehyde reductase from Drosophila melanogaster, aldo-keto reductase from Bombyx mori, which correspond to aldo-keto reductase family 2 member E1, E2, E3 and E5 (AKR2E1/2/3/5), respectively.
Pssm-ID: 381342 [Multi-domain] Cd Length: 292 Bit Score: 324.62 E-value: 2.71e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 6 PIFTLSNGVLMPSIGLGTWQMTGEEG-KTVIRNAVLAGYRHIDTATLYQNEHQIGDALAELFAEGILKREDIFITTKAFC 84
Cdd:cd19116 1 PTIKLNDGNEIPAIALGTWKLKDDEGvRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 85 HEVAPDVVEEALRNSLKRLRLDYVDLYLAHIPASTKDDGSFR-------SDVKVEDIWRGFEKVYGLGLTKAIGVSNFNE 157
Cdd:cd19116 81 SYHEREQVEPALRESLKRLGLDYVDLYLIHWPVAFKENNDSEsngdgslSDIDYLETWRGMEDLVKLGLTRSIGVSNFNS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 158 SQIVRIMNIQKVPIHASQLELHLYLPQKAHRELCKKHNILITAYATLGSPgrmsvVGSNGrplfestQNSENEMNDKHVK 237
Cdd:cd19116 161 EQINRLLSNCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRL-----VPRGQ-------TNPPPRLDDPTLV 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 17566692 238 ALAQKYSKTPAQILLRATVEMGIIVIPKTTNPERMKENINIFDFNISNAEVNLLEA 293
Cdd:cd19116 229 AIAKKYGKTTAQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNS 284
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
12-307 |
4.46e-105 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 307.37 E-value: 4.46e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 12 NGVLMPSIGLGTWQMTGEEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAELfaeGIlKREDIFITTKAFCHEVAPDV 91
Cdd:COG0656 1 NGVEIPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAAS---GV-PREELFVTTKVWNDNHGYDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 92 VEEALRNSLKRLRLDYVDLYLAHIPAstkddgsfrsDVKVEDIWRGFEKVYGLGLTKAIGVSNFNESQIVRIMNIQKVPI 171
Cdd:COG0656 77 TLAAFEESLERLGLDYLDLYLIHWPG----------PGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETGVKP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 172 HASQLELHLYLPQKAHRELCKKHNILITAYATLGSpGRMsvvgsngrplfestqnseneMNDKHVKALAQKYSKTPAQIL 251
Cdd:COG0656 147 AVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGR-GKL--------------------LDDPVLAEIAEKHGKTPAQVV 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 17566692 252 LRATVEMGIIVIPKTTNPERMKENINIFDFNISNAEVNLLEAHERTkqERLFWWPN 307
Cdd:COG0656 206 LRWHLQRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRG--ERLGPDPD 259
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
8-303 |
1.81e-96 |
|
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase (ALR) from Hordeum vulgare (AKR4C1), Bromus inermis (AKR4C2), Avena fatua (AKR4C3), and Xerophyta viscosa (AKR4C4), two aldose reductases, DpAR1 (AKR4C5) and DpAR2(AKR4C6), from Digitalis purpurea, aldehyde reductase from Zea mays (AKR4C7), four aldo-keto reductases from Arabidopsis thaliana (AKR4C8-11), and another three aldo-keto reductases from Aloe arborescens (AKR4C12) and Oryza sativa (AKR4C14/15). ALR (EC 1.1.1.21), also called AR, aldehyde reductase, or polyol dehydrogenase (NADP(+)), is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. Both DpAR1 and DpAR2 reduce the ketone group of steroid structures. They may be involved in plant steroid metabolism in general and in cardenolide biosynthesis in particular. Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops.
Pssm-ID: 381351 [Multi-domain] Cd Length: 287 Bit Score: 286.93 E-value: 1.81e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 8 FTLSNGVLMPSIGLGTWQMTGEEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAELFAEGILKREDIFITTKAFCHEV 87
Cdd:cd19125 3 FKLNTGAKIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLWCTDH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 88 APDVVEEALRNSLKRLRLDYVDLYLAHIPASTKDDGSFRS-----DVKVEDIWRGFEKVYGLGLTKAIGVSNFNESQIVR 162
Cdd:cd19125 83 APEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKGAHMPEpeevlPPDIPSTWKAMEKLVDSGKVRAIGVSNFSVKKLED 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 163 IMNIQKVPIHASQLELHLYLPQKAHRELCKKHNILITAYATLGSPGRMSVVGsngrplfestqnseNEMNDKHVKALAQK 242
Cdd:cd19125 163 LLAVARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGTTWVKK--------------NVLKDPIVTKVAEK 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17566692 243 YSKTPAQILLRATVEMGIIVIPKTTNPERMKENINIFDFNISNaevNLLEAHERTKQERLF 303
Cdd:cd19125 229 LGKTPAQVALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPE---EDFAKFSSIEQQRRV 286
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
9-303 |
5.71e-94 |
|
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381381 [Multi-domain] Cd Length: 307 Bit Score: 281.34 E-value: 5.71e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 9 TLSNGVLMPSIGLGTWQMTGEEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAELFAEGILKREDIFITTKAFCHEVA 88
Cdd:cd19155 5 TFNNGEKMPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLPPGGNR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 89 PDVVEEALRNSLKRLRLDYVDLYLAHIPAS--TKDDGSFRSDVKVE----------DIWRGFEKVYGLGLTKAIGVSNFN 156
Cdd:cd19155 85 REKVEKFLLKSLEKLQLDYVDLYLIHFPVGslSKEDDSGKLDPTGEhkqdyttdllDIWKAMEAQVDQGLTRSIGLSNFN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 157 ESQIVRIMNIQKVPIHASQLELHLYLPQKAHRELCKKHNILITAYATLGSPGRMSVVGSNGRPlfesTQNSENEMNDKHV 236
Cdd:cd19155 165 REQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPGAAHFSPGTGSP----SGSSPDLLQDPVV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17566692 237 KALAQKYSKTPAQILLRATVEMGIIVIPKTTNPERMKENINIFDFNISNAEVNLLEahERTKQERLF 303
Cdd:cd19155 241 KAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLS--SLDKNIRGR 305
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
10-296 |
1.09e-89 |
|
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol dehydrogenase [NADP(+)] (ALR, EC 1.1.1.2) from Homo sapiens (AKR1A1), Sus scrofa (AKR1A2), Rattus norvegicus (liver, AKR1A3), and Mus musculus (AKR1A4). ALR, also known as aldehyde reductase, or ALDR1, catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid.
Pssm-ID: 381332 [Multi-domain] Cd Length: 305 Bit Score: 270.03 E-value: 1.09e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 10 LSNGVLMPSIGLGTWQMTGEEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAELFAEG-ILKREDIFITTKAFCHEVA 88
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPGkAVPREDLFVTSKLWNTKHH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 89 PDVVEEALRNSLKRLRLDYVDLYLAHIPASTK---------DDGSFR-SDVKVEDIWRGFEKVYGLGLTKAIGVSNFNES 158
Cdd:cd19106 81 PEDVEPALRKTLKDLQLDYLDLYLIHWPYAFErgdnpfpknPDGTIRyDSTHYKETWKAMEKLVDKGLVKAIGLSNFNSR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 159 QIVRIMNIQKVPIHASQLELHLYLPQKAHRELCKKHNILITAYATLGSPGRMSVvgSNGRPLFestqnseneMNDKHVKA 238
Cdd:cd19106 161 QIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPDRPWA--KPDEPVL---------LEEPKVKA 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 17566692 239 LAQKYSKTPAQILLRATVEMGIIVIPKTTNPERMKENINIFDFNISNAEVNLLEAHER 296
Cdd:cd19106 230 LAKKYNKSPAQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNR 287
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
16-293 |
4.89e-89 |
|
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like protein is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase similar to Bacillus subtilis glyoxal reductase (YvgN) that reduces glyoxal and methylglyoxal (2-oxopropanal).
Pssm-ID: 381362 [Multi-domain] Cd Length: 262 Bit Score: 266.80 E-value: 4.89e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 16 MPSIGLGTWQMTG-EEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAELFAEGILKREDIFITTKAFCHEVAPDVVEE 94
Cdd:cd19136 1 MPILGLGTFRLRGeEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 95 ALRNSLKRLRLDYVDLYLAHIPASTKDDGS------FRSDVkvediWRGFEKVYGLGLTKAIGVSNFNESQIVRIMNIQK 168
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWPGVQGLKPSdprnaeLRRES-----WRALEDLYKEGKLRAIGVSNYTVRHLEELLKYCE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 169 VPIHASQLELHLYLPQKAHRELCKKHNILITAYATLGSPGrmsvvgsnGRPLFESTqnsenemndkhVKALAQKYSKTPA 248
Cdd:cd19136 156 VPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGD--------LRLLEDPT-----------VLAIAKKYGRTPA 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 17566692 249 QILLRATVEMGIIVIPKTTNPERMKENINIFDFNISNAEVNLLEA 293
Cdd:cd19136 217 QVLLRWALQQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNA 261
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
8-296 |
5.03e-88 |
|
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a founding member of aldo-keto reductase family 3 member G1 (AKR3G1). It is an aldo/keto reductase that catalyzes the NADPH-dependent reduction of aldehyde- and ketone-groups of different classes of carbonyl compounds to the corresponding alcohols.
Pssm-ID: 381349 [Multi-domain] Cd Length: 297 Bit Score: 265.43 E-value: 5.03e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 8 FTLSNGVLMPSIGLGTWQMT-GEEGKTViRNAVLAGYRHIDTATLYQNEHQIGDALAELFAEGILKREDIFITTKAFCHE 86
Cdd:cd19123 4 LPLSNGDLIPALGLGTWKSKpGEVGQAV-KQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLWNNS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 87 VAPDVVEEALRNSLKRLRLDYVDLYLAHIPASTK---------DDGSFRSDVKVEDIWRGFEKVYGLGLTKAIGVSNFNE 157
Cdd:cd19123 83 HAPEDVLPALEKTLADLQLDYLDLYLMHWPVALKkgvgfpesgEDLLSLSPIPLEDTWRAMEELVDKGLCRHIGVSNFSV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 158 SQIVRIMNIQKVPIHASQLELHLYLPQKAHRELCKKHNILITAYATLGSPGRMSVVGSNGRP-LFEstqnsenemnDKHV 236
Cdd:cd19123 163 KKLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDRPAAMKAEGEPvLLE----------DPVI 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17566692 237 KALAQKYSKTPAQILLRATVEMGIIVIPKTTNPERMKENINIFDFNISNAE---VNLLEAHER 296
Cdd:cd19123 233 NKIAEKHGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDmatIAALDRHHR 295
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
12-287 |
5.35e-83 |
|
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes Glycine max NAD(P)H-dependent 6'-deoxychalcone synthase (6DCS, EC 3.1.170), chalcone reductase (CHR, EC 2.3.1.74) from Medicago sativa, Glycyrrhiza echinate, and Glycyrrhiza glabra, which are founding members of aldo-keto reductase family 4 member A1 (AKR4A1), A2 (AKR4A2), A3 (AKR4A3), and A4 (AKR4A4), respectively. NAD(P)H-6DCS co-acts with chalcone synthase in formation of 4,2',4'-trihydroxychalcone, involved in the biosynthesis of glyceollin type phytoalexins. CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. The AKR4B family of AKR includes Sesbania rostrate chalcone reductase (CHR, AKR4B1), Papaver somniferum codeinone reductase (COR, AKR4B2/ AKR4B3), Fragaria x ananassa D-galacturonate reductase (GalUR, AKR4B4), deoxymugineic acid synthase 1 (DMAS1) from Zea mays (AKR4B5), Oryza sativa (AKR4B6), Hordeum vulgare (AKR4B7), Triticum aestivum (AKR4B8), and Erythroxylum coca methylecgonone reductase (MecgoR, AKR4B10). CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. NADPH-dependent COR and non-functional NADPH-dependent COR from Papaver somniferum are founding members of aldo-keto reductase family 4 member B2 (AKR4B2) and B3 (AKR4B3), respectively. NADPH-dependent COR (EC 1.1.1.247) reduces codeinone to codeine in the penultimate step in morphine biosynthesis. It can use morphinone, hydrocodone, and hydromorphone as substrates during reductive reaction with NADPH as cofactor, and morphine and dihydrocodeine as substrates during oxidative reaction with NADP as cofactor. GalUR (EC 1.1.1.365), also called aldo-keto reductase 2 (AKR2), is involved in ascorbic acid (vitamin C) biosynthesis by catalyzing the conversion from L-galactonate and NADP(+) to D-galacturonate and NADPH. DMAS1 (EC 1.1.1.285) catalyzes the reduction of a 3''-keto intermediate during the biosynthesis of 2'-deoxymugineic acid (DMA) from L-Met. It is involved in the formation of phytosiderophores (MAs) belonging to the mugineic acid family and required to acquire iron. MecgoR catalyzes the stereospecific reduction of methylecgonone to methylecgonine, the penultimate step in cocaine biosynthesis.
Pssm-ID: 381350 [Multi-domain] Cd Length: 281 Bit Score: 252.19 E-value: 5.35e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 12 NGVLMPSIGLGTWQMTG--EEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAELFAEG-ILKREDIFITTKAFCHEVA 88
Cdd:cd19124 1 SGQTMPVIGMGTASDPPspEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGlVKSRDELFVTSKLWCSDAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 89 PDVVEEALRNSLKRLRLDYVDLYLAHIPASTKDdGSFRSDVKVEDI--------WRGFEKVYGLGLTKAIGVSNFNESQI 160
Cdd:cd19124 81 PDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKP-GKFSFPIEEEDFlpfdikgvWEAMEECQRLGLTKAIGVSNFSCKKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 161 VRIMNIQKVPIHASQLELHLYLPQKAHRELCKKHNILITAYATLGSPGrmSVVGSNGrplfestqnsenEMNDKHVKALA 240
Cdd:cd19124 160 QELLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPG--TKWGSNA------------VMESDVLKEIA 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 17566692 241 QKYSKTPAQILLRATVEMGIIVIPKTTNPERMKENINIFDFNISNAE 287
Cdd:cd19124 226 AAKGKTVAQVSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEED 272
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
9-293 |
4.10e-81 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; Escherichia coli DkgA/YqhE is a founding member of aldo-keto reductase family 5 member C2 (AKR5C2). DkgA/YqhE (EC 1.1.1.274), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives.
Pssm-ID: 381357 [Multi-domain] Cd Length: 256 Bit Score: 246.52 E-value: 4.10e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 9 TLSNGVLMPSIGLGTWQMTGEEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALaelfAEGILKREDIFITTKAFCHEVA 88
Cdd:cd19131 3 TLNDGNTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAI----RASGVPREELFITTKLWNSDQG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 89 PDVVEEALRNSLKRLRLDYVDLYLAHIPASTKDdgsfrsdvKVEDIWRGFEKVYGLGLTKAIGVSNFNESQIVRIMNIQK 168
Cdd:cd19131 79 YDSTLRAFDESLRKLGLDYVDLYLIHWPVPAQD--------KYVETWKALIELKKEGRVKSIGVSNFTIEHLQRLIDETG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 169 VPIHASQLELHLYLPQKAHRELCKKHNILITAYATLGSPGRMSvvgsngrplfestqnsenemnDKHVKALAQKYSKTPA 248
Cdd:cd19131 151 VVPVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGGLLS---------------------DPVIGEIAEKHGKTPA 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 17566692 249 QILLRATVEMGIIVIPKTTNPERMKENINIFDFNISNAEVNLLEA 293
Cdd:cd19131 210 QVVIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELDADDMQAIAG 254
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
6-304 |
2.40e-80 |
|
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 (NADP-dependent D-sorbitol-6-phosphate dehydrogenase or NADP-S6PDH) from Malus domestica, and AKR2A2 (NADPH-dependent mannose-6-phosphate reductase or NADPH-M6PR) from Apium graveolens. NADP-S6PDH (EC 1.1.1.200), also called aldose-6-phosphate reductase [NADPH], synthesizes sorbitol-6-phosphate, a key intermediate in the synthesis of sorbitol which is a major photosynthetic product in many members of the Rosaceae family. NADPH-M6PR (EC 1.1.1.224), also called NADPH-dependent M6P reductase, is a key enzyme involved in mannitol biosynthesis.
Pssm-ID: 381338 [Multi-domain] Cd Length: 308 Bit Score: 246.24 E-value: 2.40e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 6 PIFTLSNGVLMPSIGLGTWQMTGEEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAELFAEGILKREDIFITTKAFC- 84
Cdd:cd19112 1 STITLNSGHKMPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLWNs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 85 -HEvapdVVEEALRNSLKRLRLDYVDLYLAHIPASTK------------DDGSFRSDVKV--EDIWRGFEKVYGLGLTKA 149
Cdd:cd19112 81 dHG----HVIEACKDSLKKLQLDYLDLYLVHFPVATKhtgvgttgsalgEDGVLDIDVTIslETTWHAMEKLVSAGLVRS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 150 IGVSNFNESQIVRIMNIQKVPIHASQLELHLYLPQKAHRELCKKHNILITAYATLGSpgrmsvvGSNGRPLFestqNSEN 229
Cdd:cd19112 157 IGISNYDIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGG-------AAANAEWF----GSVS 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17566692 230 EMNDKHVKALAQKYSKTPAQILLRATVEMGIIVIPKTTNPERMKENINIFDFNISNAEVNLLEAHE---RTKQERLFW 304
Cdd:cd19112 226 PLDDPVLKDLAKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDrkyRTNQPAKFW 303
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
13-316 |
9.31e-78 |
|
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes 3-oxo-5-beta-steroid 4-dehydrogenase (EC 1.3.1.3) from Homo sapiens (AKR1D1), Rattus norvegicus (liver, AKR1D2), and Oryctolagus cuniculus (AKR1D3). 3-oxo-5-beta-steroid 4-dehydrogenase, also called delta(4)-3-ketosteroid 5-beta-reductase (EC 1.3.99.6), or delta(4)-3-oxosteroid 5-beta-reductase, or 5-beta-reductase, efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites.
Pssm-ID: 381335 [Multi-domain] Cd Length: 308 Bit Score: 239.70 E-value: 9.31e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 13 GVLMPSIGLGTWQMTGE----EGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAELFAEGILKREDIFITTKAFCHEVA 88
Cdd:cd19109 1 GNSIPIIGLGTYSEPKTtpkgACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 89 PDVVEEALRNSLKRLRLDYVDLYLAHIPASTK---------DDGSFRSD-VKVEDIWRGFEKVYGLGLTKAIGVSNFNES 158
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAFKpgdeiyprdENGKWLYHkTNLCATWEALEACKDAGLVKSIGVSNFNRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 159 QIVRIMN---IQKVPIhASQLELHLYLPQKAHRELCKKHNILITAYATLGSPGRMSVVGSNGRPLFEstqnsenemnDKH 235
Cdd:cd19109 161 QLELILNkpgLKHKPV-SNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDPIWVNVSSPPLLE----------DPL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 236 VKALAQKYSKTPAQILLRATVEMGIIVIPKTTNPERMKENINIFDFNISNAEVNLLEA-HERTKQERLFWWpnvADHPED 314
Cdd:cd19109 230 LNSIGKKYNKTAAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEAlNKNVRYVELLMW---RDHPEY 306
|
..
gi 17566692 315 PF 316
Cdd:cd19109 307 PF 308
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
11-293 |
1.44e-77 |
|
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381366 [Multi-domain] Cd Length: 253 Bit Score: 237.16 E-value: 1.44e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 11 SNGVLMPSIGLGTWQMTGEEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAelfAEGIlKREDIFITTKAFCHEVAPD 90
Cdd:cd19140 3 VNGVRIPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIA---ASGV-PRDELFLTTKVWPDNYSPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 91 VVEEALRNSLKRLRLDYVDLYLAHIPAstkddgsfrSDVKVEDIWRGFEKVYGLGLTKAIGVSNFNESQIVRIMNIQKVP 170
Cdd:cd19140 79 DFLASVEESLRKLRTDYVDLLLLHWPN---------KDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSEAP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 171 IHASQLELHLYLPQKAHRELCKKHNILITAYATLGSpGRMsvvgsngrplfestqnseneMNDKHVKALAQKYSKTPAQI 250
Cdd:cd19140 150 LFTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLAR-GEV--------------------LKDPVLQEIGRKHGKTPAQV 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 17566692 251 LLRATVE-MGIIVIPKTTNPERMKENINIFDFNISNAEVNLLEA 293
Cdd:cd19140 209 ALRWLLQqEGVAAIPKATNPERLEENLDIFDFTLSDEEMARIAA 252
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
13-316 |
7.13e-77 |
|
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase (AR, EC 1.1.1.21) from Homo sapiens (AKR1B1), Oryctolagus cuniculus (kidney, AKR1B2), Mus musculus (AKR1B3), Rattus norvegicus (lens, AKR1B4), Bos taurus (lens/testis, AKR1B5), and Sus scrofa (lens, AKR1B6), aldose reductase-related protein 1 (ALD1, EC1.1.1.21) from Mus musculus (AKR1B7), Rattus norvegicus (AKR1B14), and Homo sapiens (AKR1B15), Mus musculus fibroblast growth factor induced protein (FR-1 or AKR1B8, EC 1.1.1.21), Cricetulus griseus aldose reductase-related protein 2 (ALD2 or AKR1B9, EC 1.1.1.21), aldose reductase-like from Homo sapiens (ARL-1 or AKR1B10) and Rattus norvegicus (AKR1B13), aldo-keto reductase from Gallus domesticus (eye, tongue, esophagus, AKR1B12), and Oryctolagus cuniculus AR-like protein (3beta-HSD, AKR1B19). AR, also called aldehyde reductase, catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. ALD1 reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. It may play a role in the metabolism of xenobiotic aromatic aldehydes. FR-1, also called aldose reductase-related protein 2, or fibroblast growth factor-regulated protein (FGFRP), is induced by fibroblast growth factor-1. It may play a role in the regulation of the cell cycle. FR-1 belongs to the NADPH-dependent aldo-keto reductase family. ALD2 is an inducible aldo-keto reductase with a preference for aliphatic substrates. It can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. ARL-1, also called aldose reductase-like, or aldose reductase-related protein (ARP), or small intestine reductase, or SI reductase, acts as all-trans-retinaldehyde reductase that can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). It may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. AKR1B15, also called estradiol 17-beta-dehydrogenase AKR1B15, is a mitochondrial aldo-keto reductase that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. It has a strong selectivity towards NADP(H). AKR1B19 is aldose reductase-like that may show 3-beta-hydroxysteroid dehydrogenase (3beta-HSD) activity.
Pssm-ID: 381333 [Multi-domain] Cd Length: 307 Bit Score: 237.32 E-value: 7.13e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 13 GVLMPSIGLGTWQMTGEEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAELFAEGILKREDIFITTKAFCHEVAPDVV 92
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEKGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 93 EEALRNSLKRLRLDYVDLYLAHIPASTK---------DDGS-FRSDVKVEDIWRGFEKVYGLGLTKAIGVSNFNESQIVR 162
Cdd:cd19107 81 KGACQKTLSDLKLDYLDLYLIHWPTGFKpgkelfpldESGNvIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 163 IMN---IQKVPIhASQLELHLYLPQKAHRELCKKHNILITAYATLGSPgrmsvvgsnGRPLFESTQNSENEmnDKHVKAL 239
Cdd:cd19107 161 ILNkpgLKYKPA-VNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSP---------DRPWAKPEDPSLLE--DPKIKEI 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17566692 240 AQKYSKTPAQILLRATVEMGIIVIPKTTNPERMKENINIFDFNISNAEVNLLEAHERtkQERLFWWPNVADHPEDPF 316
Cdd:cd19107 229 AAKHNKTTAQVLIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNR--NWRACALLSCSSHKDYPF 303
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
10-293 |
2.53e-76 |
|
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381361 [Multi-domain] Cd Length: 265 Bit Score: 234.53 E-value: 2.53e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 10 LSNGVLMPSIGLGTWQMTGEEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAElfaEGIlKREDIFITTKAFCHEVAP 89
Cdd:cd19135 7 LSNGVEMPILGLGTSHSGGYSHEAVVYALKECGYRHIDTAKRYGCEELLGKAIKE---SGV-PREDLFLTTKLWPSDYGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 90 DVVEEALRNSLKRLRLDYVDLYLAHIP---ASTKDDGSFRsdvkvEDIWRGFEKVYGLGLTKAIGVSNFNESQIVRIMNI 166
Cdd:cd19135 83 ESTKQAFEASLKRLGVDYLDLYLLHWPdcpSSGKNVKETR-----AETWRALEELYDEGLCRAIGVSNFLIEHLEQLLED 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 167 QKVPIHASQLELHLYLPQKAHRELCKKHNILITAYATLgspgrmsvvgSNGRPLfestqnsenemNDKHVKALAQKYSKT 246
Cdd:cd19135 158 CSVVPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPL----------AKGKAL-----------EEPTVTELAKKYQKT 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 17566692 247 PAQILLRATVEMGIIVIPKTTNPERMKENINIFDFNISNAEVNLLEA 293
Cdd:cd19135 217 PAQILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDS 263
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
16-288 |
3.61e-76 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti isatin reductase and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381299 [Multi-domain] Cd Length: 243 Bit Score: 233.32 E-value: 3.61e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 16 MPSIGLGTWQMTGEEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAElfaEGIlKREDIFITTKAFCHEVAPDVVEEA 95
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAE---SGV-PREDLFITTKVWRDHLRPEDLKKS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 96 LRNSLKRLRLDYVDLYLAHIPASTKDdgsfrsdvkVEDIWRGFEKVYGLGLTKAIGVSNFNESQIVRIMNIQKVPIHASQ 175
Cdd:cd19073 77 VDRSLEKLGTDYVDLLLIHWPNPTVP---------LEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPLPIAVNQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 176 LELHLYLPQKAHRELCKKHNILITAYATLGspgrmsvvgsNGRPLfestqnsenemNDKHVKALAQKYSKTPAQILLRAT 255
Cdd:cd19073 148 VEFHPFLYQAELLEYCRENDIVITAYSPLA----------RGEVL-----------RDPVIQEIAEKYDKTPAQVALRWL 206
|
250 260 270
....*....|....*....|....*....|...
gi 17566692 256 VEMGIIVIPKTTNPERMKENINIFDFNISNAEV 288
Cdd:cd19073 207 VQKGIVVIPKASSEDHLKENLAIFDWELTSEDV 239
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
10-284 |
1.74e-75 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 233.66 E-value: 1.74e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 10 LSNGVLMPSIGLGTW---QMTGEEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAELFAEGILKREDIFITTKAFCHE 86
Cdd:cd19108 5 LNDGHFIPVLGFGTYapeEVPKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKLWCTF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 87 VAPDVVEEALRNSLKRLRLDYVDLYLAHIPASTK---------DDGSFRSD-VKVEDIWRGFEKVYGLGLTKAIGVSNFN 156
Cdd:cd19108 85 HRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKpgeelfpkdENGKLIFDtVDLCATWEAMEKCKDAGLAKSIGVSNFN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 157 ESQIVRIMN---IQKVPIhASQLELHLYLPQKAHRELCKKHNILITAYATLGSPgrmsvvgsngRPLFESTQNSENEMND 233
Cdd:cd19108 165 RRQLEMILNkpgLKYKPV-CNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQ----------RDKEWVDQNSPVLLED 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 17566692 234 KHVKALAQKYSKTPAQILLRATVEMGIIVIPKTTNPERMKENINIFDFNIS 284
Cdd:cd19108 234 PVLCALAKKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLT 284
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
9-293 |
1.79e-75 |
|
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid reductase (2,5-DKG reductase) is a founding member of aldo-keto reductase family 5 member F1 (AKR5F1). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381359 [Multi-domain] Cd Length: 255 Bit Score: 232.08 E-value: 1.79e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 9 TLSNGVLMPSIGLGTWQMTG-EEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAElfaEGIlKREDIFITTKAFCHEV 87
Cdd:cd19133 2 TLNNGVEMPILGFGVFQIPDpEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKK---SGI-PREELFITTKLWIQDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 88 APDVVEEALRNSLKRLRLDYVDLYLAHIPAStkddgsfrsdvKVEDIWRGFEKVYGLGLTKAIGVSNFNESQIVRIMNIQ 167
Cdd:cd19133 78 GYEKAKKAFERSLKRLGLDYLDLYLIHQPFG-----------DVYGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLILHN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 168 KVPIHASQLELHLYLPQKAHRELCKKHNILITAYATLGspgrmsvvgsNGRPlfestqnseNEMNDKHVKALAQKYSKTP 247
Cdd:cd19133 147 EVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFA----------EGRN---------NLFENPVLTEIAEKYGKSV 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 17566692 248 AQILLRATVEMGIIVIPKTTNPERMKENINIFDFNISNAEVNLLEA 293
Cdd:cd19133 208 AQVILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAA 253
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
9-293 |
3.15e-75 |
|
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) is a founding member of the aldo-keto reductase family 5 member B1 (AKR5B1). M6DH (EC 1.1.1.218), also called naloxone reductase, oxidizes the C-6 hydroxy group of morphine and codeine.
Pssm-ID: 381353 [Multi-domain] Cd Length: 268 Bit Score: 231.91 E-value: 3.15e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 9 TLSNGVLMPSIGLGTWQMTGEEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAElfaEGIlKREDIFITTKAFCHEVA 88
Cdd:cd19127 2 TLNNGVEMPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRR---SGV-DRSDIFVTTKLWISDYG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 89 PDVVEEALRNSLKRLRLDYVDLYLAHIPASTKDDGSFRSdvkvediWRGFEKVYGLGLTKAIGVSNFNESQIVRIMNIQK 168
Cdd:cd19127 78 YDKALRGFDASLRRLGLDYVDLYLLHWPVPNDFDRTIQA-------YKALEKLLAEGRVRAIGVSNFTPEHLERLIDATT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 169 VPIHASQLELHLYLPQKAHRELCKKHNILITAYATLGSPGRMSVVGSNGRPlfestqnseNEMNDKHVKALAQKYSKTPA 248
Cdd:cd19127 151 VVPAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGGVMRYGASGPTGPG---------DVLQDPTITGLAEKYGKTPA 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 17566692 249 QILLRATVEMGIIVIPKTTNPERMKENINIFDFNISNAEVNLLEA 293
Cdd:cd19127 222 QIVLRWHLQNGVSAIPKSVHPERIAENIDIFDFALSAEDMAAIDA 266
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
8-293 |
4.73e-75 |
|
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 231.51 E-value: 4.73e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 8 FTLSNGVLMPSIGLGTWQM-TGEEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAElfaeGILKREDIFITTKAFCHE 86
Cdd:cd19157 2 VTLNNGVKMPWLGLGVFKVeEGSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKE----SGIPREELFITSKVWNAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 87 VAPDVVEEALRNSLKRLRLDYVDLYLAHIPASTKDdgsfrsdvkvEDIWRGFEKVYGLGLTKAIGVSNFNESQIVRIMNI 166
Cdd:cd19157 78 QGYDSTLKAFEASLERLGLDYLDLYLIHWPVKGKY----------KETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLAD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 167 QKVPIHASQLELHLYLPQKAHRELCKKHNILITAYAtlgspgrmsvvgsngrPLFEStQNSENEMndkhVKALAQKYSKT 246
Cdd:cd19157 148 AEIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWS----------------PLMQG-QLLDNPV----LKEIAEKYNKS 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 17566692 247 PAQILLRATVEMGIIVIPKTTNPERMKENINIFDFNISNAEVNLLEA 293
Cdd:cd19157 207 VAQVILRWDLQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDA 253
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
9-293 |
1.15e-74 |
|
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes prostaglandin F2-alpha synthase (PGFS) from Leishmania major (AKR5A1) and Trypanosoma brucei (AKR5A2). PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity for synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde. The AKR5G family of AKR includes Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase, which corresponds to aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381352 [Multi-domain] Cd Length: 254 Bit Score: 230.02 E-value: 1.15e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 9 TLSNGVLMPSIGLGTWQM-TGEEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAElfaEGIlKREDIFITTKAFCHEV 87
Cdd:cd19126 2 TLNNGTRMPWLGLGVFQTpDGDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRE---SGV-PREELFVTTKLWNDDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 88 APDVVEEALRNSLKRLRLDYVDLYLAHIPAstKDdgsfrsdvKVEDIWRGFEKVYGLGLTKAIGVSNFNESQIVRIMNIQ 167
Cdd:cd19126 78 RARRTEDAFQESLDRLGLDYVDLYLIHWPG--KD--------KFIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 168 KVPIHASQLELHLYLPQKAHRELCKKHNILITAYATLGSPGRMSvvgsngrplfestqnsenemnDKHVKALAQKYSKTP 247
Cdd:cd19126 148 DVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQGGLLS---------------------NPVLAAIGEKYGKSA 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 17566692 248 AQILLRATVEMGIIVIPKTTNPERMKENINIFDFNISNAEVNLLEA 293
Cdd:cd19126 207 AQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAIDA 252
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
8-292 |
1.62e-72 |
|
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, EC 1.1.1.365), also called D-galacturonic acid reductase, or GalUR, is a founding member of aldo-keto reductase family 3 member D1 (AKR3D1). It mediates the reduction of D-galacturonate to L-galactonate, the first step in D-galacturonate catabolic process. It also has activity with D-glucuronate and DL-glyceraldehyde. Its activity is seen only with NADPH and not with NADH.
Pssm-ID: 381347 [Multi-domain] Cd Length: 279 Bit Score: 225.49 E-value: 1.62e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 8 FTLSNGVLMPSIGLGTWQMTGEEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAELFAEGIlKREDIFITTKafCHEV 87
Cdd:cd19121 4 FKLNTGASIPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAIAGGV-KREDLFVTTK--LWST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 88 APDVVEEALRNSLKRLRLDYVDLYLAHIPAS-----------TKDDGS--FRSDVKVEDIWRGFEKVYGLGLTKAIGVSN 154
Cdd:cd19121 81 YHRRVELCLDRSLKSLGLDYVDLYLVHWPVLlnpngnhdlfpTLPDGSrdLDWDWNHVDTWKQMEKVLKTGKTKAIGVSN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 155 FNESQIVRIMNIQKVPIHASQLELHLYLPQKAHRELCKKHNILITAYATLgspgrmsvvGSNGRPLFEstqnsenemnDK 234
Cdd:cd19121 161 YSIPYLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPL---------GSTGSPLIS----------DE 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 17566692 235 HVKALAQKYSKTPAQILLRATVEMGIIVIPKTTNPERMKENINIFDFNisNAEVNLLE 292
Cdd:cd19121 222 PVVEIAKKHNVGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDLD--DEDMNKLN 277
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
13-293 |
4.32e-72 |
|
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis NADPH-dependent conjugated polyketone reductase C2 (CPR), and similar proteins; Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase (EC 1.1.1.190/EC 1.1.1.191) and Candida parapsilosis NADPH-dependent CPR (EC 1.1.1.358/EC 1.1.1.168) are founding members of aldo-keto reductase family 3 member C2 (AKR3C2) and C3 (AKR3C3), respectively. Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase catalyzes the conversion from (Indol-3-yl)ethanol to (indol-3-yl)acetaldehyde in a NAD/NADP-dependent manner. CPR, also called 2-dehydropantolactone reductase, or 2-dehydropantolactone reductase (A-specific), or ketopantoyl-lactone reductase, acts as a NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. It reduces ketopantoyl lactone and isatin.
Pssm-ID: 381346 [Multi-domain] Cd Length: 269 Bit Score: 224.03 E-value: 4.32e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 13 GVLMPSIGLGT---W--QMTGEEGKTVIRNAVLA---GYRHIDTATLYQNEHQIGDALAELfaegILKREDIFITTKAFC 84
Cdd:cd19120 1 GSKIPAIAFGTgtaWykSGDDDIQRDLVDSVKLAlkaGFRHIDTAEMYGNEKEVGEALKES----GVPREDLFITTKVSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 85 hevAPDVVEEALRNSLKRLRLDYVDLYLAHIPASTKDdgsfrSDVKVEDIWRGFEKVYGLGLTKAIGVSNFNESQIVRIM 164
Cdd:cd19120 77 ---GIKDPREALRKSLAKLGVDYVDLYLIHSPFFAKE-----GGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 165 NIQKVPIHASQLELH--LYLPQKAHRELCKKHNILITAYATLgSPgrmsVVGSNGRPLfestqnsenemnDKHVKALAQK 242
Cdd:cd19120 149 DTAKIKPAVNQIEFHpyLYPQQPALLEYCREHGIVVSAYSPL-SP----LTRDAGGPL------------DPVLEKIAEK 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 17566692 243 YSKTPAQILLRATVEMGIIVIPKTTNPERMKENINIFDFNISNAEVNLLEA 293
Cdd:cd19120 212 YGVTPAQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEIDK 262
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
16-316 |
1.97e-70 |
|
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) from Mus musculus (liver, AKR1E1) and Homo sapiens (AKR1E2). 1,5-anhydro-D-fructose reductase), also called AF reductase, or aldo-keto reductase family 1 member C-like protein 2 (AKR1CL2), catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. AKR1E2 is a testis aldo-keto reductase (tAKR), which is also known as testis-specific protein (TSP), or LoopADR.
Pssm-ID: 381336 [Multi-domain] Cd Length: 301 Bit Score: 220.99 E-value: 1.97e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 16 MPSIGLGTWQMTGEEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAELFAEGILKREDIFITTKAFCHEVAPDVVEEA 95
Cdd:cd19110 4 IPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKSLVKTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 96 LRNSLKRLRLDYVDLYLAHIPASTKD-------DGS---FRSDVKVEDIWRGFEKVYGLGLTKAIGVSNFNESQIVRIMN 165
Cdd:cd19110 84 CTRSLKALKLNYLDLYLIHWPMGFKPgepdlplDRSgmvIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLERLLN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 166 ---IQKVPIhASQLELHLYLPQKAHRELCKKHNILITAYATLGSPGrmsvvgsNGRPLfestqnseneMNDKHVKALAQK 242
Cdd:cd19110 164 kpgLRVKPV-TNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSC-------EGVDL----------IDDPVIQRIAKK 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17566692 243 YSKTPAQILLRATVEMGIIVIPKTTNPERMKENINIFDFNISNAEVNLLEAHERTKqeRLFWWPNVADHPEDPF 316
Cdd:cd19110 226 HGKSPAQILIRFQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNL--RLATFPITENHKDYPF 297
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
9-297 |
4.46e-70 |
|
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from Leishmania major and Trypanosoma brucei are founding members of aldo-keto reductase family 5 member A1 (AKR5A1) and A2 (AKR5A2), respectively. PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity toward the synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde.
Pssm-ID: 381382 [Multi-domain] Cd Length: 266 Bit Score: 218.54 E-value: 4.46e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 9 TLSNGVLMPSIGLGTWQMT-GEEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAElfaEGIlKREDIFITTKAFCHEV 87
Cdd:cd19156 2 KLANGVEMPRLGLGVWRVQdGAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRE---SGV-PREEVFVTTKLWNSDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 88 APDVVEEALRNSLKRLRLDYVDLYLAHIPASTKddgsfrsdvkVEDIWRGFEKVYGLGLTKAIGVSNFNESQIVRIMNIQ 167
Cdd:cd19156 78 GYESTLAAFEESLEKLGLDYVDLYLIHWPVKGK----------FKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSC 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 168 KVPIHASQLELHLYLPQKAHRELCKKHNILITAYATLGSpGRMsvvgsngrplfestqnseneMNDKHVKALAQKYSKTP 247
Cdd:cd19156 148 KVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQ-GKL--------------------LSNPVLKAIGKKYGKSA 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 17566692 248 AQILLRATVEMGIIVIPKTTNPERMKENINIFDFNISNAEV---NLLEAHERT 297
Cdd:cd19156 207 AQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIrqiDGLNTDHRY 259
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
10-296 |
3.28e-69 |
|
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B (DkgB) from Corynebacterium sp. and 2,5-diketo-D-gluconic acid reductase Zymomonas mobilis are founding members of aldo-keto reductase family 5 member D1 (AKR5D1) and E1 (AKR5E1), respectively. DkgB (EC 1.1.1.274), also called 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381358 [Multi-domain] Cd Length: 255 Bit Score: 215.98 E-value: 3.28e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 10 LSNGVLMPSIGLGTWQMTGEEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAElfaEGIlKREDIFITTKAFCHEVAP 89
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRR---SGV-PREELFVTTKLPGRHHGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 90 DVVEEALRNSLKRLRLDYVDLYLAHIPASTKDdgsfrsdvKVEDIWRGFEKVYGLGLTKAIGVSNFNESQIVRImnIQKV 169
Cdd:cd19132 77 EEALRTIEESLYRLGLDYVDLYLIHWPNPSRD--------LYVEAWQALIEAREEGLVRSIGVSNFLPEHLDRL--IDET 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 170 PIHAS--QLELHLYLPQKAHRELCKKHNILITAYATLGSPgrmsvvgsngrplfestqnsENEMNDKHVKALAQKYSKTP 247
Cdd:cd19132 147 GVTPAvnQIELHPYFPQAEQRAYHREHGIVTQSWSPLGRG--------------------SGLLDEPVIKAIAEKHGKTP 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 17566692 248 AQILLRATVEMGIIVIPKTTNPERMKENINIFDFNISNAEVNLLEAHER 296
Cdd:cd19132 207 AQVVLRWHVQLGVVPIPKSANPERQRENLAIFDFELSDEDMAAIAALDR 255
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
8-278 |
5.24e-69 |
|
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar proteins; Saccharomyces cerevisiae Ara1p (EC 1.1.1.117), also called D-arabinose 1-dehydrogenase (NAD(P)(+)), is a founding members of aldo-keto reductase family 3 member C1 (AKR3C1). It catalyzes the oxidation of D-arabinose, L-xylose, L-fucose, and L-galactose in the presence of NADP(+).
Pssm-ID: 381345 [Multi-domain] Cd Length: 294 Bit Score: 216.98 E-value: 5.24e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 8 FTLSNGVLMPSIGLGTW--QMTGEEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAELFAEGILKREDIFITTKafch 85
Cdd:cd19119 4 FKLNTGASIPALGLGTAspHEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTK---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 86 eVAP---DVVEEALRNSLKRLRLDYVDLYLAHIPASTK--------------DDGSFRSDVKVE--DIWRGFEKVYGLGL 146
Cdd:cd19119 80 -VWPtfyDEVERSLDESLKALGLDYVDLLLVHWPVCFEkdsddsgkpftpvnDDGKTRYAASGDhiTTYKQLEKIYLDGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 147 TKAIGVSNFNESQIVRIMNIQKVPIHASQLELHLYLPQKAHRELCKKHNILITAYATLgspgrmsvvGSNGRPLFestqn 226
Cdd:cd19119 159 AKAIGVSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPL---------GSHGAPNL----- 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 17566692 227 sENEMndkhVKALAQKYSKTPAQILLRATVEMGIIVIPKTTNPERMKENINI 278
Cdd:cd19119 225 -KNPL----VKKIAEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKI 271
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
10-293 |
7.38e-69 |
|
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde reductase 1 (ARI, EC 1.1.1.2), Trichosporonoides megachilieni NADPH-dependent erthyrose reductase (ER) 1/2 and 3, are founding members of aldo-keto reductase family 3 member B1 (AKR3B1), B2 (AKR3B2), and B3 (AKR3B3), respectively. Sporidiobolus salmonicolor NADPH-ARI, also called alcohol dehydrogenase [NADP(+)], or aldehyde reductase I, or ALR 1, catalyzes the asymmetric reduction of aliphatic and aromatic aldehydes and ketones to an R-enantiomer. It reduces ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Trichosporonoides megachilieni NADPH-ERs catalyze the reduction of D-erythrose.
Pssm-ID: 381344 [Multi-domain] Cd Length: 283 Bit Score: 216.12 E-value: 7.38e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 10 LSNGVLMPSIGLGTWQMTGEEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAELFAE-GILKREDIFITTKAFCHEVA 88
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEePGVKREDLFITSKLWNNSHR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 89 PDVVEEALRNSLKRLRLDYVDLYLAHIPASTKDDGSFRSD---------------VKVEDIWRGFEKVYGLGLTKAIGVS 153
Cdd:cd19118 81 PEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTGDLNPLtavptnggevdldlsVSLVDTWKAMVELKKTGKVKSIGVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 154 NFNESQIVRIMNIQKVPIHASQLELHLYLPQKAHRELCKKHNILITAYATLGSpgrmsvvGSNGRPLFesTQNSEnemnd 233
Cdd:cd19118 161 NFSIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGN-------NLAGLPLL--VQHPE----- 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 234 khVKALAQKYSKTPAQILLRATVEMGIIVIPKTTNPERMKENINifDFNISNAEVNLLEA 293
Cdd:cd19118 227 --VKAIAAKLGKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVTA 282
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
7-279 |
3.95e-66 |
|
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are founding members of aldo-keto reductase family 3 member A1 (AKR3A1) and A2 (AKR3A2), respectively. Gcy1p, also called galactose-inducible crystallin-like protein 1, is a glycerol dehydrogenase involved in glycerol catabolism under microaerobic conditions. It has mRNA binding activity. Ypr1p acts as a 2-methylbutyraldehyde reductase that displays high specific activity towards 2-methylbutyraldehyde, as well as other aldehydes such as hexanal.
Pssm-ID: 381343 [Multi-domain] Cd Length: 284 Bit Score: 209.28 E-value: 3.95e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 7 IFTLSNGVLMPSIGLGTWQMTGEEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAelfAEGIlKREDIFITTKAFC-- 84
Cdd:cd19117 5 TFKLNTGAEIPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIK---DSGV-PREEIFITTKLWCtw 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 85 -HEvapdvVEEALRNSLKRLRLDYVDLYLAHIPASTKDDGSFRSDVK------------VEDIWRGFEKVYGLGLTKAIG 151
Cdd:cd19117 81 hRR-----VEEALDQSLKKLGLDYVDLYLMHWPVPLDPDGNDFLFKKddgtkdhepdwdFIKTWELMQKLPATGKVKAIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 152 VSNFNESQIVRIMNIQ--KVPIHASQLELHLYLPQKAHRELCKKHNILITAYATLGSpgrmsvvgSNGrPLfestqnsen 229
Cdd:cd19117 156 VSNFSIKNLEKLLASPsaKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGS--------TNA-PL--------- 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 17566692 230 eMNDKHVKALAQKYSKTPAQILLRATVEMGIIVIPKTTNPERMKENINIF 279
Cdd:cd19117 218 -LKEPVIIKIAKKHGKTPAQVIISWGLQRGYSVLPKSVTPSRIESNFKLF 266
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
6-288 |
5.61e-66 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 208.39 E-value: 5.61e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 6 PIFTLSNGVLMPSIGLGTWQMTGEEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAElfaeGILKREDIFITTKAFCH 85
Cdd:PRK11565 5 TVIKLQDGNVMPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKE----ASVAREELFITTKLWND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 86 EvaPDVVEEALRNSLKRLRLDYVDLYLAHIPASTKDdgsfrsdvKVEDIWRGFEKVYGLGLTKAIGVSNFNESQIVRIMN 165
Cdd:PRK11565 81 D--HKRPREALEESLKKLQLDYVDLYLMHWPVPAID--------HYVEAWKGMIELQKEGLIKSIGVCNFQIHHLQRLID 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 166 IQKVPIHASQLELHLYLPQKAHRELCKKHNILITAYATLgspgrmsvvgsngrplfesTQNSENEMNDKHVKALAQKYSK 245
Cdd:PRK11565 151 ETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPL-------------------AQGGKGVFDQKVIRDLADKYGK 211
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 17566692 246 TPAQILLRATVEMGIIVIPKTTNPERMKENINIFDFNISNAEV 288
Cdd:PRK11565 212 TPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRLDKDEL 254
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
6-296 |
1.53e-64 |
|
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose reductase xyl1 (XR, EC 1.1.1.307) is a founding member of aldo-keto reductase family 2 member D1 (AKR2D1). It catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol in a NAD(P)H dependent manner.
Pssm-ID: 381341 [Multi-domain] Cd Length: 311 Bit Score: 206.12 E-value: 1.53e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 6 PIFTLSNGVLMPSIGLGTWQMTGEEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAELFAEGILKREDIFITTKAFCH 85
Cdd:cd19115 3 PTVKLNSGYDMPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLWNT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 86 EVAPDVVEEALRNSLKRLRLDYVDLYLAHIPASTKD-DGSFR--------------SDVKVEDIWRGFEKVYGLGLTKAI 150
Cdd:cd19115 83 FHDGERVEPICRKQLADWGIDYFDLFLIHFPIALKYvDPAVRyppgwfydgkkvefSNAPIQETWTAMEKLVDKGLARSI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 151 GVSNFNESQIVRIMNIQKVPIHASQLELHLYLPQKAHRELCKKHNILITAYATLGSPGRMSVVGSNGR---PLFESTQns 227
Cdd:cd19115 163 GVSNFSAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGPQSFLELDLPGAKdtpPLFEHDV-- 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17566692 228 enemndkhVKALAQKYSKTPAQILLRATVEMGIIVIPKTTNPERMKENINIFDFNISNAEVNLLEAHER 296
Cdd:cd19115 241 --------IKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDI 301
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
6-287 |
2.67e-64 |
|
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent D-xylose reductase (XR) from Pichia stipites, Kluyveromyces lactis, Pachysolen tannophilus, Candida tropicalis, and Candida tenuis, Gre3p from Saccharomyces cerevisiae, XR from Candida tropicalis, Pichia guilliermondii, Debaryomyces hansenli, and Debaryomyces nepalensis, which correspond to aldo-keto reductase family 2 member B1-B10 (AKR2B1-10), respectively. XR (EC1.1.1.307) catalyzes the NAD(P)H dependent reduction of xylose to xylitol.
Pssm-ID: 381339 [Multi-domain] Cd Length: 310 Bit Score: 205.37 E-value: 2.67e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 6 PIFTLSNGVLMPSIGLGTWQMTGEEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAELFAEGILKREDIFITTKAFCH 85
Cdd:cd19113 1 PDIKLNSGYKMPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 86 EVAPDVVEEALRNSLKRLRLDYVDLYLAHIPASTK----------------DDGSFRSDVKVEDIWRGFEKVYGLGLTKA 149
Cdd:cd19113 81 FHDPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKfvpieekyppgfycgdGDNFVYEDVPILDTWKALEKLVDAGKIKS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 150 IGVSNFNESQIVRIMNIQKVPIHASQLELHLYLPQKAHRELCKKHNILITAYATLGSPGRMSVvgSNGR-----PLFEst 224
Cdd:cd19113 161 IGVSNFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGPQSFVEL--NQGRalntpTLFE-- 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17566692 225 qnsenemnDKHVKALAQKYSKTPAQILLRATVEMGIIVIPKTTNPERMKENINIFDFNISNAE 287
Cdd:cd19113 237 --------HDTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKED 291
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
6-293 |
3.28e-64 |
|
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding member of aldo-keto reductase family 5 member H1 (AKR5H1). It is a NADPH-dependent aldo-keto reductase that reduces methylglyoxal and phenylglyoxal.
Pssm-ID: 381360 [Multi-domain] Cd Length: 263 Bit Score: 203.55 E-value: 3.28e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 6 PIFTLSNGVLMPSIGLGTWQMTGEEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAelfAEGIlKREDIFITTKAFCH 85
Cdd:cd19134 1 PTVTLNDDNTMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIA---ASGI-PRGELFVTTKLATP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 86 EVAPDVVEEALRNSLKRLRLDYVDLYLAHIPAStkddgsfrSDVKVEDIWRGFEKVYGLGLTKAIGVSNFNESQIVRIMN 165
Cdd:cd19134 77 DQGFTASQAACRASLERLGLDYVDLYLIHWPAG--------REGKYVDSWGGLMKLREEGLARSIGVSNFTAEHLENLID 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 166 IQKVPIHASQLELHLYLPQKAHRELCKKHNILITAYATLGSpGRMsvvgsngrplfestqnseneMNDKHVKALAQKYSK 245
Cdd:cd19134 149 LTFFTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGV-GRL--------------------LDNPAVTAIAAAHGR 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 17566692 246 TPAQILLRATVEMGIIVIPKTTNPERMKENINIFDFNISNAEVNLLEA 293
Cdd:cd19134 208 TPAQVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDALDG 255
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
17-291 |
1.53e-63 |
|
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), also called aldehyde reductase, is the prototype of this family. It catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
Pssm-ID: 381354 [Multi-domain] Cd Length: 277 Bit Score: 202.37 E-value: 1.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 17 PSIGLGTWQMTGEEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAELFAEGILKREDIFITTKAFCHEVAPDVVEEAL 96
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVKEQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 97 RNSLKRLRLDYVDLYLAHIPASTK--DDGSFRSD--------VKVEDIWRGFEKVYGLGLTKAIGVSNFNESQIVRIMNI 166
Cdd:cd19128 82 LITLQDLQLEYLDLFLIHWPLAFDmdTDGDPRDDnqiqslskKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLNY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 167 QKVPIHASQLELHLYLPQKAHRELCKKHNILITAYATLGspgrmsvvGSNGRPlfestqnSENEMNDKHVKALAQKYSKT 246
Cdd:cd19128 162 CKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLG--------GSYGDG-------NLTFLNDSELKALATKYNTT 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 17566692 247 PAQILLRATVEM---GIIVIPKTTNPERMKENINIFDFNISNAEVNLL 291
Cdd:cd19128 227 PPQVIIAWHLQKwpkNYSVIPKSANKSRCQQNFDINDLALTKEDMDAI 274
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
16-299 |
3.39e-59 |
|
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.
Pssm-ID: 381340 [Multi-domain] Cd Length: 302 Bit Score: 192.00 E-value: 3.39e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 16 MPSIGLGTWQMTGEEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAELFAEGILKREDIFITTKAFCHEVAPDVVEEA 95
Cdd:cd19114 4 MPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGKDHVREA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 96 LRNSLKRLRLDYVDLYLAHIPASTK------------DDGSFRS----DVKVEDIWRGFEKVYGLGLTKAIGVSNFNESQ 159
Cdd:cd19114 84 FDRQLKDYGLDYIDLYLIHFPIPAAyvdpaenypflwKDKELKKfpleQSPMQECWREMEKLVDAGLVRNIGIANFNVQL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 160 IVRIMNIQKVPIHASQLELHLYLPQKAHRELCKKHNILITAYATLGSPGRMSVVgsngrplfESTQNSENEMNDKHVKAL 239
Cdd:cd19114 164 ILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAVYTKVT--------KHLKHFTNLLEHPVVKKL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17566692 240 AQKYSKTPAQILLRATVEMGIIVIPKTTNPERMKENINIFDFNISNAEVN---LLEAHERTKQ 299
Cdd:cd19114 236 ADKHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEalyELEANARFND 298
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
8-287 |
2.04e-58 |
|
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis.
Pssm-ID: 381348 [Multi-domain] Cd Length: 291 Bit Score: 189.76 E-value: 2.04e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 8 FTLSNGVLMPSIGLGTWQMTGEEGKT--VIRNAVLAGYRHIDTATLYQNEHQIGDALAELFAEG-ILKREDIFITTKAFC 84
Cdd:cd19122 1 FTLNNGVKIPAVGFGTFANEGAKGETyaAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKVWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 85 HEVAPDVVEEALRNSLKRLRLDYVDLYLAHIP-ASTKDDgsfRSDVKV----------------EDIWRGFEKVYGLGLT 147
Cdd:cd19122 81 HLHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPiAAEKND---QRSPKLgpdgkyvilkdltenpEPTWRAMEEIYESGKA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 148 KAIGVSNFNESQIVRIMNIQKVPIHASQLELHLYLPQKAHRELCKKHNILITAYATLGSPGRMSVVGsngrplfestqns 227
Cdd:cd19122 158 KAIGVSNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQVPSTG------------- 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 228 ENEMNDKHVKALAQKYSKTPAQILLRATVEMGIIVIPKTTNPERMKENINIFDFNISNAE 287
Cdd:cd19122 225 ERVSENPTLNEVAEKGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIELSDEDFE 284
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
11-278 |
4.29e-58 |
|
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family.
Pssm-ID: 381355 [Multi-domain] Cd Length: 295 Bit Score: 188.82 E-value: 4.29e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 11 SNGVLMPSIGLGTWQMTGEEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAELFAEGILKREDIFITTKAFCHEVAPD 90
Cdd:cd19129 1 NGSGAIPALGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNHRPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 91 VVEEALRNSLKRLRLDYVDLYLAHIPASTK--DDGSFR---------SDVKVEDIWRGFEKVYGLGLTKAIGVSNFNESQ 159
Cdd:cd19129 81 RVKPAFEASLKRLQLDYLDLYLIHTPFAFQpgDEQDPRdangnviydDGVTLLDTWRAMERLVDEGRCKAIGLSDVSLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 160 IVRIMNIQKVPIHASQLELHLYLPQKAHRELCKKHNILITAYATLGSpgrmsvvGSNGRPLfestqnsenemNDKHVKAL 239
Cdd:cd19129 161 LREIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGH-------GMEPKLL-----------EDPVITAI 222
|
250 260 270
....*....|....*....|....*....|....*....
gi 17566692 240 AQKYSKTPAQILLRATVEMGIIVIPKTTNPERMKENINI 278
Cdd:cd19129 223 ARRVNKTPAQVLLAWAIQRGTALLTTSKTPSRIRENFDI 261
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
16-287 |
4.88e-56 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 182.17 E-value: 4.88e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 16 MPSIGLGTWQMTGEEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAElfaEGIlKREDIFITTKAFCHEVAPDVVEEA 95
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAE---SGV-PRDELFITTKIWIDNLSKDKLLPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 96 LRNSLKRLRLDYVDLYLAHIPAStkDDGsfrsdVKVEDIWRGFEKVYGLGLTKAIGVSNFNESQIVR-IMNIQKVPIHAS 174
Cdd:cd19139 77 LEESLEKLRTDYVDLTLIHWPSP--NDE-----VPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEaIAVVGAGAIATN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 175 QLELHLYLPQKAHRELCKKHNILITAYATLGSpGRMsvvgsngrplfestqnseneMNDKHVKALAQKYSKTPAQILLRA 254
Cdd:cd19139 150 QIELSPYLQNRKLVAHCKQHGIHVTSYMTLAY-GKV--------------------LDDPVLAAIAERHGATPAQIALAW 208
|
250 260 270
....*....|....*....|....*....|...
gi 17566692 255 TVEMGIIVIPKTTNPERMKENINIFDFNISNAE 287
Cdd:cd19139 209 AMARGYAVIPSSTKREHLRSNLLALDLTLDADD 241
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
16-292 |
1.43e-54 |
|
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase. Escherichia coli YeaE may act as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381298 [Multi-domain] Cd Length: 263 Bit Score: 178.58 E-value: 1.43e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 16 MPSIGLGTWQMTGEEGKT---------VIRNAVLAGYRHIDTATLYQNEHQ---IGDALAELfaegilKREDIFITTKAF 83
Cdd:cd19072 4 VPVLGLGTWGIGGGMSKDysddkkaieALRYAIELGINLIDTAEMYGGGHAeelVGKAIKGF------DREDLFITTKVS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 84 CHEVAPDVVEEALRNSLKRLRLDYVDLYLAHIPastkddgsfRSDVKVEDIWRGFEKVYGLGLTKAIGVSNFNESQIVRI 163
Cdd:cd19072 78 PDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWP---------NPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 164 MN-IQKVPIHASQLELHLYLpQKAHREL---CKKHNILITAYATLgspGRMSVVGSNGRPLFEStqnsenemndkhvkaL 239
Cdd:cd19072 149 QSyLKKGPIVANQVEYNLFD-REEESGLlpyCQKNGIAIIAYSPL---EKGKLSNAKGSPLLDE---------------I 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 17566692 240 AQKYSKTPAQILLRATV-EMGIIVIPKTTNPERMKENINIFDFNISNAEVNLLE 292
Cdd:cd19072 210 AKKYGKTPAQIALNWLIsKPNVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
9-293 |
1.15e-52 |
|
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; Corynebacterium sp. DkgA is a founding member of aldo-keto reductase family 5 member C1 (AKR5C1). DkgA (EC 1.1.1.346), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates.
Pssm-ID: 381356 [Multi-domain] Cd Length: 256 Bit Score: 173.56 E-value: 1.15e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 9 TLSNGVLMPSIGLGTWQMTGEEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAelfAEGIlKREDIFITTKAFCHEVA 88
Cdd:cd19130 3 VLNDGNSIPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIA---ASGI-PRDELFVTTKLWNDRHD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 89 PDVVEEALRNSLKRLRLDYVDLYLAHIPASTKDDgsfrsdvkVEDIWRGFEKVYGLGLTKAIGVSNFNESQIVRIMNIQK 168
Cdd:cd19130 79 GDEPAAAFAESLAKLGLDQVDLYLVHWPTPAAGN--------YVHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVAATG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 169 VPIHASQLELHLYLPQKAHRELCKKHNILITAYATLGSpGRMsvvgsngrplfestqnseneMNDKHVKALAQKYSKTPA 248
Cdd:cd19130 151 VVPAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQ-GKL--------------------LGDPPVGAIAAAHGKTPA 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 17566692 249 QILLRATVEMGIIVIPKTTNPERMKENINIFDFNISNAEVNLLEA 293
Cdd:cd19130 210 QIVLRWHLQKGHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAIDA 254
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
19-294 |
2.24e-52 |
|
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain regulatory domains - these are reported to have oxidoreductase activity.
Pssm-ID: 425554 [Multi-domain] Cd Length: 290 Bit Score: 174.04 E-value: 2.24e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 19 IGLGTWQMTGEEGKT-------VIRNAVLAGYRHIDTATLY---QNEHQIGDALAELFAegilKREDIFITTK------- 81
Cdd:pfam00248 1 IGLGTWQLGGGWGPIskeealeALRAALEAGINFIDTAEVYgdgKSEELLGEALKDYPV----KRDKVVIATKvpdgdgp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 82 -AFCHEvaPDVVEEALRNSLKRLRLDYVDLYLAHIPastkdDGsfrsDVKVEDIWRGFEKVYGLGLTKAIGVSNFNESQI 160
Cdd:pfam00248 77 wPSGGS--KENIRKSLEESLKRLGTDYIDLYYLHWP-----DP----DTPIEETWDALEELKKEGKIRAIGVSNFDAEQI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 161 VRIMNIQKVPIHASQLELHLYLPQKAH--RELCKKHNILITAYATLGSP------GRMSVVGSNGRPLFESTQNSENEMN 232
Cdd:pfam00248 146 EKALTKGKIPIVAVQVEYNLLRRRQEEelLEYCKKNGIPLIAYSPLGGGlltgkyTRDPDKGPGERRRLLKKGTPLNLEA 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17566692 233 DKHVKALAQKYSKTPAQILLR--ATVEMGIIVIPKTTNPERMKENINIFDFNISNAEVNLLEAH 294
Cdd:pfam00248 226 LEALEEIAKEHGVSPAQVALRwaLSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDEL 289
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
16-300 |
3.87e-51 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 170.20 E-value: 3.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 16 MPSIGLGTWQMTGEEGKTVIRNAVLAGYRHIDTATLYQNEHQIGDALAElfaEGIlKREDIFITTKAFCHEVAPDVVEEA 95
Cdd:PRK11172 3 IPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAE---SGV-PRDELFITTKIWIDNLAKDKLIPS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 96 LRNSLKRLRLDYVDLYLAHIPAStkDDGsfrsdVKVEDIWRGFEKVYGLGLTKAIGVSNFNESQIVR-IMNIQKVPIHAS 174
Cdd:PRK11172 79 LKESLQKLRTDYVDLTLIHWPSP--NDE-----VSVEEFMQALLEAKKQGLTREIGISNFTIALMKQaIAAVGAENIATN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 175 QLELHLYLPQKAHRELCKKHNILITAYATLGSpgrmsvvgsnGRPLfestqnsenemNDKHVKALAQKYSKTPAQILLRA 254
Cdd:PRK11172 152 QIELSPYLQNRKVVAFAKEHGIHVTSYMTLAY----------GKVL-----------KDPVIARIAAKHNATPAQVILAW 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 17566692 255 TVEMGIIVIPKTTNPERMKENINIFDFNISNAEVNLLEAHERTKQE 300
Cdd:PRK11172 211 AMQLGYSVIPSSTKRENLASNLLAQDLQLDAEDMAAIAALDRNGRL 256
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
13-294 |
3.15e-43 |
|
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme transport and metabolism, General function prediction only];
Pssm-ID: 440431 [Multi-domain] Cd Length: 316 Bit Score: 150.71 E-value: 3.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 13 GVLMPSIGLGTWQMTG-------EEGKTVIRNAVLAGYRHIDTATLY---QNEHQIGDALAELfaegilKREDIFITTKA 82
Cdd:COG0667 10 GLKVSRLGLGTMTFGGpwggvdeAEAIAILDAALDAGINFFDTADVYgpgRSEELLGEALKGR------PRDDVVIATKV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 83 FCHEVA--------PDVVEEALRNSLKRLRLDYVDLYLAHIPastkDDgsfrsDVKVEDIWRGFEKvygL---GLTKAIG 151
Cdd:COG0667 84 GRRMGPgpngrglsREHIRRAVEASLRRLGTDYIDLYQLHRP----DP-----DTPIEETLGALDE---LvreGKIRYIG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 152 VSNFNESQIVRIMNIQK--VPIHASQLELHLyLPQKAHREL---CKKHNILITAYATLGS--------PGRMSVVGSNGR 218
Cdd:COG0667 152 VSNYSAEQLRRALAIAEglPPIVAVQNEYSL-LDRSAEEELlpaARELGVGVLAYSPLAGglltgkyrRGATFPEGDRAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 219 PLFESTQNSEN--EMNDKhVKALAQKYSKTPAQI-----LLRATVemgIIVIPKTTNPERMKENINIFDFNISNAEVNLL 291
Cdd:COG0667 231 TNFVQGYLTERnlALVDA-LRAIAAEHGVTPAQLalawlLAQPGV---TSVIPGARSPEQLEENLAAADLELSAEDLAAL 306
|
...
gi 17566692 292 EAH 294
Cdd:COG0667 307 DAA 309
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
9-275 |
4.08e-43 |
|
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this family. It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381364 [Multi-domain] Cd Length: 266 Bit Score: 149.32 E-value: 4.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 9 TLSNGVLMPSIGLGTWQM-----TGEEGKTVIRNAVLAGYRHIDTATLYQN---EHQIGDALAELfaegilkREDIFITT 80
Cdd:cd19138 4 TLPDGTKVPALGQGTWYMgedpaKRAQEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR-------RDKVFLVS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 81 KAFCHEVAPDVVEEALRNSLKRLRLDYVDLYLAHipastkddgsFRSDVKVEDIWRGFEKVYGLGLTKAIGVSNFNES-- 158
Cdd:cd19138 77 KVLPSNASRQGTVRACERSLRRLGTDYLDLYLLH----------WRGGVPLAETVAAMEELKKEGKIRAWGVSNFDTDdm 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 159 -QIVRIMNIQKVPihASQLELHLylpqkAHR----EL---CKKHNILITAYATLGSPGRMsvvgsnGRPLFESTQnsene 230
Cdd:cd19138 147 eELWAVPGGGNCA--ANQVLYNL-----GSRgieyDLlpwCREHGVPVMAYSPLAQGGLL------RRGLLENPT----- 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 17566692 231 mndkhVKALAQKYSKTPAQILLRATV-EMGIIVIPKTTNPERMKEN 275
Cdd:cd19138 209 -----LKEIAARHGATPAQVALAWVLrDGNVIAIPKSGSPEHAREN 249
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
13-292 |
2.07e-41 |
|
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381363 [Multi-domain] Cd Length: 260 Bit Score: 144.64 E-value: 2.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 13 GVLMPSIGLGTWQMTG---------EEGKTVIRNAVLAGYRHIDTATLYQNEHQigdalAELFAEGIL--KREDIFITTK 81
Cdd:cd19137 1 GEKIPALGLGTWGIGGfltpdysrdEEMVELLKTAIELGYTHIDTAEMYGGGHT-----EELVGKAIKdfPREDLFIVTK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 82 AFCHEVAPDVVEEALRNSLKRLRLDYVDLYLAHIPastkddgsfRSDVKVEDIWRGFEKVYGLGLTKAIGVSNFNESQIV 161
Cdd:cd19137 76 VWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWP---------NPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 162 RIMNIQKVPIHASQLELHLYLPQKAHREL---CKKHNILITAYatlgSPGRMSVVGSNgrplfestqnsenemndKHVKA 238
Cdd:cd19137 147 EAISKSQTPIVCNQVKYNLEDRDPERDGLleyCQKNGITVVAY----SPLRRGLEKTN-----------------RTLEE 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 17566692 239 LAQKYSKTPAQILLRATVEM-GIIVIPKTTNPERMKENINIFDFNISNAEVNLLE 292
Cdd:cd19137 206 IAKNYGKTIAQIALAWLIQKpNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
17-292 |
8.43e-39 |
|
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR (EC 1.1.1.65) is the prototype of this family. It catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+), and is involved in the PLP salvage pathway.
Pssm-ID: 381319 [Multi-domain] Cd Length: 293 Bit Score: 138.51 E-value: 8.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 17 PSIGLGTWQ----MTG-------EEGKTVIRNAVLAGYRHIDTATLYqnehqiGDALAEL----FAEGILKREDIFITTK 81
Cdd:cd19093 3 SPLGLGTWQwgdrLWWgygeygdEDLQAAFDAALEAGVNLFDTAEVY------GTGRSERllgrFLKELGDRDEVVIATK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 82 --AFCHEVAPDVVEEALRNSLKRLRLDYVDLYLAHIPASTkddgsfrsDVKVEDIWRGFEKVYGLGLTKAIGVSNFNESQ 159
Cdd:cd19093 77 faPLPWRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPW--------YSQIEALMDGLADAVEEGLVRAVGVSNYSADQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 160 IVRI---MNIQKVPIHASQLELHL--YLP-QKAHRELCKKHNILITAYATLGSpGRMSvvG--------SNGRPLFESTQ 225
Cdd:cd19093 149 LRRAhkaLKERGVPLASNQVEYSLlyRDPeQNGLLPACDELGITLIAYSPLAQ-GLLT--GkyspenppPGGRRRLFGRK 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17566692 226 NSE------NEMndkhvKALAQKYSKTPAQILLRATVEMGIIVIPKTTNPERMKENINIFDFNISNAEVNLLE 292
Cdd:cd19093 226 NLEkvqpllDAL-----EEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
17-292 |
1.09e-38 |
|
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381310 [Multi-domain] Cd Length: 296 Bit Score: 138.43 E-value: 1.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 17 PSIGLGTWQMTG--------EEGKTVIRNAVLAGYRHIDTATLYQN---EHQIGDALAElfaegilKREDIFITTK---- 81
Cdd:cd19084 5 SRIGLGTWAIGGtwwgevddQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKG-------RRDDVVIATKcglr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 82 -----AFCHEVAPDVVEEALRNSLKRLRLDYVDLYLAHIPastkdDGsfrsDVKVEDIWRGFEKVYGLGLTKAIGVSNFN 156
Cdd:cd19084 78 wdggkGVTKDLSPESIRKEVEQSLRRLQTDYIDLYQIHWP-----DP----NTPIEETAEALEKLKKEGKIRYIGVSNFS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 157 ESQIVRIMNIqkVPIHASQLELHLyLPQKAHREL---CKKHNILITAYATL------GSPGRMSVVGSNGR--------- 218
Cdd:cd19084 149 VEQLEEARKY--GPIVSLQPPYSM-LEREIEEELlpyCRENGIGVLPYGPLaqglltGKYKKEPTFPPDDRrsrfpffrg 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17566692 219 PLFESTQNSENEMndkhvKALAQKYSKTPAQILLRATV--EMGIIVIPKTTNPERMKENINIFDFNISNAEVNLLE 292
Cdd:cd19084 226 ENFEKNLEIVDKL-----KEIAEKYGKSLAQLAIAWTLaqPGVTSAIVGAKNPEQLEENAGALDWELTEEELKEID 296
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
17-206 |
4.87e-36 |
|
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications. Members have very distinct functions and include the prokaryotic 2,5-diketo-D-gluconic acid reductases and beta-keto ester reductases, the eukaryotic aldose reductases, aldehyde reductases, hydroxysteroid dehydrogenases, steroid 5beta-reductases, potassium channel beta-subunits, and aflatoxin aldehyde reductases, among others.
Pssm-ID: 381296 [Multi-domain] Cd Length: 232 Bit Score: 129.56 E-value: 4.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 17 PSIGLGTWQMTG----EEGKTVIRNAVLAGYRHIDTATLY---QNEHQIGDALAELFaegilKREDIFITTKAFCHE--- 86
Cdd:cd06660 1 SRLGLGTMTFGGdgdeEEAFALLDAALEAGGNFFDTADVYgdgRSERLLGRWLKGRG-----NRDDVVIATKGGHPPggd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 87 -----VAPDVVEEALRNSLKRLRLDYVDLYLAHipastKDDgsfrSDVKVEDIWRGFEKVYGLGLTKAIGVSNFNESQIV 161
Cdd:cd06660 76 psrsrLSPEHIRRDLEESLRRLGTDYIDLYYLH-----RDD----PSTPVEETLEALNELVREGKIRYIGVSNWSAERLA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17566692 162 RIMNIQK----VPIHASQLELHLYLPQKAHREL---CKKHNILITAYATLGS 206
Cdd:cd06660 147 EALAYAKahglPGFAAVQPQYSLLDRSPMEEELldwAEENGLPLLAYSPLAR 198
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
17-293 |
1.28e-35 |
|
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is a founding member of aldo-keto reductase family 11 member B3(AKR11B3). It is responsible for methylglyoxal detoxification.
Pssm-ID: 381311 [Multi-domain] Cd Length: 292 Bit Score: 130.40 E-value: 1.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 17 PSIGLGTWQMTG---------EEGKTVIRNAVLAGYRHIDTATLYQN---EHQIGDALAElfaegilKREDIFITTKAFC 84
Cdd:cd19085 2 SRLGLGCWQFGGgywwgdqddEESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKG-------RRDDVVIATKVSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 85 HEVAPDVVEEALRNSLKRLRLDYVDLYLAHIPastkddgsfRSDVKVEDIWRGFEKVYGLGLTKAIGVSNFNESQIVRIM 164
Cdd:cd19085 75 DNLTPEDVRKSCERSLKRLGTDYIDLYQIHWP---------SSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 165 NIQKVPIHasQLELHL--------YLPqkahreLCKKHNILITAYATLGS--------------PGRMsvvGSNGRPLFE 222
Cdd:cd19085 146 DAGRIDSN--QLPYNLlwraieyeILP------FCREHGIGVLAYSPLAQglltgkfssaedfpPGDA---RTRLFRHFE 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17566692 223 StQNSENEMN--DKhVKALAQKYSKTPAQ-----ILLRATVEmGIIVIPKttNPERMKENINIFDFNISNAEVNLLEA 293
Cdd:cd19085 215 P-GAEEETFEalEK-LKEIADELGVTMAQlalawVLQQPGVT-SVIVGAR--NPEQLEENAAAVDLELSPSVLERLDE 287
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
19-293 |
2.02e-26 |
|
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1).
Pssm-ID: 381309 [Multi-domain] Cd Length: 307 Bit Score: 105.96 E-value: 2.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 19 IGLGTWQMTG---------EEGKTVIRNAVLAGYRHIDTATLY---QNEHQIGDALAELfaegilKREDIFITTKAFCHE 86
Cdd:cd19083 14 IGLGTNAVGGhnlypnldeEEGKDLVREALDNGVNLLDTAFIYglgRSEELVGEVLKEY------NRNEVVIATKGAHKF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 87 VA--------PDVVEEALRNSLKRLRLDYVDLYLAHIPastkdDGsfrsDVKVEDIWRGFEKVYGLGLTKAIGVSNFNES 158
Cdd:cd19083 88 GGdgsvlnnsPEFLRSAVEKSLKRLNTDYIDLYYIHFP-----DG----ETPKAEAVGALQELKDEGKIRAIGVSNFSLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 159 QIVRIMNIQKVPIHASQLELHLYLPQKAHRELCKKHNILITAYATLGS---PGRMSVVGS-------NGRPLFESTQNSE 228
Cdd:cd19083 159 QLKEANKDGYVDVLQGEYNLLQREAEEDILPYCVENNISFIPYFPLASgllAGKYTKDTKfpdndlrNDKPLFKGERFSE 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 229 NEMNDKHVKALAQKYSKTPAQILL-----RATVEmgiIVIPKTTNPERMKENINIFDFNISNAEVNLLEA 293
Cdd:cd19083 239 NLDKVDKLKSIADEKGVTVAHLALawyltRPAID---VVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDA 305
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
12-288 |
1.17e-25 |
|
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor.
Pssm-ID: 381370 [Multi-domain] Cd Length: 323 Bit Score: 104.45 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 12 NGVLMPSIGLGTWQM--------TGEEGKTVIRNAVLAGYRHIDTATLYQ-NEHQIGdalaELFAEGILKREDIFITTKa 82
Cdd:cd19144 9 NGPSVPALGFGAMGLsafygppkPDEERFAVLDAAFELGCTFWDTADIYGdSEELIG----RWFKQNPGKREKIFLATK- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 83 FCHEV-----------APDVVEEALRNSLKRLRLDYVDLYLAHipastkddgSFRSDVKVEDIWRGFEKVYGLGLTKAIG 151
Cdd:cd19144 84 FGIEKnvetgeysvdgSPEYVKKACETSLKRLGVDYIDLYYQH---------RVDGKTPIEKTVAAMAELVQEGKIKHIG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 152 VSNFNESQIVRIMNIQkvPIHASQLE-----LHLYLPQKAHRELCKKHNILITAYATLgspGRMSVVGSNGRPL-FESTQ 225
Cdd:cd19144 155 LSECSAETLRRAHAVH--PIAAVQIEyspfsLDIERPEIGVLDTCRELGVAIVAYSPL---GRGFLTGAIRSPDdFEEGD 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17566692 226 --------NSEN-----EMNDKhVKALAQKYSKTPAQILLRATVEMG--IIVIPKTTNPERMKENINIFDFNISNAEV 288
Cdd:cd19144 230 frrmaprfQAENfpknlELVDK-IKAIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLEENLGALKVKLTEEEE 306
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
13-284 |
1.96e-25 |
|
Shaker potassium channel beta subunit family and similar proteins; This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. The family also includes Drosophila melanogaster Hk protein, a founding member of aldo-keto reductase family 6 member B1 (AKR6B1), as well as voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa, founding members of AKR6C1and AKR6C2, respectively. Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381300 [Multi-domain] Cd Length: 297 Bit Score: 103.06 E-value: 1.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 13 GVLMPSIGLGTW-----QMTGEEGKTVIRNAVLAGYRHIDTATLY---QNEHQIGDALAELfaegilKREDIFITTKAFc 84
Cdd:cd19074 1 GLKVSELSLGTWltfggQVDDEDAKACVRKAYDLGINFFDTADVYaagQAEEVLGKALKGW------PRESYVISTKVF- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 85 HEVAPDVVE---------EALRNSLKRLRLDYVDLYLAHipastkddgSFRSDVKVEDIWRGFEKVYGLGLTKAIGVSNF 155
Cdd:cd19074 74 WPTGPGPNDrglsrkhifESIHASLKRLQLDYVDIYYCH---------RYDPETPLEETVRAMDDLIRQGKILYWGTSEW 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 156 NESQIVRIMNIQK----VPIHASQLELHLYLPQKAH--RELCKKHNILITAYatlgSPGRMSVV---GSNGRPLFESTQN 226
Cdd:cd19074 145 SAEQIAEAHDLARqfglIPPVVEQPQYNMLWREIEEevIPLCEKNGIGLVVW----SPLAQGLLtgkYRDGIPPPSRSRA 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17566692 227 SENEMND--------------KHVKALAQKYSKTPAQ-----ILLRATVEMGIIvipKTTNPERMKENINIFDFNIS 284
Cdd:cd19074 221 TDEDNRDkkrrlltdenlekvKKLKPIADELGLTLAQlalawCLRNPAVSSAII---GASRPEQLEENVKASGVKLS 294
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
22-292 |
2.28e-25 |
|
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381305 [Multi-domain] Cd Length: 312 Bit Score: 103.05 E-value: 2.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 22 GTWQMTGEEGKTVIRNAVLAGYRHIDTATLYQN---EHQIGDALAELfaegiLKREDIFITTKaFCHEVAPDV------- 91
Cdd:cd19079 28 RPWVLDEEESRPIIKRALDLGINFFDTANVYSGgasEEILGRALKEF-----APRDEVVIATK-VYFPMGDGPngrglsr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 92 --VEEALRNSLKRLRLDYVDLYLAHipastkddgSFRSDVKVEDIWRGFEKVYGLGLTKAIGVSNFNESQIVRIMNIQKV 169
Cdd:cd19079 102 khIMAEVDASLKRLGTDYIDLYQIH---------RWDYETPIEETLEALHDVVKSGKVRYIGASSMYAWQFAKALHLAEK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 170 ----PIHASQLELHLyLPQKAHRE---LCKKHNILITAYATLGSpGRMS----VVGSNGRPLFESTQNSENEMNDK---- 234
Cdd:cd19079 173 ngwtKFVSMQNHYNL-LYREEEREmipLCEEEGIGVIPWSPLAR-GRLArpwgDTTERRRSTTDTAKLKYDYFTEAdkei 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17566692 235 --HVKALAQKYSKTPAQILLRATVEMGIIVIP--KTTNPERMKENINIFDFNISNAEVNLLE 292
Cdd:cd19079 251 vdRVEEVAKERGVSMAQVALAWLLSKPGVTAPivGATKLEHLEDAVAALDIKLSEEEIKYLE 312
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
11-291 |
3.26e-25 |
|
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor. Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381302 [Multi-domain] Cd Length: 303 Bit Score: 102.68 E-value: 3.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 11 SNGVLMPSIGLGTWQMTG-------EEGKTVIRNAVLAGYRHIDTATLYQ---NEHQIGDALAElfaegilKREDIFITT 80
Cdd:cd19076 7 TQGLEVSALGLGCMGMSAfygpadeEESIATLHRALELGVTFLDTADMYGpgtNEELLGKALKD-------RRDEVVIAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 81 K----------AFCHEVAPDVVEEALRNSLKRLRLDYVDLYLAHIPastkDdgsfrSDVKVEDIWRGFEKVYGLGLTKAI 150
Cdd:cd19076 80 KfgivrdpgsgFRGVDGRPEYVRAACEASLKRLGTDVIDLYYQHRV----D-----PNVPIEETVGAMAELVEEGKVRYI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 151 GVSNFNESQIVRimnIQKV-PIHASQLELHLY--------LPqkAHRELckkhNILITAYATLG--------------SP 207
Cdd:cd19076 151 GLSEASADTIRR---AHAVhPITAVQSEYSLWtrdiedevLP--TCREL----GIGFVAYSPLGrgfltgaikspedlPE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 208 GRMSvvGSNGRPLFESTQNseNEMNDKHVKALAQKYSKTPAQILLRATVEMG--IIVIPKTTNPERMKENINIFDFNISN 285
Cdd:cd19076 222 DDFR--RNNPRFQGENFDK--NLKLVEKLEAIAAEKGCTPAQLALAWVLAQGddIVPIPGTKRIKYLEENVGALDVVLTP 297
|
....*.
gi 17566692 286 AEVNLL 291
Cdd:cd19076 298 EELAEI 303
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-293 |
3.96e-25 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 102.37 E-value: 3.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 19 IGLGTWQMTG------------EEGKTVIRNAVLAGYRHIDTATLY---QNEHQIGDALAELfaegilkREDIFITTKaf 83
Cdd:cd19102 4 IGLGTWAIGGggwgggwgpqddRDSIAAIRAALDLGINWIDTAAVYglgHSEEVVGRALKGL-------RDRPIVATK-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 84 C-----------HEVAPDVVEEALRNSLKRLRLDYVDLYLAHIPASTKDdgsfrsdvkVEDIWRGFEKVYGLGLTKAIGV 152
Cdd:cd19102 75 CgllwdeegrirRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEP---------IEEAWGALAELKEEGKVRAIGV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 153 SNFNESQIVRIMNIQkvPIHASQLELHLyLPQKAHREL---CKKHNILITAYATLGS--------PGRMSVVGSNGR--- 218
Cdd:cd19102 146 SNFSVDQMKRCQAIH--PIASLQPPYSL-LRRGIEAEIlpfCAEHGIGVIVYSPMQSglltgkmtPERVASLPADDWrrr 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 219 -PLFESTQNSENEMNDKHVKALAQKYSKTPAQI----LLRATVEMGIIVipKTTNPERMKENINIFDFNISNAEVNLLEA 293
Cdd:cd19102 223 sPFFQEPNLARNLALVDALRPIAERHGRTVAQLaiawVLRRPEVTSAIV--GARRPDQIDETVGAADLRLTPEELAEIEA 300
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
11-287 |
9.51e-25 |
|
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and Escherichia coli YdhF are prototypes of this family. They are uncharacterized aldo/keto reductase family oxidoreductases.
Pssm-ID: 381318 [Multi-domain] Cd Length: 287 Bit Score: 101.09 E-value: 9.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 11 SNGVLMPSIGLGTW-----QMTGEEGKTVIRNAVLAGYRHIDTA---TLYQNEHQIGDALAElfaEGILkREDIFITTKA 82
Cdd:cd19092 1 PEGLEVSRLVLGCMrladwGESAEELLSLIEAALELGITTFDHAdiyGGGKCEELFGEALAL---NPGL-REKIEIQTKC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 83 ---FCHEVAPDVVE----------EALRNSLKRLRLDYVDLYLAHipastkddgsfRSD--VKVEDIWRGFEKVYGLGLT 147
Cdd:cd19092 77 girLGDDPRPGRIKhydtskehilASVEGSLKRLGTDYLDLLLLH-----------RPDplMDPEEVAEAFDELVKSGKV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 148 KAIGVSNFNESQIVRIMNIQKVPIHASQLE---LHLYLPQKAHRELCKKHNILITAYATLGspgrmsvvgsNGRpLFEST 224
Cdd:cd19092 146 RYFGVSNFTPSQIELLQSYLDQPLVTNQIElslLHTEAIDDGTLDYCQLLDITPMAWSPLG----------GGR-LFGGF 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17566692 225 QNSENEMNDKhVKALAQKYSKTPAQI----LLRATVemGIIVIPKTTNPERMKENINIFDFNISNAE 287
Cdd:cd19092 215 DERFQRLRAA-LEELAEEYGVTIEAIalawLLRHPA--RIQPILGTTNPERIRSAVKALDIELTREE 278
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
19-204 |
1.61e-24 |
|
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381374 [Multi-domain] Cd Length: 302 Bit Score: 100.84 E-value: 1.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 19 IGLGTWQMTG--------EEGKTVIRNAVLAGYRHIDTATLY---QNEHQIGDALaelfaEGILKREDIFITTKA----- 82
Cdd:cd19148 7 IALGTWAIGGwmwggtdeKEAIETIHKALDLGINLIDTAPVYgfgLSEEIVGKAL-----KEYGKRDRVVIATKVglewd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 83 ----FCHEVAPDVVEEALRNSLKRLRLDYVDLYLAHIPastkDDGsfrsdVKVEDIWRGFEKVYGLGLTKAIGVSNFNES 158
Cdd:cd19148 82 eggeVVRNSSPARIRKEVEDSLRRLQTDYIDLYQVHWP----DPL-----VPIEETAEALKELLDEGKIRAIGVSNFSPE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17566692 159 QIVRIMniQKVPIHASQLELHLYLPQkAHREL---CKKHNILITAYATL 204
Cdd:cd19148 153 QMETFR--KVAPLHTVQPPYNLFERE-IEKDVlpyARKHNIVTLAYGAL 198
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
20-287 |
1.69e-24 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 100.61 E-value: 1.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 20 GLGTWQMTGEEGKTVIRNAVLAGYRHIDTA---TLYQNEHQIGDALAElfaEGILkREDIFITTKA---FCHEVAPDVVE 93
Cdd:COG4989 22 RLGEWDLSPAEAAALIEAALELGITTFDHAdiyGGYTCEALFGEALKL---SPSL-REKIELQTKCgirLPSEARDNRVK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 94 ----------EALRNSLKRLRLDYVDLYLAHipastkddgsfRSD--VKVEDIWRGFEKVYGLGLTKAIGVSNFNESQIV 161
Cdd:COG4989 98 hydtskehiiASVEGSLRRLGTDYLDLLLLH-----------RPDplMDPEEVAEAFDELKASGKVRHFGVSNFTPSQFE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 162 RIMNIQKVPIHASQLELHLylpqkAHREL--------CKKHNILITAYATLGSpGRmsvvgsngrplFESTQNSEN-EMN 232
Cdd:COG4989 167 LLQSALDQPLVTNQIELSL-----LHTDAfddgtldyCQLNGITPMAWSPLAG-GR-----------LFGGFDEQFpRLR 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17566692 233 DKhVKALAQKYSKTPAQI----LLR--AtvemGIIVIPKTTNPERMKENINIFDFNISNAE 287
Cdd:COG4989 230 AA-LDELAEKYGVSPEAIalawLLRhpA----GIQPVIGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
17-276 |
4.15e-24 |
|
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde dehydrogenase is a founding member of aldo-keto reductase family 13 member B1 (AKR13B1). phenylacetaldehyde dehydrogenase (EC 1.2.1.39) catalyzes the NAD+-dependent oxidation of phenylactealdehyde to phenylacetic acid.
Pssm-ID: 381314 [Multi-domain] Cd Length: 256 Bit Score: 98.44 E-value: 4.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 17 PSIGLGTWQMTG----------EEGKTVIRNAVLAGYRHIDTATLY---QNEHQIGDALAElfaegilKREDIFITTKA- 82
Cdd:cd19088 2 SRLGYGAMRLTGpgiwgppadrEEAIAVLRRALELGVNFIDTADSYgpdVNERLIAEALHP-------YPDDVVIATKGg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 83 --------FCHEVAPDVVEEALRNSLKRLRLDYVDLYLAHIPastkDDgsfrsDVKVEDIWRGFEKVYGLGLTKAIGVSN 154
Cdd:cd19088 75 lvrtgpgwWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRI----DP-----KVPFEEQLGALAELQDEGLIRHIGLSN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 155 FNESQIVRIMNIqkVPIHASQLELHLylpqkAHR------ELCKKHNILITAYATLGSpgrmsvvgsnGRPLFESTQnse 228
Cdd:cd19088 146 VTVAQIEEARAI--VRIVSVQNRYNL-----ANRddegvlDYCEAAGIAFIPWFPLGG----------GDLAQPGGL--- 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 17566692 229 nemndkhVKALAQKYSKTPAQILLRATVEMG--IIVIPKTTNPERMKENI 276
Cdd:cd19088 206 -------LAEVAARLGATPAQVALAWLLARSpvMLPIPGTSSVEHLEENL 248
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
13-293 |
6.46e-23 |
|
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381375 [Multi-domain] Cd Length: 315 Bit Score: 96.57 E-value: 6.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 13 GVLMPSIGLGTWQMTG---------EEGKTVIRNAVLAGYRHIDTATLYQN---EHQIGDALAElfaegilKREDIFITT 80
Cdd:cd19149 8 GIEASVIGLGTWAIGGgpwwggsddNESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKG-------RRDKVVLAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 81 K----------AFCHE---------VAPDVVEEALRNSLKRLRLDYVDLYLAHIPASTkddgsfrsdVKVEDIWRGFEKV 141
Cdd:cd19149 81 KcglrwdreggSFFFVrdgvtvyknLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVE---------TPIEETMEALEEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 142 YGLGLTKAIGVSNFNESQI---VRIMNIQKVPIHASQLELHL---YLPqkahreLCKKHNILITAYATLGS--------P 207
Cdd:cd19149 152 KRQGKIRAIGASNVSVEQIkeyVKAGQLDIIQEKYSMLDRGIekeLLP------YCKKNNIAFQAYSPLEQglltgkitP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 208 GRMSVVGS--NGRPLFeSTQNSE--NEMNDKhVKALAQKYSKTPAQILLRATVEMG--IIVIPKTTNPERMKENINIFDF 281
Cdd:cd19149 226 DREFDAGDarSGIPWF-SPENREkvLALLEK-WKPLCEKYGCTLAQLVIAWTLAQPgiTSALCGARKPEQAEENAKAGDI 303
|
330
....*....|..
gi 17566692 282 NISNAEVNLLEA 293
Cdd:cd19149 304 RLSAEDIATMRS 315
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
19-276 |
1.51e-22 |
|
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381321 [Multi-domain] Cd Length: 253 Bit Score: 94.22 E-value: 1.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 19 IGLGTWQ-------MTGEEGKTVIRNAVLAGYRHIDTATLYQN-EHQIGDALAELFaegilkREDIFITTKAFCHEVA-- 88
Cdd:cd19095 3 LGLGTSGigrvwgvPSEAEAARLLNTALDLGINLIDTAPAYGRsEERLGRALAGLR------RDDLFIATKVGTHGEGgr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 89 ------PDVVEEALRNSLKRLRLDYVDLYLAHIPAstkddgsfrSDVKVEDIWRGFEKVYGLGLTKAIGVSNFNEsQIVR 162
Cdd:cd19095 77 drkdfsPAAIRASIERSLRRLGTDYIDLLQLHGPS---------DDELTGEVLETLEDLKAAGKVRYIGVSGDGE-ELEA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 163 ImnIQKVPIHASQLELHLYLPQKAHR-ELCKKHNILITAYATLGspgrmsvvgsNGRPLFESTQNSENEMNDKHVKALAQ 241
Cdd:cd19095 147 A--IASGVFDVVQLPYNVLDREEEELlPLAAEAGLGVIVNRPLA----------NGRLRRRVRRRPLYADYARRPEFAAE 214
|
250 260 270
....*....|....*....|....*....|....*..
gi 17566692 242 KYSKTPAQILLRATV-EMGI-IVIPKTTNPERMKENI 276
Cdd:cd19095 215 IGGATWAQAALRFVLsHPGVsSAIVGTTNPEHLEENL 251
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-276 |
2.38e-22 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 93.80 E-value: 2.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 13 GVLMPSIGLGTwQMTGEEGKTVIRNAVLAGYRHIDTATLYQN---EHQIGDALAELfaegilKREDIFITTKAFCHEVAP 89
Cdd:cd19105 10 GLKVSRLGFGG-GGLPRESPELLRRALDLGINYFDTAEGYGNgnsEEIIGEALKGL------RRDKVFLATKASPRLDKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 90 DV--VEEALRNSLKRLRLDYVDLYLAHipASTKDDgsfrSDVKVEDIWRGFEKVYGLGLTKAIGVS-NFNESQIVRIMnI 166
Cdd:cd19105 83 DKaeLLKSVEESLKRLQTDYIDIYQLH--GVDTPE----ERLLNEELLEALEKLKKEGKVRFIGFStHDNMAEVLQAA-I 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 167 QKVPIHASQLElHLYLPQKAHRE----LCKKHNILITAYATLGspgrmsvvgsnGRPLFEstqnsenemnDKHVKALAQK 242
Cdd:cd19105 156 ESGWFDVIMVA-YNFLNQPAELEealaAAAEKGIGVVAMKTLA-----------GGYLQP----------ALLSVLKAKG 213
|
250 260 270
....*....|....*....|....*....|....*.
gi 17566692 243 YSktPAQILLRATVEMGII--VIPKTTNPERMKENI 276
Cdd:cd19105 214 FS--LPQAALKWVLSNPRVdtVVPGMRNFAELEENL 247
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
19-198 |
4.21e-22 |
|
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase YqkF is a founding member of aldo-keto reductase family 11 member C1 (AKR11C1). It may function as oxidoreductase. This family also includes Bacillus halodurans AKR11C1, an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase.
Pssm-ID: 381312 [Multi-domain] Cd Length: 238 Bit Score: 92.54 E-value: 4.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 19 IGLGTWQMTG--------EEGKTVIRNAVLAGYRHIDTATLYQN---EHQIGDALAElfaegilKREDIFITTKAFCHEV 87
Cdd:cd19086 6 IGFGTWGLGGdwwgdvddAEAIRALRAALDLGINFFDTADVYGDghsERLLGKALKG-------RRDKVVIATKFGNRFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 88 A---------PDVVEEALRNSLKRLRLDYVDLYLAHIPastkddgsFRSDVKVEDIWRGFEKVYGLGLTKAIGVS--NFN 156
Cdd:cd19086 79 GgperpqdfsPEYIREAVEASLKRLGTDYIDLYQLHNP--------PDEVLDNDELFEALEKLKQEGKIRAYGVSvgDPE 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17566692 157 ESQIVrimnIQKVPIHASQLELHLyLPQKAHREL---CKKHNILI 198
Cdd:cd19086 151 EALAA----LRRGGIDVVQVIYNL-LDQRPEEELfplAEEHGVGV 190
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
18-294 |
4.94e-22 |
|
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli aldehyde reductase (AKR13C1) and Thermotoga maritima aldo-keto reductase (AKR13C2). Aldehyde reductase (EC 1.1.1.21), also called aldose reductase, is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides.
Pssm-ID: 381304 [Multi-domain] Cd Length: 301 Bit Score: 93.84 E-value: 4.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 18 SIGLGTWQMT--------GEEGKTVIRNAVLAGYRHIDTATLY---QNEHQIGDALAElfaegilKREDIFITTKaFCHE 86
Cdd:cd19078 6 AIGLGCMGMShgygpppdKEEMIELIRKAVELGITFFDTAEVYgpyTNEELVGEALKP-------FRDQVVIATK-FGFK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 87 VA------------PDVVEEALRNSLKRLRLDYVDLYLAHipastkddgsfRSD--VKVEDIWRGFEKVYGLGLTKAIGV 152
Cdd:cd19078 78 IDggkpgplgldsrPEHIRKAVEGSLKRLQTDYIDLYYQH-----------RVDpnVPIEEVAGTMKELIKEGKIRHWGL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 153 SNFNESQIVRIMNIQkvPIHASQLELHLYL--PQKAHRELCKKHNILITAYATLGS---PGRMsvvgsNGRPLFESTQ-- 225
Cdd:cd19078 147 SEAGVETIRRAHAVC--PVTAVQSEYSMMWrePEKEVLPTLEELGIGFVPFSPLGKgflTGKI-----DENTKFDEGDdr 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 226 ------NSEN-EMNDKHV---KALAQKYSKTPAQILLRATVEMG--IIVIPKTTNPERMKENINIFDFNISNAEVNLLEA 293
Cdd:cd19078 220 aslprfTPEAlEANQALVdllKEFAEEKGATPAQIALAWLLAKKpwIVPIPGTTKLSRLEENIGAADIELTPEELREIED 299
|
.
gi 17566692 294 H 294
Cdd:cd19078 300 A 300
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
11-276 |
4.36e-21 |
|
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381371 [Multi-domain] Cd Length: 304 Bit Score: 91.34 E-value: 4.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 11 SNGVLMPSIGLGTWQMTG--------EEGKTVIRNAVLAGYRHIDTATLY---QNEHQIGDALAELfaegilKREDIFIT 79
Cdd:cd19145 7 SQGLEVSAQGLGCMGLSGdygapkpeEEGIALIHHAFNSGVTFLDTSDIYgpnTNEVLLGKALKDG------PREKVQLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 80 TKAFCHEVA---------PDVVEEALRNSLKRLRLDYVDLYLAHipastkddgsfRSDVKV--EDIWRGFEKVYGLGLTK 148
Cdd:cd19145 81 TKFGIHEIGgsgvevrgdPAYVRAACEASLKRLDVDYIDLYYQH-----------RIDTTVpiEITMGELKKLVEEGKIK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 149 AIGVSNFNESQIVRIMNIQkvPIHASQLELHLYlPQKAHRE---LCKKHNILITAYATLG-----SPGRMSVVGSNGR-- 218
Cdd:cd19145 150 YIGLSEASADTIRRAHAVH--PITAVQLEWSLW-TRDIEEEiipTCRELGIGIVPYSPLGrgffaGKAKLEELLENSDvr 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17566692 219 ---PLFESTQNSENEMNDKHVKALAQKYSKTPAQILLRATVEMG--IIVIPKTTNPERMKENI 276
Cdd:cd19145 227 kshPRFQGENLEKNKVLYERVEALAKKKGCTPAQLALAWVLHQGedVVPIPGTTKIKNLNQNI 289
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-293 |
5.51e-21 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 90.86 E-value: 5.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 15 LMPSIGLGTWQ--MTGEEGKTVIRNavlagyrHIDTATL---YQNEHQIGDAL---AELFAEG----IL-------KRED 75
Cdd:cd19103 3 KLPKIALGTWSwgSGGAGGDQVFGN-------HLDEDTLkavFDKAMAAGLNLwdtAAVYGMGasekILgeflkryPRED 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 76 IFITTKaFCHEVA---PDVVEEALRNSLKRLRLDYVDLYLAHIPAstkddgsfrsdvkveDIWRGFEKVYGL---GLTKA 149
Cdd:cd19103 76 YIISTK-FTPQIAgqsADPVADMLEGSLARLGTDYIDIYWIHNPA---------------DVERWTPELIPLlksGKVKH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 150 IGVSNFNESQIVR---IMNIQKVPIHASQleLHLYLPQKAHREL-----CKKHNILITAYATLgSPGRMSVVGSNGRPLF 221
Cdd:cd19103 140 VGVSNHNLAEIKRaneILAKAGVSLSAVQ--NHYSLLYRSSEEAgildyCKENGITFFAYMVL-EQGALSGKYDTKHPLP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 222 ESTQNSEN---------EMNDKhVKALAQKYSKTPAQILLRATVEMGIIVIPKTTNPERMKENINIFDFNISNAEVNLLE 292
Cdd:cd19103 217 EGSGRAETynpllpqleELTAV-MAEIGAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDDEIKELE 295
|
.
gi 17566692 293 A 293
Cdd:cd19103 296 Q 296
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
12-289 |
2.77e-20 |
|
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding members of aldo-keto reductase family 8 member A1-2 (AKR8A1-2), respectively. PLR (EC 1.1.1.65), also called PL reductase (PL-red), catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+).
Pssm-ID: 381303 [Multi-domain] Cd Length: 302 Bit Score: 89.22 E-value: 2.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 12 NGVLMPSIGLGTWQMTGEEGKT-------VIRNAVLAGYRHIDTATLY------QNEHQIGDALAElFAEgilKREDIFI 78
Cdd:cd19077 1 NGKLVGPIGLGLMGLTWRPNPTpdeeafeTMKAALDAGSNLWNGGEFYgppdphANLKLLARFFRK-YPE---YADKVVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 79 TTKAFCHE--VAPDVVEEALRNSLK----RLR-LDYVDLYlahiPASTKDDgsfrsDVKVEDIWRGFEKVYGLGLTKAIG 151
Cdd:cd19077 77 SVKGGLDPdtLRPDGSPEAVRKSIEnilrALGgTKKIDIF----EPARVDP-----NVPIEETIKALKELVKEGKIRGIG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 152 VSNFNESQIVRIMNIqkVPIHASQLELHLYLPQKAHR---ELCKKHNILITAYATLGSpGRMSVVGSNGRPL----FEST 224
Cdd:cd19077 148 LSEVSAETIRRAHAV--HPIAAVEVEYSLFSREIEENgvlETCAELGIPIIAYSPLGR-GLLTGRIKSLADIpegdFRRH 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17566692 225 Q---NSEN-EMNDKHVKAL---AQKYSKTPAQILL---RATVEMGIIVIPKTTNPERMKENINIFDFNISNAEVN 289
Cdd:cd19077 225 LdrfNGENfEKNLKLVDALqelAEKKGCTPAQLALawiLAQSGPKIIPIPGSTTLERVEENLKAANVELTDEELK 299
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
8-276 |
2.81e-19 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 86.60 E-value: 2.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 8 FTLSngvlmpSIGLGTWQM-----TGEEGKTVIRNAVLAGYRHIDTATLYQN---EHQIGDALAELFAEGILKREDIFIT 79
Cdd:cd19099 1 LTLS------SLGLGTYRGdsddeTDEEYREALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGIKRDEVVIV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 80 TKA---------------------------------FCHEVAPDVVEEALRNSLKRLRLDYVDLYLAHIPAstkddgSFR 126
Cdd:cd19099 75 TKAgyipgdgdeplrplkyleeklgrglidvadsagLRHCISPAYLEDQIERSLKRLGLDTIDLYLLHNPE------EQL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 127 SDVKVEDIWRGFEKVYGL-------GLTKAIGVSNfNESQIV-----RIMNIQKVPIHAS------------QLELHLYL 182
Cdd:cd19099 149 LELGEEEFYDRLEEAFEAleeavaeGKIRYYGIST-WDGFRAppalpGHLSLEKLVAAAEevggdnhhfkviQLPLNLLE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 183 PQKAHR------------ELCKKHNILITAYATLGSpgrmsvvGSNGRPLFESTQnsenemndkhvkaLAQKYSKTPAQI 250
Cdd:cd19099 228 PEALTEkntvkgealsllEAAKELGLGVIASRPLNQ-------GQLLGELRLADL-------------LALPGGATLAQR 287
|
330 340
....*....|....*....|....*...
gi 17566692 251 LLRATVEM-GII-VIPKTTNPERMKENI 276
Cdd:cd19099 288 ALQFARSTpGVDsALVGMRRPEHVDENL 315
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
12-253 |
1.81e-18 |
|
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a founding member of aldo-keto reductase family 9 member C1 (AKR9C1).
Pssm-ID: 381307 [Multi-domain] Cd Length: 308 Bit Score: 84.19 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 12 NGVLMPSIGLGTWQM---TGEEGKTVIRNA-VLAGYRHIDTATLY----------QNEHQIGDALAELfaegiLKREDIF 77
Cdd:cd19081 5 TGLSVSPLCLGTMVFgwtADEETSFALLDAfVDAGGNFIDTADVYsawvpgnaggESETIIGRWLKSR-----GKRDRVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 78 ITTKAFCHEVAPDV------VEEALRNSLKRLRLDYVDLYLAHipastKDDGSfrsdVKVEDIWRGFEKVYGLGLTKAIG 151
Cdd:cd19081 80 IATKVGFPMGPNGPglsrkhIRRAVEASLRRLQTDYIDLYQAH-----WDDPA----TPLEETLGALNDLIRQGKVRYIG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 152 VSNFNESQIVRIMNIQK----VPIHASQLELHLYLPQKAHREL---CKKHNILITAYATLGS---PGRMS----VVGSNG 217
Cdd:cd19081 151 ASNYSAWRLQEALELSRqhglPRYVSLQPEYNLVDRESFEGELlplCREEGIGVIPYSPLAGgflTGKYRseadLPGSTR 230
|
250 260 270
....*....|....*....|....*....|....*....
gi 17566692 218 RPlfESTQNSENEMNDKHVKAL---AQKYSKTPAQILLR 253
Cdd:cd19081 231 RG--EAAKRYLNERGLRILDALdevAAEHGATPAQVALA 267
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-200 |
2.65e-18 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 82.14 E-value: 2.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 19 IGLGT---WQMTGEEGKTVIRNAVLAGYRHIDTATLYQN-EHQIGDALAElfaegilKREDIFITTKafCHEVAPDVVEE 94
Cdd:cd19100 14 LGFGGgplGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKG-------RRDKVFLATK--TGARDYEGAKR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 95 ALRNSLKRLRLDYVDLYLAHipastkddgsfrsDVKVEDIWRGFEKVYGL----------GLTKAIGVSNFNESQIVRIM 164
Cdd:cd19100 85 DLERSLKRLGTDYIDLYQLH-------------AVDTEEDLDQVFGPGGAlealleakeeGKIRFIGISGHSPEVLLRAL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17566692 165 N------IQkVPIHAsqLELHLYLPQKAHRELCKKHNILITA 200
Cdd:cd19100 152 EtgefdvVL-FPINP--AGDHIDSFREELLPLAREKGVGVIA 190
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
17-153 |
3.00e-18 |
|
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH) and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. The family also includes L-galactose dehydrogenase (L-galDH) and D-arabinose 1-dehydrogenase (ARA2). L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381316 [Multi-domain] Cd Length: 278 Bit Score: 82.99 E-value: 3.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 17 PSIGLGTWQMTG-------EEGKTVIRNAVLAGYRHIDTATLYQN-EHQIGDALAELfaegilKREDIFITTKAFCHEVA 88
Cdd:cd19090 1 SALGLGTAGLGGvfggvddDEAVATIRAALDLGINYIDTAPAYGDsEERLGLALAEL------PREPLVLSTKVGRLPED 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 89 -----PDVVEEALRNSLKRLRLDYVDLYLAHIPASTKDDGSFRSDVKVEdiwrGFEKVYGLGLTKAIGVS 153
Cdd:cd19090 75 tadysADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILAPGGALE----ALLELKEEGLIKHIGLG 140
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
21-292 |
1.76e-16 |
|
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD), are founding members of aldo-keto reductase family 9 member A1-3 (AKR9A1-3), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis. AAD (EC1.1.1.91) is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). The AKR9B family includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381306 [Multi-domain] Cd Length: 307 Bit Score: 78.42 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 21 LGT--------WQMTGEEGKTVIRNAVLAGYRHIDTATLYQN---EHQIGdalaELFAEgilKREDIFITTKaFCHEVAP 89
Cdd:cd19080 15 LGTmtfgtewgWGADREEARAMFDAYVEAGGNFIDTANNYTNgtsERLLG----EFIAG---NRDRIVLATK-YTMNRRP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 90 DVVE----------EALRNSLKRLRLDYVDLYLAHIPastkdDGSfrsdVKVEDIWRGFEKVYGLGLTKAIGVSNFNESQ 159
Cdd:cd19080 87 GDPNaggnhrknlrRSVEASLRRLQTDYIDLLYVHAW-----DFT----TPVEEVMRALDDLVRAGKVLYVGISDTPAWV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 160 IVRIMNIQKV----PIHASQLELHLyLPQKAHREL---CKKHNILITAYATLGS--------PGRMSVVGSNGRPLFEST 224
Cdd:cd19080 158 VARANTLAELrgwsPFVALQIEYSL-LERTPERELlpmARALGLGVTPWSPLGGglltgkyqRGEEGRAGEAKGVTVGFG 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17566692 225 QNSENEMN--DKhVKALAQKYSKTPAQILL-----RATVemgIIVIPKTTNPERMKENINIFDFNISNAEVNLLE 292
Cdd:cd19080 237 KLTERNWAivDV-VAAVAEELGRSAAQVALawvrqKPGV---VIPIIGARTLEQLKDNLGALDLTLSPEQLARLD 307
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
17-276 |
2.76e-16 |
|
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) and Streptomyces glaucescens aldo-keto reductase (StrT) are founding members of aldo-keto reductase family 10 member A1 (AKR10A1) and A2 (AKR10A2). BlmT is bluensomycin aldo-keto reductase (AKR) and StrT is streptomycin AKR.
Pssm-ID: 381308 [Multi-domain] Cd Length: 291 Bit Score: 77.59 E-value: 2.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 17 PSIGLGT----WQMTGEEGKTVIRNAVLAGYRHIDTATLYQN-------EHQIGDALAELFaegilKREDIFITTKAfCH 85
Cdd:cd19082 1 SRIVLGTadfgTRIDEEEAFALLDAFVELGGNFIDTARVYGDwvergasERVIGEWLKSRG-----NRDKVVIATKG-GH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 86 ---------EVAPDVVEEALRNSLKRLRLDYVDLYLAHipastKDDgsfrSDVKVEDIWRGFEKVYGLGLTKAIGVSNFN 156
Cdd:cd19082 75 pdledmsrsRLSPEDIRADLEESLERLGTDYIDLYFLH-----RDD----PSVPVGEIVDTLNELVRAGKIRAFGASNWS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 157 esqIVRI-------MNIQKVPIHASQLELHLYLPQKAH-------------RELCKKHNILITAYATLGSpGRMSVVGSN 216
Cdd:cd19082 146 ---TERIaeanayaKAHGLPGFAASSPQWSLARPNEPPwpgptlvamdeemRAWHEENQLPVFAYSSQAR-GFFSKRAAG 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17566692 217 G-RPLFESTQNSENEMNDK---HVKALAQKYSKTPAQILLRATVEMGIIVIP--KTTNPERMKENI 276
Cdd:cd19082 222 GaEDDSELRRVYYSEENFErleRAKELAEEKGVSPTQIALAYVLNQPFPTVPiiGPRTPEQLRDSL 287
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
12-153 |
4.03e-16 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 77.94 E-value: 4.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 12 NGVLMPSIGLGTW---QMTGEEGKTVIRNAVLAGYRHIDTATLY-QNEHQIGDALAELfaegilkREDIFITTKAFCHEV 87
Cdd:COG1453 9 TGLEVSVLGFGGMrlpRKDEEEAEALIRRAIDNGINYIDTARGYgDSEEFLGKALKGP-------RDKVILATKLPPWVR 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17566692 88 APDVVEEALRNSLKRLRLDYVDLYLAHipaSTKDDGSFRSDVKVEDIWRGFEKVYGLGLTKAIGVS 153
Cdd:COG1453 82 DPEDMRKDLEESLKRLQTDYIDLYLIH---GLNTEEDLEKVLKPGGALEALEKAKAEGKIRHIGFS 144
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
13-293 |
4.59e-16 |
|
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an uncharacterized aldo-keto reductase from Polaromonas sp.
Pssm-ID: 381317 [Multi-domain] Cd Length: 319 Bit Score: 77.27 E-value: 4.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 13 GVLMPSIGLGT-------------WQMTGEEGKTVIRNAVLAGYRHIDTATLY---QNEHQIGDALAElfaegilKREDI 76
Cdd:cd19091 10 GLKVSELALGTmtfgggggffgawGGVDQEEADRLVDIALDAGINFFDTADVYsegESEEILGKALKG-------RRDDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 77 FITTKAFcHEVAPDVVE---------EALRNSLKRLRLDYVDLYLAHIpastkddgsFRSDVKVEDIWRGFEKVYGLGLT 147
Cdd:cd19091 83 LIATKVR-GRMGEGPNDvglsrhhiiRAVEASLKRLGTDYIDLYQLHG---------FDALTPLEETLRALDDLVRQGKV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 148 KAIGVSNFNESQIVRIMNIQK----VPIHASQLELHLyLPQKAHRE---LCKKHNILITAYATLGSpGRMSVVGSNGRPL 220
Cdd:cd19091 153 RYIGVSNFSAWQIMKALGISErrglARFVALQAYYSL-LGRDLEHElmpLALDQGVGLLVWSPLAG-GLLSGKYRRGQPA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 221 FESTQNSENE-----MNDKH-------VKALAQKYSKTPAQILL-----RATVEmgiIVIPKTTNPERMKENINIFDFNI 283
Cdd:cd19091 231 PEGSRLRRTGfdfppVDRERgydvvdaLREIAKETGATPAQVALawllsRPTVS---SVIIGARNEEQLEDNLGAAGLSL 307
|
330
....*....|
gi 17566692 284 SNAEVNLLEA 293
Cdd:cd19091 308 TPEEIARLDK 317
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
13-250 |
7.20e-16 |
|
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, Saccharopolyspora erythraea EryBII, and Streptomyces avermitilis aveBVIII are founding members of aldo-keto reductase family 12 member A1 (AKR12A1), B1 (AKR12B1), and C1(AKR12C1), respectively. TylCII acts as a NDP-hexose 2,3-enoyl reductase. EryBII is a mycarose/desosamine reductase involved in L-mycarose and D-desosamine production. aveBVIII functions as a dTDP-4-keto-6-deoxy-L-hexose-2,3-reductase.
Pssm-ID: 381313 [Multi-domain] Cd Length: 310 Bit Score: 76.84 E-value: 7.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 13 GVLMPSIGLGTW----QMTGEEGKTVIRNAVLAGYRHIDTATLYQN---EHQIGDALAElfaegilKREDIFITTKAFcH 85
Cdd:cd19087 10 GLKVSRLCLGTMnfggRTDEETSFAIMDRALDAGINFFDTADVYGGgrsEEIIGRWIAG-------RRDDIVLATKVF-G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 86 EVAPDV---------VEEALRNSLKRLRLDYVDLYLAHipastkddgSFRSDVKVEDIWRGFEKVYGLGLTKAIGVSNFN 156
Cdd:cd19087 82 PMGDDPndrglsrrhIRRAVEASLRRLQTDYIDLYQMH---------HFDRDTPLEETLRALDDLVRQGKIRYIGVSNFA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 157 ESQIVRIMNIQKVpIHASQLELH--LY--LPQKAHREL---CKKHNILITAYATLGSpGRMS-VVGSNGRP----LFEST 224
Cdd:cd19087 153 AWQIAKAQGIAAR-RGLLRFVSEqpMYnlLKRQAELEIlpaARAYGLGVIPYSPLAG-GLLTgKYGKGKRPesgrLVERA 230
|
250 260 270
....*....|....*....|....*....|..
gi 17566692 225 QNSENEMNDKHV------KALAQKYSKTPAQI 250
Cdd:cd19087 231 RYQARYGLEEYRdiaerfEALAAEAGLTPASL 262
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
29-260 |
3.45e-15 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 74.99 E-value: 3.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 29 EEGKTVIRNAVLAGYRHIDTATLY---QNEHQIGDALAELfaegilkREDIFITTK----AFCHEVAPDVVEEALRNSLK 101
Cdd:cd19104 32 EEQIAAVRRALDLGINFFDTAPSYgdgKSEENLGRALKGL-------PAGPYITTKvrldPDDLGDIGGQIERSVEKSLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 102 RLRLDYVDLYLAH---IPASTKDDGSFRS---DVKVEDIWRGFEKVYGLGLTKAIGVSNFNESQIVRiMNIQKVPIHASQ 175
Cdd:cd19104 105 RLKRDSVDLLQLHnriGDERDKPVGGTLSttdVLGLGGVADAFERLRSEGKIRFIGITGLGNPPAIR-ELLDSGKFDAVQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 176 LELHLYLPQKAHR--------------ELCKKHNILITAYATLGSpGRMSVVGSNGR--PLFESTQNSENEMNDKHVKAL 239
Cdd:cd19104 184 VYYNLLNPSAAEArprgwsaqdyggiiDAAAEHGVGVMGIRVLAA-GALTTSLDRGReaPPTSDSDVAIDFRRAAAFRAL 262
|
250 260
....*....|....*....|....*....
gi 17566692 240 AQKYSKTPAQILLR--------ATVEMGI 260
Cdd:cd19104 263 AREWGETLAQLAHRfalsnpgvSTVLVGV 291
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
19-114 |
4.99e-14 |
|
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381322 [Multi-domain] Cd Length: 255 Bit Score: 70.67 E-value: 4.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 19 IGLGTWQMTGEEGKTV--------IRNAVLAGYRHIDTATLY---QNEHQIGDALAELfaegilKREDIFITTKAFCHEV 87
Cdd:cd19096 3 LGFGTMRLPESDDDSIdeekaiemIRYAIDAGINYFDTAYGYgggKSEEILGEALKEG------PREKFYLATKLPPWSV 76
|
90 100
....*....|....*....|....*...
gi 17566692 88 -APDVVEEALRNSLKRLRLDYVDLYLAH 114
Cdd:cd19096 77 kSAEDFRRILEESLKRLGVDYIDFYLLH 104
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
18-166 |
1.07e-13 |
|
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1/AKR7A3/AFAR) from Rattus norvegicus, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR1/AFAR) and aflatoxin B1 aldehyde reductase member 3 (AKR7A3/AFAR2) from Homo sapiens, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR2) from Rattus norvegicus, and aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AKR7A5/AFAR) from Mus musculus, are founding members of aldo-keto reductase family 7 member A1-5 (AKR7A1-5), respectively. AKR7A2 (EC 1.1.1.n11), also called AFB1 aldehyde reductase 1, or AFB1-AR 1, or aldoketoreductase 7, or succinic semialdehyde reductase, or SSA reductase, catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate (GHB). It has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). AKR7A2, AKR7A3 (also called AFB1 aldehyde reductase 2 or AFB1-AR 2), and AKR7A4 (also called AFB1 aldehyde reductase 3, or AFB1-AR 3, or aldoketoreductase 7-like), may be involved in protection of liver against the toxic and carcinogenic effects of aflatoxin B1 (AFB1), a potent hepatocarcinogen. They can reduce the dialdehyde protein-binding form of AFB1 to the non-binding AFB1 dialcohol.
Pssm-ID: 381301 [Multi-domain] Cd Length: 304 Bit Score: 70.28 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 18 SIGLGTWQMTGEEGKTVIRNAVLAGYRHIDTATLYQNehqiGDAlAELFAEGILKREDIFITTKAF-----CHevAPDVV 92
Cdd:cd19075 9 TFGSQGRFTTAEAAAELLDAFLERGHTEIDTARVYPD----GTS-EELLGELGLGERGFKIDTKANpgvggGL--SPENV 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17566692 93 EEALRNSLKRLRLDYVDLYLAHIPastkDDGsfrsdVKVEDIWRGFEKVYGLGLTKAIGVSNFNESQIVRIMNI 166
Cdd:cd19075 82 RKQLETSLKRLKVDKVDVFYLHAP----DRS-----TPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEI 146
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
19-284 |
2.46e-13 |
|
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the prototype of this family. It is an NADP(H)-dependent aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NADP(H) as a hydride donor.
Pssm-ID: 381320 [Multi-domain] Cd Length: 328 Bit Score: 69.52 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 19 IGLGT--W--QMTGEEGKTVIRNAVLAGYRHIDTATLY----QNEHQ------IGDALAelfAEGilKREDIFITTKA-- 82
Cdd:cd19094 4 ICLGTmtWgeQNTEAEAHEQLDYAFDEGVNFIDTAEMYpvppSPETQgrteeiIGSWLK---KKG--NRDKVVLATKVag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 83 ------FCHEVAPDV----VEEALRNSLKRLRLDYVDLYLAHIPAST---------KDDGSFRSDVKVEDIWRGFEKVYG 143
Cdd:cd19094 79 pgegitWPRGGGTRLdrenIREAVEGSLKRLGTDYIDLYQLHWPDRYtplfgggyyTEPSEEEDSVSFEEQLEALGELVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 144 LGLTKAIGVSN---FNESQIVRIMNIQKVPIHAS-QLELHLyLPQK---AHRELCKKHNILITAYATLG----------- 205
Cdd:cd19094 159 AGKIRHIGLSNetpWGVMKFLELAEQLGLPRIVSiQNPYSL-LNRNfeeGLAEACHRENVGLLAYSPLAggvltgkyldg 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 206 ----SPGRMSvvgsngrpLFESTQNS-ENEMNDKHVKA---LAQKYSKTPAQILL-----RATVEMGIIvipKTTNPERM 272
Cdd:cd19094 238 aarpEGGRLN--------LFPGYMARyRSPQALEAVAEyvkLARKHGLSPAQLALawvrsRPFVTSTII---GATTLEQL 306
|
330
....*....|..
gi 17566692 273 KENINIFDFNIS 284
Cdd:cd19094 307 KENIDAFDVPLS 318
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-276 |
1.24e-12 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 66.97 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 19 IGLGTWQMTG----EEGKTVIRNAVLAGYRHIDTATLY----------QNEHQIGDALAElfaEGilKREDIFITTK--- 81
Cdd:cd19752 3 LCLGTMYFGTrtdeETSFAILDRYVAAGGNFLDTANNYafwteggvggESERLIGRWLKD---RG--NRDDVVIATKvga 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 82 --------AFCHE-VAPDVVEEALRNSLKRLRLDYVDLYLAHIpastkDDgsfrSDVKVEDIWRGFEKVYGLGLTKAIGV 152
Cdd:cd19752 78 gprdpdggPESPEgLSAETIEQEIDKSLRRLGTDYIDLYYAHV-----DD----RDTPLEETLEAFNELVKAGKVRAIGA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 153 SNFNESQIVRIMNI---QKVPIHASQLELHLYLPQKA-------------HRELCKKHNIL-ITAYATL--GSPGRmsvv 213
Cdd:cd19752 149 SNFAAWRLERARQIarqQGWAEFSAIQQRHSYLRPRPgadfgvqrivtdeLLDYASSRPDLtLLAYSPLlsGAYTR---- 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17566692 214 gsNGRPLFESTQNSENEMNDKHVKALAQKYSKTPAQI----LLRATVemGIIVIPKTTNPERMKENI 276
Cdd:cd19752 225 --PDRPLPEQYDGPDSDARLAVLEEVAGELGATPNQVvlawLLHRTP--AIIPLLGASTVEQLEENL 287
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-169 |
2.40e-12 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 66.01 E-value: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 19 IGLGTWQ---------MTG----EEGKTVIRNAVLAGYRHIDTATLYQN-EHQIGDALaelfaegiLKREDIFITTK--- 81
Cdd:cd19097 3 LALGTAQfgldygianKSGkpseKEAKKILEYALKAGINTLDTAPAYGDsEKVLGKFL--------KRLDKFKIITKlpp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 82 -AFCHEVAPDVVEEALRNSLKRLRLDYVDLYLAHIPASTKDDGsfrsdvkvEDIWRGFEKVYGLGLTKAIGVSNFNESQI 160
Cdd:cd19097 75 lKEDKKEDEAAIEASVEASLKRLKVDSLDGLLLHNPDDLLKHG--------GKLVEALLELKKEGLIRKIGVSVYSPEEL 146
|
....*....
gi 17566692 161 VRIMNIQKV 169
Cdd:cd19097 147 EKALESFKI 155
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-293 |
8.16e-12 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 64.92 E-value: 8.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 16 MPSIGLGTWQMTGEEGKTVIRNAVL--------AGYRHIDTATLYQN-EHQIGDALAELFAEGILkREDIFITTKAFC-- 84
Cdd:cd19101 2 ISRVINGMWQLSGGHGGIRDEDAAVramaayvdAGLTTFDCADIYGPaEELIGEFRKRLRRERDA-ADDVQIHTKWVPdp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 85 --HEVAPDVVEEALRNSLKRLRLDYVDLYLAHipasTKDDgsfrSDVKVEDIWRGFEKVYGLGLTKAIGVSNFNESQIVR 162
Cdd:cd19101 81 geLTMTRAYVEAAIDRSLKRLGVDRLDLVQFH----WWDY----SDPGYLDAAKHLAELQEEGKIRHLGLTNFDTERLRE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 163 IMNiQKVPIHASQLELHLyL---PQKAHRELCKKHNILITAYATLG------------SPGRMSvvgSNGRPLFESTQns 227
Cdd:cd19101 153 ILD-AGVPIVSNQVQYSL-LdrrPENGMAALCEDHGIKLLAYGTLAggllsekylgvpEPTGPA---LETRSLQKYKL-- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 228 eneMNDKH------------VKALAQKYSKTPAQILLRATVEM----GIIVipKTTNPERMKENINIFDFNISNAEVNLL 291
Cdd:cd19101 226 ---MIDEWggwdlfqellrtLKAIADKHGVSIANVAVRWVLDQpgvaGVIV--GARNSEHIDDNVRAFSFRLDDEDRAAI 300
|
..
gi 17566692 292 EA 293
Cdd:cd19101 301 DA 302
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
13-116 |
2.25e-11 |
|
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381369 [Multi-domain] Cd Length: 319 Bit Score: 63.77 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 13 GVLMPSIGLGTW-----QMTGEEGKTVIRNAVLAGYRHIDTATLYQN---EHQIGDALAELfaegILKREDIFITTKAFC 84
Cdd:cd19143 10 GLKVSALSFGSWvtfgnQVDVDEAKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIKEL----GWPRSDYVVSTKIFW 85
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 17566692 85 HEVAPDV---------VEEALRNSLKRLRLDYVDLYLAHIP 116
Cdd:cd19143 86 GGGGPPPndrglsrkhIVEGTKASLKRLQLDYVDLVFCHRP 126
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
34-153 |
2.82e-11 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 63.06 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 34 VIRNAVLAGYRHIDTATLYQN-EHQIGDALAELFAEgiLKREDIFITTKA----FC-HEVAPDVVEEALRNSLKRLRLDY 107
Cdd:cd19164 39 IVRRALELGIRAFDTSPYYGPsEIILGRALKALRDE--FPRDTYFIITKVgrygPDdFDYSPEWIRASVERSLRRLHTDY 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 17566692 108 VDLYLAHipastkdDGSFrsdVKVEDIWRGFEKVYGL---GLTKAIGVS 153
Cdd:cd19164 117 LDLVYLH-------DVEF---VADEEVLEALKELFKLkdeGKIRNVGIS 155
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
17-286 |
1.40e-10 |
|
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381378 [Multi-domain] Cd Length: 308 Bit Score: 61.09 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 17 PSIGLGT-------WQMTGEEGKTVIRNAVLAGYRHIDTATLYQN---EHQIGDALAElfaegiLKREDIFITTKA---- 82
Cdd:cd19152 1 PKLGFGTaplgnlyEAVSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALRE------LGREDYVISTKVgrll 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 83 -----------FCHEVAPDV----------VEEALRNSLKRLRLDYVDLYLAHIP----ASTKDDGSFRSDVKveDIWRG 137
Cdd:cd19152 75 vplqeveptfePGFWNPLPFdavfdysydgILRSIEDSLQRLGLSRIDLLSIHDPdedlAGAESDEHFAQAIK--GAFRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 138 FEKVYGLGLTKAIGVSnFNESQIVRIMniqkvpIHASQLELHL----Y--LPQKAHREL---CKKHNILITAYATLGSpG 208
Cdd:cd19152 153 LEELREEGVIKAIGLG-VNDWEVILRI------LEEADLDWVMlagrYtlLDHSAARELlpeCEKRGVKVVNAGPFNS-G 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 209 RMsvVGSNGRPLFESTQNSEnEMNDK--HVKALAQKYSKTPAQI-----LLRATVEMgiiVIPKTTNPERMKENINIFDF 281
Cdd:cd19152 225 FL--AGGDNFDYYEYGPAPP-ELIARrdRIEALCEQHGVSLAAAalqfaLAPPAVAS---VAPGASSPERVEENVALLAT 298
|
....*
gi 17566692 282 NISNA 286
Cdd:cd19152 299 EIPAA 303
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
17-153 |
1.90e-10 |
|
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381388 [Multi-domain] Cd Length: 290 Bit Score: 60.45 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 17 PSIGLGTWQM------TGEEGKTVIRNAVLAGYRHIDTATLY---QNEHQIGDALAELfaegilKREDIFITTKA----- 82
Cdd:cd19162 1 PRLGLGAASLgnlaraGEDEAAATLDAAWDAGIRYFDTAPLYglgLSERRLGAALARH------PRAEYVVSTKVgrlle 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 83 -------FCHEVAPDVVEEALR----NSLKRLRLDYVDLYLAHIPASTKDDGsfrsdvkVEDIWRGFEKVYGLGLTKAIG 151
Cdd:cd19162 75 pgaagrpAGADRRFDFSADGIRrsieASLERLGLDRLDLVFLHDPDRHLLQA-------LTDAFPALEELRAEGVVGAIG 147
|
..
gi 17566692 152 VS 153
Cdd:cd19162 148 VG 149
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
13-189 |
1.57e-09 |
|
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381367 [Multi-domain] Cd Length: 310 Bit Score: 58.23 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 13 GVLMPSIGLGTW-----QMTGEEGKTVIRNAVLAGYRHIDTATLYQNEHqigdalAELFAEGILK-----REDIFITTKA 82
Cdd:cd19141 9 GLRVSCLGLGTWvtfgsQISDEVAEELVTLAYENGINLFDTAEVYAAGK------AEIVLGKILKkkgwrRSSYVITTKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 83 FCHEVAPDV-------VEEALRNSLKRLRLDYVDLYLAHIPASTkddgsfrsdVKVEDIWRGFEKVYGLGLTKAIGVSNF 155
Cdd:cd19141 83 FWGGKAETErglsrkhIIEGLKASLERLQLEYVDIVFANRPDPN---------TPMEEIVRAFTHVINQGMAMYWGTSRW 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 17566692 156 NESQIVRIMNIQK----VPIHASQLELHLYlpqkaHRE 189
Cdd:cd19141 154 SAMEIMEAYSVARqfnlIPPIVEQAEYHLF-----QRE 186
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
12-294 |
7.97e-09 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 56.15 E-value: 7.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 12 NGVLMPSIGLGTWQMTG-----EEGKTVIRNAVLAGYRHIDTATLY-----QNEHQIGDALAELFAEgilKREDIFITTK 81
Cdd:PRK09912 21 SGLRLPALSLGLWHNFGhvnalESQRAILRKAFDLGITHFDLANNYgpppgSAEENFGRLLREDFAA---YRDELIISTK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 82 AfCHEVAP---------DVVEEALRNSLKRLRLDYVDLYLAHipastkddgsfRSD--VKVEDIWRGFEKVYGLGLTKAI 150
Cdd:PRK09912 98 A-GYDMWPgpygsggsrKYLLASLDQSLKRMGLEYVDIFYSH-----------RVDenTPMEETASALAHAVQSGKALYV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 151 GVSNFNES---QIVRIMNIQKVP--IHASQLE-LHLYLPQKAHRELCKKHNILITAYATL-----------GSP--GRMS 211
Cdd:PRK09912 166 GISSYSPErtqKMVELLREWKIPllIHQPSYNlLNRWVDKSGLLDTLQNNGVGCIAFTPLaqglltgkylnGIPqdSRMH 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 212 VVGSNGRPLFESTQNSENEMNDKHVKALAQKYSKTPAQILLRATV--EMGIIVIPKTTNPERMKENINIF-DFNISNAEV 288
Cdd:PRK09912 246 REGNKVRGLTPKMLTEANLNSLRLLNEMAQQRGQSMAQMALSWLLkdERVTSVLIGASRAEQLEENVQALnNLTFSTEEL 325
|
....*.
gi 17566692 289 NLLEAH 294
Cdd:PRK09912 326 AQIDQH 331
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
12-190 |
1.02e-08 |
|
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo sapiens, Rattus norvegicus, and Mus musculus, are founding members of aldo-keto reductase family 6 member A9 (AKR6A9), A12 (AKR6A12), A14 (AKR6A14), respectively. KCAB3B, also called Shaker channel b-subunit 3 (Kvb3), K(+) channel subunit beta-3, or Kv-beta-3, is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. It alters the functional properties of Kv1.5.
Pssm-ID: 381386 [Multi-domain] Cd Length: 325 Bit Score: 55.76 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 12 NGVLMPSIGLGTW-----QMTGEEGKTVIRNAVLAGYRHIDTATLY---QNEHQIGDALAelfAEGiLKREDIFITTKAF 83
Cdd:cd19160 11 SGLRVSCLGLGTWvtfgsQISDETAEDLLTVAYEHGVNLFDTAEVYaagKAERTLGNILK---SKG-WRRSSYVVTTKIY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 84 CHEVAPDV-------VEEALRNSLKRLRLDYVDLYLAHipastkddgsfRSDVK--VEDIWRGFEKVYGLGLTKAIGVSN 154
Cdd:cd19160 87 WGGQAETErglsrkhIIEGLRGSLDRLQLEYVDIVFAN-----------RSDPNspMEEIVRAMTYVINQGMAMYWGTSR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17566692 155 FNESQIVRIMNIQK----VPIHASQLELHLYLPQKAHREL 190
Cdd:cd19160 156 WSAMEIMEAYSVARqfnlIPPVCEQAEYHLFQREKVEMQL 195
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
12-190 |
1.02e-08 |
|
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo sapiens, Mus musculus, Mustela putorius, Rattus norvegicus, and Kvb1.1, Kvb1.2 from Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A3 (AKR6A3), A8 (AKR6A8), A10a (AKR6A10a), A13 (AKR6A13), A7 (AKR6A7) and A10b (AKR6A10b), respectively. KCAB1B, also called Shaker channel b-subunit 1(Kvb1), K(+) channel subunit beta-1, or Kv-beta-1, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It modulates action potentials via its effect on the pore-forming alpha subunits.
Pssm-ID: 381385 [Multi-domain] Cd Length: 323 Bit Score: 55.82 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 12 NGVLMPSIGLGTW-----QMTGEEGKTVIRNAVLAGYRHIDTATLYqnehqiGDALAELFAEGILK-----REDIFITTK 81
Cdd:cd19159 9 SGLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVY------AAGKAEVILGSIIKkkgwrRSSLVITTK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 82 AFC-------HEVAPDVVEEALRNSLKRLRLDYVDLYLAHIPastkddgsfRSDVKVEDIWRGFEKVYGLGLTKAIGVSN 154
Cdd:cd19159 83 LYWggkaeteRGLSRKHIIEGLKGSLQRLQLEYVDVVFANRP---------DSNTPMEEIVRAMTHVINQGMAMYWGTSR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17566692 155 FNESQIVRIMNIQK----VPIHASQLELHLYLPQKAHREL 190
Cdd:cd19159 154 WSAMEIMEAYSVARqfnmIPPVCEQAEYHLFQREKVEVQL 193
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
13-277 |
1.10e-08 |
|
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo. Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2). It catalyzes the conversion of 3-hydroxybutanal (3-HB) to 1,3-butanediol (1,3-BDO) by using NADPH as a cofactor.
Pssm-ID: 381315 [Multi-domain] Cd Length: 308 Bit Score: 55.34 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 13 GVLMPSIGLGTWQMTG-----EEGKTVIRNAVLAGYRHIDTATLYQNEHQ-----IGDALAELFAEgilKREDIFITTKA 82
Cdd:cd19089 8 GLHLPAISLGLWHNFGdytspEEARELLRTAFDLGITHFDLANNYGPPPGsaeenFGRILKRDLRP---YRDELVISTKA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 83 fCHEVAPDV---------VEEALRNSLKRLRLDYVDLYLAHIPastkDdgsfrSDVKVEDIWRGFEKVYGLGLTKAIGVS 153
Cdd:cd19089 85 -GYGMWPGPygdggsrkyLLASLDQSLKRMGLDYVDIFYHHRY----D-----PDTPLEETMTALADAVRSGKALYVGIS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 154 NFNESQIVR---IMNIQKVPIHASQLELHLY--LPQKAHRELCKKHNILITAYATLgSPGRMSVVGSNGRPLFESTQNSE 228
Cdd:cd19089 155 NYPGAKARRaiaLLRELGVPLIIHQPRYSLLdrWAEDGLLEVLEEAGIGFIAFSPL-AQGLLTDKYLNGIPPDSRRAAES 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17566692 229 NEMNDKHVKA-----------LAQKYSKTPAQILLRATVEMGII--VIPKTTNPERMKENIN 277
Cdd:cd19089 234 KFLTEEALTPekleqlrklnkIAAKRGQSLAQLALSWVLRDPRVtsVLIGASSPSQLEDNVA 295
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
12-190 |
4.46e-07 |
|
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.
Pssm-ID: 381384 [Multi-domain] Cd Length: 324 Bit Score: 50.85 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 12 NGVLMPSIGLGTW-----QMTGEEGKTVIRNAVLAGYRHIDTATLYqnehqiGDALAELFAEGILK-----REDIFITTK 81
Cdd:cd19158 9 SGLRVSCLGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVY------AAGKAEVVLGNIIKkkgwrRSSLVITTK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 82 AFC-------HEVAPDVVEEALRNSLKRLRLDYVDLYLAHIPastkddgsfRSDVKVEDIWRGFEKVYGLGLTKAIGVSN 154
Cdd:cd19158 83 IFWggkaeteRGLSRKHIIEGLKASLERLQLEYVDVVFANRP---------DPNTPMEETVRAMTHVINQGMAMYWGTSR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17566692 155 FNESQIVRIMNIQK----VPIHASQLELHLYLPQKAHREL 190
Cdd:cd19158 154 WSSMEIMEAYSVARqfnlIPPICEQAEYHMFQREKVEVQL 193
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
17-162 |
4.66e-07 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 50.40 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 17 PSIGLGTWQMTG-------EEGKTVIRNAVLAGYRHIDTATLYQN---EHQIGDALAElfaegiLKREDIFITTKA---- 82
Cdd:cd19161 1 SELGLGTAGLGNlytavsnADADATLDAAWDSGIRYFDTAPMYGHglaEHRLGDFLRE------KPRDEFVLSTKVgrll 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 83 ----FCHEVAPDVVEEALRN-----------------SLKRLRLDYVDLYLAHipastkDDGSFRSDVKVEDIW------ 135
Cdd:cd19161 75 kparEGSVPDPNGFVDPLPFeivydysydgimrsfedSLQRLGLNRIDILYVH------DIGVYTHGDRKERHHfaqlms 148
|
170 180 190
....*....|....*....|....*....|
gi 17566692 136 ---RGFEKVYGLGLTKAIGVSnFNESQIVR 162
Cdd:cd19161 149 ggfKALEELKKAGVIKAFGLG-VNEVQICL 177
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
12-250 |
1.22e-06 |
|
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.
Pssm-ID: 381368 [Multi-domain] Cd Length: 325 Bit Score: 49.38 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 12 NGVLMPSIGLGTWQMTG-----EEGKTVIRNAVLAGYRHIDTATLYQN---EHQIGDALAElfaeGILKREDIFITTKAF 83
Cdd:cd19142 9 SGLRVSNVGLGTWSTFStaiseEQAEEIVTLAYENGINYFDTSDAFTSgqaETELGRILKK----KGWKRSSYIVSTKIY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 84 CHEVAPD------VVEEALRNSLKRLRLDYVDLYLAHipastKDDGSfrsdVKVEDIWRGFEKVYGLGLTKAIGVSNFNE 157
Cdd:cd19142 85 WSYGSEErglsrkHIIESVRASLRRLQLDYIDIVIIH-----KADPM----CPMEEVVRAMSYLIDNGLIMYWGTSRWSP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 158 SQIVRIMNIQK-----VPIhASQLELH--------LYLPqkahrELCKKHNI-LITayatlGSPGRMSVVGSNGrplFES 223
Cdd:cd19142 156 VEIMEAFSIARqfncpTPI-CEQSEYHmfcrekmeLYMP-----ELYNKVGVgLIT-----WSPLSLGLDPGIS---EET 221
|
250 260
....*....|....*....|....*..
gi 17566692 224 TQNSENEMNDKHVKALAQKYSKTPAQI 250
Cdd:cd19142 222 RRLVTKLSFKSSKYKVGSDGNGIHEET 248
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
3-155 |
2.54e-06 |
|
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381379 [Multi-domain] Cd Length: 294 Bit Score: 48.30 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 3 SKVPIFTLS-NGVLMPSIGLGTwQMTGEEGKT----VIRNAVLAGYRHIDTATLYQN---EHQIGDALAELfaegILKRE 74
Cdd:cd19153 3 ETLEIALGNvSPVGLGTAALGG-VYGDGLEQDeavaIVAEAFAAGINHFDTSPYYGAessEAVLGKALAAL----QVPRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 75 DIFITTK-----AFCHEVAPDVVEEALRNSLKRLRLDYVDLYLAHipastkdDGSFRS-DVKVEDIWRGFEKVYGLGLTK 148
Cdd:cd19153 78 SYTVATKvgryrDSEFDYSAERVRASVATSLERLHTTYLDVVYLH-------DIEFVDyDTLVDEALPALRTLKDEGVIK 150
|
....*..
gi 17566692 149 AIGVSNF 155
Cdd:cd19153 151 RIGIAGY 157
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
6-114 |
3.07e-06 |
|
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+).
Pssm-ID: 381389 [Multi-domain] Cd Length: 293 Bit Score: 47.93 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 6 PIFTLSN-GVLMPSIGLGT-------WQMTGEEGKTVIRNAVLAGYRHIDTATLY---QNEHQIGDALaelfaEGIlKRE 74
Cdd:cd19163 2 KYRKLGKtGLKVSKLGFGAsplggvfGPVDEEEAIRTVHEALDSGINYIDTAPWYgqgRSETVLGKAL-----KGI-PRD 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 17566692 75 DIFITTKAFCHEVAPDV--------VEEALRNSLKRLRLDYVDLYLAH 114
Cdd:cd19163 76 SYYLATKVGRYGLDPDKmfdfsaerITKSVEESLKRLGLDYIDIIQVH 123
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
13-288 |
1.17e-05 |
|
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
Pssm-ID: 381376 [Multi-domain] Cd Length: 309 Bit Score: 46.29 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 13 GVLMPSIGLGTWQMTG-----EEGKTVIRNAVLAGYRHIDTATLY-----QNEHQIGDALAELFAEgilKREDIFITTKA 82
Cdd:cd19150 9 GLKLPALSLGLWHNFGddtplETQRAILRTAFDLGITHFDLANNYgpppgSAEENFGRILREDFAG---YRDELIISTKA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 83 fCHEVAPDVVEE---------ALRNSLKRLRLDYVDLYLAHipastkddgSFRSDVKVEDIWRGFEKVYGLGLTKAIGVS 153
Cdd:cd19150 86 -GYDMWPGPYGEwgsrkyllaSLDQSLKRMGLDYVDIFYSH---------RFDPDTPLEETMGALDHAVRSGKALYVGIS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 154 NFNES---QIVRIMNIQKVP--IH-ASQLELHLYLPQKAHRELCKKHNILITAYATL-----------GSP--GRMSVvg 214
Cdd:cd19150 156 SYSPErtrEAAAILRELGTPllIHqPSYNMLNRWVEESGLLDTLQELGVGCIAFTPLaqglltdkylnGIPegSRASK-- 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17566692 215 snGRPLFESTQNSENEMNDKHVKALAQKYSKTPAQILLRATVEMGII--VIPKTTNPERMKENINIFD-FNISNAEV 288
Cdd:cd19150 234 --ERSLSPKMLTEANLNSIRALNEIAQKRGQSLAQMALAWVLRDGRVtsALIGASRPEQLEENVGALDnLTFSADEL 308
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
18-296 |
2.97e-05 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 45.23 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 18 SIGLGTwqMT-GEEGKTV-----IRNAVLAGYRHIDTATLY----QNEHQigdALAELFAEGILK----REDIFITTKAF 83
Cdd:PRK10625 15 TLGLGT--MTfGEQNSEAdahaqLDYAVAQGINLIDVAEMYpvppRPETQ---GLTETYIGNWLAkrgsREKLIIASKVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 84 C------HEVAPDV------VEEALRNSLKRLRLDYVDLYLAHIPA-----------STKDDGSFRSDVKVEDIWRGFEK 140
Cdd:PRK10625 90 GpsrnndKGIRPNQaldrknIREALHDSLKRLQTDYLDLYQVHWPQrptncfgklgySWTDSAPAVSLLETLDALAEQQR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 141 VyglGLTKAIGVSN------------FNESQIVRIMNIQKvPIHASQLELHLYLPQKAHRElckkhNILITAYATLGSpG 208
Cdd:PRK10625 170 A---GKIRYIGVSNetafgvmrylhlAEKHDLPRIVTIQN-PYSLLNRSFEVGLAEVSQYE-----GVELLAYSCLAF-G 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 209 RMSVVGSNG-RP------LFESTQNSENEMNDKHVK---ALAQKYSKTPAQILLrATVEMGIIVIPK---TTNPERMKEN 275
Cdd:PRK10625 240 TLTGKYLNGaKPagarntLFSRFTRYSGEQTQKAVAayvDIAKRHGLDPAQMAL-AFVRRQPFVASTllgATTMEQLKTN 318
|
330 340
....*....|....*....|..
gi 17566692 276 INIFDFNISNAEVNLLEA-HER 296
Cdd:PRK10625 319 IESLHLTLSEEVLAEIEAvHQV 340
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
1-293 |
2.28e-04 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 42.26 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 1 MSSKVP--IFTLSnGVLMPSIGLGTWQMTG----------EEGKTVIRNAVLAGYRHIDTATLY----QNEhQIGDALAE 64
Cdd:PRK10376 1 MSTIMSsgTFTLG-GRSVNRLGYGAMQLAGpgvfgppkdrDAAIAVLREAVALGVNHIDTSDFYgphvTNQ-LIREALHP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 65 LfaegilkREDIFITTK---------AFCHEVAPDVVEEALRNSLKRL---RLDYVDLYL---AHIPAstkdDGSfrsdv 129
Cdd:PRK10376 79 Y-------PDDLTIVTKvgarrgedgSWLPAFSPAELRRAVHDNLRNLgldVLDVVNLRLmgdGHGPA----EGS----- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 130 kvedIWRGFEKVYGL---GLTKAIGVSNFNESQIVRIMNIqkVPIHASQLELHLylpqkAHRElckkHNILITAYATLGs 206
Cdd:PRK10376 143 ----IEEPLTVLAELqrqGLVRHIGLSNVTPTQVAEARKI--AEIVCVQNHYNL-----AHRA----DDALIDALARDG- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566692 207 pgrMSVVGSngRPL--FESTQNSEnemndkhVKALAQKYSKTPAQILL-----RATvemGIIVIPKTTNPERMKENINIF 279
Cdd:PRK10376 207 ---IAYVPF--FPLggFTPLQSST-------LSDVAASLGATPMQVALawllqRSP---NILLIPGTSSVAHLRENLAAA 271
|
330
....*....|....
gi 17566692 280 DFNISNAEVNLLEA 293
Cdd:PRK10376 272 ELVLSEEVLAELDG 285
|
|
| |
