|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
11-320 |
0e+00 |
|
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: 574.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 11 LSSVTFHNGRKMPVVGLGTWQSPPEEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKKWFDSGKLKREDVFIVTKLPP 90
Cdd:cd19155 1 RNCVTFNNGEKMPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 91 IGNRAESVEKFLTKSLEALQLDYVDLYLIHLPVGFQYKGDDNLWpRGEAGEFLIDTSTDLISLWKAMEAQVDAGRTRSVG 170
Cdd:cd19155 81 GGNRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLSKEDDSGK-LDPTGEHKQDYTTDLLDIWKAMEAQVDQGLTRSIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 171 LSNFNSRQIARIVKSARIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIGSPGLANVIKARGaeVPESAKFDPLTD 250
Cdd:cd19155 160 LSNFNREQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPGAAHFSPGTG--SPSGSSPDLLQD 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 251 PVVLKIAEHHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDELDSLDKRAAGRRF 320
Cdd:cd19155 238 PVVKAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIRGRTF 307
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
19-320 |
0e+00 |
|
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: 507.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 19 GRKMPVVGLGTWQSPPEEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKKWFDSGKLKREDVFIVTKLPPIGNRAESV 98
Cdd:cd19111 1 GFPMPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLEFKDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 99 EKFLTKSLEALQLDYVDLYLIHLPVGFQYKGDDnlwprgeagEFLIDTSTDLISLWKAMEAQVDAGRTRSVGLSNFNSRQ 178
Cdd:cd19111 81 EKSLEKSLENLKLPYVDLYLIHHPCGFVNKKDK---------GERELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 179 IARIVKSARIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIGSPGLANVIKargaevpESAKFDPLTDPVVLKIAE 258
Cdd:cd19111 152 INKILAYAKVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSPGRANQSL-------WPDQPDLLEDPTVLAIAK 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
5KET_A 259 HHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDELDSLDKRAAGRRF 320
Cdd:cd19111 225 ELDKTPAQVLLRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMKYFDF 286
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
12-314 |
8.32e-135 |
|
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: 385.61 E-value: 8.32e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 12 SSVTFHNGRKMPVVGLGTWQSPPEEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKKWFDSGKLKREDVFIVTKLPPI 91
Cdd:cd19154 2 ASITLSNGVKMPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLWTH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 92 GNRAESVEKFLTKSLEALQLDYVDLYLIHLPVGFqyKGDDNLWPRGEAGEfLIDTSTDLISLWKAMEAQVDAGRTRSVGL 171
Cdd:cd19154 82 EHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAF--KDDEGESGTMENGM-SIHDAVDVEDVWRGMEKVYDEGLTKAIGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 172 SNFNSRQIARIVKSARIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIGSPGLANVIKARGAEVPEsakfDPLTDP 251
Cdd:cd19154 159 SNFNNDQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSPGRANFTKSTGVSPAP----NLLQDP 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
5KET_A 252 VVLKIAEHHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDELDSLDKR 314
Cdd:cd19154 235 IVKAIAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKS 297
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
22-309 |
4.92e-122 |
|
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: 351.01 E-value: 4.92e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 22 MPVVGLGTWQSPPEEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKKWFdsgkLKREDVFIVTKLPPIGNRAESVEKF 101
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESG----VPREELFITTKLWPTDHGYERVREA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 102 LTKSLEALQLDYVDLYLIHLPVGFQYKGDDNLWprgeageflIDTstdlislWKAMEAQVDAGRTRSVGLSNFNSRQIAR 181
Cdd:cd19071 77 LEESLKDLGLDYLDLYLIHWPVPGKEGGSKEAR---------LET-------WRALEELVDEGLVRSIGVSNFNVEHLEE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 182 IVKSARIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIGSPGLanvikargaevpesakfDPLTDPVVLKIAEHHK 261
Cdd:cd19071 141 LLAAARIKPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRR-----------------PLLDDPVLKEIAKKYG 203
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
5KET_A 262 KTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDELD 309
Cdd:cd19071 204 KTPAQVLLRWALQRGVVVIPKSSNPERIKENLDVFDFELSEEDMAAID 251
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
18-313 |
1.19e-118 |
|
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: 344.27 E-value: 1.19e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 18 NGRKMPVVGLGTWQS-PPEEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKKWFDSGKLKREDVFIVTKLPPIGNRAE 96
Cdd:cd19116 7 DGNEIPAIALGTWKLkDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLWNSYHERE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 97 SVEKFLTKSLEALQLDYVDLYLIHLPVGFQYKGDDnlwprgEAGEFLIDTSTDLISLWKAMEAQVDAGRTRSVGLSNFNS 176
Cdd:cd19116 87 QVEPALRESLKRLGLDYVDLYLIHWPVAFKENNDS------ESNGDGSLSDIDYLETWRGMEDLVKLGLTRSIGVSNFNS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 177 RQIARIVKSARIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIGSPglanviKARGAEVPEsakfDPLTDPVVLKI 256
Cdd:cd19116 161 EQINRLLSNCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRL------VPRGQTNPP----PRLDDPTLVAI 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
5KET_A 257 AEHHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDELDSLDK 313
Cdd:cd19116 231 AKKYGKTTAQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNT 287
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
16-313 |
4.51e-118 |
|
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: 343.21 E-value: 4.51e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 16 FHNGRKMPVVGLGTWQSPPEEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKKWFDSGK-LKREDVFIVTKLPPIGNR 94
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPGKaVPREDLFVTSKLWNTKHH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 95 AESVEKFLTKSLEALQLDYVDLYLIHLPVGFqyKGDDNLWPRGEAGEFLIDtSTDLISLWKAMEAQVDAGRTRSVGLSNF 174
Cdd:cd19106 81 PEDVEPALRKTLKDLQLDYLDLYLIHWPYAF--ERGDNPFPKNPDGTIRYD-STHYKETWKAMEKLVDKGLVKAIGLSNF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 175 NSRQIARIVKSARIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIGSPGlanvikaRGAEVPESAKfdPLTDPVVL 254
Cdd:cd19106 158 NSRQIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPD-------RPWAKPDEPV--LLEEPKVK 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
5KET_A 255 KIAEHHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDELDSLDK 313
Cdd:cd19106 229 ALAKKYNKSPAQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNR 287
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
18-323 |
7.56e-116 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 335.49 E-value: 7.56e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 18 NGRKMPVVGLGTWQSPPEEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKkwfDSGkLKREDVFIVTKLPPIGNRAES 97
Cdd:COG0656 1 NGVEIPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIA---ASG-VPREELFVTTKVWNDNHGYDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 98 VEKFLTKSLEALQLDYVDLYLIHlpvgfqykgddnlWPRGEAgefLIDTstdlislWKAMEAQVDAGRTRSVGLSNFNSR 177
Cdd:COG0656 77 TLAAFEESLERLGLDYLDLYLIH-------------WPGPGP---YVET-------WRALEELYEEGLIRAIGVSNFDPE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 178 QIARIVKSARIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIGSPGLanvikargaevpesakfdpLTDPVVLKIA 257
Cdd:COG0656 134 HLEELLAETGVKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGRGKL-------------------LDDPVLAEIA 194
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
5KET_A 258 EHHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDELDSLDKraaGRRFRMD 323
Cdd:COG0656 195 EKHGKTPAQVVLRWHLQRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDR---GERLGPD 257
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
19-321 |
2.16e-106 |
|
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: 312.74 E-value: 2.16e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 19 GRKMPVVGLGTWQSPPEEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKKWFDSGKLKREDVFIVTKLPPIGNRAESV 98
Cdd:cd19125 8 GAKIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLWCTDHAPEDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 99 EKFLTKSLEALQLDYVDLYLIHLPVGFQyKGDdnlwPRGEAGEFLidtSTDLISLWKAMEAQVDAGRTRSVGLSNFNSRQ 178
Cdd:cd19125 88 PPALEKTLKDLQLDYLDLYLIHWPVRLK-KGA----HMPEPEEVL---PPDIPSTWKAMEKLVDSGKVRAIGVSNFSVKK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 179 IARIVKSARIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIGSPGLANVIKargaevpesakfDPLTDPVVLKIAE 258
Cdd:cd19125 160 LEDLLAVARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGTTWVKK------------NVLKDPIVTKVAE 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
5KET_A 259 HHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDELDSLDKRaagRRFR 321
Cdd:cd19125 228 KLGKTPAQVALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSIEQQ---RRVL 287
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
11-320 |
2.66e-104 |
|
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: 307.80 E-value: 2.66e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 11 LSSVTFHNGRKMPVVGLGTWQSPPEEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKKWFDSGKLKREDVFIVTKLPP 90
Cdd:cd19123 1 MKTLPLSNGDLIPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 91 IGNRAESVEKFLTKSLEALQLDYVDLYLIHLPVGFQykgDDNLWPRgEAGEFLIDTSTDLISLWKAMEAQVDAGRTRSVG 170
Cdd:cd19123 81 NSHAPEDVLPALEKTLADLQLDYLDLYLMHWPVALK---KGVGFPE-SGEDLLSLSPIPLEDTWRAMEELVDKGLCRHIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 171 LSNFNSRQIARIVKSARIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIGSPGLANVIKARGAEVpesakfdPLTD 250
Cdd:cd19123 157 VSNFSVKKLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDRPAAMKAEGEPV-------LLED 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 251 PVVLKIAEHHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDELDSLDKraaGRRF 320
Cdd:cd19123 230 PVINKIAEKHGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDR---HHRY 296
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
19-340 |
1.71e-102 |
|
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: 303.57 E-value: 1.71e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 19 GRKMPVVGLGTWQSPPEEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKKWFDSGKLKREDVFIVTKLPPIGNRAESV 98
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEKGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 99 EKFLTKSLEALQLDYVDLYLIHLPVGFQyKGDDnLWPRGEAGEfLIDTSTDLISLWKAMEAQVDAGRTRSVGLSNFNSRQ 178
Cdd:cd19107 81 KGACQKTLSDLKLDYLDLYLIHWPTGFK-PGKE-LFPLDESGN-VIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 179 IARIVKSA--RIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIGSPGlanvikaRGAEVPEsakfDP--LTDPVVL 254
Cdd:cd19107 158 IERILNKPglKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPD-------RPWAKPE----DPslLEDPKIK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 255 KIAEHHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDELDSLDkraagRRFRMDQYKGLREHPEH 334
Cdd:cd19107 227 EIAAKHNKTTAQVLIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFN-----RNWRACALLSCSSHKDY 301
|
....*.
5KET_A 335 PYDEPY 340
Cdd:cd19107 302 PFHAEY 307
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
13-313 |
1.61e-96 |
|
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: 288.36 E-value: 1.61e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 13 SVTFHNGRKMPVVGLGTWQS---PPEEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKKWFDSGKLKREDVFIVTKLP 89
Cdd:cd19108 2 RVKLNDGHFIPVLGFGTYAPeevPKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 90 PIGNRAESVEKFLTKSLEALQLDYVDLYLIHLPVGFqyKGDDNLWPRGEAGEFLIDTsTDLISLWKAMEAQVDAGRTRSV 169
Cdd:cd19108 82 CTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVAL--KPGEELFPKDENGKLIFDT-VDLCATWEAMEKCKDAGLAKSI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 170 GLSNFNSRQIARIVKSA--RIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIGSpglanvikARGAE-VPESAkfd 246
Cdd:cd19108 159 GVSNFNRRQLEMILNKPglKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGS--------QRDKEwVDQNS--- 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
5KET_A 247 P--LTDPVVLKIAEHHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDELDSLDK 313
Cdd:cd19108 228 PvlLEDPVLCALAKKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNR 296
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
22-311 |
3.94e-94 |
|
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: 280.67 E-value: 3.94e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 22 MPVVGLGTWQ-SPPEEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKKWFDSGKLKREDVFIVTKLPPIGNRAESVEK 100
Cdd:cd19136 1 MPILGLGTFRlRGEEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 101 FLTKSLEALQLDYVDLYLIHLPVGFQYKGDDnlwPRGEagEFLIDTstdlislWKAMEAQVDAGRTRSVGLSNFNSRQIA 180
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWPGVQGLKPSD---PRNA--ELRRES-------WRALEDLYKEGKLRAIGVSNYTVRHLE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 181 RIVKSARIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIGSPGLAnvikargaevpesakfdPLTDPVVLKIAEHH 260
Cdd:cd19136 149 ELLKYCEVPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGDLR-----------------LLEDPTVLAIAKKY 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
5KET_A 261 KKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDELDSL 311
Cdd:cd19136 212 GRTPAQVLLRWALQQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
21-340 |
4.93e-93 |
|
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: 279.54 E-value: 4.93e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 21 KMPVVGLGTWQSPPEEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKKWFDSGKLKREDVFIVTKLPPIGNRAESVEK 100
Cdd:cd19110 3 DIPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKSLVKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 101 FLTKSLEALQLDYVDLYLIHLPVGFQyKGDDNLwPRGEAGeFLIDTSTDLISLWKAMEAQVDAGRTRSVGLSNFNSRQIA 180
Cdd:cd19110 83 ACTRSLKALKLNYLDLYLIHWPMGFK-PGEPDL-PLDRSG-MVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 181 RIVKSA--RIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIGSPGlanvikargaevpesAKFDPLTDPVVLKIAE 258
Cdd:cd19110 160 RLLNKPglRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSC---------------EGVDLIDDPVIQRIAK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 259 HHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDELDSLDkraagRRFRMDQYKGLREHPEHPYDE 338
Cdd:cd19110 225 KHGKSPAQILIRFQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLD-----RNLRLATFPITENHKDYPFHI 299
|
..
5KET_A 339 PY 340
Cdd:cd19110 300 EY 301
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
12-314 |
1.13e-91 |
|
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: 275.90 E-value: 1.13e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 12 SSVTFHNGRKMPVVGLGTWQSPPEEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKKWFDSGKLKREDVFIVTKLppI 91
Cdd:cd19112 1 STITLNSGHKMPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKL--W 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 92 GNRAESVEKFLTKSLEALQLDYVDLYLIHLPVGFQYKG-DDNLWPRGEAGEFLIDTSTDLISLWKAMEAQVDAGRTRSVG 170
Cdd:cd19112 79 NSDHGHVIEACKDSLKKLQLDYLDLYLVHFPVATKHTGvGTTGSALGEDGVLDIDVTISLETTWHAMEKLVSAGLVRSIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 171 LSNFNSRQIARIVKSARIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIGSpGLANvikargAEVPESAKfdPLTD 250
Cdd:cd19112 159 ISNYDIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGG-AAAN------AEWFGSVS--PLDD 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
5KET_A 251 PVVLKIAEHHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDELDSLDKR 314
Cdd:cd19112 230 PVLKDLAKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRK 293
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
19-336 |
6.64e-91 |
|
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: 273.98 E-value: 6.64e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 19 GRKMPVVGLGTWQSP----PEEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKKWFDSGKLKREDVFIVTKLPPIGNR 94
Cdd:cd19109 1 GNSIPIIGLGTYSEPkttpKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 95 AESVEKFLTKSLEALQLDYVDLYLIHLPVGFqyKGDDNLWPRGEAGEFLIDtSTDLISLWKAMEAQVDAGRTRSVGLSNF 174
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAF--KPGDEIYPRDENGKWLYH-KTNLCATWEALEACKDAGLVKSIGVSNF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 175 NSRQIARIVKSA--RIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIGSPglanvikarGAEVPESAKFDP-LTDP 251
Cdd:cd19109 158 NRRQLELILNKPglKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTC---------RDPIWVNVSSPPlLEDP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 252 VVLKIAEHHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDELDSLDKRAAGRRFRMdqykgLREH 331
Cdd:cd19109 229 LLNSIGKKYNKTAAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYVELLM-----WRDH 303
|
....*
5KET_A 332 PEHPY 336
Cdd:cd19109 304 PEYPF 308
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
13-312 |
1.34e-90 |
|
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: 271.55 E-value: 1.34e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 13 SVTFHNGRKMPVVGLGTWQSPPEEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKkwfDSGkLKREDVFIVTKLPPIG 92
Cdd:cd19131 1 TITLNDGNTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIR---ASG-VPREELFITTKLWNSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 93 NRAESVEKFLTKSLEALQLDYVDLYLIHlpvgfqykgddnlWPRGEAGEFlIDTstdlislWKAMEAQVDAGRTRSVGLS 172
Cdd:cd19131 77 QGYDSTLRAFDESLRKLGLDYVDLYLIH-------------WPVPAQDKY-VET-------WKALIELKKEGRVKSIGVS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 173 NFNSRQIARIVKSARIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIGSPGLanvikargaevpesakfdpLTDPV 252
Cdd:cd19131 136 NFTIEHLQRLIDETGVVPVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGGL-------------------LSDPV 196
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 253 VLKIAEHHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDELDSLD 312
Cdd:cd19131 197 IGEIAEKHGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELDADDMQAIAGLD 256
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
18-311 |
3.45e-90 |
|
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: 271.21 E-value: 3.45e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 18 NGRKMPVVGLGTWQSPPEEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKKWFDS-GKLKREDVFIVTKLPPIGNRAE 96
Cdd:cd19118 3 TGNKIPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEePGVKREDLFITSKLWNNSHRPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 97 SVEKFLTKSLEALQLDYVDLYLIHLPVGFQYKGDDNLWP--RGEAGEFLIDTSTDLISLWKAMEAQVDAGRTRSVGLSNF 174
Cdd:cd19118 83 YVEPALDDTLKELGLDYLDLYLIHWPVAFKPTGDLNPLTavPTNGGEVDLDLSVSLVDTWKAMVELKKTGKVKSIGVSNF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 175 NSRQIARIVKSARIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIGSpglaNVIKArgaevpesakfDPLTD-PVV 253
Cdd:cd19118 163 SIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGN----NLAGL-----------PLLVQhPEV 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
5KET_A 254 LKIAEHHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQvfDFELSKAEVDELDSL 311
Cdd:cd19118 228 KAIAAKLGKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVTAL 283
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
14-312 |
2.00e-89 |
|
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: 268.29 E-value: 2.00e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 14 VTFHNGRKMPVVGLGTWQ-SPPEEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKKwfdSGkLKREDVFIVTKLPPIG 92
Cdd:cd19133 1 VTLNNGVEMPILGFGVFQiPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKK---SG-IPREELFITTKLWIQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 93 NRAESVEKFLTKSLEALQLDYVDLYLIHLPVGfqykgddnlwprgeageflidtstDLISLWKAMEAQVDAGRTRSVGLS 172
Cdd:cd19133 77 AGYEKAKKAFERSLKRLGLDYLDLYLIHQPFG------------------------DVYGAWRAMEELYKEGKIRAIGVS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 173 NFNSRQIARIVKSARIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIGSpglanvikargaevpesAKFDPLTDPV 252
Cdd:cd19133 133 NFYPDRLVDLILHNEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAE-----------------GRNNLFENPV 195
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 253 VLKIAEHHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDELDSLD 312
Cdd:cd19133 196 LTEIAEKYGKSVAQVILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAALD 255
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
22-309 |
3.93e-86 |
|
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: 259.51 E-value: 3.93e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 22 MPVVGLGTWQSPPEEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKkwfDSGkLKREDVFIVTKLPPIGNRAESVEKF 101
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIA---ESG-VPREDLFITTKVWRDHLRPEDLKKS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 102 LTKSLEALQLDYVDLYLIHlpvgfqykgddnlWPRGE--AGEFLidtstdlislwKAMEAQVDAGRTRSVGLSNFNSRQI 179
Cdd:cd19073 77 VDRSLEKLGTDYVDLLLIH-------------WPNPTvpLEETL-----------GALKELKEAGKVKSIGVSNFTIELL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 180 ARIVKSARIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIgspglanvikARGaEVPEsakfdpltDPVVLKIAEH 259
Cdd:cd19073 133 EEALDISPLPIAVNQVEFHPFLYQAELLEYCRENDIVITAYSPL----------ARG-EVLR--------DPVIQEIAEK 193
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
5KET_A 260 HKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDELD 309
Cdd:cd19073 194 YDKTPAQVALRWLVQKGIVVIPKASSEDHLKENLAIFDWELTSEDVAKID 243
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
18-311 |
5.73e-85 |
|
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: 257.97 E-value: 5.73e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 18 NGRKMPVVGLGTWQSP--PEEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKKWFDSGKLK-REDVFIVTKLPPIGNR 94
Cdd:cd19124 1 SGQTMPVIGMGTASDPpsPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKLWCSDAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 95 AESVEKFLTKSLEALQLDYVDLYLIHLPVGFQyKGddNLWPRGEAGEFLidtSTDLISLWKAMEAQVDAGRTRSVGLSNF 174
Cdd:cd19124 81 PDLVLPALKKSLRNLQLEYVDLYLIHWPVSLK-PG--KFSFPIEEEDFL---PFDIKGVWEAMEECQRLGLTKAIGVSNF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 175 NSRQIARIVKSARIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIGSPGlanvIKARGAEVPESakfdpltdPVVL 254
Cdd:cd19124 155 SCKKLQELLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPG----TKWGSNAVMES--------DVLK 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
5KET_A 255 KIAEHHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDELDSL 311
Cdd:cd19124 223 EIAAAKGKTVAQVSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
12-299 |
6.61e-83 |
|
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: 252.84 E-value: 6.61e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 12 SSVTFHNGRKMPVVGLGTWQSPPEEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKKWFDSGkLKREDVFIVTKLPPI 91
Cdd:cd19121 2 TSFKLNTGASIPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAIAGG-VKREDLFVTTKLWST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 92 GNRaeSVEKFLTKSLEALQLDYVDLYLIHLPVGFQYKGDDNLWPRGEAGEFLIDTSTDLISLWKAMEAQVDAGRTRSVGL 171
Cdd:cd19121 81 YHR--RVELCLDRSLKSLGLDYVDLYLVHWPVLLNPNGNHDLFPTLPDGSRDLDWDWNHVDTWKQMEKVLKTGKTKAIGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 172 SNFNSRQIARIVKSARIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIGSPGlanvikargaevpesakfDPL-TD 250
Cdd:cd19121 159 SNYSIPYLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTG------------------SPLiSD 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
5KET_A 251 PVVLKIAEHHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVFDFE 299
Cdd:cd19121 221 EPVVEIAKKHNVGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDLD 269
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
14-312 |
1.97e-82 |
|
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: 251.17 E-value: 1.97e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 14 VTFHNGRKMPVVGLGTWQSPPEEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKKwfdSGkLKREDVFIVTKLPPIGN 93
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRR---SG-VDRSDIFVTTKLWISDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 94 RAESVEKFLTKSLEALQLDYVDLYLIHLPVgfqykgdDNLWPRgeageflidtstdLISLWKAMEAQVDAGRTRSVGLSN 173
Cdd:cd19127 77 GYDKALRGFDASLRRLGLDYVDLYLLHWPV-------PNDFDR-------------TIQAYKALEKLLAEGRVRAIGVSN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 174 FNSRQIARIVKSARIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIGSpglanvIKARGAEVPESAKfDPLTDPVV 253
Cdd:cd19127 137 FTPEHLERLIDATTVVPAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGG------VMRYGASGPTGPG-DVLQDPTI 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
5KET_A 254 LKIAEHHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDELDSLD 312
Cdd:cd19127 210 TGLAEKYGKTPAQIVLRWHLQNGVSAIPKSVHPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
14-312 |
1.97e-81 |
|
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: 248.12 E-value: 1.97e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 14 VTFHNGRKMPVVGLGTWQSPP-EEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKKwfdSGkLKREDVFIVTKLPPIG 92
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQTPDgDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRE---SG-VPREELFVTTKLWNDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 93 NRAESVEKFLTKSLEALQLDYVDLYLIHlpvgfqykgddnlWPrgeAGEFLIDTstdlislWKAMEAQVDAGRTRSVGLS 172
Cdd:cd19126 77 QRARRTEDAFQESLDRLGLDYVDLYLIH-------------WP---GKDKFIDT-------WKALEKLYASGKVKAIGVS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 173 NFNSRQIARIVKSARIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIGSPGLanvikargaevpesakfdpLTDPV 252
Cdd:cd19126 134 NFQEHHLEELLAHADVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQGGL-------------------LSNPV 194
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 253 VLKIAEHHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDELDSLD 312
Cdd:cd19126 195 LAAIGEKYGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAIDALN 254
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
15-315 |
3.25e-81 |
|
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: 248.57 E-value: 3.25e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 15 TFHNGRKMPVVGLGTWQSPPEEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKkwfDSGkLKREDVFIVTKLPpiGNR 94
Cdd:cd19117 7 KLNTGAEIPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIK---DSG-VPREEIFITTKLW--CTW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 95 AESVEKFLTKSLEALQLDYVDLYLIHLPVGFQYKGDDNLwPRGEAGEFLIDTSTDLISLWKAMEAQVDAGRTRSVGLSNF 174
Cdd:cd19117 81 HRRVEEALDQSLKKLGLDYVDLYLMHWPVPLDPDGNDFL-FKKDDGTKDHEPDWDFIKTWELMQKLPATGKVKAIGVSNF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 175 NSRQIARIVK--SARIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIGSPGlANVIKargaevpesakfdpltDPV 252
Cdd:cd19117 160 SIKNLEKLLAspSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTN-APLLK----------------EPV 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
5KET_A 253 VLKIAEHHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVfdFELSKAEVDELDSLDKRA 315
Cdd:cd19117 223 IIKIAKKHGKTPAQVIISWGLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEIDELHKEY 283
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
17-295 |
5.69e-81 |
|
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: 248.14 E-value: 5.69e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 17 HNGRKMPVVGLGTWQSPPEEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKKWFDSGKLKREDVFIVTKLPPIGNRAE 96
Cdd:cd19129 1 NGSGAIPALGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNHRPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 97 SVEKFLTKSLEALQLDYVDLYLIHLPVGFQyKGDDNLwPRGEAGEFLIDTSTDLISLWKAMEAQVDAGRTRSVGLSNFNS 176
Cdd:cd19129 81 RVKPAFEASLKRLQLDYLDLYLIHTPFAFQ-PGDEQD-PRDANGNVIYDDGVTLLDTWRAMERLVDEGRCKAIGLSDVSL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 177 RQIARIVKSARIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIGspglanvikargaevpESAKFDPLTDPVVLKI 256
Cdd:cd19129 159 EKLREIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLG----------------HGMEPKLLEDPVITAI 222
|
250 260 270
....*....|....*....|....*....|....*....
5KET_A 257 AEHHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQV 295
Cdd:cd19129 223 ARRVNKTPAQVLLAWAIQRGTALLTTSKTPSRIRENFDI 261
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
19-315 |
1.53e-80 |
|
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: 246.38 E-value: 1.53e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 19 GRKMPVVGLGT----WQSPP----EEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKKWfdsgKLKREDVFIVTKLpp 90
Cdd:cd19120 1 GSKIPAIAFGTgtawYKSGDddiqRDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALKES----GVPREDLFITTKV-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 91 iGNRAESVEKFLTKSLEALQLDYVDLYLIHLPvgFQYKGDDnlwprgeageflidtsTDLISLWKAMEAQVDAGRTRSVG 170
Cdd:cd19120 75 -SPGIKDPREALRKSLAKLGVDYVDLYLIHSP--FFAKEGG----------------PTLAEAWAELEALKDAGLVRSIG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 171 LSNFNSRQIARIVKSARIRPANLQVELNVYF--QQRELVAFCRALDITVCAYAPigspgLANVIKARGaevpesakfDPL 248
Cdd:cd19120 136 VSNFRIEDLEELLDTAKIKPAVNQIEFHPYLypQQPALLEYCREHGIVVSAYSP-----LSPLTRDAG---------GPL 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
5KET_A 249 tDPVVLKIAEHHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDELDSLDKRA 315
Cdd:cd19120 202 -DPVLEKIAEKYGVTPAQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEIDKAGKQK 267
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
13-320 |
1.13e-78 |
|
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: 243.10 E-value: 1.13e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 13 SVTFHNGRKMPVVGLGTWQSPPEEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKKWFDSGKLKREDVFIVTKLPPIG 92
Cdd:cd19115 4 TVKLNSGYDMPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLWNTF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 93 NRAESVEKFLTKSLEALQLDYVDLYLIHLPVGFQYKGDDNLWPRG--EAGEFLIDTSTDLISLWKAMEAQVDAGRTRSVG 170
Cdd:cd19115 84 HDGERVEPICRKQLADWGIDYFDLFLIHFPIALKYVDPAVRYPPGwfYDGKKVEFSNAPIQETWTAMEKLVDKGLARSIG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 171 LSNFNSRQIARIVKSARIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIGSPGLANVikargaEVPESAKFDPLTD 250
Cdd:cd19115 164 VSNFSAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGPQSFLEL------DLPGAKDTPPLFE 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
5KET_A 251 -PVVLKIAEHHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDELDSLDKraaGRRF 320
Cdd:cd19115 238 hDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDI---GLRF 305
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
13-313 |
1.25e-76 |
|
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: 236.13 E-value: 1.25e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 13 SVTFHNGRKMPVVGLGTWQSPP-EEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKkwfDSGKlKREDVFIVTKLPPI 91
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEEgSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIK---ESGI-PREELFITSKVWNA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 92 GNRAESVEKFLTKSLEALQLDYVDLYLIHLPVGFQYKgddnlwprgeagefliDTstdlislWKAMEAQVDAGRTRSVGL 171
Cdd:cd19157 77 DQGYDSTLKAFEASLERLGLDYLDLYLIHWPVKGKYK----------------ET-------WKALEKLYKDGRVRAIGV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 172 SNFNSRQIARIVKSARIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIGSPGLanvikargaevpesakfdpLTDP 251
Cdd:cd19157 134 SNFQVHHLEDLLADAEIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQL-------------------LDNP 194
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
5KET_A 252 VVLKIAEHHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDELDSLDK 313
Cdd:cd19157 195 VLKEIAEKYNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNE 256
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
12-320 |
4.16e-76 |
|
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: 236.19 E-value: 4.16e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 12 SSVTFHNGRKMPVVGLGTWQSPPEEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKKWFDSGKLKREDVFIVTKLPPI 91
Cdd:cd19113 1 PDIKLNSGYKMPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 92 GNRAESVEKFLTKSLEALQLDYVDLYLIHLPVGFQYKGDDNLWPRG---EAGEFLIDTSTDLISLWKAMEAQVDAGRTRS 168
Cdd:cd19113 81 FHDPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKFVPIEEKYPPGfycGDGDNFVYEDVPILDTWKALEKLVDAGKIKS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 169 VGLSNFNSRQIARIVKSARIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIGSPGLANVIKARGAEVPesakfdPL 248
Cdd:cd19113 161 IGVSNFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGPQSFVELNQGRALNTP------TL 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
5KET_A 249 -TDPVVLKIAEHHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDELDSLDkraAGRRF 320
Cdd:cd19113 235 fEHDTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLD---IGLRF 304
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
14-313 |
2.25e-75 |
|
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: 233.18 E-value: 2.25e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 14 VTFHNGRKMPVVGLGTWQSPP-EEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKKwfdSGkLKREDVFIVTKLPPIG 92
Cdd:cd19156 1 VKLANGVEMPRLGLGVWRVQDgAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRE---SG-VPREEVFVTTKLWNSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 93 NRAESVEKFLTKSLEALQLDYVDLYLIHLPVGFQYKgddnlwprgeagefliDTstdlislWKAMEAQVDAGRTRSVGLS 172
Cdd:cd19156 77 QGYESTLAAFEESLEKLGLDYVDLYLIHWPVKGKFK----------------DT-------WKAFEKLYKEKKVRAIGVS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 173 NFNSRQIARIVKSARIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIGSPGLanvikargaevpesakfdpLTDPV 252
Cdd:cd19156 134 NFHEHHLEELLKSCKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGKL-------------------LSNPV 194
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
5KET_A 253 VLKIAEHHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDELDSLDK 313
Cdd:cd19156 195 LKAIGKKYGKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNT 255
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
17-311 |
2.36e-75 |
|
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: 232.53 E-value: 2.36e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 17 HNGRKMPVVGLGTWQSPPEEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKkwfDSGkLKREDVFIVTKLPPIGNRAE 96
Cdd:cd19140 3 VNGVRIPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIA---ASG-VPRDELFLTTKVWPDNYSPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 97 SVEKFLTKSLEALQLDYVDLYLIHlpvgfqykgddnlWPRGEageflidtsTDLISLWKAMEAQVDAGRTRSVGLSNFNS 176
Cdd:cd19140 79 DFLASVEESLRKLRTDYVDLLLLH-------------WPNKD---------VPLAETLGALNEAQEAGLARHIGVSNFTV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 177 RQIARIVKSARIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIgspglanvikARGaEVpesakfdpLTDPVVLKI 256
Cdd:cd19140 137 ALLREAVELSEAPLFTNQVEYHPYLDQRKLLDAAREHGIALTAYSPL----------ARG-EV--------LKDPVLQEI 197
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
5KET_A 257 AEHHKKTPAQVLLR-HCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDELDSL 311
Cdd:cd19140 198 GRKHGKTPAQVALRwLLQQEGVAAIPKATNPERLEENLDIFDFTLSDEEMARIAAL 253
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
14-311 |
8.38e-75 |
|
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: 231.44 E-value: 8.38e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 14 VTFHNGRKMPVVGLGTWQSPPEEVTAAIdVAL-EVGYRHIDTAFMYQNEAAIGKTLKKwfdSGkLKREDVFIVTKLPPIG 92
Cdd:cd19135 5 VRLSNGVEMPILGLGTSHSGGYSHEAVV-YALkECGYRHIDTAKRYGCEELLGKAIKE---SG-VPREDLFLTTKLWPSD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 93 NRAESVEKFLTKSLEALQLDYVDLYLIHLPVGfQYKGDDNLWPRGEAgeflidtstdlislWKAMEAQVDAGRTRSVGLS 172
Cdd:cd19135 80 YGYESTKQAFEASLKRLGVDYLDLYLLHWPDC-PSSGKNVKETRAET--------------WRALEELYDEGLCRAIGVS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 173 NFNSRQIARIVKSARIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIgspglanvikargaevpesAKFDPLTDPV 252
Cdd:cd19135 145 NFLIEHLEQLLEDCSVVPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPL-------------------AKGKALEEPT 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
5KET_A 253 VLKIAEHHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDELDSL 311
Cdd:cd19135 206 VTELAKKYQKTPAQILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
19-320 |
1.03e-72 |
|
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: 227.44 E-value: 1.03e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 19 GRKMPVVGLGTWQSPPEEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKKWFDSGKLKREDVFIVTKLPPIGNRAESV 98
Cdd:cd19114 1 GDKMPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGKDHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 99 EKFLTKSLEALQLDYVDLYLIHLPVGFQYKGDDN----LWPRGEAGEFLIDTSTdLISLWKAMEAQVDAGRTRSVGLSNF 174
Cdd:cd19114 81 REAFDRQLKDYGLDYIDLYLIHFPIPAAYVDPAEnypfLWKDKELKKFPLEQSP-MQECWREMEKLVDAGLVRNIGIANF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 175 NSRQIARIVKSARIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIGSPGLANVIKargaevpESAKFDPLTD-PVV 253
Cdd:cd19114 160 NVQLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAVYTKVTK-------HLKHFTNLLEhPVV 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
5KET_A 254 LKIAEHHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDELDSLDkraAGRRF 320
Cdd:cd19114 233 KKLADKHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELE---ANARF 296
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
16-312 |
6.17e-72 |
|
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: 223.69 E-value: 6.17e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 16 FHNGRKMPVVGLGTWQSPPEEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKkwfDSGkLKREDVFIVTKLPPIGNRA 95
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVR---RSG-VPREELFVTTKLPGRHHGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 96 ESVEKFLTKSLEALQLDYVDLYLIHlpvgfqykgddnlWPrgeagefliDTSTDL-ISLWKAM-EAQvDAGRTRSVGLSN 173
Cdd:cd19132 77 EEALRTIEESLYRLGLDYVDLYLIH-------------WP---------NPSRDLyVEAWQALiEAR-EEGLVRSIGVSN 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 174 FNSRQIARIVKSARIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIGspglanvikaRGAEVpesakfdpLTDPVV 253
Cdd:cd19132 134 FLPEHLDRLIDETGVTPAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLG----------RGSGL--------LDEPVI 195
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
5KET_A 254 LKIAEHHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDELDSLD 312
Cdd:cd19132 196 KAIAEKHGKTPAQVVLRWHVQLGVVPIPKSANPERQRENLAIFDFELSDEDMAAIAALD 254
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
14-319 |
1.90e-70 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 220.71 E-value: 1.90e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 14 VTFHNGRKMPVVGLGTWQSPPEEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKkwfdSGKLKREDVFIVTKLppIGN 93
Cdd:PRK11565 7 IKLQDGNVMPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALK----EASVAREELFITTKL--WND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 94 RAESVEKFLTKSLEALQLDYVDLYLIHlpvgfqykgddnlWPRGEAGEFlidtstdlISLWKAMEAQVDAGRTRSVGLSN 173
Cdd:PRK11565 81 DHKRPREALEESLKKLQLDYVDLYLMH-------------WPVPAIDHY--------VEAWKGMIELQKEGLIKSIGVCN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 174 FNSRQIARIVKSARIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIgspglanvikARGAEvpesAKFDpltDPVV 253
Cdd:PRK11565 140 FQIHHLQRLIDETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPL----------AQGGK----GVFD---QKVI 202
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
5KET_A 254 LKIAEHHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDELDSLDKraaGRR 319
Cdd:PRK11565 203 RDLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRLDKDELGEIAKLDQ---GKR 265
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
23-311 |
5.06e-70 |
|
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: 219.70 E-value: 5.06e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 23 PVVGLGTWQSPPEEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKKWFDSGKLKREDVFIVTKLPPIGNRAESVEKFL 102
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVKEQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 103 TKSLEALQLDYVDLYLIHLPVGFQYkgDDNLWPRGEAGEFLIDTSTdLISLWKAMEAQVDAGRTRSVGLSNFNSRQIARI 182
Cdd:cd19128 82 LITLQDLQLEYLDLFLIHWPLAFDM--DTDGDPRDDNQIQSLSKKP-LEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 183 VKSARIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIGSPglanviKARGAEVpesakfdPLTDPVVLKIAEHHKK 262
Cdd:cd19128 159 LNYCKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGS------YGDGNLT-------FLNDSELKALATKYNT 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
5KET_A 263 TPAQVLLRHCMQR---DIVVIPKSTNAGRIKENFQVFDFELSKAEVDELDSL 311
Cdd:cd19128 226 TPPQVIIAWHLQKwpkNYSVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
13-319 |
2.75e-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: 218.52 E-value: 2.75e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 13 SVTFHNGRKMPVVGLGTWqSPPE---EVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKKWFDSGKLKREDVFIVTKL- 88
Cdd:cd19119 3 SFKLNTGASIPALGLGTA-SPHEdraEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVw 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 89 PPIGNRaesVEKFLTKSLEALQLDYVDLYLIHLPVGFQYKGDDN---LWPRGEAGEFLIDTSTDLISLWKAMEAQVDAGR 165
Cdd:cd19119 82 PTFYDE---VERSLDESLKALGLDYVDLLLVHWPVCFEKDSDDSgkpFTPVNDDGKTRYAASGDHITTYKQLEKIYLDGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 166 TRSVGLSNFNSRQIARIVKSARIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIGSPGLANvikargaevpesakf 245
Cdd:cd19119 159 AKAIGVSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAPN--------------- 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
5KET_A 246 dpLTDPVVLKIAEHHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVfdFELSKAEVDELDSLDKRAAGRR 319
Cdd:cd19119 224 --LKNPLVKKIAEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLDDIGEKYPVRF 293
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
13-321 |
1.54e-65 |
|
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: 207.79 E-value: 1.54e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 13 SVTFHNGRKMPVVGLGTWQSPPEEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKKwfdSGkLKREDVFIVTKLPPIG 92
Cdd:cd19134 2 TVTLNDDNTMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAA---SG-IPRGELFVTTKLATPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 93 NRAESVEKFLTKSLEALQLDYVDLYLIHlpvgfqykgddnlWPRGEAGEFlIDTstdlislWKAMEAQVDAGRTRSVGLS 172
Cdd:cd19134 78 QGFTASQAACRASLERLGLDYVDLYLIH-------------WPAGREGKY-VDS-------WGGLMKLREEGLARSIGVS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 173 NFNSRQIARIVKSARIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIGSPGLanvikargaevpesakfdpLTDPV 252
Cdd:cd19134 137 NFTAEHLENLIDLTFFTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGRL-------------------LDNPA 197
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
5KET_A 253 VLKIAEHHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDELDSLDKraaGRRFR 321
Cdd:cd19134 198 VTAIAAAHGRTPAQVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDALDGLDD---GTRFR 263
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
25-312 |
9.42e-65 |
|
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: 206.39 E-value: 9.42e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 25 VGLGTWQ-------SPPEEVTAAIDVALEVGYRHIDTAFMY---QNEAAIGKTLKKWFDsgklKREDVFIVTKLP----- 89
Cdd:pfam00248 1 IGLGTWQlgggwgpISKEEALEALRAALEAGINFIDTAEVYgdgKSEELLGEALKDYPV----KRDKVVIATKVPdgdgp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 90 -PIGNRAESVEKFLTKSLEALQLDYVDLYLIHlpvgfqykgddnlWPrgeagefliDTSTDLISLWKAMEAQVDAGRTRS 168
Cdd:pfam00248 77 wPSGGSKENIRKSLEESLKRLGTDYIDLYYLH-------------WP---------DPDTPIEETWDALEELKKEGKIRA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 169 VGLSNFNSRQIARIVKSARIRPANLQVELNVYF--QQRELVAFCRALDITVCAYAPIGSPGLA-----NVIKARGAEVPE 241
Cdd:pfam00248 135 IGVSNFDAEQIEKALTKGKIPIVAVQVEYNLLRrrQEEELLEYCKKNGIPLIAYSPLGGGLLTgkytrDPDKGPGERRRL 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
5KET_A 242 SAKFDPLT---DPVVLKIAEHHKKTPAQVLLRHCMQRD--IVVIPKSTNAGRIKENFQVFDFELSKAEVDELDSLD 312
Cdd:pfam00248 215 LKKGTPLNleaLEALEEIAKEHGVSPAQVALRWALSKPgvTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
13-312 |
4.88e-62 |
|
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: 198.60 E-value: 4.88e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 13 SVTFHNGRKMPVVGLGTWQSPPEEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKKwfdSGkLKREDVFIVTKLPPIG 92
Cdd:cd19130 1 SIVLNDGNSIPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIAA---SG-IPRDELFVTTKLWNDR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 93 NRAESVEKFLTKSLEALQLDYVDLYLIHlpvgfqykgddnlWPRGEAGEFlidtstdlISLWKAMEAQVDAGRTRSVGLS 172
Cdd:cd19130 77 HDGDEPAAAFAESLAKLGLDQVDLYLVH-------------WPTPAAGNY--------VHTWEAMIELRAAGRTRSIGVS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 173 NFNSRQIARIVKSARIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIGSPGLanvikargaevpesakfdpLTDPV 252
Cdd:cd19130 136 NFLPPHLERIVAATGVVPAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQGKL-------------------LGDPP 196
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 253 VLKIAEHHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDELDSLD 312
Cdd:cd19130 197 VGAIAAAHGKTPAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAIDALD 256
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
22-311 |
2.92e-60 |
|
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: 193.72 E-value: 2.92e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 22 MPVVGLGTWQSPPEEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKkwfDSGkLKREDVFIVTKLPPIGNRAESVEKF 101
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIA---ESG-VPRDELFITTKIWIDNLSKDKLLPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 102 LTKSLEALQLDYVDLYLIHLPVgfqykgddnlwPRGE--AGEFLidtstdlislwKAMEAQVDAGRTRSVGLSNFN---S 176
Cdd:cd19139 77 LEESLEKLRTDYVDLTLIHWPS-----------PNDEvpVEEYI-----------GALAEAKEQGLTRHIGVSNFTialL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 177 RQIARIVKSARIrpANLQVELNVYFQQRELVAFCRALDITVCAYAPIgspglanvikARGAevpesakfdPLTDPVVLKI 256
Cdd:cd19139 135 DEAIAVVGAGAI--ATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTL----------AYGK---------VLDDPVLAAI 193
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
5KET_A 257 AEHHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDELDSL 311
Cdd:cd19139 194 AERHGATPAQIALAWAMARGYAVIPSSTKREHLRSNLLALDLTLDADDMAAIAAL 248
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
19-309 |
1.56e-56 |
|
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: 184.35 E-value: 1.56e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 19 GRKMPVVGLGTW-----QSPP----EEVTAAIDVALEVGYRHIDTAFMYQN---EAAIGKTLKKWfdsgklKREDVFIVT 86
Cdd:cd19072 1 GEEVPVLGLGTWgigggMSKDysddKKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAIKGF------DREDLFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 87 KLPPIGNRAESVEKFLTKSLEALQLDYVDLYLIHlpvgfqykgddnlWPrgeagefliDTSTDLISLWKAMEAQVDAGRT 166
Cdd:cd19072 75 KVSPDHLKYDDVIKAAKESLKRLGTDYIDLYLIH-------------WP---------NPSIPIEETLRAMEELVEEGKI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 167 RSVGLSNFNSRQIARIVKSA-RIRPANLQVELNVYFQ--QRELVAFCRALDITVCAYAPIGSPGLANVIkargaevpesa 243
Cdd:cd19072 133 RYIGVSNFSLEELEEAQSYLkKGPIVANQVEYNLFDReeESGLLPYCQKNGIAIIAYSPLEKGKLSNAK----------- 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
5KET_A 244 kfdplTDPVVLKIAEHHKKTPAQVLLRHCMQRD-IVVIPKSTNAGRIKENFQVFDFELSKAEVDELD 309
Cdd:cd19072 202 -----GSPLLDEIAKKYGKTPAQIALNWLISKPnVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
15-313 |
2.79e-55 |
|
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: 182.05 E-value: 2.79e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 15 TFHNGRKMPVVGLGTWQSPPE--EVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKKWF-DSGKLKREDVFIVTKLPPI 91
Cdd:cd19122 2 TLNNGVKIPAVGFGTFANEGAkgETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLkENPSVKREDLFICTKVWNH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 92 GNRAESVEKFLTKSLEALQLDYVDLYLIHLPVGFQyKGDDNLWPRGEAGEFLI--DTSTDLISLWKAMEAQVDAGRTRSV 169
Cdd:cd19122 82 LHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAE-KNDQRSPKLGPDGKYVIlkDLTENPEPTWRAMEEIYESGKAKAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 170 GLSNFNSRQIARIVKSARIRPANLQVELNVYFQQRELVAFCRALDITVCAYAPIGSpglANVIKARGAEVPEsakfdplt 249
Cdd:cd19122 161 GVSNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGS---QNQVPSTGERVSE-------- 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
5KET_A 250 DPVVLKIAEHHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVfdFELSKAEVDELDSLDK 313
Cdd:cd19122 230 NPTLNEVAEKGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKS--IELSDEDFEAINQVAK 291
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
19-311 |
2.25e-51 |
|
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: 172.67 E-value: 2.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 19 GRKMPVVGLGTWQ-------SPPEEVTAAIDVALEVGYRHIDTAFMY---QNEAAIGKTLKKWfdsgklKREDVFIVTKL 88
Cdd:COG0667 10 GLKVSRLGLGTMTfggpwggVDEAEAIAILDAALDAGINFFDTADVYgpgRSEELLGEALKGR------PRDDVVIATKV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 89 --------PPIGNRAESVEKFLTKSLEALQLDYVDLYLIHlpvgfqykgddnlWPrgeagefliDTSTDLISLWKAMEAQ 160
Cdd:COG0667 84 grrmgpgpNGRGLSREHIRRAVEASLRRLGTDYIDLYQLH-------------RP---------DPDTPIEETLGALDEL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 161 VDAGRTRSVGLSNFNSRQIARIVKSAR--IRPANLQVELNVYFQQ--RELVAFCRALDITVCAYAPIGSPGLANVIKaRG 236
Cdd:COG0667 142 VREGKIRYIGVSNYSAEQLRRALAIAEglPPIVAVQNEYSLLDRSaeEELLPAARELGVGVLAYSPLAGGLLTGKYR-RG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 237 AEVPESAK-----FDPLTDPVVLK-------IAEHHKKTPAQVLLRHCMQRD--IVVIPKSTNAGRIKENFQVFDFELSK 302
Cdd:COG0667 221 ATFPEGDRaatnfVQGYLTERNLAlvdalraIAAEHGVTPAQLALAWLLAQPgvTSVIPGARSPEQLEENLAAADLELSA 300
|
....*....
5KET_A 303 AEVDELDSL 311
Cdd:COG0667 301 EDLAALDAA 309
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
21-313 |
5.28e-50 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 167.89 E-value: 5.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 21 KMPVVGLGTWQSPPEEVTAAIDVALEVGYRHIDTAFMYQNEAAIGKTLKkwfDSGkLKREDVFIVTKLpPIGNRAEsvEK 100
Cdd:PRK11172 2 SIPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIA---ESG-VPRDELFITTKI-WIDNLAK--DK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 101 F---LTKSLEALQLDYVDLYLIHlpvgfqykgddnlWPrgeageflidTSTDLISLWKAMEAQVDA---GRTRSVGLSNF 174
Cdd:PRK11172 75 LipsLKESLQKLRTDYVDLTLIH-------------WP----------SPNDEVSVEEFMQALLEAkkqGLTREIGISNF 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 175 N---SRQIARIVKSARIrpANLQVELNVYFQQRELVAFCRALDITVCAYAPIgspglanvikARGaEVpesakfdpLTDP 251
Cdd:PRK11172 132 TialMKQAIAAVGAENI--ATNQIELSPYLQNRKVVAFAKEHGIHVTSYMTL----------AYG-KV--------LKDP 190
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
5KET_A 252 VVLKIAEHHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDELDSLDK 313
Cdd:PRK11172 191 VIARIAAKHNATPAQVILAWAMQLGYSVIPSSTKRENLASNLLAQDLQLDAEDMAAIAALDR 252
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
21-309 |
5.60e-48 |
|
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: 163.17 E-value: 5.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 21 KMPVVGLGTWQ-----------SPPEEVTAAIDVALEVGYRHIDTAFMY---QNEAAIGKTLKkwfdsGKLKREDVFIVT 86
Cdd:cd19093 1 EVSPLGLGTWQwgdrlwwgygeYGDEDLQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFLK-----ELGDRDEVVIAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 87 KLPPIGNRA--ESVEKFLTKSLEALQLDYVDLYLIHLPvGFQYKGDDnlwprgeageflidtstdliSLWKAMEAQVDAG 164
Cdd:cd19093 76 KFAPLPWRLtrRSVVKALKASLERLGLDSIDLYQLHWP-GPWYSQIE--------------------ALMDGLADAVEEG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 165 RTRSVGLSNFNSRQIARIV---KSARIRPANLQVE---LNVYFQQRELVAFCRALDITVCAYAPIGSPGLANVIKARGAe 238
Cdd:cd19093 135 LVRAVGVSNYSADQLRRAHkalKERGVPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAQGLLTGKYSPENP- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 239 vPE-------SAKFDPLTDPVVL---KIAEHHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDEL 308
Cdd:cd19093 214 -PPggrrrlfGRKNLEKVQPLLDaleEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAEL 292
|
.
5KET_A 309 D 309
Cdd:cd19093 293 D 293
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
19-309 |
1.55e-47 |
|
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: 161.20 E-value: 1.55e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 19 GRKMPVVGLGTWQ---------SPPEEVTAAIDVALEVGYRHIDTAFMY---QNEAAIGKTLKKWfdsgklKREDVFIVT 86
Cdd:cd19137 1 GEKIPALGLGTWGiggfltpdySRDEEMVELLKTAIELGYTHIDTAEMYgggHTEELVGKAIKDF------PREDLFIVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 87 KLPPIGNRAESVEKFLTKSLEALQLDYVDLYLIHlpvgfqykgddnlWPRGEageflidtstdlISL---WKAMEAQVDA 163
Cdd:cd19137 75 KVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIH-------------WPNPN------------IPLeetLSAMAEGVRQ 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 164 GRTRSVGLSNFNSRQIARIVKSARIRPANLQVELNVY---FQQRELVAFCRALDITVCAYAPIgspglanvikARGAEvp 240
Cdd:cd19137 130 GLIRYIGVSNFNRRLLEEAISKSQTPIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPL----------RRGLE-- 197
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 241 esakfdpLTDPVVLKIAEHHKKTPAQVLLRHCMQR-DIVVIPKSTNAGRIKENFQVFDFELSKAEVDELD 309
Cdd:cd19137 198 -------KTNRTLEEIAKNYGKTIAQIALAWLIQKpNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
14-309 |
4.49e-46 |
|
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: 157.41 E-value: 4.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 14 VTFHNGRKMPVVGLGTWQ-----SPPEEVTAAIDVALEVGYRHIDTAFMYQN---EAAIGKTLKKwfdsgklKREDVFIV 85
Cdd:cd19138 3 VTLPDGTKVPALGQGTWYmgedpAKRAQEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRG-------RRDKVFLV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 86 TKLPPIGNRAESVEKFLTKSLEALQLDYVDLYLIHlpvgfqykgddnlWpRGeageflidtSTDLISLWKAMEAQVDAGR 165
Cdd:cd19138 76 SKVLPSNASRQGTVRACERSLRRLGTDYLDLYLLH-------------W-RG---------GVPLAETVAAMEELKKEGK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 166 TRSVGLSNFNSRQIARIVKSARIRP--ANlQVELNVyfQQR----ELVAFCRALDITVCAYAPIGSPGLanvikargaev 239
Cdd:cd19138 133 IRAWGVSNFDTDDMEELWAVPGGGNcaAN-QVLYNL--GSRgieyDLLPWCREHGVPVMAYSPLAQGGL----------- 198
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
5KET_A 240 pesAKFDPLTDPVVLKIAEHHKKTPAQVLLRHCMQRDIVV-IPKSTNAGRIKENFQVFDFELSKAEVDELD 309
Cdd:cd19138 199 ---LRRGLLENPTLKEIAARHGATPAQVALAWVLRDGNVIaIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
23-314 |
3.35e-45 |
|
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: 155.82 E-value: 3.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 23 PVVGLGTWQ---------SPPEEVTAAIDVALEVGYRHIDTAFMYQN---EAAIGKTLKKwfdsgklKREDVFIVTKLPP 90
Cdd:cd19085 2 SRLGLGCWQfgggywwgdQDDEESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKG-------RRDDVVIATKVSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 91 IGNRAESVEKFLTKSLEALQLDYVDLYLIHlpvgfqykgddnlWPrgeagefliDTSTDLISLWKAMEAQVDAGRTRSVG 170
Cdd:cd19085 75 DNLTPEDVRKSCERSLKRLGTDYIDLYQIH-------------WP---------SSDVPLEETMEALEKLKEEGKIRAIG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 171 LSNFNSRQIARIVKSARIrpANLQVELNVYFQQ--RELVAFCRALDITVCAYAPIGSpGLANVIKARGAEVPESAK---- 244
Cdd:cd19085 133 VSNFGPAQLEEALDAGRI--DSNQLPYNLLWRAieYEILPFCREHGIGVLAYSPLAQ-GLLTGKFSSAEDFPPGDArtrl 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 245 ---FDPLTDPVVLK-------IAEHHKKTPAQVLLRHCMQRDIV--VIPKSTNAGRIKENFQVFDFELSKAEVDELDSLD 312
Cdd:cd19085 210 frhFEPGAEEETFEaleklkeIADELGVTMAQLALAWVLQQPGVtsVIVGARNPEQLEENAAAVDLELSPSVLERLDEIS 289
|
..
5KET_A 313 KR 314
Cdd:cd19085 290 DP 291
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
23-294 |
1.49e-37 |
|
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: 134.18 E-value: 1.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 23 PVVGLGTWQ----SPPEEVTAAIDVALEVGYRHIDTAFMY---QNEAAIGKTLKkwfdsGKLKREDVFIVTK--LPPIGN 93
Cdd:cd06660 1 SRLGLGTMTfggdGDEEEAFALLDAALEAGGNFFDTADVYgdgRSERLLGRWLK-----GRGNRDDVVIATKggHPPGGD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 94 R------AESVEKFLTKSLEALQLDYVDLYLIHlpvgfqykGDDNLWPRGEageflidtstdlisLWKAMEAQVDAGRTR 167
Cdd:cd06660 76 PsrsrlsPEHIRRDLEESLRRLGTDYIDLYYLH--------RDDPSTPVEE--------------TLEALNELVREGKIR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 168 SVGLSNFNSRQIARIVKSAR----IRPANLQVELNVY---FQQRELVAFCRALDITVCAYAPIgspglanvikARGaevp 240
Cdd:cd06660 134 YIGVSNWSAERLAEALAYAKahglPGFAAVQPQYSLLdrsPMEEELLDWAEENGLPLLAYSPL----------ARG---- 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
5KET_A 241 esakfdpltdpvvlkiaehhkktPAQVLLRHCMQRD--IVVIPKSTNAGRIKENFQ 294
Cdd:cd06660 200 -----------------------PAQLALAWLLSQPfvTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
21-309 |
7.98e-35 |
|
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: 128.80 E-value: 7.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 21 KMPVVGLGTWQ--------SPPEEVTAAIDVALEVGYRHIDTAFMYQN---EAAIGKTLKKwfdsgklKREDVFIVTK-- 87
Cdd:cd19084 3 KVSRIGLGTWAiggtwwgeVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKG-------RRDDVVIATKcg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 88 LPPIG-------NRAESVEKFLTKSLEALQLDYVDLYLIHlpvgfqykgddnlWPrgeagefliDTSTDLISLWKAMEAQ 160
Cdd:cd19084 76 LRWDGgkgvtkdLSPESIRKEVEQSLRRLQTDYIDLYQIH-------------WP---------DPNTPIEETAEALEKL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 161 VDAGRTRSVGLSNFNSRQIARIVKSARIrpANLQVELNVYFQQ--RELVAFCRALDITVCAYAPIGSPGLANVIKARGAE 238
Cdd:cd19084 134 KKEGKIRYIGVSNFSVEQLEEARKYGPI--VSLQPPYSMLEREieEELLPYCRENGIGVLPYGPLAQGLLTGKYKKEPTF 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 239 VPESAK-FDPLTDP-----------VVLKIAEHHKKTPAQVLLRHCMQRDIV--VIPKSTNAGRIKENFQVFDFELSKAE 304
Cdd:cd19084 212 PPDDRRsRFPFFRGenfeknleivdKLKEIAEKYGKSLAQLAIAWTLAQPGVtsAIVGAKNPEQLEENAGALDWELTEEE 291
|
....*
5KET_A 305 VDELD 309
Cdd:cd19084 292 LKEID 296
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
24-311 |
6.57e-33 |
|
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: 123.94 E-value: 6.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 24 VVGLGTWQS---------PPE---EVTAAIDVALEVGYRHIDTAFMY---QNEAAIGKTLKKWfdsgklkREDVFIVTKL 88
Cdd:cd19102 3 TIGLGTWAIggggwgggwGPQddrDSIAAIRAALDLGINWIDTAAVYglgHSEEVVGRALKGL-------RDRPIVATKC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 89 PPIGN---------RAESVEKFLTKSLEALQLDYVDLYLIHlpvgfqykgddnlWPrgeagefliDTSTDLISLWKAMEA 159
Cdd:cd19102 76 GLLWDeegrirrslKPASIRAECEASLRRLGVDVIDLYQIH-------------WP---------DPDEPIEEAWGALAE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 160 QVDAGRTRSVGLSNFNSRQIARIvksARIRP-ANLQVELNVYFQ--QRELVAFCRALDITVCAYAPIGSpGLANvikarG 236
Cdd:cd19102 134 LKEEGKVRAIGVSNFSVDQMKRC---QAIHPiASLQPPYSLLRRgiEAEILPFCAEHGIGVIVYSPMQS-GLLT-----G 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 237 AEVPESAKFDPLTD-----PV--------------VLK-IAEHHKKTPAQVLLRHCMQRDIV--VIPKSTNAGRIKENFQ 294
Cdd:cd19102 205 KMTPERVASLPADDwrrrsPFfqepnlarnlalvdALRpIAERHGRTVAQLAIAWVLRRPEVtsAIVGARRPDQIDETVG 284
|
330
....*....|....*..
5KET_A 295 VFDFELSKAEVDELDSL 311
Cdd:cd19102 285 AADLRLTPEELAEIEAL 301
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
18-308 |
1.69e-32 |
|
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: 122.71 E-value: 1.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 18 NGRKMPVVGLG----TW---QSPPEEVTAAIDVALEVGYRHIDTAFMYQ---NEAAIGKTLKKWfdsgklkREDVFIVTK 87
Cdd:cd19076 8 QGLEVSALGLGcmgmSAfygPADEEESIATLHRALELGVTFLDTADMYGpgtNEELLGKALKDR-------RDEVVIATK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 88 L--------PPIG--NRAESVEKFLTKSLEALQLDYVDLYLIHlpvgfqykgddnlwpRgeageflIDTSTDLISLWKAM 157
Cdd:cd19076 81 FgivrdpgsGFRGvdGRPEYVRAACEASLKRLGTDVIDLYYQH---------------R-------VDPNVPIEETVGAM 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 158 EAQVDAGRTRSVGLSNFNSRQIARivkSARIRP-ANLQVELNVYFQ--QRELVAFCRALDITVCAYAPIGSPGLANVIKA 234
Cdd:cd19076 139 AELVEEGKVRYIGLSEASADTIRR---AHAVHPiTAVQSEYSLWTRdiEDEVLPTCRELGIGFVAYSPLGRGFLTGAIKS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 235 RgAEVPESA--KFDP------------LTDPVVlKIAEHHKKTPAQVLLRHCMQR--DIVVIPKSTNAGRIKENFQVFDF 298
Cdd:cd19076 216 P-EDLPEDDfrRNNPrfqgenfdknlkLVEKLE-AIAAEKGCTPAQLALAWVLAQgdDIVPIPGTKRIKYLEENVGALDV 293
|
330
....*....|
5KET_A 299 ELSKAEVDEL 308
Cdd:cd19076 294 VLTPEELAEI 303
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
18-320 |
6.51e-31 |
|
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: 119.08 E-value: 6.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 18 NGRKMPVVGLGTW--------QSPPEEVTAAIDVALEVGYRHIDTAFMYQ-NEAAIGKtlkkWFDSGKLKREDVFIVTKL 88
Cdd:cd19144 9 NGPSVPALGFGAMglsafygpPKPDEERFAVLDAAFELGCTFWDTADIYGdSEELIGR----WFKQNPGKREKIFLATKF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 89 ----------PPIGNRAESVEKFLTKSLEALQLDYVDLYLIHLpvgfqykgddnlwprgeageflIDTSTDLISLWKAME 158
Cdd:cd19144 85 gieknvetgeYSVDGSPEYVKKACETSLKRLGVDYIDLYYQHR----------------------VDGKTPIEKTVAAMA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 159 AQVDAGRTRSVGLSNFNSRQIARivkSARIRP-ANLQVE-----LNVYFQQRELVAFCRALDITVCAYAPIGSPGLANVI 232
Cdd:cd19144 143 ELVQEGKIKHIGLSECSAETLRR---AHAVHPiAAVQIEyspfsLDIERPEIGVLDTCRELGVAIVAYSPLGRGFLTGAI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 233 KARgAEVPE------SAKFDPLTDPVVL-------KIAEHHKKTPAQVLLRHCMQR--DIVVIPKSTNAGRIKENFQVFD 297
Cdd:cd19144 220 RSP-DDFEEgdfrrmAPRFQAENFPKNLelvdkikAIAKKKNVTAGQLTLAWLLAQgdDIIPIPGTTKLKRLEENLGALK 298
|
330 340
....*....|....*....|....*
5KET_A 298 FELSKAEVDELDSLDKRA--AGRRF 320
Cdd:cd19144 299 VKLTEEEEKEIREIAEEAevVGERY 323
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
17-319 |
1.04e-30 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 119.15 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 17 HNGRKMPVVGLGTW---QSPPEEVTAAIDVALEVGYRHIDTAFMY-QNEAAIGKTLKKWfdsgklkREDVFIVTKLPPIG 92
Cdd:COG1453 8 KTGLEVSVLGFGGMrlpRKDEEEAEALIRRAIDNGINYIDTARGYgDSEEFLGKALKGP-------RDKVILATKLPPWV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 93 NRAESVEKFLTKSLEALQLDYVDLYLIHlpvgfqYKGDDNLWPR-GEAGEFLidtstdlislwKAMEAQVDAGRTRSVGL 171
Cdd:COG1453 81 RDPEDMRKDLEESLKRLQTDYIDLYLIH------GLNTEEDLEKvLKPGGAL-----------EALEKAKAEGKIRHIGF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 172 SNFNSRQIAR-IVKSARIRPANLQveLNVYFQQ----RELVAFCRALDItvcayapigspGLAnVIKA-RG---AEVPES 242
Cdd:COG1453 144 STHGSLEVIKeAIDTGDFDFVQLQ--YNYLDQDnqagEEALEAAAEKGI-----------GVI-IMKPlKGgrlANPPEK 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 243 AKfdpltdpvvlKIAEhHKKTPAQVLLRHCMQRD--IVVIPKSTNAGRIKENFQVFD-FE-LSKAEVDELDSLdKRAAGR 318
Cdd:COG1453 210 LV----------ELLC-PPLSPAEWALRFLLSHPevTTVLSGMSTPEQLDENLKTADnLEpLTEEELAILERL-AEELGE 277
|
.
5KET_A 319 R 319
Cdd:COG1453 278 L 278
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
25-309 |
1.39e-28 |
|
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: 112.31 E-value: 1.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 25 VGLGTWQ---SPPEEVTAAI-DVALEVGYRHIDTAFMY----------QNEAAIGKTLKKwfdsgKLKREDVFIVTKL-- 88
Cdd:cd19081 12 LCLGTMVfgwTADEETSFALlDAFVDAGGNFIDTADVYsawvpgnaggESETIIGRWLKS-----RGKRDRVVIATKVgf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 89 PPIGNR----AESVEKFLTKSLEALQLDYVDLYLIHLPvgfqykgddnlwprgeagefliDTSTDLISLWKAMEAQVDAG 164
Cdd:cd19081 87 PMGPNGpglsRKHIRRAVEASLRRLQTDYIDLYQAHWD----------------------DPATPLEETLGALNDLIRQG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 165 RTRSVGLSNFNSRQIARIVKSAR----IRPANLQVELNVYFQQ---RELVAFCRALDITVCAYAPIGSPGLANVIKaRGA 237
Cdd:cd19081 145 KVRYIGASNYSAWRLQEALELSRqhglPRYVSLQPEYNLVDREsfeGELLPLCREEGIGVIPYSPLAGGFLTGKYR-SEA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 238 EVPESA----KFDPLTDP-------VVLKIAEHHKKTPAQVLLRHCMQRDIV--VIPKSTNAGRIKENFQVFDFELSKAE 304
Cdd:cd19081 224 DLPGSTrrgeAAKRYLNErglrildALDEVAAEHGATPAQVALAWLLARPGVtaPIAGARTVEQLEDLLAAAGLRLTDEE 303
|
....*
5KET_A 305 VDELD 309
Cdd:cd19081 304 VARLD 308
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
22-301 |
2.42e-27 |
|
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: 107.69 E-value: 2.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 22 MPVVGLGTWQSPPEEvTAAIDV---ALEVGYRHIDTAFMY---QNEAAIGKTLKKWfdsgklkREDVFIVTK-------- 87
Cdd:cd19088 9 MRLTGPGIWGPPADR-EEAIAVlrrALELGVNFIDTADSYgpdVNERLIAEALHPY-------PDDVVIATKgglvrtgp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 88 --LPPIGnRAESVEKFLTKSLEALQLDYVDLYLIHLPvgfqykgdDNLWPRGEAGEflidtstdlislwkAMEAQVDAGR 165
Cdd:cd19088 81 gwWGPDG-SPEYLRQAVEASLRRLGLDRIDLYQLHRI--------DPKVPFEEQLG--------------ALAELQDEGL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 166 TRSVGLSNFNSRQIARIVKSARIrpANLQVELNVYFQQRE-LVAFCRALDITVCAYAPIGSPGLAnviKARGAevpesak 244
Cdd:cd19088 138 IRHIGLSNVTVAQIEEARAIVRI--VSVQNRYNLANRDDEgVLDYCEAAGIAFIPWFPLGGGDLA---QPGGL------- 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
5KET_A 245 fdpltdpvVLKIAEHHKKTPAQVLLRHCMQR--DIVVIPKSTNAGRIKENFQVFDFELS 301
Cdd:cd19088 206 --------LAEVAARLGATPAQVALAWLLARspVMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
24-292 |
5.81e-27 |
|
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: 106.41 E-value: 5.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 24 VVGLGTWQ--------SPPEEVTAAIDVALEVGYRHIDTAFMYQN---EAAIGKTLKKwfdsgklKREDVFIVTKLPPIG 92
Cdd:cd19086 5 EIGFGTWGlggdwwgdVDDAEAIRALRAALDLGINFFDTADVYGDghsERLLGKALKG-------RRDKVVIATKFGNRF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 93 NR---------AESVEKFLTKSLEALQLDYVDLYLIHLPvgfqykgDDNLWPRGEageflidtstdlisLWKAMEAQVDA 163
Cdd:cd19086 78 DGgperpqdfsPEYIREAVEASLKRLGTDYIDLYQLHNP-------PDEVLDNDE--------------LFEALEKLKQE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 164 GRTRSVGLSNFNSRQIARIVKSARIrpANLQVELNVYFQQ--RELVAFCRALDITVCAYAPIGSpGLanvikargaevpe 241
Cdd:cd19086 137 GKIRAYGVSVGDPEEALAALRRGGI--DVVQVIYNLLDQRpeEELFPLAEEHGVGVIARVPLAS-GL------------- 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
5KET_A 242 sakfdpLTDpvvlkiaehhkkTPAQVLLRHCMQRDIV--VIPKSTNAGRIKEN 292
Cdd:cd19086 201 ------LTG------------KLAQAALRFILSHPAVstVIPGARSPEQVEEN 235
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
18-309 |
1.45e-25 |
|
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: 103.86 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 18 NGRKMPVVGLG----TW---QSPPEEVTAAIDVALEVGYRHIDTAFMYQNEAAIG--KTLKKWFDSGKLKREDVFIVTK- 87
Cdd:cd19077 1 NGKLVGPIGLGlmglTWrpnPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHAnlKLLARFFRKYPEYADKVVLSVKg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 88 ------LPPIGNRaESVEKFLTKSLEAL-QLDYVDLYlihlpvgfqykgddnlwprgEAGEflIDTSTDLISLWKAMEAQ 160
Cdd:cd19077 81 gldpdtLRPDGSP-EAVRKSIENILRALgGTKKIDIF--------------------EPAR--VDPNVPIEETIKALKEL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 161 VDAGRTRSVGLSNFNSRQIARIVKSARIrpANLQVELNVYFQ---QRELVAFCRALDITVCAYAPIGSPGLANVIKARgA 237
Cdd:cd19077 138 VKEGKIRGIGLSEVSAETIRRAHAVHPI--AAVEVEYSLFSReieENGVLETCAELGIPIIAYSPLGRGLLTGRIKSL-A 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 238 EVPE------SAKFDP--------LTDPVVlKIAEHHKKTPAQVLL---RHCMQRDIVVIPKSTNAGRIKENFQVFDFEL 300
Cdd:cd19077 215 DIPEgdfrrhLDRFNGenfeknlkLVDALQ-ELAEKKGCTPAQLALawiLAQSGPKIIPIPGSTTLERVEENLKAANVEL 293
|
....*....
5KET_A 301 SKAEVDELD 309
Cdd:cd19077 294 TDEELKEIN 302
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
17-311 |
2.24e-25 |
|
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: 103.85 E-value: 2.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 17 HNGRKMPVVGLGT-------------WQSPPEEVTAAIDVALEVGYRHIDTAFMY---QNEAAIGKTLKKwfdsgklKRE 80
Cdd:cd19091 8 RSGLKVSELALGTmtfgggggffgawGGVDQEEADRLVDIALDAGINFFDTADVYsegESEEILGKALKG-------RRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 81 DVFIVTKLP-PIGN--------RA---ESVEKfltkSLEALQLDYVDLYLIHlpvGFqykgddnlwprgeagefliDTST 148
Cdd:cd19091 81 DVLIATKVRgRMGEgpndvglsRHhiiRAVEA----SLKRLGTDYIDLYQLH---GF-------------------DALT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 149 DLISLWKAMEAQVDAGRTRSVGLSNFNSRQIARIVKSARIRpaNLQ--VELNVYFQ------QRELVAFCRALDITVCAY 220
Cdd:cd19091 135 PLEETLRALDDLVRQGKVRYIGVSNFSAWQIMKALGISERR--GLArfVALQAYYSllgrdlEHELMPLALDQGVGLLVW 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 221 APIGSPGLANVIKaRGAEVPESAK-------FDPLTDP-------VVLKIAEHHKKTPAQVLLRHCMQRDIV--VIPKST 284
Cdd:cd19091 213 SPLAGGLLSGKYR-RGQPAPEGSRlrrtgfdFPPVDRErgydvvdALREIAKETGATPAQVALAWLLSRPTVssVIIGAR 291
|
330 340
....*....|....*....|....*..
5KET_A 285 NAGRIKENFQVFDFELSKAEVDELDSL 311
Cdd:cd19091 292 NEEQLEDNLGAAGLSLTPEEIARLDKV 318
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
17-304 |
3.26e-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: 102.63 E-value: 3.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 17 HNGRKMPVVGLGTW-----QSPPEEVTAAIDVALEVGYRHIDTA---FMYQNEAAIGKTLKKWfdsgKLKREDVFIVTKL 88
Cdd:cd19092 1 PEGLEVSRLVLGCMrladwGESAEELLSLIEAALELGITTFDHAdiyGGGKCEELFGEALALN----PGLREKIEIQTKC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 89 ------PPIGNRAE-----------SVEKfltkSLEALQLDYVDLYLIHLPvgfqykgdDNLWPRGEAGEflidtstdli 151
Cdd:cd19092 77 girlgdDPRPGRIKhydtskehilaSVEG----SLKRLGTDYLDLLLLHRP--------DPLMDPEEVAE---------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 152 slwkAMEAQVDAGRTRSVGLSNFNSRQIaRIVKSARIRP--ANlQVELNVYFQQ---RELVAFCRALDITVCAYAPIGSP 226
Cdd:cd19092 135 ----AFDELVKSGKVRYFGVSNFTPSQI-ELLQSYLDQPlvTN-QIELSLLHTEaidDGTLDYCQLLDITPMAWSPLGGG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 227 GLANVIKARGAEVPEsakfdpltdpVVLKIAEHHKKTPAQV----LLRHCMQrdIVVIPKSTNAGRIKENFQVFDFELSK 302
Cdd:cd19092 209 RLFGGFDERFQRLRA----------ALEELAEEYGVTIEAIalawLLRHPAR--IQPILGTTNPERIRSAVKALDIELTR 276
|
..
5KET_A 303 AE 304
Cdd:cd19092 277 EE 278
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-295 |
4.23e-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: 381331 [Multi-domain] Cd Length: 250 Bit Score: 101.51 E-value: 4.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 19 GRKMPVVGLGTWQSPPEEVtAAIDVALEVGYRHIDTAFMYQN---EAAIGKTLKKwfdsgkLKREDVFIVTK--LPPIGN 93
Cdd:cd19105 10 GLKVSRLGFGGGGLPRESP-ELLRRALDLGINYFDTAEGYGNgnsEEIIGEALKG------LRRDKVFLATKasPRLDKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 94 RAESVEKFLTKSLEALQLDYVDLYLIHlpvgfqykGDDNLWPRGEAGEFLidtstdlislwKAMEAQVDAGRTRSVGLS- 172
Cdd:cd19105 83 DKAELLKSVEESLKRLQTDYIDIYQLH--------GVDTPEERLLNEELL-----------EALEKLKKEGKVRFIGFSt 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 173 -NFNSRQIARIVKSARIRPAnlQVELNVYFQQREL---VAFCRALDITVCAYAPIGSpglanvikarGAEVPESAKFDPL 248
Cdd:cd19105 144 hDNMAEVLQAAIESGWFDVI--MVAYNFLNQPAELeeaLAAAAEKGIGVVAMKTLAG----------GYLQPALLSVLKA 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
5KET_A 249 TDPvvlkiaehhkkTPAQVLLRHCMQRDIV--VIPKSTNAGRIKENFQV 295
Cdd:cd19105 212 KGF-----------SLPQAALKWVLSNPRVdtVVPGMRNFAELEENLAA 249
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
27-309 |
3.48e-24 |
|
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: 100.37 E-value: 3.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 27 LGT--------WQSPPEEVTAAIDVALEVGYRHIDTAFMYQN---EAAIGKTLKKwfdsgklKREDVFIVTKL----PPI 91
Cdd:cd19080 15 LGTmtfgtewgWGADREEARAMFDAYVEAGGNFIDTANNYTNgtsERLLGEFIAG-------NRDRIVLATKYtmnrRPG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 92 -----GNRAESVEKFLTKSLEALQLDYVDLYLIHlpvgfqykgddnLWprgeagefliDTSTDLISLWKAMEAQVDAGRT 166
Cdd:cd19080 88 dpnagGNHRKNLRRSVEASLRRLQTDYIDLLYVH------------AW----------DFTTPVEEVMRALDDLVRAGKV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 167 RSVGLSNFNSRQIARIVKSARIR----PANLQVELNVYFQ--QRELVAFCRALDITVCAYAPIGS--------PGLANVI 232
Cdd:cd19080 146 LYVGISDTPAWVVARANTLAELRgwspFVALQIEYSLLERtpERELLPMARALGLGVTPWSPLGGglltgkyqRGEEGRA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 233 KARGAEVPESAKFDPLTDP---VVLKIAEHHKKTPAQVLLRHCMQRDIVVIP--KSTNAGRIKENFQVFDFELSKAEVDE 307
Cdd:cd19080 226 GEAKGVTVGFGKLTERNWAivdVVAAVAEELGRSAAQVALAWVRQKPGVVIPiiGARTLEQLKDNLGALDLTLSPEQLAR 305
|
..
5KET_A 308 LD 309
Cdd:cd19080 306 LD 307
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
17-309 |
2.24e-23 |
|
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: 98.04 E-value: 2.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 17 HNGRKMPVVGLGT----------WQSPPEEVTAAIDVALEVGYRHIDTAFMYQN---EAAIGKTLKKWfdsgkLKREDVF 83
Cdd:cd19079 7 NSGLKVSRLCLGCmsfgdpkwrpWVLDEEESRPIIKRALDLGINFFDTANVYSGgasEEILGRALKEF-----APRDEVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 84 IVTKL-PPIGNRA-------ESVEKFLTKSLEALQLDYVDLYLIHlpvgfqykgddnlwprgeagefLIDTSTDLISLWK 155
Cdd:cd19079 82 IATKVyFPMGDGPngrglsrKHIMAEVDASLKRLGTDYIDLYQIH----------------------RWDYETPIEETLE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 156 AMEAQVDAGRTRSVGLSNFNSRQIARIVKSARI----RPANLQVELNVYFQ--QRELVAFCRALDITVCAYAPIGSPGLA 229
Cdd:cd19079 140 ALHDVVKSGKVRYIGASSMYAWQFAKALHLAEKngwtKFVSMQNHYNLLYReeEREMIPLCEEEGIGVIPWSPLARGRLA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 230 -----NVIKARGAEVPESAKFDPLTD---PV---VLKIAEHHKKTPAQVLLRHCMQRDIVVIP--KSTNAGRIKENFQVF 296
Cdd:cd19079 220 rpwgdTTERRRSTTDTAKLKYDYFTEadkEIvdrVEEVAKERGVSMAQVALAWLLSKPGVTAPivGATKLEHLEDAVAAL 299
|
330
....*....|...
5KET_A 297 DFELSKAEVDELD 309
Cdd:cd19079 300 DIKLSEEEIKYLE 312
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
24-311 |
4.23e-23 |
|
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: 97.24 E-value: 4.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 24 VVGLGTW-----QSPPEEVTAAIDVALEVGYRHIDTAFMYQN---EAAIGKTlkkwfdsgKLKREDVFIVTKLPPI---G 92
Cdd:cd19075 4 ILGTMTFgsqgrFTTAEAAAELLDAFLERGHTEIDTARVYPDgtsEELLGEL--------GLGERGFKIDTKANPGvggG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 93 NRAESVEKFLTKSLEALQLDYVDLYLIHLPvgfqykgddnlwprgeagefliDTSTDLISLWKAMEAQVDAGRTRSVGLS 172
Cdd:cd19075 76 LSPENVRKQLETSLKRLKVDKVDVFYLHAP----------------------DRSTPLEETLAAIDELYKEGKFKEFGLS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 173 NFNSRQIARIVKSAR----IRPA------NL---QVElnvyfqqRELVAFCRALDITVCAYAPIGSPGLANVIKaRGAEV 239
Cdd:cd19075 134 NYSAWEVAEIVEICKengwVLPTvyqgmyNAitrQVE-------TELFPCLRKLGIRFYAYSPLAGGFLTGKYK-YSEDK 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 240 PESAKFDPLTDP------------------VVLKIAEHHKKTPAQVLLR----HCM----QRDIVVIPKStNAGRIKENf 293
Cdd:cd19075 206 AGGGRFDPNNALgklyrdrywkpsyfealeKVEEAAEKEGISLAEAALRwlyhHSAldgeKGDGVILGAS-SLEQLEEN- 283
|
330 340
....*....|....*....|.
5KET_A 294 qVFDFE---LSKAEVDELDSL 311
Cdd:cd19075 284 -LAALEkgpLPEEVVKAIDEA 303
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
23-272 |
7.49e-23 |
|
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: 95.71 E-value: 7.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 23 PVVGLGT--------WQSPPEEVTAAIDVALEVGYRHIDTAFMY---QNEAAIGKTLKKWfdsgklKREDVFIVTKLPP- 90
Cdd:cd19096 1 SVLGFGTmrlpesddDSIDEEKAIEMIRYAIDAGINYFDTAYGYgggKSEEILGEALKEG------PREKFYLATKLPPw 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 91 IGNRAESVEKFLTKSLEALQLDYVDLYLIHlpvGFqykGDDNLWPRGEAGEflidtstdlisLWKAMEAQVDAGRTRSVG 170
Cdd:cd19096 75 SVKSAEDFRRILEESLKRLGVDYIDFYLLH---GL---NSPEWLEKARKGG-----------LLEFLEKAKKEGLIRHIG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 171 LSnF--NSRQIARIVKSARIRPANLQveLNV----YFQQRELVAFCRALDITVCAYAPIGSPGLANVIKARGAEVPESak 244
Cdd:cd19096 138 FS-FhdSPELLKEILDSYDFDFVQLQ--YNYldqeNQAGRPGIEYAAKKGMGVIIMEPLKGGGLANNPPEALAILCGA-- 212
|
250 260
....*....|....*....|....*...
5KET_A 245 fdpltdpvvlkiaehhKKTPAQVLLRHC 272
Cdd:cd19096 213 ----------------PLSPAEWALRFL 224
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-219 |
8.81e-23 |
|
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: 94.86 E-value: 8.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 19 GRKMPVVGLGT---WQSPPEEVTAAIDVALEVGYRHIDTAFMYQN-EAAIGKTLKKwfdsgklKREDVFIVTKlppIGNR 94
Cdd:cd19100 8 GLKVSRLGFGGgplGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKG-------RRDKVFLATK---TGAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 95 -AESVEKFLTKSLEALQLDYVDLYLIHLpVGFQYKGDDNLWPRGeageflidtstdlisLWKAMEAQVDAGRTRSVGLSN 173
Cdd:cd19100 78 dYEGAKRDLERSLKRLGTDYIDLYQLHA-VDTEEDLDQVFGPGG---------------ALEALLEAKEEGKIRFIGISG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
5KET_A 174 FNSRQIARIVKSARIrpANLQVELNVYFQQ-----RELVAFCRALDITVCA 219
Cdd:cd19100 142 HSPEVLLRALETGEF--DVVLFPINPAGDHidsfrEELLPLAREKGVGVIA 190
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
25-308 |
1.25e-22 |
|
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: 96.48 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 25 VGLGT--W--QSPPEEVTAAIDVALEVGYRHIDTAFMY----------QNEAAIGKTLKKwfdsgKLKREDVFIVTKL-- 88
Cdd:cd19094 4 ICLGTmtWgeQNTEAEAHEQLDYAFDEGVNFIDTAEMYpvppspetqgRTEEIIGSWLKK-----KGNRDKVVLATKVag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 89 -----------PPIGNRA---ESVEKfltkSLEALQLDYVDLYLIHLP---VGFQYKGDDNLWPRGEageflidTSTDLI 151
Cdd:cd19094 79 pgegitwprggGTRLDREnirEAVEG----SLKRLGTDYIDLYQLHWPdryTPLFGGGYYTEPSEEE-------DSVSFE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 152 SLWKAMEAQVDAGRTRSVGLSNFNSRQIARIVKSARI----RPANLQVELNVYFQQRE--LVAFCRALDITVCAYAPIGs 225
Cdd:cd19094 148 EQLEALGELVKAGKIRHIGLSNETPWGVMKFLELAEQlglpRIVSIQNPYSLLNRNFEegLAEACHRENVGLLAYSPLA- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 226 pglANVIKAR---GAEVPESAKFD-----------PLTDPVVL---KIAEHHKKTPAQVLLRHCMQRDIV--VIPKSTNA 286
Cdd:cd19094 227 ---GGVLTGKyldGAARPEGGRLNlfpgymaryrsPQALEAVAeyvKLARKHGLSPAQLALAWVRSRPFVtsTIIGATTL 303
|
330 340
....*....|....*....|....*
5KET_A 287 GRIKENFQVFDFELSK---AEVDEL 308
Cdd:cd19094 304 EQLKENIDAFDVPLSDellAEIDAV 328
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-272 |
5.45e-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: 381330 [Multi-domain] Cd Length: 321 Bit Score: 94.64 E-value: 5.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 10 QLSSVTFHNGRKMPVVGLGTwqspPEEVTAAIDVALEVGYRHIDTAFMY---QNEAAIGKTLKKwfdsgklKREDVFIVT 86
Cdd:cd19104 11 KVSELTFGGGGIGGLMGRTT----REEQIAAVRRALDLGINFFDTAPSYgdgKSEENLGRALKG-------LPAGPYITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 87 K----LPPIGNRAESVEKFLTKSLEALQLDYVDLYLIHLPVgfqykGDDNLWPRGEAGEflIDTSTDLISLWKAMEAQVD 162
Cdd:cd19104 80 KvrldPDDLGDIGGQIERSVEKSLKRLKRDSVDLLQLHNRI-----GDERDKPVGGTLS--TTDVLGLGGVADAFERLRS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 163 AGRTRSVGLSNF-NSRQIARIVKSAriRPANLQVELN--------------VYFQQRELVAFCRALDITVCAYAPIGSPG 227
Cdd:cd19104 153 EGKIRFIGITGLgNPPAIRELLDSG--KFDAVQVYYNllnpsaaearprgwSAQDYGGIIDAAAEHGVGVMGIRVLAAGA 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
5KET_A 228 LANVIKARGAEVPES-----------AKFDPLtdpvvlkIAEHHkKTPAQVLLRHC 272
Cdd:cd19104 231 LTTSLDRGREAPPTSdsdvaidfrraAAFRAL-------AREWG-ETLAQLAHRFA 278
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
19-301 |
6.21e-22 |
|
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: 93.81 E-value: 6.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 19 GRKMPVVGLGTW-----QSPPEEVTAAIDVALEVGYRHIDTAFMY---QNEAAIGKTLKKWfdsgklKREDVFIVTKL-- 88
Cdd:cd19074 1 GLKVSELSLGTWltfggQVDDEDAKACVRKAYDLGINFFDTADVYaagQAEEVLGKALKGW------PRESYVISTKVfw 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 89 ---PPIGNRA-------ESVEKfltkSLEALQLDYVDLYLIHLPvgfqykgddnlwprgeagefliDTSTDLISLWKAME 158
Cdd:cd19074 75 ptgPGPNDRGlsrkhifESIHA----SLKRLQLDYVDIYYCHRY----------------------DPETPLEETVRAMD 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 159 AQVDAGRTRSVGLSNFNSRQIARIVKSAR----IRPANLQVELNVYFQQR--ELVAFCRALDITVCAYAPIgSPGLANVI 232
Cdd:cd19074 129 DLIRQGKILYWGTSEWSAEQIAEAHDLARqfglIPPVVEQPQYNMLWREIeeEVIPLCEKNGIGLVVWSPL-AQGLLTGK 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 233 KARGAEVPESAKFDP----------LTDPVV------LKIAEHHKKTPAQVLLRHCMQRDIV--VIPKSTNAGRIKENFQ 294
Cdd:cd19074 208 YRDGIPPPSRSRATDednrdkkrrlLTDENLekvkklKPIADELGLTLAQLALAWCLRNPAVssAIIGASRPEQLEENVK 287
|
....*..
5KET_A 295 VFDFELS 301
Cdd:cd19074 288 ASGVKLS 294
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
25-271 |
1.22e-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: 381325 [Multi-domain] Cd Length: 316 Bit Score: 93.54 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 25 VGLGTWQSPP-----EEVTAAIDVALEVGYRHIDTAFMYQN---EAAIGKTLKKWFDSGKLKREDVFIVTK--------- 87
Cdd:cd19099 6 LGLGTYRGDSddetdEEYREALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGIKRDEVVIVTKagyipgdgd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 88 --LPPIGNRAESVEKF----------------------LTKSLEALQLDYVDLYLIHLP-VGFQYKGDDNLWPRGEAgef 142
Cdd:cd19099 86 epLRPLKYLEEKLGRGlidvadsaglrhcispayledqIERSLKRLGLDTIDLYLLHNPeEQLLELGEEEFYDRLEE--- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 143 lidtstdlisLWKAMEAQVDAGRTRSVGLSNFNS----------------RQIARIVKSARIRPANLQVELNVYFQQ--- 203
Cdd:cd19099 163 ----------AFEALEEAVAEGKIRYYGISTWDGfrappalpghlsleklVAAAEEVGGDNHHFKVIQLPLNLLEPEalt 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
5KET_A 204 ---------RELVAFCRALDITVCAYAPIGSPGLANVIkargaevpesakfdpltdPVVLKIAEHHKKTPAQVLLRH 271
Cdd:cd19099 233 ekntvkgeaLSLLEAAKELGLGVIASRPLNQGQLLGEL------------------RLADLLALPGGATLAQRALQF 291
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
17-310 |
1.69e-21 |
|
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: 93.11 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 17 HNGRKMPVVGLGTW---------QSPPEEVTAAIDVALEVGYRHIDTAFMYQN---EAAIGKTLKKwfdsgklKREDVFI 84
Cdd:cd19149 6 KSGIEASVIGLGTWaigggpwwgGSDDNESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKG-------RRDKVVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 85 VTK-----------LPPIGN--------RAESVEKFLTKSLEALQLDYVDLYLIHlpvgfqykgddnlWPrgeagefliD 145
Cdd:cd19149 79 ATKcglrwdreggsFFFVRDgvtvyknlSPESIREEVEQSLKRLGTDYIDLYQTH-------------WQ---------D 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 146 TSTDLISLWKAMEAQVDAGRTRSVGLSNFNSRQIARIVKSARIrpANLQVELNVY--FQQRELVAFCRALDITVCAYAPI 223
Cdd:cd19149 137 VETPIEETMEALEELKRQGKIRAIGASNVSVEQIKEYVKAGQL--DIIQEKYSMLdrGIEKELLPYCKKNNIAFQAYSPL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 224 GSpGL--ANVIKARGAEVPESAKFDPLTDP------VVLK-----IAEHHKKTPAQVLLRHCM-QRDIV-VIPKSTNAGR 288
Cdd:cd19149 215 EQ-GLltGKITPDREFDAGDARSGIPWFSPenrekvLALLekwkpLCEKYGCTLAQLVIAWTLaQPGITsALCGARKPEQ 293
|
330 340
....*....|....*....|..
5KET_A 289 IKENFQVFDFELSKAEVDELDS 310
Cdd:cd19149 294 AEENAKAGDIRLSAEDIATMRS 315
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
21-311 |
2.30e-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: 92.40 E-value: 2.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 21 KMPVVGLGTWQ--SP-------------PEEVTAAIDVALEVGYRHIDTAFMY---QNEAAIGKTLKKWfdsgklKREDV 82
Cdd:cd19103 3 KLPKIALGTWSwgSGgaggdqvfgnhldEDTLKAVFDKAMAAGLNLWDTAAVYgmgASEKILGEFLKRY------PREDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 83 FIVTKLPPI--GNRAESVEKFLTKSLEALQLDYVDLYLIHLPVgfqykgDDNLWprgeageflidtSTDLISLWKameaq 160
Cdd:cd19103 77 IISTKFTPQiaGQSADPVADMLEGSLARLGTDYIDIYWIHNPA------DVERW------------TPELIPLLK----- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 161 vdAGRTRSVGLSNFNSRQIAR---IVKSARIRPANLQVELNVYFQQRE---LVAFCRALDITVCAYA------------- 221
Cdd:cd19103 134 --SGKVKHVGVSNHNLAEIKRaneILAKAGVSLSAVQNHYSLLYRSSEeagILDYCKENGITFFAYMvleqgalsgkydt 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 222 ----PIGSpglanvikARGAEV-PESAKFDPLTDpVVLKIAEHHKKTPAQVLLRHCMQRDIVVIPKSTNAGRIKENFQVF 296
Cdd:cd19103 212 khplPEGS--------GRAETYnPLLPQLEELTA-VMAEIGAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAA 282
|
330
....*....|....*
5KET_A 297 DFELSKAEVDELDSL 311
Cdd:cd19103 283 SITLTDDEIKELEQL 297
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
25-223 |
6.11e-21 |
|
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: 91.21 E-value: 6.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 25 VGLGTWQ--------SPPEEVTAAIDVALEVGYRHIDTAFMY---QNEAAIGKTLKkwfdsGKLKREDVFIVTKL----- 88
Cdd:cd19148 7 IALGTWAiggwmwggTDEKEAIETIHKALDLGINLIDTAPVYgfgLSEEIVGKALK-----EYGKRDRVVIATKVglewd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 89 ---PPIGN-RAESVEKFLTKSLEALQLDYVDLYLIHlpvgfqykgddnlWPrgeagefliDTSTDLISLWKAMEAQVDAG 164
Cdd:cd19148 82 eggEVVRNsSPARIRKEVEDSLRRLQTDYIDLYQVH-------------WP---------DPLVPIEETAEALKELLDEG 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
5KET_A 165 RTRSVGLSNFNSRQIARIVKSARIrpANLQVELNVYFQQ--RELVAFCRALDITVCAYAPI 223
Cdd:cd19148 140 KIRAIGVSNFSPEQMETFRKVAPL--HTVQPPYNLFEREieKDVLPYARKHNIVTLAYGAL 198
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
44-311 |
8.66e-20 |
|
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: 88.24 E-value: 8.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 44 ALEVGYRHIDTAFMY---QNEAAIGKTLKKWfdsgklKREDVFIVTKLP--------PIGNRAESVEKFLTKSLEALQLD 112
Cdd:cd19083 42 ALDNGVNLLDTAFIYglgRSEELVGEVLKEY------NRNEVVIATKGAhkfggdgsVLNNSPEFLRSAVEKSLKRLNTD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 113 YVDLYLIHLPvgfqykgDDNLwPRGEAgeflidtstdlislWKAMEAQVDAGRTRSVGLSNFNSRQIARIVKSARIRPan 192
Cdd:cd19083 116 YIDLYYIHFP-------DGET-PKAEA--------------VGALQELKDEGKIRAIGVSNFSLEQLKEANKDGYVDV-- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 193 LQVELNVYfqQRE----LVAFCRALDITVCAYAPIGSPGLA-----------NVIKARGAEVPESA------KFDPLTDp 251
Cdd:cd19083 172 LQGEYNLL--QREaeedILPYCVENNISFIPYFPLASGLLAgkytkdtkfpdNDLRNDKPLFKGERfsenldKVDKLKS- 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
5KET_A 252 vvlkIAEHHKKTPAQVLLRHCMQRDIV--VIPKSTNAGRIKENFQVFDFELSKAEVDELDSL 311
Cdd:cd19083 249 ----IADEKGVTVAHLALAWYLTRPAIdvVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
23-292 |
5.83e-19 |
|
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: 84.59 E-value: 5.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 23 PVVGLGTWQ------SPPEEVTAA-IDVALEVGYRHIDTAFMYQN-EAAIGKTLKKwfdsgkLKREDVFIVTKLPPIGNR 94
Cdd:cd19095 1 SVLGLGTSGigrvwgVPSEAEAARlLNTALDLGINLIDTAPAYGRsEERLGRALAG------LRRDDLFIATKVGTHGEG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 95 AESVEKF--------LTKSLEALQLDYVDLYLIHLPVGFQYKGDdnlwprgeagefLIDTstdlislwkaMEAQVDAGRT 166
Cdd:cd19095 75 GRDRKDFspaairasIERSLRRLGTDYIDLLQLHGPSDDELTGE------------VLET----------LEDLKAAGKV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 167 RSVGLSNFNSRqIARIVKSARIrpANLQVELNVYFQ-QRELVAFCRALDITVCAYAPIGSPGLANVIKARGAEVPESAKF 245
Cdd:cd19095 133 RYIGVSGDGEE-LEAAIASGVF--DVVQLPYNVLDReEEELLPLAAEAGLGVIVNRPLANGRLRRRVRRRPLYADYARRP 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
5KET_A 246 DPLtdpvvlkiAEHHKKTPAQVLLRHCMQRDIV--VIPKSTNAGRIKEN 292
Cdd:cd19095 210 EFA--------AEIGGATWAQAALRFVLSHPGVssAIVGTTNPEHLEEN 250
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
27-311 |
1.55e-18 |
|
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: 84.55 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 27 LGTW----QSPPEEVTAAIDVALEVGYRHIDTAFMYQN---EAAIGKTLKKwfdsgklKREDVFIVTKL-PPIGNRAE-- 96
Cdd:cd19087 18 LGTMnfggRTDEETSFAIMDRALDAGINFFDTADVYGGgrsEEIIGRWIAG-------RRDDIVLATKVfGPMGDDPNdr 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 97 ---------SVEKfltkSLEALQLDYVDLYLIHLpvgfqykgddnlwprgeageflIDTSTDLISLWKAMEAQVDAGRTR 167
Cdd:cd19087 91 glsrrhirrAVEA----SLRRLQTDYIDLYQMHH----------------------FDRDTPLEETLRALDDLVRQGKIR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 168 SVGLSNFNSRQIARIVKSARIR----------PANL---QVELnvyfqqrELVAFCRALDITVCAYAPIG---------- 224
Cdd:cd19087 145 YIGVSNFAAWQIAKAQGIAARRgllrfvseqpMYNLlkrQAEL-------EILPAARAYGLGVIPYSPLAgglltgkygk 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 225 ---SPGLANVIKARGAEVPESAKFDPLTDPVVlKIAEHHKKTPAQVLLRHCMQRDIV--VIPKSTNAGRIKENFQVFDFE 299
Cdd:cd19087 218 gkrPESGRLVERARYQARYGLEEYRDIAERFE-ALAAEAGLTPASLALAWVLSHPAVtsPIIGPRTLEQLEDSLAALEIT 296
|
330
....*....|..
5KET_A 300 LSKAEVDELDSL 311
Cdd:cd19087 297 LTPELLAEIDEL 308
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
19-310 |
4.08e-18 |
|
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: 83.44 E-value: 4.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 19 GRKMPVVGLG------TWQSPP--EEVTAAIDVALEVGYRHIDTAFMY---QNEAAIGKTLKKwfdsgklKREDVFIVTK 87
Cdd:cd19078 1 GLEVSAIGLGcmgmshGYGPPPdkEEMIELIRKAVELGITFFDTAEVYgpyTNEELVGEALKP-------FRDQVVIATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 88 L----------PPIGN-RAESVEKFLTKSLEALQLDYVDLYLIHlpvgfqykgddnlwpRgeageflIDTSTDLISLWKA 156
Cdd:cd19078 74 FgfkidggkpgPLGLDsRPEHIRKAVEGSLKRLQTDYIDLYYQH---------------R-------VDPNVPIEEVAGT 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 157 MEAQVDAGRTRSVGLSNFNSRQIARIVKsarIRP-ANLQVELNVYFQ--QRELVAFCRALDITVCAYAPIGSPGLANVIK 233
Cdd:cd19078 132 MKELIKEGKIRHWGLSEAGVETIRRAHA---VCPvTAVQSEYSMMWRepEKEVLPTLEELGIGFVPFSPLGKGFLTGKID 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 234 ARgaevpesAKFD--------------------PLTDpVVLKIAEHHKKTPAQVLLRHCMQRD--IVVIPKSTNAGRIKE 291
Cdd:cd19078 209 EN-------TKFDegddraslprftpealeanqALVD-LLKEFAEEKGATPAQIALAWLLAKKpwIVPIPGTTKLSRLEE 280
|
330
....*....|....*....
5KET_A 292 NFQVFDFELSKAEVDELDS 310
Cdd:cd19078 281 NIGAADIELTPEELREIED 299
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
23-303 |
4.35e-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: 4.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 23 PVVGLGT------WQS-PPEEVTAAIDVALEVGYRHIDTAFMYQN-EAAIGKTLKKWfdsgklKREDVFIVTKlppIGNR 94
Cdd:cd19090 1 SALGLGTaglggvFGGvDDDEAVATIRAALDLGINYIDTAPAYGDsEERLGLALAEL------PREPLVLSTK---VGRL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 95 --------AESVEKFLTKSLEALQLDYVDLYLIHLPvgfqykGDDNLWP---RGEAGEFLidtstdlislwkamEAQVDA 163
Cdd:cd19090 72 pedtadysADRVRRSVEESLERLGRDRIDLLMIHDP------ERVPWVDilaPGGALEAL--------------LELKEE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 164 GRTRSVGLSNFNSRQIARIVKSAR---IRPANlqvELNVYFQQ--RELVAFCRALDITVCAYAPIGSPGLANVIKARGAE 238
Cdd:cd19090 132 GLIKHIGLGGGPPDLLRRAIETGDfdvVLTAN---RYTLLDQSaaDELLPAAARHGVGVINASPLGMGLLAGRPPERVRY 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
5KET_A 239 VPESAkFDPLTDPV--VLKIAEHHKKTPAQVLLRHCMQ--RDIVVIPKSTNAGRIKENFQVFDFELSKA 303
Cdd:cd19090 209 TYRWL-SPELLDRAkrLYELCDEHGVPLPALALRFLLRdpRISTVLVGASSPEELEQNVAAAEGPLPEE 276
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
26-308 |
4.07e-17 |
|
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: 80.55 E-value: 4.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 26 GLGTWQSPPEEVTAAIDV---ALEVGYRHIDTAFMY---QNEAAIGKTLKKwfdsgkLKREDVFIVTKL---------PP 90
Cdd:cd19145 21 GLSGDYGAPKPEEEGIALihhAFNSGVTFLDTSDIYgpnTNEVLLGKALKD------GPREKVQLATKFgiheiggsgVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 91 IGNRAESVEKFLTKSLEALQLDYVDLYLIHlpvgfqykgddnlwprgeagefLIDTSTDLISLWKAMEAQVDAGRTRSVG 170
Cdd:cd19145 95 VRGDPAYVRAACEASLKRLDVDYIDLYYQH----------------------RIDTTVPIEITMGELKKLVEEGKIKYIG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 171 LSNFNSRQIARivkSARIRPAN-LQVELNVYFQ--QRELVAFCRALDITVCAYAPIGSPGLANviKARGAEVPESAKFdP 247
Cdd:cd19145 153 LSEASADTIRR---AHAVHPITaVQLEWSLWTRdiEEEIIPTCRELGIGIVPYSPLGRGFFAG--KAKLEELLENSDV-R 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
5KET_A 248 LTDP---------------VVLKIAEHHKKTPAQVLLR--HCMQRDIVVIPKSTNAGRIKENFQVFDFELSKAEVDEL 308
Cdd:cd19145 227 KSHPrfqgenleknkvlyeRVEALAKKKGCTPAQLALAwvLHQGEDVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
23-297 |
4.55e-17 |
|
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: 80.29 E-value: 4.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 23 PVVGLGT----WQSPPEEVTAAIDVALEVGYRHIDTAFMYQNEAAIG---KTLKKWFDSGKlKREDVFIVTKL--PPIGN 93
Cdd:cd19082 1 SRIVLGTadfgTRIDEEEAFALLDAFVELGGNFIDTARVYGDWVERGaseRVIGEWLKSRG-NRDKVVIATKGghPDLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 94 R------AESVEKFLTKSLEALQLDYVDLYLIHLpvgfqykgDDnlwPRGEAGEFLidtstdlislwKAMEAQVDAGRTR 167
Cdd:cd19082 80 MsrsrlsPEDIRADLEESLERLGTDYIDLYFLHR--------DD---PSVPVGEIV-----------DTLNELVRAGKIR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 168 SVGLSNFNSRQIARIVKSARIR----PANLQVELN-------------VYFQQRELVAFCRALDITVCAYAPIGSpGLAN 230
Cdd:cd19082 138 AFGASNWSTERIAEANAYAKAHglpgFAASSPQWSlarpneppwpgptLVAMDEEMRAWHEENQLPVFAYSSQAR-GFFS 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
5KET_A 231 VIKARGAEVPESAKFDPLTDP------VVLKIAEHHKKTPAQVLLRHCMQRDIVVIP--KSTNAGRIKENFQVFD 297
Cdd:cd19082 217 KRAAGGAEDDSELRRVYYSEEnferleRAKELAEEKGVSPTQIALAYVLNQPFPTVPiiGPRTPEQLRDSLAAAD 291
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
22-310 |
7.42e-16 |
|
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: 76.86 E-value: 7.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 22 MPVVGLGTWQ--------SPPEEVTAAIDVALEVGYRHIDTAFMYQN-EAAIGKTLKKWFDSGKLkREDVFIVTKLPPIG 92
Cdd:cd19101 2 ISRVINGMWQlsgghggiRDEDAAVRAMAAYVDAGLTTFDCADIYGPaEELIGEFRKRLRRERDA-ADDVQIHTKWVPDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 93 NRA----ESVEKFLTKSLEALQLDYVDLylihlpVGFQYkgddnlWPRGEAGefLIDTSTDLISLwkameaqVDAGRTRS 168
Cdd:cd19101 81 GELtmtrAYVEAAIDRSLKRLGVDRLDL------VQFHW------WDYSDPG--YLDAAKHLAEL-------QEEGKIRH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 169 VGLSNFNSRQIARIVkSARIRPANLQVELNVyFQQR---ELVAFCRALDITVCAYAPIGSPGLANviKARGaeVPESAKF 245
Cdd:cd19101 140 LGLTNFDTERLREIL-DAGVPIVSNQVQYSL-LDRRpenGMAALCEDHGIKLLAYGTLAGGLLSE--KYLG--VPEPTGP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 246 DPLT----------------DPV-----VLK-IAEHHKKTPAQVLLRHCMQRDIV--VIPKSTNAGRIKENFQVFDFELS 301
Cdd:cd19101 214 ALETrslqkyklmidewggwDLFqellrTLKaIADKHGVSIANVAVRWVLDQPGVagVIVGARNSEHIDDNVRAFSFRLD 293
|
....*....
5KET_A 302 KAEVDELDS 310
Cdd:cd19101 294 DEDRAAIDA 302
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
23-281 |
1.26e-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: 381391 [Multi-domain] Cd Length: 291 Bit Score: 75.83 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 23 PVVGLGTWQ----SPPEEVTAAIDVALEVGYRHIDTAFMY----------QNEAAIGKTLKkwfDSGKlkREDVFIVTKL 88
Cdd:cd19752 1 SELCLGTMYfgtrTDEETSFAILDRYVAAGGNFLDTANNYafwteggvggESERLIGRWLK---DRGN--RDDVVIATKV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 89 ---PPI---------GNRAESVEKFLTKSLEALQLDYVDLYLIHLpvgfqykgDDnlwPRgeageflidtsTDLISLWKA 156
Cdd:cd19752 76 gagPRDpdggpespeGLSAETIEQEIDKSLRRLGTDYIDLYYAHV--------DD---RD-----------TPLEETLEA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 157 MEAQVDAGRTRSVGLSNFNSRQIARIVKSAR----------------IRP---ANLQVELNVyfqQRELVAFCRAL-DIT 216
Cdd:cd19752 134 FNELVKAGKVRAIGASNFAAWRLERARQIARqqgwaefsaiqqrhsyLRPrpgADFGVQRIV---TDELLDYASSRpDLT 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
5KET_A 217 VCAYAPIgspglanvikARGA----EVPESAKFD-PLTD---PVVLKIAEHHKKTPAQVLLRHCMQRDIVVIP 281
Cdd:cd19752 211 LLAYSPL----------LSGAytrpDRPLPEQYDgPDSDarlAVLEEVAGELGATPNQVVLAWLLHRTPAIIP 273
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
26-280 |
3.37e-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: 381323 [Multi-domain] Cd Length: 267 Bit Score: 74.49 E-value: 3.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 26 GLGTWQ-------------SPPEEVTAAIDVALEVGYRHIDTAFMYQN-EAAIGKTLKKWfdsgklkrEDVFIVTKLPPI 91
Cdd:cd19097 4 ALGTAQfgldygianksgkPSEKEAKKILEYALKAGINTLDTAPAYGDsEKVLGKFLKRL--------DKFKIITKLPPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 92 GNRAESVEKFLTKSLEA----LQLDYVDLYLIHLPvgfqykgDDNLWPRGEageflidtstdlisLWKAMEAQVDAGRTR 167
Cdd:cd19097 76 KEDKKEDEAAIEASVEAslkrLKVDSLDGLLLHNP-------DDLLKHGGK--------------LVEALLELKKEGLIR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 168 SVGLSNFNSRQIARIVKsaRIRPANLQVELNVyFQQRelvafcralditvcayapIGSPGLANVIKARGAEV-------- 239
Cdd:cd19097 135 KIGVSVYSPEELEKALE--SFKIDIIQLPFNI-LDQR------------------FLKSGLLAKLKKKGIEIharsvflq 193
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
5KET_A 240 ------PE--SAKFDPLTDPV--VLKIAEHHKKTPAQVLLRHCMQR---DIVVI 280
Cdd:cd19097 194 glllmePDklPAKFAPAKPLLkkLHELAKKLGLSPLELALGFVLSLpeiDKIVV 247
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
17-314 |
1.28e-11 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 64.88 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 17 HNGRKMPVVGLGTW----QSPPEEVTAAIDVALEVGYRHIDTAFMYQ----------NEAAIGKTLKKwfdsgKLKREDV 82
Cdd:PRK10625 8 HSSLEVSTLGLGTMtfgeQNSEADAHAQLDYAVAQGINLIDVAEMYPvpprpetqglTETYIGNWLAK-----RGSREKL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 83 FIVTKL--PPIGNRA----------ESVEKFLTKSLEALQLDYVDLYLIHlpvgfqykgddnlWPRGEAGEF--LIDTST 148
Cdd:PRK10625 83 IIASKVsgPSRNNDKgirpnqaldrKNIREALHDSLKRLQTDYLDLYQVH-------------WPQRPTNCFgkLGYSWT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 149 D---LISLWKAMEA---QVDAGRTRSVGLSNFNSRQIARIVKSA------RI----RPANLqveLNVYFQQrELVAFCRA 212
Cdd:PRK10625 150 DsapAVSLLETLDAlaeQQRAGKIRYIGVSNETAFGVMRYLHLAekhdlpRIvtiqNPYSL---LNRSFEV-GLAEVSQY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 213 LDITVCAYAPIGSPGLA----NVIKARGAEVPESAKFDPLTDPVVLK-------IAEHHKKTPAQVLLRHCMQRDIV--V 279
Cdd:PRK10625 226 EGVELLAYSCLAFGTLTgkylNGAKPAGARNTLFSRFTRYSGEQTQKavaayvdIAKRHGLDPAQMALAFVRRQPFVasT 305
|
330 340 350
....*....|....*....|....*....|....*
5KET_A 280 IPKSTNAGRIKENFQVFDFELSKAEVDELDSLDKR 314
Cdd:PRK10625 306 LLGATTMEQLKTNIESLHLTLSEEVLAEIEAVHQV 340
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
19-222 |
2.09e-11 |
|
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: 63.82 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 19 GRKMPVVGLGTWQ-----SPPEEVTAAIDVALEVGYRHIDTAFMY-----QNEAAIGKTLKKWFdsgKLKREDVFIVTKL 88
Cdd:cd19089 8 GLHLPAISLGLWHnfgdyTSPEEARELLRTAFDLGITHFDLANNYgpppgSAEENFGRILKRDL---RPYRDELVISTKA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 89 ------PPIGNRaeSVEKFLTKSLEA----LQLDYVDLYLIHLPvgfqykgddnlwprgeagefliDTSTDLISLWKAME 158
Cdd:cd19089 85 gygmwpGPYGDG--GSRKYLLASLDQslkrMGLDYVDIFYHHRY----------------------DPDTPLEETMTALA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
5KET_A 159 AQVDAGRTRSVGLSNFNSRQIARIVK---SARIRPANLQVELNVYFQQRE--LVAFCRALDITVCAYAP 222
Cdd:cd19089 141 DAVRSGKALYVGISNYPGAKARRAIAllrELGVPLIIHQPRYSLLDRWAEdgLLEVLEEAGIGFIAFSP 209
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
7-311 |
9.21e-10 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 58.83 E-value: 9.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 7 MPKQLSSVTFH-NGRKMPVVGLGTWQ-------SPPEEVTAAIDV---ALEVGYRHIDTAFMY----QNEAaIGKTLKKW 71
Cdd:PRK10376 1 MSTIMSSGTFTlGGRSVNRLGYGAMQlagpgvfGPPKDRDAAIAVlreAVALGVNHIDTSDFYgphvTNQL-IREALHPY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 72 fdsgklkREDVFIVTKLP---------PIGNRAESVEKFLTKSLEALQLDYVDLylihlpVGFQYKGDdnlwPRGEAGEf 142
Cdd:PRK10376 80 -------PDDLTIVTKVGarrgedgswLPAFSPAELRRAVHDNLRNLGLDVLDV------VNLRLMGD----GHGPAEG- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 143 lidtstdliSLWKAMEAQVD---AGRTRSVGLSNFNSRQIARIVKSARIrpANLQVELNVyfQQRELVAFCRALDITVCA 219
Cdd:PRK10376 142 ---------SIEEPLTVLAElqrQGLVRHIGLSNVTPTQVAEARKIAEI--VCVQNHYNL--AHRADDALIDALARDGIA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 220 YAPIGSPGlanvikargaevpesaKFDPLTDPVVLKIAEHHKKTPAQVLLRHCMQR--DIVVIPKSTNAGRIKENFQVFD 297
Cdd:PRK10376 209 YVPFFPLG----------------GFTPLQSSTLSDVAASLGATPMQVALAWLLQRspNILLIPGTSSVAHLRENLAAAE 272
|
330
....*....|....
5KET_A 298 FELSKAEVDELDSL 311
Cdd:PRK10376 273 LVLSEEVLAELDGI 286
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
25-195 |
1.88e-09 |
|
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: 57.93 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 25 VGLGTWQSPPEEVTAAIDV---ALEVGYRHIDTAFMYQN---EAAIGKTLKkwfdSGKLKREDVFIVTKLPPIGNR---- 94
Cdd:cd19153 20 AALGGVYGDGLEQDEAVAIvaeAFAAGINHFDTSPYYGAessEAVLGKALA----ALQVPRSSYTVATKVGRYRDSefdy 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 95 -AESVEKFLTKSLEALQLDYVDLYLIHlpvgfqykgddnlwprgeAGEFLiDTSTDLISLWKAMEAQVDAGRTRSVGLSN 173
Cdd:cd19153 96 sAERVRASVATSLERLHTTYLDVVYLH------------------DIEFV-DYDTLVDEALPALRTLKDEGVIKRIGIAG 156
|
170 180
....*....|....*....|..
5KET_A 174 FNSRQIARIVKsaRIRPANLQV 195
Cdd:cd19153 157 YPLDTLTRATR--RCSPGSLDA 176
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
18-120 |
2.45e-09 |
|
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: 57.86 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 18 NGRKMPVVGLGTWQS----PPEEVTAAI-DVALEVGYRHIDTAFMYQNEAA---IGKTLKK--WfdsgklKREDVFIVTK 87
Cdd:cd19142 9 SGLRVSNVGLGTWSTfstaISEEQAEEIvTLAYENGINYFDTSDAFTSGQAeteLGRILKKkgW------KRSSYIVSTK 82
|
90 100 110 120
....*....|....*....|....*....|....*....|.
5KET_A 88 L----PPIGnRAESvEKFLTKSLEA----LQLDYVDLYLIH 120
Cdd:cd19142 83 IywsyGSEE-RGLS-RKHIIESVRAslrrLQLDYIDIVIIH 121
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
19-120 |
5.30e-08 |
|
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: 53.32 E-value: 5.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 19 GRKMPVVGLGT-------WQSPPEEVTAAIDVALEVGYRHIDTAFMY---QNEAAIGKTLKKwfdsgkLKREDVFIVTKL 88
Cdd:cd19163 10 GLKVSKLGFGAsplggvfGPVDEEEAIRTVHEALDSGINYIDTAPWYgqgRSETVLGKALKG------IPRDSYYLATKV 83
|
90 100 110 120
....*....|....*....|....*....|....*....|
5KET_A 89 PPIGN--------RAESVEKFLTKSLEALQLDYVDLYLIH 120
Cdd:cd19163 84 GRYGLdpdkmfdfSAERITKSVEESLKRLGLDYIDIIQVH 123
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
23-308 |
5.96e-08 |
|
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: 53.38 E-value: 5.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 23 PVVGLGT-------WQSPPEEVTAAIDVALEVGYRHIDTAFMYQN---EAAIGKTLKKwfdsgkLKREDVFIVTKL---- 88
Cdd:cd19152 1 PKLGFGTaplgnlyEAVSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALRE------LGREDYVISTKVgrll 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 89 ---------------PPIGNR------AESVEKFLTKSLEALQLDYVDLYLIHLPvgfqykGDDNLWPRGEAGEFlidts 147
Cdd:cd19152 75 vplqeveptfepgfwNPLPFDavfdysYDGILRSIEDSLQRLGLSRIDLLSIHDP------DEDLAGAESDEHFA----- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 148 TDLISLWKAMEAQVDAGRTRSVGL-SNFnSRQIARIVKSARIRPANLQVELNVYFQQ--RELVAFCRALDITVCAYAPIG 224
Cdd:cd19152 144 QAIKGAFRALEELREEGVIKAIGLgVND-WEVILRILEEADLDWVMLAGRYTLLDHSaaRELLPECEKRGVKVVNAGPFN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 225 SPGLAnvikarGAEVPESAKFDPLTDPVVLK------IAEHHKKTPAQVLLRHCMQRDIV--VIPKSTNAGRIKENFQVF 296
Cdd:cd19152 223 SGFLA------GGDNFDYYEYGPAPPELIARrdrieaLCEQHGVSLAAAALQFALAPPAVasVAPGASSPERVEENVALL 296
|
330
....*....|..
5KET_A 297 DFELSKAEVDEL 308
Cdd:cd19152 297 ATEIPAAFWEEL 308
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
18-311 |
8.82e-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: 53.12 E-value: 8.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 18 NGRKMPVVGLGTW-----QSPPEEVTAAIDVALEVGYRHIDTAFMY---QNEAAIGKTLKK--WfdsgklKREDVFIVTK 87
Cdd:cd19159 9 SGLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKkgW------RRSSLVITTK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 88 LPpIGNRAESvEKFLTK---------SLEALQLDYVDLYLIHLPvgfqykgddnlwprgeagefliDTSTDLISLWKAME 158
Cdd:cd19159 83 LY-WGGKAET-ERGLSRkhiieglkgSLQRLQLEYVDVVFANRP----------------------DSNTPMEEIVRAMT 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 159 AQVDAGRTRSVGLSNFNSRQIARIVKSAR----IRPANLQVELNVyFQQRELVAFCRALDITVCAYAPIGSPGLANVIKA 234
Cdd:cd19159 139 HVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHL-FQREKVEVQLPELYHKIGVGAMTWSPLACGIISG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 235 R-GAEVPESAK-----FDPLTDPVV--------------LKIAEHHKKTPAQVLLRHCMQRDIV--VIPKSTNAGRIKEN 292
Cdd:cd19159 218 KyGNGVPESSRaslkcYQWLKERIVseegrkqqnklkdlSPIAERLGCTLPQLAVAWCLRNEGVssVLLGSSTPEQLIEN 297
|
330 340
....*....|....*....|..
5KET_A 293 F---QVFDfELSKAEVDELDSL 311
Cdd:cd19159 298 LgaiQVLP-KMTSHVVNEIDNI 318
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
31-120 |
1.27e-07 |
|
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: 52.28 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 31 QSPPEEvtaAIDVALEVGYRHIDTAFMYQN-EAAIGKTLKKWFDsgKLKREDVFIVTKLPPIGNR-----AESVEKFLTK 104
Cdd:cd19164 33 SIPPVD---IVRRALELGIRAFDTSPYYGPsEIILGRALKALRD--EFPRDTYFIITKVGRYGPDdfdysPEWIRASVER 107
|
90
....*....|....*.
5KET_A 105 SLEALQLDYVDLYLIH 120
Cdd:cd19164 108 SLRRLHTDYLDLVYLH 123
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
8-310 |
1.34e-07 |
|
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins; Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis.
Pssm-ID: 381372 [Multi-domain] Cd Length: 326 Bit Score: 52.43 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 8 PKQLSSVTFHNGRKmpvVGLGTwqSPPEEVTAAIDVALEVGYRHIDTAFMYQNEAAiGKTLKKWFDSGKlKREDVFIVTK 87
Cdd:cd19146 13 PLCLGAMSFGEAWK---SMMGE--CDKETAFKLLDAFYEQGGNFIDTANNYQGEES-ERWVGEWMASRG-NRDEMVLATK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 88 LP---------PI-----GNRAESVEKFLTKSLEALQLDYVDLYLIHLpvgfqykgddnlWprgeagefliDTSTDLISL 153
Cdd:cd19146 86 YTtgyrrggpiKIksnyqGNHAKSLRLSVEASLKKLQTSYIDILYVHW------------W----------DYTTSIPEL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 154 WKAMEAQVDAGRTRSVGLSNFNSRQIARIVKSAR---IRPANL-QVELNVYFQ--QRELVAFCRALDItvcAYAPIGSPG 227
Cdd:cd19146 144 MQSLNHLVAAGKVLYLGVSDTPAWVVSKANAYARahgLTQFVVyQGHWSAAFRdfERDILPMCEAEGM---ALAPWGVLG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 228 LANV-----IKARGAEvpeSAKFDPLTDP------VVLKIAEHHKKTPAQVLLRHCMQRDIVVIPksTNAGR----IKEN 292
Cdd:cd19146 221 QGQFrteeeFKRRGRS---GRKGGPQTEKerkvseKLEKVAEEKGTAITSVALAYVMHKAPYVFP--IVGGRkvehLKGN 295
|
330
....*....|....*...
5KET_A 293 FQVFDFELSKAEVDELDS 310
Cdd:cd19146 296 IEALGISLSDEEIQEIED 313
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
19-207 |
2.09e-07 |
|
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: 51.68 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 19 GRKMPVVGLGTW-----QSPPEEVTAAIDVALEVGYRHIDTAFMY---QNEAAIGKTLKK--WfdsgklKREDVFIVTKL 88
Cdd:cd19141 9 GLRVSCLGLGTWvtfgsQISDEVAEELVTLAYENGINLFDTAEVYaagKAEIVLGKILKKkgW------RRSSYVITTKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 89 PpIGNRAESvEKFLTK---------SLEALQLDYVDLYLIHLPvgfqykgddnlwprgeagefliDTSTDLISLWKAMEA 159
Cdd:cd19141 83 F-WGGKAET-ERGLSRkhiieglkaSLERLQLEYVDIVFANRP----------------------DPNTPMEEIVRAFTH 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
5KET_A 160 QVDAGRTRSVGLSNFNSRQIARIVKSAR----IRPANLQVELNVYfqQRELV 207
Cdd:cd19141 139 VINQGMAMYWGTSRWSAMEIMEAYSVARqfnlIPPIVEQAEYHLF--QREKV 188
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
23-292 |
2.61e-07 |
|
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: 51.21 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 23 PVVGLGTWQ------SPPEEVTAAIDVALEVGYRHIDTAFMY---QNEAAIGKTLKKWfdsgklKREDVFIVTKL----- 88
Cdd:cd19162 1 PRLGLGAASlgnlarAGEDEAAATLDAAWDAGIRYFDTAPLYglgLSERRLGAALARH------PRAEYVVSTKVgrlle 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 89 PPIGNR-----------AESVEKFLTKSLEALQLDYVDLYLIHLPVGFQYKGDDNLWPrgeageflidtstdlislwkAM 157
Cdd:cd19162 75 PGAAGRpagadrrfdfsADGIRRSIEASLERLGLDRLDLVFLHDPDRHLLQALTDAFP--------------------AL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 158 EAQVDAGRTRSVGLSNFNSRQIARIVKSAR---IRPANLQVELNVYFQQrELVAFCRALDITVCAYAPIGSPGLAnvika 234
Cdd:cd19162 135 EELRAEGVVGAIGVGVTDWAALLRAARRADvdvVMVAGRYTLLDRRAAT-ELLPLCAAKGVAVVAAGVFNSGILA----- 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
5KET_A 235 rgAEVPESAKFD--PLTDPV---VLKIAE----HHKKTPAQVL---LRHCMQRDIVVIPKS-----TNAGRIKEN 292
Cdd:cd19162 209 --TDDPAGDRYDyrPATPEVlarARRLAAvcrrYGVPLPAAALqfpLRHPAVASVVVGAASpaelrDNLALLRTP 281
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
18-207 |
5.19e-07 |
|
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: 50.75 E-value: 5.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 18 NGRKMPVVGLGTW-----QSPPEEVTAAIDVALEVGYRHIDTAFMY---QNEAAIGKTLKKwfdsgKLKREDVFIVTKLP 89
Cdd:cd19160 11 SGLRVSCLGLGTWvtfgsQISDETAEDLLTVAYEHGVNLFDTAEVYaagKAERTLGNILKS-----KGWRRSSYVVTTKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 90 PIGNRAESvEKFLTK---------SLEALQLDYVDLYlihlpvgFQYKGDDNLwPRGEageflidtstdlisLWKAMEAQ 160
Cdd:cd19160 86 YWGGQAET-ERGLSRkhiieglrgSLDRLQLEYVDIV-------FANRSDPNS-PMEE--------------IVRAMTYV 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
5KET_A 161 VDAGRTRSVGLSNFNSRQIARIVKSAR----IRPANLQVELNVYfqQRELV 207
Cdd:cd19160 143 INQGMAMYWGTSRWSAMEIMEAYSVARqfnlIPPVCEQAEYHLF--QREKV 191
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
17-122 |
1.09e-06 |
|
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: 49.52 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 17 HNGRKMPVVGLGTW-----QSPPEEVTAAIDVALEVGYRHIDTAFMYQN---EAAIGKTLKKwfdsGKLKREDVFIVTKL 88
Cdd:cd19143 8 RSGLKVSALSFGSWvtfgnQVDVDEAKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIKE----LGWPRSDYVVSTKI 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....
5KET_A 89 ------PPIGNRAESvEKFLT----KSLEALQLDYVDLYLIHLP 122
Cdd:cd19143 84 fwggggPPPNDRGLS-RKHIVegtkASLKRLQLDYVDLVFCHRP 126
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
17-185 |
4.81e-05 |
|
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2).
Pssm-ID: 381377 [Multi-domain] Cd Length: 309 Bit Score: 44.32 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 17 HNGRKMPVVGLGTWQS-----PPEEVTAAIDVALEVGYRHIDTAFMY-----QNEAAIGKTLKKWFdsgKLKREDVFIVT 86
Cdd:cd19151 7 RSGLKLPAISLGLWHNfgdvdRYENSRAMLRRAFDLGITHFDLANNYgpppgSAEENFGRILKEDL---KPYRDELIIST 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 87 KLP------PIGNRAEsvEKFLTKSLEA----LQLDYVDLYLIHLPvgfqykgddnlwprgeagefliDTSTDLISLWKA 156
Cdd:cd19151 84 KAGytmwpgPYGDWGS--KKYLIASLDQslkrMGLDYVDIFYHHRP----------------------DPETPLEETMGA 139
|
170 180 190
....*....|....*....|....*....|..
5KET_A 157 MEAQVDAGRTRSVGLSNFNS---RQIARIVKS 185
Cdd:cd19151 140 LDQIVRQGKALYVGISNYPPeeaREAAAILKD 171
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
18-311 |
8.90e-05 |
|
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: 43.92 E-value: 8.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 18 NGRKMPVVGLGTW-----QSPPEEVTAAIDVALEVGYRHIDTAFMY---QNEAAIGKTLKK--WfdsgklKREDVFIVTK 87
Cdd:cd19158 9 SGLRVSCLGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKkgW------RRSSLVITTK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 88 LPpIGNRAES--------VEKFLTKSLEALQLDYVDLYLIHLPvgfqykgddnlwprgeagefliDTSTDLISLWKAMEA 159
Cdd:cd19158 83 IF-WGGKAETerglsrkhIIEGLKASLERLQLEYVDVVFANRP----------------------DPNTPMEETVRAMTH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 160 QVDAGRTRSVGLSNFNSRQIARIVKSAR----IRPANLQVELNVyFQQRELVAFCRALDITVCAYAPIGSPGLANVIKAR 235
Cdd:cd19158 140 VINQGMAMYWGTSRWSSMEIMEAYSVARqfnlIPPICEQAEYHM-FQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 236 -GAEVPESAK-----FDPLTDPVV----------LK----IAEHHKKTPAQVLLRHCMQRDIV--VIPKSTNAGRIKENF 293
Cdd:cd19158 219 yDSGIPPYSRaslkgYQWLKDKILseegrrqqakLKelqaIAERLGCTLPQLAIAWCLRNEGVssVLLGASNAEQLMENI 298
|
330 340
....*....|....*....|
5KET_A 294 QVFDF--ELSKAEVDELDSL 311
Cdd:cd19158 299 GAIQVlpKLSSSIVHEIDSI 318
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
18-316 |
1.66e-04 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 43.05 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 18 NGRKMPVVGLGTWQS-----PPEEVTAAIDVALEVGYRHIDTAFMY-----QNEAAIGKTLKKWFdsgKLKREDVFIVTK 87
Cdd:PRK09912 21 SGLRLPALSLGLWHNfghvnALESQRAILRKAFDLGITHFDLANNYgpppgSAEENFGRLLREDF---AAYRDELIISTK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 88 L-----P-PIGnrAESVEKFL----TKSLEALQLDYVDLYLIHlpvgfqykgddnlwprgeagefLIDTSTDLISLWKAM 157
Cdd:PRK09912 98 AgydmwPgPYG--SGGSRKYLlaslDQSLKRMGLEYVDIFYSH----------------------RVDENTPMEETASAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 158 EAQVDAGRTRSVGLSNFNSRQIARIVKSARIRPANLQVE------LNVYFQQRELVAFCRALDITVCAYAPIGSPGLA-- 229
Cdd:PRK09912 154 AHAVQSGKALYVGISSYSPERTQKMVELLREWKIPLLIHqpsynlLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTgk 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 230 --NVIKARGAEVPESAKFDPLTDPVVL-----------KIAEHHKKTPAQVLLRHCMQRDIV--VIPKSTNAGRIKENFQ 294
Cdd:PRK09912 234 ylNGIPQDSRMHREGNKVRGLTPKMLTeanlnslrllnEMAQQRGQSMAQMALSWLLKDERVtsVLIGASRAEQLEENVQ 313
|
330 340
....*....|....*....|..
5KET_A 295 VFDfELSKAEvDELDSLDKRAA 316
Cdd:PRK09912 314 ALN-NLTFST-EELAQIDQHIA 333
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
19-120 |
1.85e-04 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 42.84 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 19 GRKMPVVGLGTwqSP--------PEEVT-AAIDVALEVGYRHIDTAFMYQN---EAAIGKTLKkwfdSGKLKREDVFIVT 86
Cdd:PLN02587 8 GLKVSSVGFGA--SPlgsvfgpvSEEDAiASVREAFRLGINFFDTSPYYGGtlsEKVLGKALK----ALGIPREKYVVST 81
|
90 100 110
....*....|....*....|....*....|....*...
5KET_A 87 KLPPIGN----RAESVEKFLTKSLEALQLDYVDLYLIH 120
Cdd:PLN02587 82 KCGRYGEgfdfSAERVTKSVDESLARLQLDYVDILHCH 119
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
17-184 |
2.06e-04 |
|
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: 42.44 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 17 HNGRKMPVVGLGTWQ-----SPPEEVTAAIDVALEVGYRHIDTAFMY-----QNEAAIGKTLKKWFDSgklKREDVFIVT 86
Cdd:cd19150 7 KSGLKLPALSLGLWHnfgddTPLETQRAILRTAFDLGITHFDLANNYgpppgSAEENFGRILREDFAG---YRDELIIST 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 87 KLP------PIGNRAEsvEKFLTKSL-EALQ---LDYVDLYLIHlpvgfqykgddnlwprgeagefLIDTSTDLISLWKA 156
Cdd:cd19150 84 KAGydmwpgPYGEWGS--RKYLLASLdQSLKrmgLDYVDIFYSH----------------------RFDPDTPLEETMGA 139
|
170 180 190
....*....|....*....|....*....|.
5KET_A 157 MEAQVDAGRTRSVGLSNFNS---RQIARIVK 184
Cdd:cd19150 140 LDHAVRSGKALYVGISSYSPertREAAAILR 170
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
41-121 |
1.83e-03 |
|
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; Phanerochaete chrysosporium ADD (EC1.1.1.91) is a founding member of aldo-keto reductase family 9 member A3. It is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). This family also 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: 381373 [Multi-domain] Cd Length: 319 Bit Score: 39.81 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KET_A 41 IDVALEVGYRHIDTAFMYQNEAA---IGKtlkkWFDSGKLkREDVFIVTKLPP---------------IGNRAESVEKFL 102
Cdd:cd19147 40 LDAFYEAGGNFIDTANNYQDEQSetwIGE----WMKSRKN-RDQIVIATKFTTdykayevgkgkavnyCGNHKRSLHVSV 114
|
90
....*....|....*....
5KET_A 103 TKSLEALQLDYVDLYLIHL 121
Cdd:cd19147 115 RDSLRKLQTDWIDILYVHW 133
|
|
| |
