|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
3-306 |
0e+00 |
|
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: 512.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 3 VDSIPLNTGAQLPLFGLGTWQVKdEAELTVALRAALDAGYRLIDTAHLYQNEHIIGKVLHEYISSGKLKREDIFVTSKLP 82
Cdd:cd19154 1 SASITLSNGVKMPLIGLGTWQSK-GAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 83 FTAHAPEDVPKCVESQLKALQLEYIDLYLIHCPFPFKHQEGSFAPlMENGELAVTEIAHIDTWRALEKLYKEGKLKALGV 162
Cdd:cd19154 80 THEHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGT-MENGMSIHDAVDVEDVWRGMEKVYDEGLTKAIGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 163 SNFSCNQLQALYDAAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGSPGRKAAR-PDGVWPEGDPLLEPIVKQ 241
Cdd:cd19154 159 SNFNNDQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSPGRANFTkSTGVSPAPNLLQDPIVKA 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831516805 242 LAAKYHKTAAQILIRHLTQHGISTIPKSVSPDRIVENISTFDFKLSDEDMHTLNSIETRTRLFIA 306
Cdd:cd19154 239 IAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLRLFLF 303
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
14-295 |
1.78e-120 |
|
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: 346.78 E-value: 1.78e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 14 LPLFGLGTWQVKDEaELTVALRAALDAGYRLIDTAHLYQNEHIIGKVLHEYIssgkLKREDIFVTSKLPFTAHAPEDVPK 93
Cdd:cd19071 1 MPLIGLGTYKLKPE-ETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESG----VPREELFITTKLWPTDHGYERVRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 94 CVESQLKALQLEYIDLYLIHCPFPFKHQEgsfaplmengelavTEIAHIDTWRALEKLYKEGKLKALGVSNFSCNQLQAL 173
Cdd:cd19071 76 ALEESLKDLGLDYLDLYLIHWPVPGKEGG--------------SKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEEL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 174 YDAAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGSPGRkaarpdgvwpegDPLLEPIVKQLAAKYHKTAAQI 253
Cdd:cd19071 142 LAAARIKPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRR------------PLLDDPVLKEIAKKYGKTPAQV 209
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1831516805 254 LIRHLTQHGISTIPKSVSPDRIVENISTFDFKLSDEDMHTLN 295
Cdd:cd19071 210 LLRWALQRGVVVIPKSSNPERIKENLDVFDFELSEEDMAAID 251
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
5-304 |
9.23e-116 |
|
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: 336.56 E-value: 9.23e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 5 SIPLNTGAQLPLFGLGTWQVKDEAELTVALRAALDAGYRLIDTAHLYQNEHIIGKVLHEYISSGKLKREDIFVTSKLPFT 84
Cdd:cd19116 2 TIKLNDGNEIPAIALGTWKLKDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLWNS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 85 AHAPEDVPKCVESQLKALQLEYIDLYLIHCPFPFKHQEGSfaplMENGELAVTEIAHIDTWRALEKLYKEGKLKALGVSN 164
Cdd:cd19116 82 YHEREQVEPALRESLKRLGLDYVDLYLIHWPVAFKENNDS----ESNGDGSLSDIDYLETWRGMEDLVKLGLTRSIGVSN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 165 FSCNQLQALYDAAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGSPgrkaaRPDGVWPEGDPLLEPIVKQLAA 244
Cdd:cd19116 158 FNSEQINRLLSNCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRL-----VPRGQTNPPPRLDDPTLVAIAK 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 245 KYHKTAAQILIRHLTQHGISTIPKSVSPDRIVENISTFDFKLSDEDMHTLNSIETRTRLF 304
Cdd:cd19116 233 KYGKTTAQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRVY 292
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
11-304 |
7.90e-114 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 330.09 E-value: 7.90e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 11 GAQLPLFGLGTWQVKDEAELTvALRAALDAGYRLIDTAHLYQNEHIIGKVLHEyisSGkLKREDIFVTSKLPFTAHAPED 90
Cdd:COG0656 2 GVEIPALGLGTWQLPGEEAAA-AVRTALEAGYRHIDTAAMYGNEEGVGEAIAA---SG-VPREELFVTTKVWNDNHGYDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 91 VPKCVESQLKALQLEYIDLYLIHCPFPfkhqegsfAPLMEngelavteiahidTWRALEKLYKEGKLKALGVSNFSCNQL 170
Cdd:COG0656 77 TLAAFEESLERLGLDYLDLYLIHWPGP--------GPYVE-------------TWRALEELYEEGLIRAIGVSNFDPEHL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 171 QALYDAAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGspgrkaarpdgvwpEGDPLLEPIVKQLAAKYHKTA 250
Cdd:COG0656 136 EELLAETGVKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLG--------------RGKLLDDPVLAEIAEKHGKTP 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1831516805 251 AQILIRHLTQHGISTIPKSVSPDRIVENISTFDFKLSDEDMHTLNSIETRTRLF 304
Cdd:COG0656 202 AQVVLRWHLQRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRGERLG 255
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
4-303 |
7.54e-113 |
|
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: 328.92 E-value: 7.54e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 4 DSIPLNTGAQLPLFGLGTWQvKDEAELTVALRAALDAGYRLIDTAHLYQNEHIIGKVLHEYISSGKLKREDIFVTSKLPF 83
Cdd:cd19125 1 RFFKLNTGAKIPAVGLGTWQ-ADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLWC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 84 TAHAPEDVPKCVESQLKALQLEYIDLYLIHCPFPFKhqEGsfAPLMENGELAVTEIAhiDTWRALEKLYKEGKLKALGVS 163
Cdd:cd19125 80 TDHAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLK--KG--AHMPEPEEVLPPDIP--STWKAMEKLVDSGKVRAIGVS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 164 NFSCNQLQALYDAAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGSPGRKaarpdgvWPEGDPLLEPIVKQLA 243
Cdd:cd19125 154 NFSVKKLEDLLAVARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGTT-------WVKKNVLKDPIVTKVA 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 244 AKYHKTAAQILIRHLTQHGISTIPKSVSPDRIVENISTFDFKLSDEDMHTLNSIETRTRL 303
Cdd:cd19125 227 EKLGKTPAQVALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSIEQQRRV 286
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
8-305 |
8.72e-112 |
|
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: 327.03 E-value: 8.72e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 8 LNTGAQLPLFGLGTW-----QVKDeaeltvALRAALDAGYRLIDTAHLYQNEHIIGKVLHEYISSGK-LKREDIFVTSKL 81
Cdd:cd19106 1 LHTGQKMPLIGLGTWkskpgQVKA------AVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPGKaVPREDLFVTSKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 82 PFTAHAPEDV-PKCVESqLKALQLEYIDLYLIHCPFPFKHQEGSFaPLMENGELAVTEIAHIDTWRALEKLYKEGKLKAL 160
Cdd:cd19106 75 WNTKHHPEDVePALRKT-LKDLQLDYLDLYLIHWPYAFERGDNPF-PKNPDGTIRYDSTHYKETWKAMEKLVDKGLVKAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 161 GVSNFSCNQLQALYDAAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGSPGRKAARPDgvwpegDPLL--EPI 238
Cdd:cd19106 153 GLSNFNSRQIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPDRPWAKPD------EPVLleEPK 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831516805 239 VKQLAAKYHKTAAQILIRHLTQHGISTIPKSVSPDRIVENISTFDFKLSDEDMHTLNSIETRTRLFI 305
Cdd:cd19106 227 VKALAKKYNKSPAQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRYIV 293
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
11-304 |
2.35e-109 |
|
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: 320.21 E-value: 2.35e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 11 GAQLPLFGLGTWQVKDEaELTVALRAALDAGYRLIDTAHLYQNEHIIGKVLHEYISSGKLKREDIFVTSKLPFTAHAPED 90
Cdd:cd19111 1 GFPMPVIGLGTYQSPPE-EVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLEFKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 91 VPKCVESQLKALQLEYIDLYLIHCPFPFKHQEgsfaplmENGELAVTEIAHIDTWRALEKLYKEGKLKALGVSNFSCNQL 170
Cdd:cd19111 80 TEKSLEKSLENLKLPYVDLYLIHHPCGFVNKK-------DKGERELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 171 QALYDAAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGSPGRKaarPDGVWPEG-DPLLEPIVKQLAAKYHKT 249
Cdd:cd19111 153 NKILAYAKVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSPGRA---NQSLWPDQpDLLEDPTVLAIAKELDKT 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1831516805 250 AAQILIRHLTQHGISTIPKSVSPDRIVENISTFDFKLSDEDMHTLNSIETRTRLF 304
Cdd:cd19111 230 PAQVLLRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMKYF 284
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
4-304 |
1.32e-108 |
|
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: 319.09 E-value: 1.32e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 4 DSIPLNTGAQLPLFGLGTWQVKDEaELTVALRAALDAGYRLIDTAHLYQNEHIIGKVLHEYISSGKLKREDIFVTSKLPF 83
Cdd:cd19155 2 NCVTFNNGEKMPVVGLGTWQSSPE-EIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 84 TAHAPEDVPKCVESQLKALQLEYIDLYLIHCPFPFKHQEGSFAPLMENGELAV-TEIAHIDTWRALEKLYKEGKLKALGV 162
Cdd:cd19155 81 GGNRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLSKEDDSGKLDPTGEHKQdYTTDLLDIWKAMEAQVDQGLTRSIGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 163 SNFSCNQLQALYDAAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGSPGRKAARPDGVWPEG---DPLLEPIV 239
Cdd:cd19155 161 SNFNREQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPGAAHFSPGTGSPSGsspDLLQDPVV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831516805 240 KQLAAKYHKTAAQILIRHLTQHGISTIPKSVSPDRIVENISTFDFKLSDEDMHTLNSIETRTRLF 304
Cdd:cd19155 241 KAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIRGR 305
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
5-304 |
1.94e-101 |
|
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: 300.10 E-value: 1.94e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 5 SIPLNTGAQLPLFGLGTWQVKdEAELTVALRAALDAGYRLIDTAHLYQNEHIIGKVLHEYISSGKLKREDIFVTSKLPFT 84
Cdd:cd19123 3 TLPLSNGDLIPALGLGTWKSK-PGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLWNN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 85 AHAPEDVPKCVESQLKALQLEYIDLYLIHCPFPFKHqeGSFAPLMENGELAVTEIAHIDTWRALEKLYKEGKLKALGVSN 164
Cdd:cd19123 82 SHAPEDVLPALEKTLADLQLDYLDLYLMHWPVALKK--GVGFPESGEDLLSLSPIPLEDTWRAMEELVDKGLCRHIGVSN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 165 FSCNQLQALYDAAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGSPGrkaaRPDGVWPEGDPLL--EPIVKQL 242
Cdd:cd19123 160 FSVKKLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGD----RPAAMKAEGEPVLleDPVINKI 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831516805 243 AAKYHKTAAQILIRHLTQHGISTIPKSVSPDRIVENISTFDFKLSDEDMHTLNSIETRTRLF 304
Cdd:cd19123 236 AEKHGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHRYV 297
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
14-297 |
1.04e-99 |
|
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: 294.54 E-value: 1.04e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 14 LPLFGLGTWQVKDEAELTVALRAALDAGYRLIDTAHLYQNEHIIGKVLHEYISSGKLKREDIFVTSKLPFTAHAPEDVPK 93
Cdd:cd19136 1 MPILGLGTFRLRGEEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 94 CVESQLKALQLEYIDLYLIHCPFPFKHQEGSfaplMENGELavteiaHIDTWRALEKLYKEGKLKALGVSNFSCNQLQAL 173
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWPGVQGLKPSD----PRNAEL------RRESWRALEDLYKEGKLRAIGVSNYTVRHLEEL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 174 YDAAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGSpgrkaarpdgvwPEGDPLLEPIVKQLAAKYHKTAAQI 253
Cdd:cd19136 151 LKYCEVPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGS------------GDLRLLEDPTVLAIAKKYGRTPAQV 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1831516805 254 LIRHLTQHGISTIPKSVSPDRIVENISTFDFKLSDEDMHTLNSI 297
Cdd:cd19136 219 LLRWALQQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
11-319 |
3.31e-99 |
|
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: 295.10 E-value: 3.31e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 11 GAQLPLFGLGTWQVKdEAELTVALRAALDAGYRLIDTAHLYQNEHIIGKVLHEYISSGKLKREDIFVTSKLPFTAHAPED 90
Cdd:cd19107 1 GAKMPILGLGTWKSP-PGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 91 VPKCVESQLKALQLEYIDLYLIHCPFPFKHQEGSFaPLMENGELAVTEIAHIDTWRALEKLYKEGKLKALGVSNFSCNQL 170
Cdd:cd19107 80 VKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKELF-PLDESGNVIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 171 QALYD--AAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGSPGRKAARPDgvwpegDP-LLE-PIVKQLAAKY 246
Cdd:cd19107 159 ERILNkpGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPE------DPsLLEdPKIKEIAAKH 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1831516805 247 HKTAAQILIRHLTQHGISTIPKSVSPDRIVENISTFDFKLSDEDMHTLNSIETRTRLFIADFAVKHPFFPHDD 319
Cdd:cd19107 233 NKTTAQVLIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRACALLSCSSHKDYPFHA 305
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
6-297 |
7.42e-92 |
|
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: 274.45 E-value: 7.42e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 6 IPLNTGAQLPLFGLGTWQVKDEAELTVALRAALDAGYRLIDTAHLYQNEHIIGKVLHEyisSGkLKREDIFVTSKLPFTA 85
Cdd:cd19133 1 VTLNNGVEMPILGFGVFQIPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKK---SG-IPREELFITTKLWIQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 86 HAPEDVPKCVESQLKALQLEYIDLYLIHCPFpfkhqeGSFaplmengelavteiahIDTWRALEKLYKEGKLKALGVSNF 165
Cdd:cd19133 77 AGYEKAKKAFERSLKRLGLDYLDLYLIHQPF------GDV----------------YGAWRAMEELYKEGKIRAIGVSNF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 166 SCNQLQALYDAAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGspgrkaarpdgvwpEGDPLL--EPIVKQLA 243
Cdd:cd19133 135 YPDRLVDLILHNEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFA--------------EGRNNLfeNPVLTEIA 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1831516805 244 AKYHKTAAQILIRHLTQHGISTIPKSVSPDRIVENISTFDFKLSDEDMHTLNSI 297
Cdd:cd19133 201 EKYGKSVAQVILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAAL 254
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
5-304 |
1.57e-90 |
|
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: 271.19 E-value: 1.57e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 5 SIPLNTGAQLPLFGLGTWQVKDEAELTVALRAALDAGYRLIDTAHLYQNEHIIGKVLHEYISSgklkREDIFVTSKLPFT 84
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEEGSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKESGIP----REELFITSKVWNA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 85 AHAPEDVPKCVESQLKALQLEYIDLYLIHCPFPFKHQEgsfaplmengelavteiahidTWRALEKLYKEGKLKALGVSN 164
Cdd:cd19157 77 DQGYDSTLKAFEASLERLGLDYLDLYLIHWPVKGKYKE---------------------TWKALEKLYKDGRVRAIGVSN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 165 FSCNQLQALYDAAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLgspgrkaarpdgvwPEGDPLLEPIVKQLAA 244
Cdd:cd19157 136 FQVHHLEDLLADAEIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPL--------------MQGQLLDNPVLKEIAE 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 245 KYHKTAAQILIRHLTQHGISTIPKSVSPDRIVENISTFDFKLSDEDMHTLNSIETRTRLF 304
Cdd:cd19157 202 KYNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNENLRVG 261
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
5-291 |
5.04e-87 |
|
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: 261.92 E-value: 5.04e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 5 SIPLNTGAQLPLFGLGTWQVKDEaELTVALRAALDAGYRLIDTAHLYQNEHIIGKVlheyISSGKLKREDIFVTSKLPFT 84
Cdd:cd19131 1 TITLNDGNTIPQLGLGVWQVSND-EAASAVREALEVGYRSIDTAAIYGNEEGVGKA----IRASGVPREELFITTKLWNS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 85 AHAPEDVPKCVESQLKALQLEYIDLYLIHCPFPFKHQegsfaplmengelavteiaHIDTWRALEKLYKEGKLKALGVSN 164
Cdd:cd19131 76 DQGYDSTLRAFDESLRKLGLDYVDLYLIHWPVPAQDK-------------------YVETWKALIELKKEGRVKSIGVSN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 165 FSCNQLQALYDAAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGSpgrkaarpdgvwpeGDPLLEPIVKQLAA 244
Cdd:cd19131 137 FTIEHLQRLIDETGVVPVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQ--------------GGLLSDPVIGEIAE 202
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1831516805 245 KYHKTAAQILIR-HLtQHGISTIPKSVSPDRIVENISTFDFKLSDEDM 291
Cdd:cd19131 203 KHGKTPAQVVIRwHL-QNGLVVIPKSVTPSRIAENFDVFDFELDADDM 249
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
8-297 |
2.77e-84 |
|
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: 256.18 E-value: 2.77e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 8 LNTGAQLPLFGLGTWQVKdEAELTVALRAALDAGYRLIDTAHLYQNEHIIGKVLHEYISS-GKLKREDIFVTSKLPFTAH 86
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAE-PGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEePGVKREDLFITSKLWNNSH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 87 APEDVPKCVESQLKALQLEYIDLYLIHCPFPFK---HQEGSFAPLMENGELAV-TEIAHIDTWRALEKLYKEGKLKALGV 162
Cdd:cd19118 80 RPEYVEPALDDTLKELGLDYLDLYLIHWPVAFKptgDLNPLTAVPTNGGEVDLdLSVSLVDTWKAMVELKKTGKVKSIGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 163 SNFSCNQLQALYDAAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGSPgrkaarpdgvwPEGDPLL--EPIVK 240
Cdd:cd19118 160 SNFSIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGNN-----------LAGLPLLvqHPEVK 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1831516805 241 QLAAKYHKTAAQILIRHLTQHGISTIPKSVSPDRIVENISTFDfkLSDEDMHTLNSI 297
Cdd:cd19118 229 AIAAKLGKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFEQVE--LSDDEFNAVTAL 283
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
4-297 |
5.55e-84 |
|
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: 254.56 E-value: 5.55e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 4 DSIPLNTGAQLPLFGLGTWQV---KDEAELtVALRaalDAGYRLIDTAHLYQNEHIIGKVLHEyisSGkLKREDIFVTSK 80
Cdd:cd19135 3 PTVRLSNGVEMPILGLGTSHSggySHEAVV-YALK---ECGYRHIDTAKRYGCEELLGKAIKE---SG-VPREDLFLTTK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 81 LPFTAHAPEDVPKCVESQLKALQLEYIDLYLIHCPFPfkhqegsfaPLMENGELAVTEiahiDTWRALEKLYKEGKLKAL 160
Cdd:cd19135 75 LWPSDYGYESTKQAFEASLKRLGVDYLDLYLLHWPDC---------PSSGKNVKETRA----ETWRALEELYDEGLCRAI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 161 GVSNFSCNQLQALYDAAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGspgrkaarpdgvwpEGDPLLEPIVK 240
Cdd:cd19135 142 GVSNFLIEHLEQLLEDCSVVPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLA--------------KGKALEEPTVT 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1831516805 241 QLAAKYHKTAAQILIRHLTQHGISTIPKSVSPDRIVENISTFDFKLSDEDMHTLNSI 297
Cdd:cd19135 208 ELAKKYQKTPAQILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
13-316 |
6.29e-84 |
|
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: 256.04 E-value: 6.29e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 13 QLPLFGLGTWQVKdEAELTVALRAALDAGYRLIDTAHLYQNEHIIGKVLHEYISSGKLKREDIFVTSKLPFTAHAPEDVP 92
Cdd:cd19110 3 DIPAVGLGTWKAS-PGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKSLVK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 93 KCVESQLKALQLEYIDLYLIHCPFPFKHQEGSFaPLMENGELAVTEIAHIDTWRALEKLYKEGKLKALGVSNFSCNQLQA 172
Cdd:cd19110 82 TACTRSLKALKLNYLDLYLIHWPMGFKPGEPDL-PLDRSGMVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 173 LYDAA--EVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGSPGrkaarpdgvwpEGDPLLE-PIVKQLAAKYHKT 249
Cdd:cd19110 161 LLNKPglRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSC-----------EGVDLIDdPVIQRIAKKHGKS 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831516805 250 AAQILIRHLTQHGISTIPKSVSPDRIVENISTFDFKLSDEDMHTLNSIETRTRLFIADFAVKHPFFP 316
Cdd:cd19110 230 PAQILIRFQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFPITENHKDYP 296
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
8-299 |
1.77e-82 |
|
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: 250.26 E-value: 1.77e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 8 LNTGAQLPLFGLGTWQVKDEaELTVALRAALDAGYRLIDTAHLYQNEHIIGkvlhEYISSGKLKREDIFVTSKLPFTAHA 87
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKGD-EGVEAVVAALQAGYRLLDTAFNYENEGAVG----EAVRRSGVPREELFVTTKLPGRHHG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 88 PEDVPKCVESQLKALQLEYIDLYLIHCPFPfkhqegsfaplmengelavTEIAHIDTWRALEKLYKEGKLKALGVSNFSC 167
Cdd:cd19132 76 YEEALRTIEESLYRLGLDYVDLYLIHWPNP-------------------SRDLYVEAWQALIEAREEGLVRSIGVSNFLP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 168 NQLQALYDAAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGspgrkaaRPDGVwpegdpLLEPIVKQLAAKYH 247
Cdd:cd19132 137 EHLDRLIDETGVTPAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLG-------RGSGL------LDEPVIKAIAEKHG 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1831516805 248 KTAAQILIRHLTQHGISTIPKSVSPDRIVENISTFDFKLSDEDMHTLNSIET 299
Cdd:cd19132 204 KTPAQVVLRWHVQLGVVPIPKSANPERQRENLAIFDFELSDEDMAAIAALDR 255
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
5-297 |
4.27e-82 |
|
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: 251.00 E-value: 4.27e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 5 SIPLNTGAQLPLFGLGTWQVKD--EAELTVALRAALDAGYRLIDTAHLYQNEHIIGKVLHEYISSGKLKREDIFVTSKLP 82
Cdd:cd19108 2 RVKLNDGHFIPVLGFGTYAPEEvpKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 83 FTAHAPEDVPKCVESQLKALQLEYIDLYLIHCPFPFKHQEGSFaPLMENGELAVTEIAHIDTWRALEKLYKEGKLKALGV 162
Cdd:cd19108 82 CTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELF-PKDENGKLIFDTVDLCATWEAMEKCKDAGLAKSIGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 163 SNFSCNQLQALYD--AAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGSpgrkAARPDGVWPEGDPLLE-PIV 239
Cdd:cd19108 161 SNFNRRQLEMILNkpGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGS----QRDKEWVDQNSPVLLEdPVL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1831516805 240 KQLAAKYHKTAAQILIRHLTQHGISTIPKSVSPDRIVENISTFDFKLSDEDMHTLNSI 297
Cdd:cd19108 237 CALAKKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGL 294
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
11-316 |
2.01e-81 |
|
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: 249.72 E-value: 2.01e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 11 GAQLPLFGLGTWQ---VKDEAELTVALRAALDAGYRLIDTAHLYQNEHIIGKVLHEYISSGKLKREDIFVTSKLPFTAHA 87
Cdd:cd19109 1 GNSIPIIGLGTYSepkTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 88 PEDVPKCVESQLKALQLEYIDLYLIHCPFPFKHQEgSFAPLMENGELAVTEIAHIDTWRALEKLYKEGKLKALGVSNFSC 167
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAFKPGD-EIYPRDENGKWLYHKTNLCATWEALEACKDAGLVKSIGVSNFNR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 168 NQLQALYD--AAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGSPGrkaarpDGVWPEGD--PLLE-PIVKQL 242
Cdd:cd19109 160 RQLELILNkpGLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCR------DPIWVNVSspPLLEdPLLNSI 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831516805 243 AAKYHKTAAQILIRHLTQHGISTIPKSVSPDRIVENISTFDFKLSDEDMHTLNSIETRTRLFIADFAVKHPFFP 316
Cdd:cd19109 234 GKKYNKTAAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYVELLMWRDHPEYP 307
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
6-298 |
1.13e-80 |
|
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: 245.81 E-value: 1.13e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 6 IPLNTGAQLPLFGLGTWQVKDEAELTVALRAALDAGYRLIDTAHLYQNEHIIGKVLHEyisSGkLKREDIFVTSKLPFTA 85
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQTPDGDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRE---SG-VPREELFVTTKLWNDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 86 HAPEDVPKCVESQLKALQLEYIDLYLIHCPFPFKHqegsfaplmengelavteiahIDTWRALEKLYKEGKLKALGVSNF 165
Cdd:cd19126 77 QRARRTEDAFQESLDRLGLDYVDLYLIHWPGKDKF---------------------IDTWKALEKLYASGKVKAIGVSNF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 166 SCNQLQALYDAAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGspgrkaarpdgvwpEGDPLLEPIVKQLAAK 245
Cdd:cd19126 136 QEHHLEELLAHADVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLG--------------QGGLLSNPVLAAIGEK 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1831516805 246 YHKTAAQILIRHLTQHGISTIPKSVSPDRIVENISTFDFKLSDEDMHTLNSIE 298
Cdd:cd19126 202 YGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAIDALN 254
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
5-297 |
2.81e-80 |
|
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: 245.90 E-value: 2.81e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 5 SIPLNTGAQLPLFGLGTWQVKdEAELTVALRAALDAGYRLIDTAHLYQNEHIIGKVLHEYISSGkLKREDIFVTSKLPFT 84
Cdd:cd19121 3 SFKLNTGASIPAVGLGTWQAK-AGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAIAGG-VKREDLFVTTKLWST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 85 AHapEDVPKCVESQLKALQLEYIDLYLIHCPFPFkHQEGS--FAPLMENGELAVT-EIAHIDTWRALEKLYKEGKLKALG 161
Cdd:cd19121 81 YH--RRVELCLDRSLKSLGLDYVDLYLVHWPVLL-NPNGNhdLFPTLPDGSRDLDwDWNHVDTWKQMEKVLKTGKTKAIG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 162 VSNFSCNQLQALYDAAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGSpgrkaarpdgvwpEGDPLL-EPIVK 240
Cdd:cd19121 158 VSNYSIPYLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGS-------------TGSPLIsDEPVV 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1831516805 241 QLAAKYHKTAAQILIRHLTQHGISTIPKSVSPDRIVENISTFDFklSDEDMHTLNSI 297
Cdd:cd19121 225 EIAKKHNVGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDL--DDEDMNKLNDI 279
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
6-297 |
4.30e-79 |
|
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: 242.31 E-value: 4.30e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 6 IPLNTGAQLPLFGLGTWQVKDEaELTVALRAALDAGYRLIDTAHLYQNEHIIGkvlhEYISSGKLKREDIFVTSKLPFTA 85
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQTPPE-ETADAVATALADGYRLIDTAAAYGNEREVG----EGIRRSGVDRSDIFVTTKLWISD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 86 HAPEDVPKCVESQLKALQLEYIDLYLIHCPFPFKHQegsfaplmengelavteiAHIDTWRALEKLYKEGKLKALGVSNF 165
Cdd:cd19127 76 YGYDKALRGFDASLRRLGLDYVDLYLLHWPVPNDFD------------------RTIQAYKALEKLLAEGRVRAIGVSNF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 166 SCNQLQALYDAAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGspGRKAARPDGVWPEGDPLLEPIVKQLAAK 245
Cdd:cd19127 138 TPEHLERLIDATTVVPAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIG--GVMRYGASGPTGPGDVLQDPTITGLAEK 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1831516805 246 YHKTAAQILIR-HLtQHGISTIPKSVSPDRIVENISTFDFKLSDEDMHTLNSI 297
Cdd:cd19127 216 YGKTPAQIVLRwHL-QNGVSAIPKSVHPERIAENIDIFDFALSAEDMAAIDAL 267
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
8-303 |
1.38e-78 |
|
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: 240.88 E-value: 1.38e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 8 LNTGAQLPLFGLGTWQVKDEAELTVALRAALDAGYRLIDTAHLYQNEHIIGKVLHEyisSGkLKREDIFVTSKLPFTAHA 87
Cdd:cd19156 3 LANGVEMPRLGLGVWRVQDGAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRE---SG-VPREEVFVTTKLWNSDQG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 88 PEDVPKCVESQLKALQLEYIDLYLIHCPfpfkhQEGSFaplmengelavteiahIDTWRALEKLYKEGKLKALGVSNFSC 167
Cdd:cd19156 79 YESTLAAFEESLEKLGLDYVDLYLIHWP-----VKGKF----------------KDTWKAFEKLYKEKKVRAIGVSNFHE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 168 NQLQALYDAAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGSpgrkaarpdgvwpeGDPLLEPIVKQLAAKYH 247
Cdd:cd19156 138 HHLEELLKSCKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQ--------------GKLLSNPVLKAIGKKYG 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1831516805 248 KTAAQILIRHLTQHGISTIPKSVSPDRIVENISTFDFKLSDEDMHTLNSIETRTRL 303
Cdd:cd19156 204 KSAAQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTDHRY 259
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
8-297 |
2.60e-77 |
|
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: 238.17 E-value: 2.60e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 8 LNTGAQLPLFGLGTWQVK-DEAELTVAlrAALDAGYRLIDTAHLYQNEHIIGKVlheyISSGKLKREDIFVTSKLPFTAH 86
Cdd:cd19117 8 LNTGAEIPAVGLGTWQSKpNEVAKAVE--AALKAGYRHIDTAAIYGNEEEVGQG----IKDSGVPREEIFITTKLWCTWH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 87 apEDVPKCVESQLKALQLEYIDLYLIHCPFPFKHQEGSFAPLMENGELAVT-EIAHIDTWRALEKLYKEGKLKALGVSNF 165
Cdd:cd19117 82 --RRVEEALDQSLKKLGLDYVDLYLMHWPVPLDPDGNDFLFKKDDGTKDHEpDWDFIKTWELMQKLPATGKVKAIGVSNF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 166 SCNQLQALYDA--AEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGSpgrkaarpdgvwpEGDPLL-EPIVKQL 242
Cdd:cd19117 160 SIKNLEKLLASpsAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGS-------------TNAPLLkEPVIIKI 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1831516805 243 AAKYHKTAAQILIRHLTQHGISTIPKSVSPDRIVENISTFDfkLSDEDMHTLNSI 297
Cdd:cd19117 227 AKKHGKTPAQVIISWGLQRGYSVLPKSVTPSRIESNFKLFT--LSDEEFKEIDEL 279
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
10-298 |
3.67e-77 |
|
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: 237.94 E-value: 3.67e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 10 TGAQLPLFGLGTW-QVKDEAELTVALRAALDAGYRLIDTAHLYQNEHIIGKVLHEYISSGKLK-REDIFVTSKLPFTAHA 87
Cdd:cd19124 1 SGQTMPVIGMGTAsDPPSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKLWCSDAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 88 PEDVPKCVESQLKALQLEYIDLYLIHcpFPFKHQEGSFAPLMENGELAVTEIAhiDTWRALEKLYKEGKLKALGVSNFSC 167
Cdd:cd19124 81 PDLVLPALKKSLRNLQLEYVDLYLIH--WPVSLKPGKFSFPIEEEDFLPFDIK--GVWEAMEECQRLGLTKAIGVSNFSC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 168 NQLQALYDAAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGSPGRKaarpdgvWPEGDPLLEPIVKQLAAKYH 247
Cdd:cd19124 157 KKLQELLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTK-------WGSNAVMESDVLKEIAAAKG 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1831516805 248 KTAAQILIRHLTQHGISTIPKSVSPDRIVENISTFDFKLSDEDMHTLNSIE 298
Cdd:cd19124 230 KTVAQVSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEIP 280
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
5-302 |
1.32e-75 |
|
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: 234.69 E-value: 1.32e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 5 SIPLNTGAQLPLFGLGTWQVkDEAELTVALRAALDAGYRLIDTAHLYQNEHIIGKVLHEYISSGKLKREDIFVTSKLPFT 84
Cdd:cd19112 2 TITLNSGHKMPVIGLGVWRM-EPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLWNS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 85 AHapEDVPKCVESQLKALQLEYIDLYLIHCPFPFKHQ--EGSFAPLMENGELAV-TEIAHIDTWRALEKLYKEGKLKALG 161
Cdd:cd19112 81 DH--GHVIEACKDSLKKLQLDYLDLYLVHFPVATKHTgvGTTGSALGEDGVLDIdVTISLETTWHAMEKLVSAGLVRSIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 162 VSNFSCNQLQALYDAAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGSPGRKAARpdgvWPEGDPLLEPIVKQ 241
Cdd:cd19112 159 ISNYDIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGGAAANAEW----FGSVSPLDDPVLKD 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831516805 242 LAAKYHKTAAQILIRHLTQHGISTIPKSVSPDRIVENISTFDFKLSDEDMHTLNSIETRTR 302
Cdd:cd19112 235 LAKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYR 295
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
14-295 |
3.29e-75 |
|
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: 231.39 E-value: 3.29e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 14 LPLFGLGTWQVKDEaELTVALRAALDAGYRLIDTAHLYQNEHIIGKVLHEYissgKLKREDIFVTSKLPFTAHAPEDVPK 93
Cdd:cd19073 1 IPALGLGTWQLRGD-DCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAES----GVPREDLFITTKVWRDHLRPEDLKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 94 CVESQLKALQLEYIDLYLIHCPFPFKHQEgsfaplmengelavteiahiDTWRALEKLYKEGKLKALGVSNFSCNQLQAL 173
Cdd:cd19073 76 SVDRSLEKLGTDYVDLLLIHWPNPTVPLE--------------------ETLGALKELKEAGKVKSIGVSNFTIELLEEA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 174 YDAAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLgspgrkaARpdgvwpeGDPLLEPIVKQLAAKYHKTAAQI 253
Cdd:cd19073 136 LDISPLPIAVNQVEFHPFLYQAELLEYCRENDIVITAYSPL-------AR-------GEVLRDPVIQEIAEKYDKTPAQV 201
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1831516805 254 LIRHLTQHGISTIPKSVSPDRIVENISTFDFKLSDEDMHTLN 295
Cdd:cd19073 202 ALRWLVQKGIVVIPKASSEDHLKENLAIFDWELTSEDVAKID 243
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
4-297 |
2.36e-74 |
|
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: 231.23 E-value: 2.36e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 4 DSIPLNTGAQLPLFGLGTWQ-VKDEAELTVALRAALDAGYRLIDTAHLYQNEHIIGKVLHEYISSGKLKREDIFVTSKLP 82
Cdd:cd19119 2 ISFKLNTGASIPALGLGTASpHEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 83 FTAHapEDVPKCVESQLKALQLEYIDLYLIHCPFPFKHQEG----SFAPLMENGELAVTEIA-HIDTWRALEKLYKEGKL 157
Cdd:cd19119 82 PTFY--DEVERSLDESLKALGLDYVDLLLVHWPVCFEKDSDdsgkPFTPVNDDGKTRYAASGdHITTYKQLEKIYLDGRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 158 KALGVSNFSCNQLQALYDAAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGSpgrkaarpdgvwpEGDPLLE- 236
Cdd:cd19119 160 KAIGVSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGS-------------HGAPNLKn 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831516805 237 PIVKQLAAKYHKTAAQILIRHLTQHGISTIPKSVSPDRIVENISTfdFKLSDEDMHTLNSI 297
Cdd:cd19119 227 PLVKKIAEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLDDI 285
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
9-303 |
6.71e-73 |
|
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: 227.34 E-value: 6.71e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 9 NTGAQLPLFGLGTWqVKDEAELTVALRAALDAGYRLIDTAHLYQNEHIIGKVLHEYISSGKLKREDIFVTSKLPFTAHAP 88
Cdd:cd19129 1 NGSGAIPALGFGTL-IPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNHRP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 89 EDVPKCVESQLKALQLEYIDLYLIHCPFPFKHQEGSfAPLMENGELAVTE-IAHIDTWRALEKLYKEGKLKALGVSNFSC 167
Cdd:cd19129 80 ERVKPAFEASLKRLQLDYLDLYLIHTPFAFQPGDEQ-DPRDANGNVIYDDgVTLLDTWRAMERLVDEGRCKAIGLSDVSL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 168 NQLQALYDAAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGspgrKAARPdgvwpegDPLLEPIVKQLAAKYH 247
Cdd:cd19129 159 EKLREIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLG----HGMEP-------KLLEDPVITAIARRVN 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1831516805 248 KTAAQILIRHLTQHGISTIPKSVSPDRIVEN--ISTfdfkLSDEDMHTLNS-IETRTRL 303
Cdd:cd19129 228 KTPAQVLLAWAIQRGTALLTTSKTPSRIRENfdIST----LPEDAMREINEgIKTRYRF 282
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
5-291 |
1.57e-71 |
|
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: 224.25 E-value: 1.57e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 5 SIPLNTGAQLPLFGLGTWQVkDEAELTVALRAALDAGYRLIDTAHLYQNEHIIGKVLHEYISSGKLKREDIFVTSKLPFT 84
Cdd:cd19113 2 DIKLNSGYKMPSVGFGCWKL-DNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 85 AHAPEDVPKCVESQLKALQLEYIDLYLIHCPFPFKhqegsFAPLME----------NGELAVTEIAHIDTWRALEKLYKE 154
Cdd:cd19113 81 FHDPKNVETALNKTLSDLKLDYVDLFLIHFPIAFK-----FVPIEEkyppgfycgdGDNFVYEDVPILDTWKALEKLVDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 155 GKLKALGVSNFSCNQLQALYDAAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGsPGRKAARPDGVWPEGDPL 234
Cdd:cd19113 156 GKIKSIGVSNFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFG-PQSFVELNQGRALNTPTL 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1831516805 235 LE-PIVKQLAAKYHKTAAQILIRHLTQHGISTIPKSVSPDRIVENISTFDFKLSDEDM 291
Cdd:cd19113 235 FEhDTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDF 292
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
11-297 |
9.27e-71 |
|
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: 220.59 E-value: 9.27e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 11 GAQLPLFGLGTWQVKDEaELTVALRAALDAGYRLIDTAHLYQNEHIIGKVLHEyisSGkLKREDIFVTSKLPFTAHAPED 90
Cdd:cd19140 5 GVRIPALGLGTYPLTGE-ECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIAA---SG-VPRDELFLTTKVWPDNYSPDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 91 VPKCVESQLKALQLEYIDLYLIHCPfpfkHQEGSFAplmengelavteiahiDTWRALEKLYKEGKLKALGVSNFSCNQL 170
Cdd:cd19140 80 FLASVEESLRKLRTDYVDLLLLHWP----NKDVPLA----------------ETLGALNEAQEAGLARHIGVSNFTVALL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 171 QALYDAAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGSpgrkaarpdgvwpeGDPLLEPIVKQLAAKYHKTA 250
Cdd:cd19140 140 REAVELSEAPLFTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLAR--------------GEVLKDPVLQEIGRKHGKTP 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1831516805 251 AQILIR-HLTQHGISTIPKSVSPDRIVENISTFDFKLSDEDMHTLNSI 297
Cdd:cd19140 206 AQVALRwLLQQEGVAAIPKATNPERLEENLDIFDFTLSDEEMARIAAL 253
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
17-291 |
7.32e-70 |
|
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: 218.64 E-value: 7.32e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 17 FGLGTWQVK-----DEAELTVALRAALDAGYRLIDTAHLYQNEHIIGKVLHEYissgKLKREDIFVTSKLpftAHAPEDV 91
Cdd:cd19120 9 FGTGTAWYKsgdddIQRDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALKES----GVPREDLFITTKV---SPGIKDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 92 PKCVESQLKALQLEYIDLYLIHCPFPFKHQEGSFAplmengelavteiahiDTWRALEKLYKEGKLKALGVSNFSCNQLQ 171
Cdd:cd19120 82 REALRKSLAKLGVDYVDLYLIHSPFFAKEGGPTLA----------------EAWAELEALKDAGLVRSIGVSNFRIEDLE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 172 ALYDAAEVKPANQQVECH--IYWPQQELRALCKKLGVTVTAYAPLGSPGRKAARPdgvwpegdplLEPIVKQLAAKYHKT 249
Cdd:cd19120 146 ELLDTAKIKPAVNQIEFHpyLYPQQPALLEYCREHGIVVSAYSPLSPLTRDAGGP----------LDPVLEKIAEKYGVT 215
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1831516805 250 AAQILIRHLTQHGISTIPKSVSPDRIVENISTFDFKLSDEDM 291
Cdd:cd19120 216 PAQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEV 257
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
5-302 |
2.40e-69 |
|
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: 218.83 E-value: 2.40e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 5 SIPLNTGAQLPLFGLGTWQV-KDEAELTValRAALDAGYRLIDTAHLYQNEHIIGKVLHEYISSGKLKREDIFVTSKLPF 83
Cdd:cd19115 4 TVKLNSGYDMPLVGFGLWKVnNDTCADQV--YNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLWN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 84 TAHAPEDVPKCVESQLKALQLEYIDLYLIHCPFPFKHQEGS--FAP--LMENGELAVTEIAHIDTWRALEKLYKEGKLKA 159
Cdd:cd19115 82 TFHDGERVEPICRKQLADWGIDYFDLFLIHFPIALKYVDPAvrYPPgwFYDGKKVEFSNAPIQETWTAMEKLVDKGLARS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 160 LGVSNFSCNQLQALYDAAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGSPG-----RKAARpdgvwpEGDPL 234
Cdd:cd19115 162 IGVSNFSAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGPQSfleldLPGAK------DTPPL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831516805 235 LE-PIVKQLAAKYHKTAAQILIRHLTQHGISTIPKSVSPDRIVENISTFDFKLSDEDMHTLNSIETRTR 302
Cdd:cd19115 236 FEhDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLR 304
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
15-297 |
4.46e-68 |
|
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: 214.31 E-value: 4.46e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 15 PLFGLGTWQVKDEAELTvALRAALDAGYRLIDTAHLYQNEHIIGKVLHEYISSGKLKREDIFVTSKLPFTAHAPEDVPKC 94
Cdd:cd19128 2 PRLGFGTYKITESESKE-AVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVKEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 95 VESQLKALQLEYIDLYLIHCPFPFKHQE-GSFAPLMENGELAVTEIAhiDTWRALEKLYKEGKLKALGVSNFSCNQLQAL 173
Cdd:cd19128 81 LLITLQDLQLEYLDLFLIHWPLAFDMDTdGDPRDDNQIQSLSKKPLE--DTWRAMEQCVDEKLTKNIGVSNYSTKLLTDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 174 YDAAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGspgrKAARPDGVWPEGDPLLepivKQLAAKYHKTAAQI 253
Cdd:cd19128 159 LNYCKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLG----GSYGDGNLTFLNDSEL----KALATKYNTTPPQV 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1831516805 254 LIR-HLTQ--HGISTIPKSVSPDRIVENISTFDFKLSDEDMHTLNSI 297
Cdd:cd19128 231 IIAwHLQKwpKNYSVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
11-302 |
1.01e-65 |
|
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: 209.34 E-value: 1.01e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 11 GAQLPLFGLGTWQVK-DEAELTValRAALDAGYRLIDTAHLYQNEHIIGKVLHEYISSGKLKREDIFVTSKLPFTAHAPE 89
Cdd:cd19114 1 GDKMPLVGFGTAKIKaNETEEVI--YNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGKD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 90 DVPKCVESQLKALQLEYIDLYLIHCPFPFKHQEGS--FAPLMENGELAVTEIAHI---DTWRALEKLYKEGKLKALGVSN 164
Cdd:cd19114 79 HVREAFDRQLKDYGLDYIDLYLIHFPIPAAYVDPAenYPFLWKDKELKKFPLEQSpmqECWREMEKLVDAGLVRNIGIAN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 165 FSCNQLQALYDAAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGSpgrkaARPDGVWPEGD---PLLE-PIVK 240
Cdd:cd19114 159 FNVQLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGN-----AVYTKVTKHLKhftNLLEhPVVK 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831516805 241 QLAAKYHKTAAQILIRHLTQHGISTIPKSVSPDRIVENISTFDFKLSDEDMHTLNSIETRTR 302
Cdd:cd19114 234 KLADKHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANAR 295
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
6-303 |
1.50e-65 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 208.00 E-value: 1.50e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 6 IPLNTGAQLPLFGLGTWQVKDEaELTVALRAALDAGYRLIDTAHLYQNEHIIGKVLHEyissGKLKREDIFVTSKLPFTA 85
Cdd:PRK11565 7 IKLQDGNVMPQLGLGVWQASNE-EVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKE----ASVAREELFITTKLWNDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 86 HApeDVPKCVESQLKALQLEYIDLYLIHCPFPFKHQegsfaplmengelavteiaHIDTWRALEKLYKEGKLKALGVSNF 165
Cdd:PRK11565 82 HK--RPREALEESLKKLQLDYVDLYLMHWPVPAIDH-------------------YVEAWKGMIELQKEGLIKSIGVCNF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 166 SCNQLQALYDAAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGSPGrkaarpDGVWPEgdpllePIVKQLAAK 245
Cdd:PRK11565 141 QIHHLQRLIDETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGG------KGVFDQ------KVIRDLADK 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1831516805 246 YHKTAAQILIR-HLtQHGISTIPKSVSPDRIVENISTFDFKLSDEDMHTLNSIETRTRL 303
Cdd:PRK11565 209 YGKTPAQIVIRwHL-DSGLVVIPKSVTPSRIAENFDVFDFRLDKDELGEIAKLDQGKRL 266
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
5-303 |
3.34e-61 |
|
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: 196.23 E-value: 3.34e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 5 SIPLNTGAQLPLFGLGTWQVKD-EAELTVAlrAALDAGYRLIDTAHLYQNEHIIGKVlheyISSGKLKREDIFVTSKLPF 83
Cdd:cd19134 2 TVTLNDDNTMPVIGLGVGELSDdEAERSVS--AALEAGYRLIDTAAAYGNEAAVGRA----IAASGIPRGELFVTTKLAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 84 TAHAPEDVPKCVESQLKALQLEYIDLYLIHCPFPfkhQEGSFaplmengelavteiahIDTWRALEKLYKEGKLKALGVS 163
Cdd:cd19134 76 PDQGFTASQAACRASLERLGLDYVDLYLIHWPAG---REGKY----------------VDSWGGLMKLREEGLARSIGVS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 164 NFSCNQLQALYDAAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGSpgrkaarpdgvwpeGDPLLEPIVKQLA 243
Cdd:cd19134 137 NFTAEHLENLIDLTFFTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGV--------------GRLLDNPAVTAIA 202
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 244 AKYHKTAAQILIRHLTQHGISTIPKSVSPDRIVENISTFDFKLSDEDMHTLNSIETRTRL 303
Cdd:cd19134 203 AAHGRTPAQVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDALDGLDDGTRF 262
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
18-297 |
7.93e-60 |
|
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: 193.68 E-value: 7.93e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 18 GLGTWQ------VKDEAELTVALRAALDAGYRLIDTAHLY---QNEHIIGKVLHEYissgKLKREDIFVTSKLPFTAHA- 87
Cdd:pfam00248 2 GLGTWQlgggwgPISKEEALEALRAALEAGINFIDTAEVYgdgKSEELLGEALKDY----PVKRDKVVIATKVPDGDGPw 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 88 -----PEDVPKCVESQLKALQLEYIDLYLIHCPFPFKHQEgsfaplmengelavteiahiDTWRALEKLYKEGKLKALGV 162
Cdd:pfam00248 78 psggsKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIE--------------------ETWDALEELKKEGKIRAIGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 163 SNFSCNQLQALYDAAEVKPANQQVECHIYWP--QQELRALCKKLGVTVTAYAPLGS------------PGRKAARPD--G 226
Cdd:pfam00248 138 SNFDAEQIEKALTKGKIPIVAVQVEYNLLRRrqEEELLEYCKKNGIPLIAYSPLGGglltgkytrdpdKGPGERRRLlkK 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1831516805 227 VWPEGDPLLEpIVKQLAAKYHKTAAQILIRHLTQH--GISTIPKSVSPDRIVENISTFDFKLSDEDMHTLNSI 297
Cdd:pfam00248 218 GTPLNLEALE-ALEEIAKEHGVSPAQVALRWALSKpgVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDEL 289
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
11-291 |
3.69e-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: 183.20 E-value: 3.69e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 11 GAQLPLFGLGTWQV--------KDEAELTVALRAALDAGYRLIDTAHLYQN---EHIIGKVLHEYissgklKREDIFVTS 79
Cdd:cd19072 1 GEEVPVLGLGTWGIgggmskdySDDKKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAIKGF------DREDLFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 80 KL-PFTAHaPEDVPKCVESQLKALQLEYIDLYLIHCPfpfkhqeGSFAPLMEngelavteiahidTWRALEKLYKEGKLK 158
Cdd:cd19072 75 KVsPDHLK-YDDVIKAAKESLKRLGTDYIDLYLIHWP-------NPSIPIEE-------------TLRAMEELVEEGKIR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 159 ALGVSNFSCNQLQALYDAAEVKP--ANqQVECHIY--WPQQELRALCKKLGVTVTAYAPLGSPGRKAARPDgvwpegdpl 234
Cdd:cd19072 134 YIGVSNFSLEELEEAQSYLKKGPivAN-QVEYNLFdrEEESGLLPYCQKNGIAIIAYSPLEKGKLSNAKGS--------- 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1831516805 235 lePIVKQLAAKYHKTAAQILIRHLTQH-GISTIPKSVSPDRIVENISTFDFKLSDEDM 291
Cdd:cd19072 204 --PLLDEIAKKYGKTPAQIALNWLISKpNVIAIPKASNIEHLEENAGALGWELSEEDL 259
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
5-298 |
6.80e-56 |
|
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: 182.42 E-value: 6.80e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 5 SIPLNTGAQLPLFGLGTWQVKDeAELTVALRAALDAGYRLIDTAHLYQNEHIIGkvlhEYISSGKLKREDIFVTSKLPFT 84
Cdd:cd19130 1 SIVLNDGNSIPQLGYGVFKVPP-ADTQRAVATALEVGYRHIDTAAIYGNEEGVG----AAIAASGIPRDELFVTTKLWND 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 85 AHAPEDVPKCVESQLKALQLEYIDLYLIHCPFPFKhqeGSFaplmengelavteiahIDTWRALEKLYKEGKLKALGVSN 164
Cdd:cd19130 76 RHDGDEPAAAFAESLAKLGLDQVDLYLVHWPTPAA---GNY----------------VHTWEAMIELRAAGRTRSIGVSN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 165 FSCNQLQALYDAAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGspgrkaarpdgvwpEGDPLLEPIVKQLAA 244
Cdd:cd19130 137 FLPPHLERIVAATGVVPAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLG--------------QGKLLGDPPVGAIAA 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1831516805 245 KYHKTAAQILIRHLTQHGISTIPKSVSPDRIVENISTFDFKLSDEDMHTLNSIE 298
Cdd:cd19130 203 AHGKTPAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAIDALD 256
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
8-297 |
1.10e-54 |
|
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: 180.51 E-value: 1.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 8 LNTGAQLPLFGLGTWQVK-DEAELTVALRAALDAGYRLIDTAHLYQNEHIIGKVLHEYISSG-KLKREDIFVTSKLPFTA 85
Cdd:cd19122 3 LNNGVKIPAVGFGTFANEgAKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKVWNHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 86 HAPEDVPKCVESQLKALQLEYIDLYLIHCPFPFKHQEGSFAPLMENGELAVTEIAHID---TWRALEKLYKEGKLKALGV 162
Cdd:cd19122 83 HEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAEKNDQRSPKLGPDGKYVILKDLTENpepTWRAMEEIYESGKAKAIGV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 163 SNFSCNQLQALYDAAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGSPGRkaarpdgVWPEGDPLLE-PIVKQ 241
Cdd:cd19122 163 SNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQ-------VPSTGERVSEnPTLNE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1831516805 242 LAAKYHKTAAQILIRHLTQHGISTIPKSVSPDRIVENISTFDfkLSDEDMHTLNSI 297
Cdd:cd19122 236 VAEKGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIE--LSDEDFEAINQV 289
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
9-297 |
3.75e-53 |
|
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: 177.29 E-value: 3.75e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 9 NTGAQLPLFGLGTWQV------KDEAELTVALRAALDAGYRLIDTAHLY---QNEHIIGKVLHEYissgklKREDIFVTS 79
Cdd:COG0667 8 RSGLKVSRLGLGTMTFggpwggVDEAEAIAILDAALDAGINFFDTADVYgpgRSEELLGEALKGR------PRDDVVIAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 80 KLPFTAHA--------PEDVPKCVESQLKALQLEYIDLYLIHCPFPfkhqegsfaplmengelaVTEIAhiDTWRALEKL 151
Cdd:COG0667 82 KVGRRMGPgpngrglsREHIRRAVEASLRRLGTDYIDLYQLHRPDP------------------DTPIE--ETLGALDEL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 152 YKEGKLKALGVSNFSCNQLQALYDAAE--VKPANQQVECHIY--WPQQELRALCKKLGVTVTAYAPLGS------PGRKA 221
Cdd:COG0667 142 VREGKIRYIGVSNYSAEQLRRALAIAEglPPIVAVQNEYSLLdrSAEEELLPAARELGVGVLAYSPLAGglltgkYRRGA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 222 ARPDG-----------VWPEGDPLLEPiVKQLAAKYHKTAAQILIRHLTQHG--ISTIPKSVSPDRIVENISTFDFKLSD 288
Cdd:COG0667 222 TFPEGdraatnfvqgyLTERNLALVDA-LRAIAAEHGVTPAQLALAWLLAQPgvTSVIPGARSPEQLEENLAAADLELSA 300
|
....*....
gi 1831516805 289 EDMHTLNSI 297
Cdd:COG0667 301 EDLAALDAA 309
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
14-291 |
4.08e-49 |
|
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: 164.45 E-value: 4.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 14 LPLFGLGTWQVKDEAeLTVALRAALDAGYRLIDTAHLYQNEHIIGKVLHEyisSGkLKREDIFVTSKLPFTAHAPEDVPK 93
Cdd:cd19139 1 IPAFGLGTFRLKDDV-VIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAE---SG-VPRDELFITTKIWIDNLSKDKLLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 94 CVESQLKALQLEYIDLYLIHCPFPfkhqegsfaplmeNGELAVTEiahidTWRALEKLYKEGKLKALGVSNFSCNQL-QA 172
Cdd:cd19139 76 SLEESLEKLRTDYVDLTLIHWPSP-------------NDEVPVEE-----YIGALAEAKEQGLTRHIGVSNFTIALLdEA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 173 LYDAAEVKPANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGspgrkaarpdgvwpEGDPLLEPIVKQLAAKYHKTAAQ 252
Cdd:cd19139 138 IAVVGAGAIATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLA--------------YGKVLDDPVLAAIAERHGATPAQ 203
|
250 260 270
....*....|....*....|....*....|....*....
gi 1831516805 253 ILIRHLTQHGISTIPKSVSPDRIVENISTFDFKLSDEDM 291
Cdd:cd19139 204 IALAWAMARGYAVIPSSTKREHLRSNLLALDLTLDADDM 242
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
8-295 |
3.56e-47 |
|
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: 160.11 E-value: 3.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 8 LNTGAQLPLFGLGTWQV----KDEAELTVALRAALDAGYRLIDTAHLYQN---EHIIGKVLHEYissgklkREDIFVTSK 80
Cdd:cd19138 5 LPDGTKVPALGQGTWYMgedpAKRAQEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR-------RDKVFLVSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 81 -LPFTAhAPEDVPKCVESQLKALQLEYIDLYLIHCPfpfkhqeGSfAPLMEngelavteiahidTWRALEKLYKEGKLKA 159
Cdd:cd19138 78 vLPSNA-SRQGTVRACERSLRRLGTDYLDLYLLHWR-------GG-VPLAE-------------TVAAMEELKKEGKIRA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 160 LGVSNFSCNQLQALYDAAEVKP-ANQQVECHI------YwpqqELRALCKKLGVTVTAYAPLGSPGRkaarpdgvwPEGD 232
Cdd:cd19138 136 WGVSNFDTDDMEELWAVPGGGNcAANQVLYNLgsrgieY----DLLPWCREHGVPVMAYSPLAQGGL---------LRRG 202
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831516805 233 PLLEPIVKQLAAKYHKTAAQILIR-HLTQHGISTIPKSVSPDRIVENISTFDFKLSDEDMHTLN 295
Cdd:cd19138 203 LLENPTLKEIAARHGATPAQVALAwVLRDGNVIAIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
18-295 |
5.16e-46 |
|
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: 157.77 E-value: 5.16e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 18 GLGTWQVKD----------EAELTVALRAALDAGYRLIDTAHLY---QNEHIIGKVLHEYissgkLKREDIFVTSKLP-- 82
Cdd:cd19093 6 GLGTWQWGDrlwwgygeygDEDLQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFLKEL-----GDRDEVVIATKFApl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 83 FTAHAPEDVPKCVESQLKALQLEYIDLYLIHCPFPFKHQEGSFaplmengelavteiahidtWRALEKLYKEGKLKALGV 162
Cdd:cd19093 81 PWRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSQIEAL-------------------MDGLADAVEEGLVRAVGV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 163 SNFSCNQLQALYDAAE---VKPANQQVECHI--YWP-QQELRALCKKLGVTVTAYAPLG--------SPGRKAARPDG-- 226
Cdd:cd19093 142 SNYSADQLRRAHKALKergVPLASNQVEYSLlyRDPeQNGLLPACDELGITLIAYSPLAqglltgkySPENPPPGGRRrl 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1831516805 227 ----VWPEGDPLLEpIVKQLAAKYHKTAAQILIRHLTQHGISTIPKSVSPDRIVENISTFDFKLSDEDMHTLN 295
Cdd:cd19093 222 fgrkNLEKVQPLLD-ALEEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
18-297 |
3.40e-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: 3.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 18 GLGTWQ--------VKDEAELTVALRAALDAGYRLIDTAHLYQN---EHIIGKVLheyissgKLKREDIFVTSKLPFTAH 86
Cdd:cd19085 5 GLGCWQfgggywwgDQDDEESIATIHAALDAGINFFDTAEAYGDghsEEVLGKAL-------KGRRDDVVIATKVSPDNL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 87 APEDVPKCVESQLKALQLEYIDLYLIHCPFPFKHqegsFAPLMEngelavteiahidtwrALEKLYKEGKLKALGVSNFS 166
Cdd:cd19085 78 TPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVP----LEETME----------------ALEKLKEEGKIRAIGVSNFG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 167 CNQLQALYDAAEVKpANqQVECHIYW--PQQELRALCKKLGVTVTAYAPLGS--------------PGRKAAR-----PD 225
Cdd:cd19085 138 PAQLEEALDAGRID-SN-QLPYNLLWraIEYEILPFCREHGIGVLAYSPLAQglltgkfssaedfpPGDARTRlfrhfEP 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831516805 226 GVWPEGDPLLEpIVKQLAAKYHKTAAQILIRHLTQH-GIST-IPKSVSPDRIVENISTFDFKLSDEDMHTLNSI 297
Cdd:cd19085 216 GAEEETFEALE-KLKEIADELGVTMAQLALAWVLQQpGVTSvIVGARNPEQLEENAAAVDLELSPSVLERLDEI 288
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
18-291 |
8.00e-44 |
|
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: 152.29 E-value: 8.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 18 GLGTWQV-------KDEAELTVALRAALDAGYRLIDTAHLYQN---EHIIGKVLheyissgKLKREDIFVTSKL------ 81
Cdd:cd19084 8 GLGTWAIggtwwgeVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKAL-------KGRRDDVVIATKCglrwdg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 82 -PFTAH--APEDVPKCVESQLKALQLEYIDLYLIHCPFPfkhqegsfaplmengelaVTEIAhiDTWRALEKLYKEGKLK 158
Cdd:cd19084 81 gKGVTKdlSPESIRKEVEQSLRRLQTDYIDLYQIHWPDP------------------NTPIE--ETAEALEKLKKEGKIR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 159 ALGVSNFSCNQLQAlydaaevkpANQQVECHIYWPQ---------QELRALCKKLGVTVTAYAPLGS---PGRkaARPDG 226
Cdd:cd19084 141 YIGVSNFSVEQLEE---------ARKYGPIVSLQPPysmlereieEELLPYCRENGIGVLPYGPLAQgllTGK--YKKEP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 227 VWPEGD----------PLLEPI------VKQLAAKYHKTAAQILIRHLTQH-GISTI---PKsvSPDRIVENISTFDFKL 286
Cdd:cd19084 210 TFPPDDrrsrfpffrgENFEKNleivdkLKEIAEKYGKSLAQLAIAWTLAQpGVTSAivgAK--NPEQLEENAGALDWEL 287
|
....*
gi 1831516805 287 SDEDM 291
Cdd:cd19084 288 TEEEL 292
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
11-295 |
1.91e-42 |
|
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: 147.72 E-value: 1.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 11 GAQLPLFGLGTWQV---------KDEaELTVALRAALDAGYRLIDTAHLY---QNEHIIGKVLHEYissgklKREDIFVT 78
Cdd:cd19137 1 GEKIPALGLGTWGIggfltpdysRDE-EMVELLKTAIELGYTHIDTAEMYgggHTEELVGKAIKDF------PREDLFIV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 79 SKLPFTAHAPEDVPKCVESQLKALQLEYIDLYLIHCPFPfkhqegsfaplmengelavtEIAHIDTWRALEKLYKEGKLK 158
Cdd:cd19137 74 TKVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNP--------------------NIPLEETLSAMAEGVRQGLIR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 159 ALGVSNFSCNQLQALYDAAEVKPANQQVECHIY---WPQQELRALCKKLGVTVTAYAPLgspgrkaARpdGVWPEGDpll 235
Cdd:cd19137 134 YIGVSNFNRRLLEEAISKSQTPIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPL-------RR--GLEKTNR--- 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831516805 236 epIVKQLAAKYHKTAAQILIRHLTQH-GISTIPKSVSPDRIVENISTFDFKLSDEDMHTLN 295
Cdd:cd19137 202 --TLEEIAKNYGKTIAQIALAWLIQKpNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
14-303 |
2.27e-42 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 147.48 E-value: 2.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 14 LPLFGLGTWQVKDEAELTvALRAALDAGYRLIDTAHLYQNEHIIGKVLHEyisSGkLKREDIFVTSKLPFTAHAPEDVPK 93
Cdd:PRK11172 3 IPAFGLGTFRLKDQVVID-SVKTALELGYRAIDTAQIYDNEAAVGQAIAE---SG-VPRDELFITTKIWIDNLAKDKLIP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 94 CVESQLKALQLEYIDLYLIHCPFPfkhqegsfaplmeNGELAVTEIAhidtwRALEKLYKEGKLKALGVSNFSCNQLQAL 173
Cdd:PRK11172 78 SLKESLQKLRTDYVDLTLIHWPSP-------------NDEVSVEEFM-----QALLEAKKQGLTREIGISNFTIALMKQA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 174 YDAAEVKP-ANQQVECHIYWPQQELRALCKKLGVTVTAYAPLGSpgrkaarpdgvwpeGDPLLEPIVKQLAAKYHKTAAQ 252
Cdd:PRK11172 140 IAAVGAENiATNQIELSPYLQNRKVVAFAKEHGIHVTSYMTLAY--------------GKVLKDPVIARIAAKHNATPAQ 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1831516805 253 ILIRHLTQHGISTIPKSVSPDRIVENISTFDFKLSDEDMHTLNSIETRTRL 303
Cdd:PRK11172 206 VILAWAMQLGYSVIPSSTKRENLASNLLAQDLQLDAEDMAAIAALDRNGRL 256
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
18-297 |
2.52e-38 |
|
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: 138.19 E-value: 2.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 18 GLGTWQV-----------KDEAELTVALRAALDAGYRLIDTAHLY---QNEHIIGKVLHEYissgklkREDIFVTSKL-- 81
Cdd:cd19102 5 GLGTWAIggggwgggwgpQDDRDSIAAIRAALDLGINWIDTAAVYglgHSEEVVGRALKGL-------RDRPIVATKCgl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 82 -------PFTAHAPEDVPKCVESQLKALQLEYIDLYLIHCPFPfkhqegsfaplMENGElavteiahiDTWRALEKLYKE 154
Cdd:cd19102 78 lwdeegrIRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDP-----------DEPIE---------EAWGALAELKEE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 155 GKLKALGVSNFSCNQL---QALYDAAEVKPANQQVECHIywpQQELRALCKKLGVTVTAYAPLGS--------PGRKAAR 223
Cdd:cd19102 138 GKVRAIGVSNFSVDQMkrcQAIHPIASLQPPYSLLRRGI---EAEILPFCAEHGIGVIVYSPMQSglltgkmtPERVASL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 224 PDGVWPEGDPLL-EP----------IVKQLAAKYHKTAAQILIRH-LTQHGI-STIPKSVSPDRIVENISTFDFKLSDED 290
Cdd:cd19102 215 PADDWRRRSPFFqEPnlarnlalvdALRPIAERHGRTVAQLAIAWvLRRPEVtSAIVGARRPDQIDETVGAADLRLTPEE 294
|
....*..
gi 1831516805 291 MHTLNSI 297
Cdd:cd19102 295 LAEIEAL 301
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
17-216 |
6.71e-36 |
|
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications. Members have very distinct functions and include the prokaryotic 2,5-diketo-D-gluconic acid reductases and beta-keto ester reductases, the eukaryotic aldose reductases, aldehyde reductases, hydroxysteroid dehydrogenases, steroid 5beta-reductases, potassium channel beta-subunits, and aflatoxin aldehyde reductases, among others.
Pssm-ID: 381296 [Multi-domain] Cd Length: 232 Bit Score: 129.56 E-value: 6.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 17 FGLGTWQV---KDEAELTVALRAALDAGYRLIDTAHLY---QNEHIIGKVLHEYIssgklKREDIFVTSKLPFTAHA--- 87
Cdd:cd06660 3 LGLGTMTFggdGDEEEAFALLDAALEAGGNFFDTADVYgdgRSERLLGRWLKGRG-----NRDDVVIATKGGHPPGGdps 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 88 -----PEDVPKCVESQLKALQLEYIDLYLIHCPFPfkhqegsfaplmengelaVTEIAhiDTWRALEKLYKEGKLKALGV 162
Cdd:cd06660 78 rsrlsPEHIRRDLEESLRRLGTDYIDLYYLHRDDP------------------STPVE--ETLEALNELVREGKIRYIGV 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831516805 163 SNFSCNQLQALYDAAEVKPANQ----QVECHIYWPQ---QELRALCKKLGVTVTAYAPLGS 216
Cdd:cd06660 138 SNWSAERLAEALAYAKAHGLPGfaavQPQYSLLDRSpmeEELLDWAEENGLPLLAYSPLAR 198
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
18-216 |
1.53e-31 |
|
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: 118.35 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 18 GLGTWQV-------KDEAELTVALRAALDAGYRLIDTAHLYQN---EHIIGKVLHEyissgklKREDIFVTSKLPFTAHA 87
Cdd:cd19086 7 GFGTWGLggdwwgdVDDAEAIRALRAALDLGINFFDTADVYGDghsERLLGKALKG-------RRDKVVIATKFGNRFDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 88 ---------PEDVPKCVESQLKALQLEYIDLYLIHCPFPfkhqegsfaPLMENGELavteiahidtWRALEKLYKEGKLK 158
Cdd:cd19086 80 gperpqdfsPEYIREAVEASLKRLGTDYIDLYQLHNPPD---------EVLDNDEL----------FEALEKLKQEGKIR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831516805 159 ALGVSnfscnqlqaLYDAAEVKPANQQVEC----HIY-----WPQQELRALCKKLGVTVTAYAPLGS 216
Cdd:cd19086 141 AYGVS---------VGDPEEALAALRRGGIdvvqVIYnlldqRPEEELFPLAEEHGVGVIARVPLAS 198
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
9-308 |
6.31e-31 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 119.54 E-value: 6.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 9 NTGAQLPLFGLGTW--QVKDEAELTVALRAALDAGYRLIDTAHLY-QNEHIIGKVLHEYissgklkREDIFVTSKLPFTA 85
Cdd:COG1453 8 KTGLEVSVLGFGGMrlPRKDEEEAEALIRRAIDNGINYIDTARGYgDSEEFLGKALKGP-------RDKVILATKLPPWV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 86 HAPEDVPKCVESQLKALQLEYIDLYLIHCPfpfkHQEGSFAPLMENGELavteiahidtWRALEKLYKEGKLKALGvsnF 165
Cdd:COG1453 81 RDPEDMRKDLEESLKRLQTDYIDLYLIHGL----NTEEDLEKVLKPGGA----------LEALEKAKAEGKIRHIG---F 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 166 SC-NQLQALYDAAEVKP---ANQQVeCHIYWPQQELRAL---CKKLGVTVTAYAPLGSpGRKAARPdgvwpegdpllEPI 238
Cdd:COG1453 144 SThGSLEVIKEAIDTGDfdfVQLQY-NYLDQDNQAGEEAleaAAEKGIGVIIMKPLKG-GRLANPP-----------EKL 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831516805 239 VKQLAAKYhkTAAQILIRHLTQH-GISTIpkSV---SPDRIVENISTFD--FKLSDEDMHTLNSIETRTRLFIADF 308
Cdd:COG1453 211 VELLCPPL--SPAEWALRFLLSHpEVTTV--LSgmsTPEQLDENLKTADnlEPLTEEELAILERLAEELGELLKDF 282
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
26-291 |
5.06e-30 |
|
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: 115.78 E-value: 5.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 26 DEAELTVALRAALDAGYRLIDTAHLYQ---NEHIIGKVLheyissgKLKREDIFVTSKLPFTAHA----------PEDVP 92
Cdd:cd19076 30 DEEESIATLHRALELGVTFLDTADMYGpgtNEELLGKAL-------KDRRDEVVIATKFGIVRDPgsgfrgvdgrPEYVR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 93 KCVESQLKALQLEYIDLYLIHCPFPfkhqegsfaplmengelaVTEIAhiDTWRALEKLYKEGKLKALGVSNFSCNQLQA 172
Cdd:cd19076 103 AACEASLKRLGTDVIDLYYQHRVDP------------------NVPIE--ETVGAMAELVEEGKVRYIGLSEASADTIRR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 173 lydAAEVKP-ANQQVEchiY--W---PQQELRALCKKLGVTVTAYAPLgspGR-----KAARPDGVwPEGD--------- 232
Cdd:cd19076 163 ---AHAVHPiTAVQSE---YslWtrdIEDEVLPTCRELGIGFVAYSPL---GRgfltgAIKSPEDL-PEDDfrrnnprfq 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831516805 233 --------PLLEPIvKQLAAKYHKTAAQILIRHLTQHG--ISTIPKSVSPDRIVENISTFDFKLSDEDM 291
Cdd:cd19076 233 genfdknlKLVEKL-EAIAAEKGCTPAQLALAWVLAQGddIVPIPGTKRIKYLEENVGALDVVLTPEEL 300
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
11-287 |
8.34e-30 |
|
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: 114.24 E-value: 8.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 11 GAqLPLFGLGTWQV-KDEAELTVALRAALDAGYRLIDTAHLY---QNEHIIGKVLHEYissgklkREDIFVTSKLPFT-- 84
Cdd:cd19088 7 GA-MRLTGPGIWGPpADREEAIAVLRRALELGVNFIDTADSYgpdVNERLIAEALHPY-------PDDVVIATKGGLVrt 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 85 -------AHAPEDVPKCVESQLKALQLEYIDLYLIHCPFPfkhqEGSFAplmengelavteiahiDTWRALEKLYKEGKL 157
Cdd:cd19088 79 gpgwwgpDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDP----KVPFE----------------EQLGALAELQDEGLI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 158 KALGVSNFSCNQLQALYDAAEV-------KPANQQVEchiywpqqELRALCKKLGVTVTAYAPLGspGRKAARPDGvwpe 230
Cdd:cd19088 139 RHIGLSNVTVAQIEEARAIVRIvsvqnryNLANRDDE--------GVLDYCEAAGIAFIPWFPLG--GGDLAQPGG---- 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1831516805 231 gdpllepIVKQLAAKYHKTAAQILIRHLTQHG--ISTIPKSVSPDRIVENISTFDFKLS 287
Cdd:cd19088 205 -------LLAEVAARLGATPAQVALAWLLARSpvMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
18-297 |
1.67e-29 |
|
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: 114.82 E-value: 1.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 18 GLGTWQVK--------DEAELTVALRAALDAGYRLIDTAHLY---QNEHIIGKVLHEYissgklKREDIFVTSK--LPFT 84
Cdd:cd19083 15 GLGTNAVGghnlypnlDEEEGKDLVREALDNGVNLLDTAFIYglgRSEELVGEVLKEY------NRNEVVIATKgaHKFG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 85 AH------APEDVPKCVESQLKALQLEYIDLYLIHcpFPFKHqegsfAPLMEngelAVTeiahidtwrALEKLYKEGKLK 158
Cdd:cd19083 89 GDgsvlnnSPEFLRSAVEKSLKRLNTDYIDLYYIH--FPDGE-----TPKAE----AVG---------ALQELKDEGKIR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 159 ALGVSNFSCNQLQA-----LYDA--AEVKPANQQVECHIYwpqqelrALCKKLGVTVTAYAPL------GSPGRKAARPD 225
Cdd:cd19083 149 AIGVSNFSLEQLKEankdgYVDVlqGEYNLLQREAEEDIL-------PYCVENNISFIPYFPLasgllaGKYTKDTKFPD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 226 GVWPEGDPL---------LEPI--VKQLAAKYHKTAAQILIR-HLTQHGIST-IPKSVSPDRIVENISTFDFKLSDEDMH 292
Cdd:cd19083 222 NDLRNDKPLfkgerfsenLDKVdkLKSIADEKGVTVAHLALAwYLTRPAIDVvIPGAKRAEQVIDNLKALDVTLTEEEIA 301
|
....*
gi 1831516805 293 TLNSI 297
Cdd:cd19083 302 FIDAL 306
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
9-296 |
3.53e-29 |
|
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: 113.91 E-value: 3.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 9 NTGAQLPLFGLGTWQV--------KDEAELTVALRAALDAGYRLIDTAHLYQN---EHIIGKVLheyissgKLKREDIFV 77
Cdd:cd19149 6 KSGIEASVIGLGTWAIgggpwwggSDDNESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAI-------KGRRDKVVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 78 TSK-----------LPFTAH--------APEDVPKCVESQLKALQLEYIDLYLIHCPFPfkhqegsfaplmengelaVTE 138
Cdd:cd19149 79 ATKcglrwdreggsFFFVRDgvtvyknlSPESIREEVEQSLKRLGTDYIDLYQTHWQDV------------------ETP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 139 IAhiDTWRALEKLYKEGKLKALGVSNFSCNQLQALYDAAEVkpANQQVECHIYWPQQELRAL--CKKLGVTVTAYAPLGS 216
Cdd:cd19149 141 IE--ETMEALEELKRQGKIRAIGASNVSVEQIKEYVKAGQL--DIIQEKYSMLDRGIEKELLpyCKKNNIAFQAYSPLEQ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 217 ---PGRkaARPDGVWPEGD-----------------PLLEPIvKQLAAKYHKTAAQILIR-HLTQHGIST-IPKSVSPDR 274
Cdd:cd19149 217 gllTGK--ITPDREFDAGDarsgipwfspenrekvlALLEKW-KPLCEKYGCTLAQLVIAwTLAQPGITSaLCGARKPEQ 293
|
330 340
....*....|....*....|..
gi 1831516805 275 IVENISTFDFKLSDEDMHTLNS 296
Cdd:cd19149 294 AEENAKAGDIRLSAEDIATMRS 315
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
18-297 |
1.54e-28 |
|
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: 112.02 E-value: 1.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 18 GLGTWQV-------KDEAELTVALRAALDAGYRLIDTAHLY---QNEHIIGKVLHEYissgkLKREDIFVTSKL------ 81
Cdd:cd19148 8 ALGTWAIggwmwggTDEKEAIETIHKALDLGINLIDTAPVYgfgLSEEIVGKALKEY-----GKRDRVVIATKVglewde 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 82 --PFTAHA-PEDVPKCVESQLKALQLEYIDLYLIHCPFPFkhqegsfAPLMEngelavteiahidTWRALEKLYKEGKLK 158
Cdd:cd19148 83 ggEVVRNSsPARIRKEVEDSLRRLQTDYIDLYQVHWPDPL-------VPIEE-------------TAEALKELLDEGKIR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 159 ALGVSNFSCNQLQALYDAAE---VKPANQQVECHIywpQQELRALCKKLGVTVTAYAPL--GSPGRKaARPDGVWPEGD- 232
Cdd:cd19148 143 AIGVSNFSPEQMETFRKVAPlhtVQPPYNLFEREI---EKDVLPYARKHNIVTLAYGALcrGLLSGK-MTKDTKFEGDDl 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 233 ----PLL-EPIVKQ-LAA----------KYHKTAAQILIRHLTQHGISTIP--KSVSPDRIVENISTFDFKLSDEDMHTL 294
Cdd:cd19148 219 rrtdPKFqEPRFSQyLAAveeldklaqeRYGKSVIHLAVRWLLDQPGVSIAlwGARKPEQLDAVDEVFGWSLNDEDMKEI 298
|
...
gi 1831516805 295 NSI 297
Cdd:cd19148 299 DAI 301
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
18-290 |
6.83e-28 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 110.24 E-value: 6.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 18 GLGTWQvKDEAELTVALRAALDAGYRLIDTAHLY---QNEHIIGKVLHEyissGKLKREDIFVTSK--LPFTAHAPEDVP 92
Cdd:COG4989 22 RLGEWD-LSPAEAAALIEAALELGITTFDHADIYggyTCEALFGEALKL----SPSLREKIELQTKcgIRLPSEARDNRV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 93 K-----------CVESQLKALQLEYIDLYLIHCPfpfkhqegsfAPLMENGELAvteiahidtwRALEKLYKEGKLKALG 161
Cdd:COG4989 97 KhydtskehiiaSVEGSLRRLGTDYLDLLLLHRP----------DPLMDPEEVA----------EAFDELKASGKVRHFG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 162 VSNFSCNQLQALYDAAEVKPANQQVECHIYWPQ---QELRALCKKLGVTVTAYAPLGSpGRKaarpDGVWPEGDPLLEPI 238
Cdd:COG4989 157 VSNFTPSQFELLQSALDQPLVTNQIELSLLHTDafdDGTLDYCQLNGITPMAWSPLAG-GRL----FGGFDEQFPRLRAA 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1831516805 239 VKQLAAKYHKTAAQILIRHLTQH--GISTIPKSVSPDRIVENISTFDFKLSDED 290
Cdd:COG4989 232 LDELAEKYGVSPEAIALAWLLRHpaGIQPVIGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
17-295 |
8.06e-28 |
|
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: 110.37 E-value: 8.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 17 FGLGTWQ--VKDEAELTVALRAALDAGYRLIDTAHLYQN---EHIIGKVLHEYIssgklKREDIFVTSKLPF-TAHAPED 90
Cdd:cd19079 22 FGDPKWRpwVLDEEESRPIIKRALDLGINFFDTANVYSGgasEEILGRALKEFA-----PRDEVVIATKVYFpMGDGPNG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 91 -------VPKCVESQLKALQLEYIDLYLIHCPFPfkhqegsFAPLMEngelavteiahidTWRALEKLYKEGKLKALGVS 163
Cdd:cd19079 97 rglsrkhIMAEVDASLKRLGTDYIDLYQIHRWDY-------ETPIEE-------------TLEALHDVVKSGKVRYIGAS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 164 NFSCNQLQALYDAAE----VKPANQQVecH---IYwpQQELRA---LCKKLGVTVTAYAPL------GSPGRKAAR---- 223
Cdd:cd19079 157 SMYAWQFAKALHLAEkngwTKFVSMQN--HynlLY--REEEREmipLCEEEGIGVIPWSPLargrlaRPWGDTTERrrst 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 224 ---PDGVWPEGDPLLEPI---VKQLAAKYHKTAAQILIRHLTQHGISTIP--KSVSPDRIVENISTFDFKLSDEDMHTLN 295
Cdd:cd19079 233 tdtAKLKYDYFTEADKEIvdrVEEVAKERGVSMAQVALAWLLSKPGVTAPivGATKLEHLEDAVAALDIKLSEEEIKYLE 312
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
9-290 |
1.06e-27 |
|
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: 109.18 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 9 NTGAQLPLFGLGTWQVKDE----AELTVALRAALDAGYRLIDTAHLY---QNEHIIGKVLHEYISsgklKREDIFVTSK- 80
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADWgesaEELLSLIEAALELGITTFDHADIYgggKCEELFGEALALNPG----LREKIEIQTKc 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 81 ---LPFTAHA---------PEDVPKCVESQLKALQLEYIDLYLIHCPfpfkhqegsfAPLMENGELAvteiahidtwRAL 148
Cdd:cd19092 77 girLGDDPRPgrikhydtsKEHILASVEGSLKRLGTDYLDLLLLHRP----------DPLMDPEEVA----------EAF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 149 EKLYKEGKLKALGVSNFSCNQLQALYDAAEVKPANQQVEC---HIYWPQQELRALCKKLGVTVTAYAPLGspgrkAARPD 225
Cdd:cd19092 137 DELVKSGKVRYFGVSNFTPSQIELLQSYLDQPLVTNQIELsllHTEAIDDGTLDYCQLLDITPMAWSPLG-----GGRLF 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831516805 226 GVWPEGDPLLEPIVKQLAAKYHKTAAQILIRHLTQH--GISTIPKSVSPDRIVENISTFDFKLSDED 290
Cdd:cd19092 212 GGFDERFQRLRAALEELAEEYGVTIEAIALAWLLRHpaRIQPILGTTNPERIRSAVKALDIELTREE 278
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
23-296 |
4.53e-27 |
|
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: 108.09 E-value: 4.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 23 QVKDEAELTVALRAALDAGYRLIDTAHLY---QNEHIIGKVLHEYissgklkREDIFVTSKLPFTAHA-----------P 88
Cdd:cd19078 20 PPPDKEEMIELIRKAVELGITFFDTAEVYgpyTNEELVGEALKPF-------RDQVVIATKFGFKIDGgkpgplgldsrP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 89 EDVPKCVESQLKALQLEYIDLYLIHCPFPfkhqegsfaplmengELAVTEIAhidtwRALEKLYKEGKLKALGVSNFSCN 168
Cdd:cd19078 93 EHIRKAVEGSLKRLQTDYIDLYYQHRVDP---------------NVPIEEVA-----GTMKELIKEGKIRHWGLSEAGVE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 169 QLQAlydAAEVKPANQ-QVECHIYW--PQQELRALCKKLGVTVTAYAPLGSpGRKAAR--PDGVWPEGD----------- 232
Cdd:cd19078 153 TIRR---AHAVCPVTAvQSEYSMMWrePEKEVLPTLEELGIGFVPFSPLGK-GFLTGKidENTKFDEGDdraslprftpe 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831516805 233 ------PLLEpIVKQLAAKYHKTAAQI-LIRHLTQHG-ISTIPKSVSPDRIVENISTFDFKLSDEDMHTLNS 296
Cdd:cd19078 229 aleanqALVD-LLKEFAEEKGATPAQIaLAWLLAKKPwIVPIPGTTKLSRLEENIGAADIELTPEELREIED 299
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
9-297 |
1.67e-26 |
|
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: 106.76 E-value: 1.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 9 NTGAQLPLFGLGTWQV-------KDEAELTVALRAALDAGYRLIDTAHLYQ-NEHIIGKvlheYISSGKLKREDIFVTSK 80
Cdd:cd19144 8 RNGPSVPALGFGAMGLsafygppKPDEERFAVLDAAFELGCTFWDTADIYGdSEELIGR----WFKQNPGKREKIFLATK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 81 L----------PFTAHAPEDVPKCVESQLKALQLEYIDLYlihcpfpFKHQEGSFAPLmENgelavteiahidTWRALEK 150
Cdd:cd19144 84 FgieknvetgeYSVDGSPEYVKKACETSLKRLGVDYIDLY-------YQHRVDGKTPI-EK------------TVAAMAE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 151 LYKEGKLKALGVSNFSCNQLQAlydAAEVKP-ANQQVE-----CHIYWPQQELRALCKKLGVTVTAYAPLGS---PGRKA 221
Cdd:cd19144 144 LVQEGKIKHIGLSECSAETLRR---AHAVHPiAAVQIEyspfsLDIERPEIGVLDTCRELGVAIVAYSPLGRgflTGAIR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 222 ARPDgvWPEGD-----------------PLLEPIvKQLAAKYHKTAAQILIRHLTQHG--ISTIPKSVSPDRIVENISTF 282
Cdd:cd19144 221 SPDD--FEEGDfrrmaprfqaenfpknlELVDKI-KAIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLEENLGAL 297
|
330
....*....|....*
gi 1831516805 283 DFKLSDEDMHTLNSI 297
Cdd:cd19144 298 KVKLTEEEEKEIREI 312
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
9-280 |
2.38e-26 |
|
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: 104.97 E-value: 2.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 9 NTGAQLPLFGLGT-WQVKDEAELtvaLRAALDAGYRLIDTAHLYQN---EHIIGKVLHeyissgKLKREDIFVTSK--LP 82
Cdd:cd19105 8 KTGLKVSRLGFGGgGLPRESPEL---LRRALDLGINYFDTAEGYGNgnsEEIIGEALK------GLRRDKVFLATKasPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 83 FTAHAPEDVPKCVESQLKALQLEYIDLYLIHcpfpfkHQEGSfAPLMENGELAvteiahidtwRALEKLYKEGKLKALGv 162
Cdd:cd19105 79 LDKKDKAELLKSVEESLKRLQTDYIDIYQLH------GVDTP-EERLLNEELL----------EALEKLKKEGKVRFIG- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 163 snFSC-----NQLQAL-----YDAAEVK--PANQqvechiYWPQQELRALCKKLGVTVTAYAPLGSPGRKAARPDGVWPE 230
Cdd:cd19105 141 --FSThdnmaEVLQAAiesgwFDVIMVAynFLNQ------PAELEEALAAAAEKGIGVVAMKTLAGGYLQPALLSVLKAK 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1831516805 231 GDPLlepivkqlaakyhktaAQILIRH-LTQHGIST-IPKSVSPDRIVENIS 280
Cdd:cd19105 213 GFSL----------------PQAALKWvLSNPRVDTvVPGMRNFAELEENLA 248
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
9-297 |
1.73e-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: 1.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 9 NTGAQLPLFGLGT------------WQVKDEAELTVALRAALDAGYRLIDTAHLY---QNEHIIGKVLheyissgKLKRE 73
Cdd:cd19091 8 RSGLKVSELALGTmtfgggggffgaWGGVDQEEADRLVDIALDAGINFFDTADVYsegESEEILGKAL-------KGRRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 74 DIFVTSKLPF-TAHAPEDVP-------KCVESQLKALQLEYIDLYLIHCpfpFKHQegsfAPLMEngelavteiahidTW 145
Cdd:cd19091 81 DVLIATKVRGrMGEGPNDVGlsrhhiiRAVEASLKRLGTDYIDLYQLHG---FDAL----TPLEE-------------TL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 146 RALEKLYKEGKLKALGVSNFSCNQL-QALYDAAE---VKPANQQVechiYWP------QQELRALCKKLGVTVTAYAPL- 214
Cdd:cd19091 141 RALDDLVRQGKVRYIGVSNFSAWQImKALGISERrglARFVALQA----YYSllgrdlEHELMPLALDQGVGLLVWSPLa 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 215 ----------GSPGRKAARPDGVWPEGDPL----LEPIVKQL---AAKYHKTAAQILIRH-LTQHGISTIPKSV-SPDRI 275
Cdd:cd19091 217 ggllsgkyrrGQPAPEGSRLRRTGFDFPPVdrerGYDVVDALreiAKETGATPAQVALAWlLSRPTVSSVIIGArNEEQL 296
|
330 340
....*....|....*....|..
gi 1831516805 276 VENISTFDFKLSDEDMHTLNSI 297
Cdd:cd19091 297 EDNLGAAGLSLTPEEIARLDKV 318
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
9-279 |
5.14e-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: 381326 [Multi-domain] Cd Length: 238 Bit Score: 101.02 E-value: 5.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 9 NTGAQLPLFGLGTWQV--KDEAELTVALRAALDAGYRLIDTAHLYQN-EHIIGKVLheyissgKLKREDIFVTSKlpFTA 85
Cdd:cd19100 6 RTGLKVSRLGFGGGPLgrLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKAL-------KGRRDKVFLATK--TGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 86 HAPEDVPKCVESQLKALQLEYIDLYLIHCPfpfKHQEGSFAPLMENGelavteiahidTWRALEKLYKEGKLKALGvsnF 165
Cdd:cd19100 77 RDYEGAKRDLERSLKRLGTDYIDLYQLHAV---DTEEDLDQVFGPGG-----------ALEALLEAKEEGKIRFIG---I 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 166 SCNQLQALYDAAEVKPanqqVEC----------HIYWPQQELRALCKKLGVTVTAYAPLGspgrkaarpDGVWPEGDPLl 235
Cdd:cd19100 140 SGHSPEVLLRALETGE----FDVvlfpinpagdHIDSFREELLPLAREKGVGVIAMKVLA---------GGRLLSGDPL- 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1831516805 236 epivkqlaakyhkTAAQiLIRH-LTQHGIST-IPKSVSPDRIVENI 279
Cdd:cd19100 206 -------------DPEQ-ALRYaLSLPPVDVvIVGMDSPEELDENL 237
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
9-295 |
4.53e-24 |
|
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: 99.98 E-value: 4.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 9 NTGAQLPLFGLGT----WQVkDEAELTVALRAALDAGYRLIDTAHLY----------QNEHIIGKVLheyisSGKLKRED 74
Cdd:cd19081 4 RTGLSVSPLCLGTmvfgWTA-DEETSFALLDAFVDAGGNFIDTADVYsawvpgnaggESETIIGRWL-----KSRGKRDR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 75 IFVTSKLPFTAHA------PEDVPKCVESQLKALQLEYIDLYLIHCPFPFKHQEgsfaplmengelavteiahiDTWRAL 148
Cdd:cd19081 78 VVIATKVGFPMGPngpglsRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLE--------------------ETLGAL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 149 EKLYKEGKLKALGVSNFSCNQLQALYDAAEVKPANQ----QVECHIYWPQ---QELRALCKKLGVTVTAYAPL------- 214
Cdd:cd19081 138 NDLIRQGKVRYIGASNYSAWRLQEALELSRQHGLPRyvslQPEYNLVDREsfeGELLPLCREEGIGVIPYSPLaggfltg 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 215 ---------GSPGRKAARPDGVWPEGDPLLEpIVKQLAAKYHKTAAQILIRHLTQH-GIST-IPKSVSPDRIVENISTFD 283
Cdd:cd19081 218 kyrseadlpGSTRRGEAAKRYLNERGLRILD-ALDEVAAEHGATPAQVALAWLLARpGVTApIAGARTVEQLEDLLAAAG 296
|
330
....*....|..
gi 1831516805 284 FKLSDEDMHTLN 295
Cdd:cd19081 297 LRLTDEEVARLD 308
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
15-283 |
5.16e-24 |
|
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: 98.40 E-value: 5.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 15 PLFGLGT------WQVKDEAELTVAL-RAALDAGYRLIDTAHLY---QNEHIIGKVLHEYissgklKREDIFVTSKLP-F 83
Cdd:cd19096 1 SVLGFGTmrlpesDDDSIDEEKAIEMiRYAIDAGINYFDTAYGYgggKSEEILGEALKEG------PREKFYLATKLPpW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 84 TAHAPEDVPKCVESQLKALQLEYIDLYLIHCPfpfkhQEGSFAPLMENGELavteiahidtWRALEKLYKEGKLKALGVS 163
Cdd:cd19096 75 SVKSAEDFRRILEESLKRLGVDYIDFYLLHGL-----NSPEWLEKARKGGL----------LEFLEKAKKEGLIRHIGFS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 164 ---------------NFSCNQLQALYdaaeVKPANQQvechiywpQQELRALCKKLGVTVTAYAPLGSpGRKAARPdgvw 228
Cdd:cd19096 140 fhdspellkeildsyDFDFVQLQYNY----LDQENQA--------GRPGIEYAAKKGMGVIIMEPLKG-GGLANNP---- 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1831516805 229 pegdpllePIVKQLAAKYHKTAAQILIRHLTQH-GISTIpkSV---SPDRIVENISTFD 283
Cdd:cd19096 203 --------PEALAILCGAPLSPAEWALRFLLSHpEVTTV--LSgmsTPEQLDENIAAAD 251
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
18-289 |
5.91e-24 |
|
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: 99.20 E-value: 5.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 18 GLGTW-----QVKDEAELTVaLRAALDAGYRLIDTAHLY---QNEHIIGKVLHEYissgklKREDIFVTSKL--PFTAHa 87
Cdd:cd19074 8 SLGTWltfggQVDDEDAKAC-VRKAYDLGINFFDTADVYaagQAEEVLGKALKGW------PRESYVISTKVfwPTGPG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 88 PED-------VPKCVESQLKALQLEYIDLYLIHCPFPfkhqegsFAPLMEngelavteiahidTWRALEKLYKEGKLKAL 160
Cdd:cd19074 80 PNDrglsrkhIFESIHASLKRLQLDYVDIYYCHRYDP-------ETPLEE-------------TVRAMDDLIRQGKILYW 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 161 GVSNFSCNQLQALYDAAE----VKPANQQVECHIYW--PQQELRALCKKLGVTVTAYAPLGS-------------PGRKA 221
Cdd:cd19074 140 GTSEWSAEQIAEAHDLARqfglIPPVVEQPQYNMLWreIEEEVIPLCEKNGIGLVVWSPLAQglltgkyrdgippPSRSR 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831516805 222 ARPDGVWP-----EGDPLLEPI--VKQLAAKYHKTAAQI----LIRHltQHGISTIPKSVSPDRIVENISTFDFKLSDE 289
Cdd:cd19074 220 ATDEDNRDkkrrlLTDENLEKVkkLKPIADELGLTLAQLalawCLRN--PAVSSAIIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
17-283 |
3.15e-22 |
|
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: 94.54 E-value: 3.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 17 FGLGT---WQVKDEAELTVALRAALDAGYRLIDTAHLYQNEHIIG---KVLHEYISSGKlKREDIFVTSKL--PFTAHA- 87
Cdd:cd19082 3 IVLGTadfGTRIDEEEAFALLDAFVELGGNFIDTARVYGDWVERGaseRVIGEWLKSRG-NRDKVVIATKGghPDLEDMs 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 88 -----PEDVPKCVESQLKALQLEYIDLYLIHcpfpfkhqegsfaplMENGELAVTEIahIDTwraLEKLYKEGKLKALGV 162
Cdd:cd19082 82 rsrlsPEDIRADLEESLERLGTDYIDLYFLH---------------RDDPSVPVGEI--VDT---LNELVRAGKIRAFGA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 163 SN--------------------FSCNQLQalYDAAEVKPANQQVEChIYWPQQELRALCKKLGVTVTAYAPLGS---PGR 219
Cdd:cd19082 142 SNwsteriaeanayakahglpgFAASSPQ--WSLARPNEPPWPGPT-LVAMDEEMRAWHEENQLPVFAYSSQARgffSKR 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1831516805 220 KAARPDGVWPEGDPLLEPI-------VKQLAAKYHKTAAQILIRHLTQHGISTIP--KSVSPDRIVENISTFD 283
Cdd:cd19082 219 AAGGAEDDSELRRVYYSEEnferlerAKELAEEKGVSPTQIALAYVLNQPFPTVPiiGPRTPEQLRDSLAAAD 291
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-266 |
1.99e-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: 92.77 E-value: 1.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 17 FGLGTWQVkDEAELTV-----ALRAALDAGYRLIDTAHLYQN---EHIIGKVLHEYISSGKLKREDIFVTSK--LPFTAH 86
Cdd:cd19099 6 LGLGTYRG-DSDDETDeeyreALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGIKRDEVVIVTKagYIPGDG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 87 APEDVPK-------------------------------CVESQLKALQLEYIDLYLIHCPFPF--KHQEGSFAPLMEnge 133
Cdd:cd19099 85 DEPLRPLkyleeklgrglidvadsaglrhcispayledQIERSLKRLGLDTIDLYLLHNPEEQllELGEEEFYDRLE--- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 134 lavteiahiDTWRALEKLYKEGKLKALGVSNFSC----------NQLQALYDAAEVKPANQ------QVECHIYWPQ--- 194
Cdd:cd19099 162 ---------EAFEALEEAVAEGKIRYYGISTWDGfrappalpghLSLEKLVAAAEEVGGDNhhfkviQLPLNLLEPEalt 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 195 ---------QELRALCKKLGVTVTAYAPLGSPGRKAARPDGVWPEGDPLlepivkqlaakyhKTAAQILIRH-LTQHGIS 264
Cdd:cd19099 233 ekntvkgeaLSLLEAAKELGLGVIASRPLNQGQLLGELRLADLLALPGG-------------ATLAQRALQFaRSTPGVD 299
|
..
gi 1831516805 265 TI 266
Cdd:cd19099 300 SA 301
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
26-226 |
3.03e-21 |
|
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: 92.25 E-value: 3.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 26 DEAELTVALRAALDAGYRLIDTAHLYQN---EHIIGKVLHEyissgklKREDIFVTSKLPF-TAHAPED-------VPKC 94
Cdd:cd19087 28 DEETSFAIMDRALDAGINFFDTADVYGGgrsEEIIGRWIAG-------RRDDIVLATKVFGpMGDDPNDrglsrrhIRRA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 95 VESQLKALQLEYIDLYLIHCPFPFkhqegsfAPLMEngelavteiahidTWRALEKLYKEGKLKALGVSNFSCNQL-QAL 173
Cdd:cd19087 101 VEASLRRLQTDYIDLYQMHHFDRD-------TPLEE-------------TLRALDDLVRQGKIRYIGVSNFAAWQIaKAQ 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1831516805 174 YDAAEVKPANQQVECHIY-----WPQQELRALCKKLGVTVTAYAPLGS-----PGRKAARPDG 226
Cdd:cd19087 161 GIAARRGLLRFVSEQPMYnllkrQAELEILPAARAYGLGVIPYSPLAGglltgKYGKGKRPES 223
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
17-216 |
1.39e-20 |
|
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: 90.31 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 17 FGLGTWQV----KDEAELTVALRAALDAGYRLIDTAHLYQN---EHIIGKVlheyissgKLKREDIFVTSKLPF---TAH 86
Cdd:cd19075 5 LGTMTFGSqgrfTTAEAAAELLDAFLERGHTEIDTARVYPDgtsEELLGEL--------GLGERGFKIDTKANPgvgGGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 87 APEDVPKCVESQLKALQLEYIDLYLIHCP---FPFKhqegsfaplmengelavteiahiDTWRALEKLYKEGKLKALGVS 163
Cdd:cd19075 77 SPENVRKQLETSLKRLKVDKVDVFYLHAPdrsTPLE-----------------------ETLAAIDELYKEGKFKEFGLS 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831516805 164 NFSCNQLQALYDAAE----VKPA---------NQQVEchiywpqQELRALCKKLGVTVTAYAPLGS 216
Cdd:cd19075 134 NYSAWEVAEIVEICKengwVLPTvyqgmynaiTRQVE-------TELFPCLRKLGIRFYAYSPLAG 192
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
18-279 |
5.08e-20 |
|
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: 87.68 E-value: 5.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 18 GLGTWQ------VKDEAELTVALRAALDAGYRLIDTAHLYQN-EHIIGKVLheyissGKLKREDIFVTSKL--------P 82
Cdd:cd19095 4 GLGTSGigrvwgVPSEAEAARLLNTALDLGINLIDTAPAYGRsEERLGRAL------AGLRRDDLFIATKVgthgeggrD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 83 FTAHAPEDVPKCVESQLKALQLEYIDLYLIHCPfpfkhqegsfAPLMENGELAvteiahidtwRALEKLYKEGKLKALGV 162
Cdd:cd19095 78 RKDFSPAAIRASIERSLRRLGTDYIDLLQLHGP----------SDDELTGEVL----------ETLEDLKAAGKVRYIGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 163 SNFSCNQLQAL----YDA--AEVKPANQQVECHIywpqQELRAlcKKLGV---TVTAYAPLGSPGRKAARPDGVWPEGDP 233
Cdd:cd19095 138 SGDGEELEAAIasgvFDVvqLPYNVLDREEEELL----PLAAE--AGLGVivnRPLANGRLRRRVRRRPLYADYARRPEF 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1831516805 234 LLEPIVkqlaakyhKTAAQILIRHLTQH-GIST-IPKSVSPDRIVENI 279
Cdd:cd19095 212 AAEIGG--------ATWAQAALRFVLSHpGVSSaIVGTTNPEHLEENL 251
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
17-295 |
7.75e-20 |
|
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding members of aldo-keto reductase family 8 member A1-2 (AKR8A1-2), respectively. PLR (EC 1.1.1.65), also called PL reductase (PL-red), catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+).
Pssm-ID: 381303 [Multi-domain] Cd Length: 302 Bit Score: 88.06 E-value: 7.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 17 FGLG----TW---QVKDEaELTVALRAALDAGYRLIDTAHLYQNEHIIG--KVLHEYISSGKLKREDIFVTSK-----LP 82
Cdd:cd19077 8 IGLGlmglTWrpnPTPDE-EAFETMKAALDAGSNLWNGGEFYGPPDPHAnlKLLARFFRKYPEYADKVVLSVKggldpDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 83 FTAHA-PEDVPKCVESQLKAL-QLEYIDLYlihcpfpfkhqegsfaplmengelavtEIAHID-------TWRALEKLYK 153
Cdd:cd19077 87 LRPDGsPEAVRKSIENILRALgGTKKIDIF---------------------------EPARVDpnvpieeTIKALKELVK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 154 EGKLKALGVSNFSCNQLQAlydAAEVKP-ANQQVECHIyW----PQQELRALCKKLGVTVTAYAPLGS---PGRKAARPD 225
Cdd:cd19077 140 EGKIRGIGLSEVSAETIRR---AHAVHPiAAVEVEYSL-FsreiEENGVLETCAELGIPIIAYSPLGRgllTGRIKSLAD 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 226 GvwPEGD-----------------PLLEpIVKQLAAKYHKTAAQI---LIRHLTQHGISTIPKSVSPDRIVENISTFDFK 285
Cdd:cd19077 216 I--PEGDfrrhldrfngenfeknlKLVD-ALQELAEKKGCTPAQLalaWILAQSGPKIIPIPGSTTLERVEENLKAANVE 292
|
330
....*....|
gi 1831516805 286 LSDEDMHTLN 295
Cdd:cd19077 293 LTDEELKEIN 302
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
17-295 |
2.37e-19 |
|
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: 86.89 E-value: 2.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 17 FGLGTWQVKDEAELTVALRAALDAGYRLIDTAHLYQN---EHIIGkvlhEYISSgklKREDIFVTSKLPFTAHaPEDVPK 93
Cdd:cd19080 20 FGTEWGWGADREEARAMFDAYVEAGGNFIDTANNYTNgtsERLLG----EFIAG---NRDRIVLATKYTMNRR-PGDPNA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 94 C----------VESQLKALQLEYIDLYLIHcpfpfkhqegsfaplMENGELAVTEIAhidtwRALEKLYKEGKLKALGVS 163
Cdd:cd19080 92 GgnhrknlrrsVEASLRRLQTDYIDLLYVH---------------AWDFTTPVEEVM-----RALDDLVRAGKVLYVGIS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 164 NF------SCNQLQALYDAAevKPANQQVEchiyW------PQQELRALCKKLGVTVTAYAPLGS--------PG-RKAA 222
Cdd:cd19080 152 DTpawvvaRANTLAELRGWS--PFVALQIE----YsllertPERELLPMARALGLGVTPWSPLGGglltgkyqRGeEGRA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 223 RPDGVWPEGDPLLEP-------IVKQLAAKYHKTAAQILIRHLTQHGISTIPkSVSPDRI---VENISTFDFKLSDEDMH 292
Cdd:cd19080 226 GEAKGVTVGFGKLTErnwaivdVVAAVAEELGRSAAQVALAWVRQKPGVVIP-IIGARTLeqlKDNLGALDLTLSPEQLA 304
|
...
gi 1831516805 293 TLN 295
Cdd:cd19080 305 RLD 307
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
18-289 |
3.58e-19 |
|
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: 85.68 E-value: 3.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 18 GLGT------WQVKDEAELTVALRAALDAGYRLIDTAHLYQN-EHIIGKVLHEYissgklKREDIFVTSKL-----PFTA 85
Cdd:cd19090 4 GLGTaglggvFGGVDDDEAVATIRAALDLGINYIDTAPAYGDsEERLGLALAEL------PREPLVLSTKVgrlpeDTAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 86 HAPEDVPKCVESQLKALQLEYIDLYLIHCPFPFKHQEGsfapLMENGELavteiahidtwRALEKLYKEGKLKALGVsnf 165
Cdd:cd19090 78 YSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDI----LAPGGAL-----------EALLELKEEGLIKHIGL--- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 166 SCNQLQAL--------YDAAEV----KPANQQVEchiywpqQELRALCKKLGVTVTAYAPLG----SPGRKAARPDGVWP 229
Cdd:cd19090 140 GGGPPDLLrraietgdFDVVLTanryTLLDQSAA-------DELLPAAARHGVGVINASPLGmgllAGRPPERVRYTYRW 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831516805 230 EGDPLLEPI--VKQLAAKYHKTAAQILIRHLTQH-GISTIPKSVS-PDRIVENISTFDFKLSDE 289
Cdd:cd19090 213 LSPELLDRAkrLYELCDEHGVPLPALALRFLLRDpRISTVLVGASsPEELEQNVAAAEGPLPEE 276
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
20-266 |
3.72e-17 |
|
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: 80.77 E-value: 3.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 20 GTWQVKDEAELTVALRAALDAGYRLIDTAHLY---QNEHIIGKVLHEyissgklKREDIFVTSKLPFTAHAPEDVPKC-- 94
Cdd:cd19104 24 GLMGRTTREEQIAAVRRALDLGINFFDTAPSYgdgKSEENLGRALKG-------LPAGPYITTKVRLDPDDLGDIGGQie 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 95 --VESQLKALQLEYIDLYLIHcpfpfkHQEGSFAPLMENGELAVTEIAH-IDTWRALEKLYKEGKLKALGVSNF----SC 167
Cdd:cd19104 97 rsVEKSLKRLKRDSVDLLQLH------NRIGDERDKPVGGTLSTTDVLGlGGVADAFERLRSEGKIRFIGITGLgnppAI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 168 NQL---------QALYD-----AAEVKPANqqvechiyWPQQELR---ALCKKLGVTVTAYAPL--GSPGRKAARPDGVW 228
Cdd:cd19104 171 RELldsgkfdavQVYYNllnpsAAEARPRG--------WSAQDYGgiiDAAAEHGVGVMGIRVLaaGALTTSLDRGREAP 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1831516805 229 PEGDPLLEP------IVKQLAAKYHKTAAQILIRH-LTQHGISTI 266
Cdd:cd19104 243 PTSDSDVAIdfrraaAFRALAREWGETLAQLAHRFaLSNPGVSTV 287
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-296 |
1.06e-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: 381329 [Multi-domain] Cd Length: 299 Bit Score: 79.30 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 14 LPLFGLGTW----------QVK----DEAELTVALRAALDAGYRLIDTAHLY---QNEHIIGKVLHEYissgklKREDIF 76
Cdd:cd19103 4 LPKIALGTWswgsggaggdQVFgnhlDEDTLKAVFDKAMAAGLNLWDTAAVYgmgASEKILGEFLKRY------PREDYI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 77 VTSKL-PFTAHAPED-VPKCVESQLKALQLEYIDLYLIHCPfpfkhqegsfaplmengelavteiAHIDTWRA-LEKLYK 153
Cdd:cd19103 78 ISTKFtPQIAGQSADpVADMLEGSLARLGTDYIDIYWIHNP------------------------ADVERWTPeLIPLLK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 154 EGKLKALGVSNFS---CNQLQALYDAAEVKPAnqQVECH---IYWPQQELRAL--CKKLGVTVTAYAPL------GSPGR 219
Cdd:cd19103 134 SGKVKHVGVSNHNlaeIKRANEILAKAGVSLS--AVQNHyslLYRSSEEAGILdyCKENGITFFAYMVLeqgalsGKYDT 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 220 KAARPDG---------VWPEGDPLLePIVKQLAAKYHKTAAQILIRHLTQHGISTIPKSVSPDRIVENISTFDFKLSDED 290
Cdd:cd19103 212 KHPLPEGsgraetynpLLPQLEELT-AVMAEIGAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDDE 290
|
....*.
gi 1831516805 291 MHTLNS 296
Cdd:cd19103 291 IKELEQ 296
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
25-294 |
1.27e-16 |
|
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: 79.01 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 25 KDEAELTVALRAALDAGYRLIDTAHLY---QNEHIIGKVLHEYIssgklkREDIFVTSKLPFTAHA---------PEDVP 92
Cdd:cd19145 30 KPEEEGIALIHHAFNSGVTFLDTSDIYgpnTNEVLLGKALKDGP------REKVQLATKFGIHEIGgsgvevrgdPAYVR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 93 KCVESQLKALQLEYIDLYlihcpfpFKHQEGSFAPLmengelavtEIahidTWRALEKLYKEGKLKALGVSNFSCNQLQA 172
Cdd:cd19145 104 AACEASLKRLDVDYIDLY-------YQHRIDTTVPI---------EI----TMGELKKLVEEGKIKYIGLSEASADTIRR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 173 lydAAEVKPANQ-QVECHIyWP---QQELRALCKKLGVTVTAYAPLGSpGRKAARPDGV-WPEGDPLLEPI--------- 238
Cdd:cd19145 164 ---AHAVHPITAvQLEWSL-WTrdiEEEIIPTCRELGIGIVPYSPLGR-GFFAGKAKLEeLLENSDVRKSHprfqgenle 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831516805 239 --------VKQLAAKYHKTAAQILIRHLTQHG--ISTIPKSVSPDRIVENISTFDFKLSDEDMHTL 294
Cdd:cd19145 239 knkvlyerVEALAKKKGCTPAQLALAWVLHQGedVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
9-297 |
1.15e-15 |
|
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: 76.48 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 9 NTGAQLPLFGLGTW-----QVkDEAELTVALRAALDAGYRLIDTAHLYQN---EHIIGKVLHEyissGKLKREDIFVTSK 80
Cdd:cd19143 8 RSGLKVSALSFGSWvtfgnQV-DVDEAKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIKE----LGWPRSDYVVSTK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 81 LPFTAHAPED----------VPKCVESqLKALQLEYIDLYLIHCPFPfkhqegsFAPLMEngelavteiahidTWRALEK 150
Cdd:cd19143 83 IFWGGGGPPPndrglsrkhiVEGTKAS-LKRLQLDYVDLVFCHRPDP-------ATPIEE-------------TVRAMND 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 151 LYKEGKLKALGVSNFSCNQLQALYDAAE----VKPANQQVECHIYWPQ---QELRALCKKLGVTVTAYAPLGS------- 216
Cdd:cd19143 142 LIDQGKAFYWGTSEWSAQQIEEAHEIADrlglIPPVMEQPQYNLFHRErveVEYAPLYEKYGLGTTTWSPLASglltgky 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 217 -----PGRKAARPDGVW------PEGDPLLEpIVKQL---AAKYHKTAAQILIRHLT--QHGISTIPKSVSPDRIVENIS 280
Cdd:cd19143 222 nngipEGSRLALPGYEWlkdrkeELGQEKIE-KVRKLkpiAEELGCSLAQLAIAWCLknPNVSTVITGATKVEQLEENLK 300
|
330
....*....|....*....
gi 1831516805 281 TFDF--KLSDEDMHTLNSI 297
Cdd:cd19143 301 ALEVlpKLTPEVMEKIEAI 319
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
15-216 |
5.11e-14 |
|
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: 71.24 E-value: 5.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 15 PLFGLGTWQV-----KDEAELTVALRAALDAGYRLIDTAHLY---QNEHIIGKVLHEYissgklKREDIFVTSKL----- 81
Cdd:cd19162 1 PRLGLGAASLgnlarAGEDEAAATLDAAWDAGIRYFDTAPLYglgLSERRLGAALARH------PRAEYVVSTKVgrlle 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 82 --PFTAHAPED---------VPKCVESQLKALQLEYIDLYLIHCPFPFKHQegsfaplmengelAVTeiahiDTWRALEK 150
Cdd:cd19162 75 pgAAGRPAGADrrfdfsadgIRRSIEASLERLGLDRLDLVFLHDPDRHLLQ-------------ALT-----DAFPALEE 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831516805 151 LYKEGKLKALGVsnfSCNQLQALYDAAE------VKPANQqvechiyW------PQQELRALCKKLGVTVTAYAPLGS 216
Cdd:cd19162 137 LRAEGVVGAIGV---GVTDWAALLRAARradvdvVMVAGR-------YtlldrrAATELLPLCAAKGVAVVAAGVFNS 204
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
18-164 |
6.08e-14 |
|
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: 71.44 E-value: 6.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 18 GLGT--WQVKD-EAELTVALRAALDAGYRLIDTAHLY----------QNEHIIGKVLHeyissGKLKREDIFVTSKL--- 81
Cdd:cd19094 5 CLGTmtWGEQNtEAEAHEQLDYAFDEGVNFIDTAEMYpvppspetqgRTEEIIGSWLK-----KKGNRDKVVLATKVagp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 82 ---------PFTAHAPEDVPKCVESQLKALQLEYIDLYLIHCPFPFKHQEGSFAPLMENGELAVTEIAhiDTWRALEKLY 152
Cdd:cd19094 80 gegitwprgGGTRLDRENIREAVEGSLKRLGTDYIDLYQLHWPDRYTPLFGGGYYTEPSEEEDSVSFE--EQLEALGELV 157
|
170
....*....|..
gi 1831516805 153 KEGKLKALGVSN 164
Cdd:cd19094 158 KAGKIRHIGLSN 169
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-175 |
1.12e-13 |
|
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: 69.86 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 17 FGLGTWQVK------------DEAELTVALRAALDAGYRLIDTAHLYQN-EHIIGKVLHEYissgklkrEDIFVTSKLPF 83
Cdd:cd19097 3 LALGTAQFGldygianksgkpSEKEAKKILEYALKAGINTLDTAPAYGDsEKVLGKFLKRL--------DKFKIITKLPP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 84 TAHAPEDVPKCVESQ----LKALQLEYIDLYLIHcpfpfkhqegSFAPLMENGElavteiahiDTWRALEKLYKEGKLKA 159
Cdd:cd19097 75 LKEDKKEDEAAIEASveasLKRLKVDSLDGLLLH----------NPDDLLKHGG---------KLVEALLELKKEGLIRK 135
|
170
....*....|....*.
gi 1831516805 160 LGVSNFSCNQLQALYD 175
Cdd:cd19097 136 IGVSVYSPEELEKALE 151
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
20-297 |
3.39e-13 |
|
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: 69.16 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 20 GTWQV-------KDEAELTVALRAALDAGYRLIDTAHLYQN-EHIIGKVLHEYISSGKLKREDIFVTSKLPFTAHA---P 88
Cdd:cd19101 8 GMWQLsgghggiRDEDAAVRAMAAYVDAGLTTFDCADIYGPaEELIGEFRKRLRRERDAADDVQIHTKWVPDPGELtmtR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 89 EDVPKCVESQLKALQLEYIDLYLIHCpfpFKHQEGSFaplmengelavteiahIDTWRALEKLYKEGKLKALGVSNFSCN 168
Cdd:cd19101 88 AYVEAAIDRSLKRLGVDRLDLVQFHW---WDYSDPGY----------------LDAAKHLAELQEEGKIRHLGLTNFDTE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 169 QLQALYDAAeVKPANQQVECHIY--WPQQELRALCKKLGVTVTAYAPLGSpG----RKAARPDGVWPEGDP--------- 233
Cdd:cd19101 149 RLREILDAG-VPIVSNQVQYSLLdrRPENGMAALCEDHGIKLLAYGTLAG-GllseKYLGVPEPTGPALETrslqkyklm 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831516805 234 ------------LLEpIVKQLAAKYHKTAAQILIRH-LTQHGI-STIPKSVSPDRIVENISTFDFKLSDEDMHTLNSI 297
Cdd:cd19101 227 idewggwdlfqeLLR-TLKAIADKHGVSIANVAVRWvLDQPGVaGVIVGARNSEHIDDNVRAFSFRLDDEDRAAIDAV 303
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
9-215 |
5.09e-13 |
|
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: 68.35 E-value: 5.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 9 NTGAQLPLFGLGT-------WQVkDEAELTVALRAALDAGYRLIDTAHLY---QNEHIIGKVL-----HEYISSGKLKRE 73
Cdd:cd19163 8 KTGLKVSKLGFGAsplggvfGPV-DEEEAIRTVHEALDSGINYIDTAPWYgqgRSETVLGKALkgiprDSYYLATKVGRY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 74 DIFVTSKLPFTAhapEDVPKCVESQLKALQLEYIDLYLIHCPfpfkhqegSFAPLMengELAVTEiahidTWRALEKLYK 153
Cdd:cd19163 87 GLDPDKMFDFSA---ERITKSVEESLKRLGLDYIDIIQVHDI--------EFAPSL---DQILNE-----TLPALQKLKE 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831516805 154 EGKLKALGVSNFSCNQLQALYDAAEVKPANQQVECHiY----WPQQELRALCKKLGVTVTAYAPLG 215
Cdd:cd19163 148 EGKVRFIGITGYPLDVLKEVLERSPVKIDTVLSYCH-YtlndTSLLELLPFFKEKGVGVINASPLS 212
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
15-289 |
2.43e-12 |
|
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: 66.48 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 15 PLFGLGT------WQVKDEAELTVALRAALDAGYRLIDTAHLYQN---EHIIGKVLHEY------ISS--GKLKREDIFV 77
Cdd:cd19152 1 PKLGFGTaplgnlYEAVSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALRELgredyvISTkvGRLLVPLQEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 78 TSKLPFTAHAPED-----------VPKCVESQLKALQLEYIDLYLIHCPFPFKHQEGSfaplmengeLAVTEIAHIDTWR 146
Cdd:cd19152 81 EPTFEPGFWNPLPfdavfdysydgILRSIEDSLQRLGLSRIDLLSIHDPDEDLAGAES---------DEHFAQAIKGAFR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 147 ALEKLYKEGKLKALGVsnfSCNQLQALYDAAE-VKP-----ANQ-----QVEChiywpqQELRALCKKLGVTVTAYAPLG 215
Cdd:cd19152 152 ALEELREEGVIKAIGL---GVNDWEVILRILEeADLdwvmlAGRytlldHSAA------RELLPECEKRGVKVVNAGPFN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 216 SpGRKAARPDGVWPEGDPLLEPIV------KQLAAKYH---KTAA-QILIRHLTQhgISTIPKSVSPDRIVENISTFDFK 285
Cdd:cd19152 223 S-GFLAGGDNFDYYEYGPAPPELIarrdriEALCEQHGvslAAAAlQFALAPPAV--ASVAPGASSPERVEENVALLATE 299
|
....
gi 1831516805 286 LSDE 289
Cdd:cd19152 300 IPAA 303
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
10-214 |
6.88e-11 |
|
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: 62.48 E-value: 6.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 10 TGAQLPLFGLGTWQV----KDEAELTVALRAALDAGYRLIDTAHLYQN---EHIIGKVLHEyissGKLKREDIFVTSKLp 82
Cdd:cd19142 9 SGLRVSNVGLGTWSTfstaISEEQAEEIVTLAYENGINYFDTSDAFTSgqaETELGRILKK----KGWKRSSYIVSTKI- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 83 FTAHAPED-------VPKCVESQLKALQLEYIDLYLIH-----CPfpfkhqegsfaplMEngelavtEIAhidtwRALEK 150
Cdd:cd19142 84 YWSYGSEErglsrkhIIESVRASLRRLQLDYIDIVIIHkadpmCP-------------ME-------EVV-----RAMSY 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831516805 151 LYKEGKLKALGVSNFSCNQLQALYDAAE----VKPANQQVECH--------IYWPQqelraLCKKLGVTVTAYAPL 214
Cdd:cd19142 139 LIDNGLIMYWGTSRWSPVEIMEAFSIARqfncPTPICEQSEYHmfcrekmeLYMPE-----LYNKVGVGLITWSPL 209
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
9-290 |
1.89e-10 |
|
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: 60.73 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 9 NTGAQLPLFGLGTWQ----VKDEAELTVALRAALDAGYRLIDTAHLY-----QNEHIIGKVLHEyisSGKLKREDIFVTS 79
Cdd:cd19089 6 RSGLHLPAISLGLWHnfgdYTSPEEARELLRTAFDLGITHFDLANNYgpppgSAEENFGRILKR---DLRPYRDELVIST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 80 KLPFTAHapeDVP-------KCVESQ----LKALQLEYIDLYLIHCPFPfkhqegsFAPLMEngelavteiahidTWRAL 148
Cdd:cd19089 83 KAGYGMW---PGPygdggsrKYLLASldqsLKRMGLDYVDIFYHHRYDP-------DTPLEE-------------TMTAL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 149 EKLYKEGKLKALGVSNFSCNQLQ---ALYDAAEVKPANQQVECHIY--WPQQELRALCKKLGVTVTAYAPL--------- 214
Cdd:cd19089 140 ADAVRSGKALYVGISNYPGAKARraiALLRELGVPLIIHQPRYSLLdrWAEDGLLEVLEEAGIGFIAFSPLaqglltdky 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 215 ---GSPGRKAARPDGVWPEG--DPLLEPIVKQL---AAKYHKTAAQILIRHLTQH-GISTIPKSVS-PDRIVENISTFD- 283
Cdd:cd19089 220 lngIPPDSRRAAESKFLTEEalTPEKLEQLRKLnkiAAKRGQSLAQLALSWVLRDpRVTSVLIGASsPSQLEDNVAALKn 299
|
....*..
gi 1831516805 284 FKLSDED 290
Cdd:cd19089 300 LDFSEEE 306
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
10-297 |
5.73e-10 |
|
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: 59.71 E-value: 5.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 10 TGAQLPLFGLGTW-----QVKDE-AELTVALraALDAGYRLIDTAHLY---QNEHIIGKVlheyISSGKLKREDIFVTSK 80
Cdd:cd19158 9 SGLRVSCLGLGTWvtfggQITDEmAEHLMTL--AYDNGINLFDTAEVYaagKAEVVLGNI----IKKKGWRRSSLVITTK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 81 LPFTAHAPED-------VPKCVESQLKALQLEYIDLYLIHCPFPFKHQEgsfaplmengelavteiahiDTWRALEKLYK 153
Cdd:cd19158 83 IFWGGKAETErglsrkhIIEGLKASLERLQLEYVDVVFANRPDPNTPME--------------------ETVRAMTHVIN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 154 EGKLKALGVSNFSCNQLQALYDAAE----VKPANQQVECHIYWPQQ---ELRALCKKLGVTVTAYAPLG----------- 215
Cdd:cd19158 143 QGMAMYWGTSRWSSMEIMEAYSVARqfnlIPPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPLAcgivsgkydsg 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 216 -SPGRKAARPDGVWPEGDPLLEPIVKQ---------LAAKYHKTAAQILIRH-LTQHGISTIPKSVS-PDRIVENISTFD 283
Cdd:cd19158 223 iPPYSRASLKGYQWLKDKILSEEGRRQqaklkelqaIAERLGCTLPQLAIAWcLRNEGVSSVLLGASnAEQLMENIGAIQ 302
|
330
....*....|....*.
gi 1831516805 284 F--KLSDEDMHTLNSI 297
Cdd:cd19158 303 VlpKLSSSIVHEIDSI 318
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
10-299 |
2.02e-09 |
|
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: 58.13 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 10 TGAQLPLFGLGTW-----QVKDE-AELTVALraALDAGYRLIDTAHLY---QNEHIIGKVlheyISSGKLKREDIFVTSK 80
Cdd:cd19159 9 SGLRVSCLGLGTWvtfggQISDEvAERLMTI--AYESGVNLFDTAEVYaagKAEVILGSI----IKKKGWRRSSLVITTK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 81 LPFTAHAPED-------VPKCVESQLKALQLEYIDLYlihcpfpFKHQEGSFAPLMEngelavteiahidTWRALEKLYK 153
Cdd:cd19159 83 LYWGGKAETErglsrkhIIEGLKGSLQRLQLEYVDVV-------FANRPDSNTPMEE-------------IVRAMTHVIN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 154 EGKLKALGVSNFSCNQLQALYDAAE----VKPANQQVECHIYWPQQ---ELRALCKKLGVTVTAYAPL-----------G 215
Cdd:cd19159 143 QGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLacgiisgkygnG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 216 SP-GRKAARPDGVW-------PEGDPL------LEPIVKQLAAKYHKTAAQILIRHltqHGISTI-PKSVSPDRIVENIS 280
Cdd:cd19159 223 VPeSSRASLKCYQWlkerivsEEGRKQqnklkdLSPIAERLGCTLPQLAVAWCLRN---EGVSSVlLGSSTPEQLIENLG 299
|
330
....*....|....*....
gi 1831516805 281 TFDFkLSDEDMHTLNSIET 299
Cdd:cd19159 300 AIQV-LPKMTSHVVNEIDN 317
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
1-164 |
5.75e-09 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 56.79 E-value: 5.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 1 MTVDSIPlNTGAQLPLFGLGTW---QVKDEAELTVALRAALDAGYRLIDTAHLYQ----------NEHIIGKVLHeyiSS 67
Cdd:PRK10625 1 MQYHRIP-HSSLEVSTLGLGTMtfgEQNSEADAHAQLDYAVAQGINLIDVAEMYPvpprpetqglTETYIGNWLA---KR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 68 GKlkREDIFVTSKL------------PFTAHAPEDVPKCVESQLKALQLEYIDLYLIHCPfpfKHQEGSFAPLMENGELA 135
Cdd:PRK10625 77 GS--REKLIIASKVsgpsrnndkgirPNQALDRKNIREALHDSLKRLQTDYLDLYQVHWP---QRPTNCFGKLGYSWTDS 151
|
170 180
....*....|....*....|....*....
gi 1831516805 136 VTEIAHIDTWRALEKLYKEGKLKALGVSN 164
Cdd:PRK10625 152 APAVSLLETLDALAEQQRAGKIRYIGVSN 180
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
10-230 |
2.31e-08 |
|
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo sapiens, Rattus norvegicus, and Mus musculus, are founding members of aldo-keto reductase family 6 member A9 (AKR6A9), A12 (AKR6A12), A14 (AKR6A14), respectively. KCAB3B, also called Shaker channel b-subunit 3 (Kvb3), K(+) channel subunit beta-3, or Kv-beta-3, is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. It alters the functional properties of Kv1.5.
Pssm-ID: 381386 [Multi-domain] Cd Length: 325 Bit Score: 54.61 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 10 TGAQLPLFGLGTW-----QVKDEAELTVaLRAALDAGYRLIDTAHLY---QNEHIIGKVLheyiSSGKLKREDIFVTSKL 81
Cdd:cd19160 11 SGLRVSCLGLGTWvtfgsQISDETAEDL-LTVAYEHGVNLFDTAEVYaagKAERTLGNIL----KSKGWRRSSYVVTTKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 82 PFTAHAPED-------VPKCVESQLKALQLEYIDLYlihcpfpFKHQEGSFAPlMEngelavtEIAhidtwRALEKLYKE 154
Cdd:cd19160 86 YWGGQAETErglsrkhIIEGLRGSLDRLQLEYVDIV-------FANRSDPNSP-ME-------EIV-----RAMTYVINQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 155 GKLKALGVSNFSCNQLQALYDAAE----VKPANQQVECHIYWPQQ---ELRALCKKLGVTVTAYAPLGSpGRKAARPDGV 227
Cdd:cd19160 146 GMAMYWGTSRWSAMEIMEAYSVARqfnlIPPVCEQAEYHLFQREKvemQLPELYHKIGVGSVTWSPLAC-GLITGKYDGR 224
|
...
gi 1831516805 228 WPE 230
Cdd:cd19160 225 VPD 227
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
38-165 |
4.73e-08 |
|
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: 53.49 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 38 LDAGYRLIDTAHLY----------QNEHIIGKVLHEyissgKLKREDIFVTSKLPF------------TAHAPEDVPKCV 95
Cdd:cd19752 27 VAAGGNFLDTANNYafwteggvggESERLIGRWLKD-----RGNRDDVVIATKVGAgprdpdggpespEGLSAETIEQEI 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 96 ESQLKALQLEYIDLYLIHCPFPFKHQEgsfaplmengelavteiahiDTWRALEKLYKEGKLKALGVSNF 165
Cdd:cd19752 102 DKSLRRLGTDYIDLYYAHVDDRDTPLE--------------------ETLEAFNELVKAGKVRAIGASNF 151
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
17-297 |
4.37e-07 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 50.74 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 17 FGLGTWQV---------KD-EAELTVaLRAALDAGYRLIDTAHLY----QNEhIIGKVLHEYissgklkREDIFVTSKLP 82
Cdd:PRK10376 20 LGYGAMQLagpgvfgppKDrDAAIAV-LREAVALGVNHIDTSDFYgphvTNQ-LIREALHPY-------PDDLTIVTKVG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 83 FT---------AHAPEDVPKCVESQLKALQLEYIDL------YLIHCPfpfkhQEGSFAPLMEngelavteiahidtwrA 147
Cdd:PRK10376 91 ARrgedgswlpAFSPAELRRAVHDNLRNLGLDVLDVvnlrlmGDGHGP-----AEGSIEEPLT----------------V 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 148 LEKLYKEGKLKALGVSNFSCNQLQALYDAAEVkpanQQVECHIYWPQQELRALCKKLGVTVTAYAPLgspgrkaarpdgv 227
Cdd:PRK10376 150 LAELQRQGLVRHIGLSNVTPTQVAEARKIAEI----VCVQNHYNLAHRADDALIDALARDGIAYVPF------------- 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831516805 228 WPEG--DPLLEPIVKQLAAKYHKTAAQILIRHLTQHG--ISTIPKSVSPDRIVENISTFDFKLSDEDMHTLNSI 297
Cdd:PRK10376 213 FPLGgfTPLQSSTLSDVAASLGATPMQVALAWLLQRSpnILLIPGTSSVAHLRENLAAAELVLSEEVLAELDGI 286
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
27-175 |
8.55e-07 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 50.02 E-value: 8.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 27 EAELTVALRAALDAGYRLIDTAHLYQN---EHIIGKVL-----HEYISSGKLKR------------EDIFVTSkLPFTAH 86
Cdd:cd19161 19 NADADATLDAAWDSGIRYFDTAPMYGHglaEHRLGDFLrekprDEFVLSTKVGRllkparegsvpdPNGFVDP-LPFEIV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 87 ---APEDVPKCVESQLKALQLEYIDLYLIHCPFPFKHQEGS----FAPLMENGelavteiahidtWRALEKLYKEGKLKA 159
Cdd:cd19161 98 ydySYDGIMRSFEDSLQRLGLNRIDILYVHDIGVYTHGDRKerhhFAQLMSGG------------FKALEELKKAGVIKA 165
|
170
....*....|....*....
gi 1831516805 160 --LGVSNF-SCNQLQALYD 175
Cdd:cd19161 166 fgLGVNEVqICLEALDEAD 184
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
10-214 |
1.42e-06 |
|
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: 48.98 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 10 TGAQLPLFGLGTW-----QVKDE-AELTVALraALDAGYRLIDTAHLY---QNEHIIGKVLheyiSSGKLKREDIFVTSK 80
Cdd:cd19141 8 SGLRVSCLGLGTWvtfgsQISDEvAEELVTL--AYENGINLFDTAEVYaagKAEIVLGKIL----KKKGWRRSSYVITTK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 81 LPFTAHAPED-------VPKCVESQLKALQLEYIDLYLIHCPFPFKHQEgsfaplmengelavtEIAhidtwRALEKLYK 153
Cdd:cd19141 82 IFWGGKAETErglsrkhIIEGLKASLERLQLEYVDIVFANRPDPNTPME---------------EIV-----RAFTHVIN 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 154 EGKLKALGVSNFSCNQLQALYDAAE----VKPANQQVECHIYwpQQE-----LRALCKKLGVTVTAYAPL 214
Cdd:cd19141 142 QGMAMYWGTSRWSAMEIMEAYSVARqfnlIPPIVEQAEYHLF--QREkvemqLPELFHKIGVGAMTWSPL 209
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
39-298 |
8.26e-06 |
|
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: 47.03 E-value: 8.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 39 DAGYRLIDTAHLYQ---NEHIIGkvlhEYISSGKlKREDIFVTSK--LPFTAHAPEDVPK------------CVESQLKA 101
Cdd:cd19146 46 EQGGNFIDTANNYQgeeSERWVG----EWMASRG-NRDEMVLATKytTGYRRGGPIKIKSnyqgnhakslrlSVEASLKK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 102 LQLEYIDLYLIHcpfpfkhqegsfaplMENGELAVTEIAHidtwrALEKLYKEGKLKALGVSNFScnqlqalydAAEVKP 181
Cdd:cd19146 121 LQTSYIDILYVH---------------WWDYTTSIPELMQ-----SLNHLVAAGKVLYLGVSDTP---------AWVVSK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 182 ANQQVECH------IY---WP------QQELRALCKKLGVTVTAYAPLGSPGRKAA----RPDGVWPEGDPLLEPIVK-- 240
Cdd:cd19146 172 ANAYARAHgltqfvVYqghWSaafrdfERDILPMCEAEGMALAPWGVLGQGQFRTEeefkRRGRSGRKGGPQTEKERKvs 251
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831516805 241 ----QLAAKYHKTAAQILIRHLTQHGISTIP----KSVspDRIVENISTFDFKLSDEDMHTLNSIE 298
Cdd:cd19146 252 ekleKVAEEKGTAITSVALAYVMHKAPYVFPivggRKV--EHLKGNIEALGISLSDEEIQEIEDAY 315
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
17-163 |
8.87e-06 |
|
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: 46.50 E-value: 8.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 17 FGLGTWQVKDEAELTVALRAALDAGYRLIDTAHLYQN-EHIIGKVLHeyISSGKLKREDIFVTSKLPFTA-----HAPED 90
Cdd:cd19164 23 FSYQYTTDPESIPPVDIVRRALELGIRAFDTSPYYGPsEIILGRALK--ALRDEFPRDTYFIITKVGRYGpddfdYSPEW 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1831516805 91 VPKCVESQLKALQLEYIDLYLIHcPFPFKHQEGSFAPLmengelavteiahidtwRALEKLYKEGKLKALGVS 163
Cdd:cd19164 101 IRASVERSLRRLHTDYLDLVYLH-DVEFVADEEVLEAL-----------------KELFKLKDEGKIRNVGIS 155
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
26-215 |
1.83e-05 |
|
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: 45.60 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 26 DEAELTValRAALDAGYRLIDTAHLYQN---EHIIGKVL-------HEYISSGKLKRediFVTSKLPFTAhapEDVPKCV 95
Cdd:cd19153 33 DEAVAIV--AEAFAAGINHFDTSPYYGAessEAVLGKALaalqvprSSYTVATKVGR---YRDSEFDYSA---ERVRASV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 96 ESQLKALQLEYIDLYLIHcPFPFkhqeGSFAPLMEngelavteiahiDTWRALEKLYKEGKLKALGVSNFScnqLQALYD 175
Cdd:cd19153 105 ATSLERLHTTYLDVVYLH-DIEF----VDYDTLVD------------EALPALRTLKDEGVIKRIGIAGYP---LDTLTR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1831516805 176 AAE-VKPANQQV---ECHIYWPQQEL----RALCKKLGVTVTAYAPLG 215
Cdd:cd19153 165 ATRrCSPGSLDAvlsYCHLTLQDARLesdaPGLVRGAGPHVINASPLS 212
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
9-215 |
5.49e-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: 5.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 9 NTGAQLPLFGLGTWQ-------VKDEAELtvaLRAALDAGYRLIDTAHLY-----QNEHIIGKVLHEYIssgKLKREDIF 76
Cdd:cd19151 7 RSGLKLPAISLGLWHnfgdvdrYENSRAM---LRRAFDLGITHFDLANNYgpppgSAEENFGRILKEDL---KPYRDELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 77 VTSKLPFTAHapeDVP-----------KCVESQLKALQLEYIDLYLIHCPFPFkhqegsfAPLMEngelavteiahidTW 145
Cdd:cd19151 81 ISTKAGYTMW---PGPygdwgskkyliASLDQSLKRMGLDYVDIFYHHRPDPE-------TPLEE-------------TM 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 146 RALEKLYKEGKLKALGVSNfscnqlqalYDAAEVKPANQQVE-----CHIY---------WPQQELRALCKKLGVTVTAY 211
Cdd:cd19151 138 GALDQIVRQGKALYVGISN---------YPPEEAREAAAILKdlgtpCLIHqpkysmfnrWVEEGLLDVLEEEGIGCIAF 208
|
....
gi 1831516805 212 APLG 215
Cdd:cd19151 209 SPLA 212
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
33-298 |
4.61e-04 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 41.30 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 33 ALRAALDAGYRLIDTAHLYQN---EHIIGKVLheyiSSGKLKREDIFVTSK-------LPFTAhapEDVPKCVESQLKAL 102
Cdd:PLN02587 36 SVREAFRLGINFFDTSPYYGGtlsEKVLGKAL----KALGIPREKYVVSTKcgrygegFDFSA---ERVTKSVDESLARL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 103 QLEYIDlyLIHCpfpfkHQegsfaplMENGEL--AVTEiahidTWRALEKLYKEGKLKALGVSNFSCNQLQALYDaaEVK 180
Cdd:PLN02587 109 QLDYVD--ILHC-----HD-------IEFGSLdqIVNE-----TIPALQKLKESGKVRFIGITGLPLAIFTYVLD--RVP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 181 PANQQV---ECHIYWPQQELRALC---KKLGVTVTAYAPLgSPGRKAARPDGVWPEGDPLLEPIVKQLAA----KYHKTA 250
Cdd:PLN02587 168 PGTVDVilsYCHYSLNDSSLEDLLpylKSKGVGVISASPL-AMGLLTENGPPEWHPAPPELKSACAAAAThckeKGKNIS 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1831516805 251 AQILIRHLTQHGISTIPKSV-SPDRIVENIST-FDFKLSDEDMHTLNSIE 298
Cdd:PLN02587 247 KLALQYSLSNKDISTTLVGMnSVQQVEENVAAaTELETSGIDEELLSEVE 296
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
26-164 |
1.24e-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: 40.19 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831516805 26 DEAELTVALRAALDAGYRLIDTAHLYQNEH---IIGkvlhEYISSGKLkREDIFVTSKlpFTAH-------APEDVPKC- 94
Cdd:cd19147 32 DKEQAFELLDAFYEAGGNFIDTANNYQDEQsetWIG----EWMKSRKN-RDQIVIATK--FTTDykayevgKGKAVNYCg 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831516805 95 ---------VESQLKALQLEYIDLYLIHcpfpFKHQEGSFAPLMEngelavteiahidtwrALEKLYKEGKLKALGVSN 164
Cdd:cd19147 105 nhkrslhvsVRDSLRKLQTDWIDILYVH----WWDYTTSIEEVMD----------------SLHILVQQGKVLYLGVSD 163
|
|
| |
