|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
5-301 |
8.84e-180 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381380 [Multi-domain] Cd Length: 303 Bit Score: 498.48 E-value: 8.84e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 5 TASIKLSNGVEMPVIGLGTWQSSPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKELLEEGVVKREELFITTKAWT 84
Cdd:cd19154 1 SASITLSNGVKMPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLWT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 85 HELAPGKLEGGLRESLKKLQLEYVDLYLAHMPAAFNDD----------MSEHIASPVEDVWRQFDAVYKAGLAKAVGVSN 154
Cdd:cd19154 81 HEHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDegesgtmengMSIHDAVDVEDVWRGMEKVYDEGLTKAIGVSN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 155 WNNDQISRALALGLTPVHNSQVELHLYFPQHDHVDFCKKHNISVTSYATLGSPGRVNFTLPTGqkldWAPAPSDLQDQNV 234
Cdd:cd19154 161 FNNDQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSPGRANFTKSTG----VSPAPNLLQDPIV 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17550248 235 LALAEKTHKTPAQVLLRYALDRGCAILPKSIQENRIKENFEVFDFSLTEEDIAKLEESKNSQRLFLQ 301
Cdd:cd19154 237 KAIAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLRLFLF 303
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
13-301 |
5.80e-176 |
|
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: 488.16 E-value: 5.80e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 13 GVEMPVIGLGTWQSSPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKELLEEGVVKREELFITTKAWTHELAPGKL 92
Cdd:cd19111 1 GFPMPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLEFKDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 93 EGGLRESLKKLQLEYVDLYLAHMPAAFNDD----MSEHIASPVEDVWRQFDAVYKAGLAKAVGVSNWNNDQISRALALGL 168
Cdd:cd19111 81 EKSLEKSLENLKLPYVDLYLIHHPCGFVNKkdkgERELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINKILAYAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 169 TPVHNSQVELHLYFPQHDHVDFCKKHNISVTSYATLGSPGRVNFTLptgqkldWAPAPSDLQDQNVLALAEKTHKTPAQV 248
Cdd:cd19111 161 VKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSPGRANQSL-------WPDQPDLLEDPTVLAIAKELDKTPAQV 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 17550248 249 LLRYALDRGCAILPKSIQENRIKENFEVFDFSLTEEDIAKLEESKNSQRLFLQ 301
Cdd:cd19111 234 LLRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMKYFDF 286
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
16-290 |
3.14e-114 |
|
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: 330.21 E-value: 3.14e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 16 MPVIGLGTWQSSPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKELLeegvVKREELFITTKAWTHELAPGKLEGG 95
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESG----VPREELFITTKLWPTDHGYERVREA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 96 LRESLKKLQLEYVDLYLAHMPAAFNDDmseHIASPVEDVWRQFDAVYKAGLAKAVGVSNWNNDQISRALALGLTPVHNSQ 175
Cdd:cd19071 77 LEESLKDLGLDYLDLYLIHWPVPGKEG---GSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAARIKPAVNQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 176 VELHLYFPQHDHVDFCKKHNISVTSYATLGSPGRvnftlptgqkldwapapSDLQDQNVLALAEKTHKTPAQVLLRYALD 255
Cdd:cd19071 154 IELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRR-----------------PLLDDPVLKEIAKKYGKTPAQVLLRWALQ 216
|
250 260 270
....*....|....*....|....*....|....*
gi 17550248 256 RGCAILPKSIQENRIKENFEVFDFSLTEEDIAKLE 290
Cdd:cd19071 217 RGVVVIPKSSNPERIKENLDVFDFELSEEDMAAID 251
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
7-299 |
9.09e-111 |
|
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a founding member of aldo-keto reductase family 2 member E4 (AKR2E4). It is a NADP-dependent oxidoreductase with high 3-dehydroecdysone reductase activity. It may play a role in the regulation of molting and has lower activity with phenylglyoxal and isatin (in vitro). This family also includes 3-dehydroecdysone 3b-reductase from Spodoptera littoralis and Trichoplusia ni, DL-glyceraldehyde reductase from Drosophila melanogaster, aldo-keto reductase from Bombyx mori, which correspond to aldo-keto reductase family 2 member E1, E2, E3 and E5 (AKR2E1/2/3/5), respectively.
Pssm-ID: 381342 [Multi-domain] Cd Length: 292 Bit Score: 323.08 E-value: 9.09e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 7 SIKLSNGVEMPVIGLGTWQSSPAEVIT-AVKTAVKAGYRLIDTASVYQNEEAIGTAIKELLEEGVVKREELFITTKAWTH 85
Cdd:cd19116 2 TIKLNDGNEIPAIALGTWKLKDDEGVRqAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLWNS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 86 ELAPGKLEGGLRESLKKLQLEYVDLYLAHMPAAF---NDDMSEHIASPVE----DVWRQFDAVYKAGLAKAVGVSNWNND 158
Cdd:cd19116 82 YHEREQVEPALRESLKRLGLDYVDLYLIHWPVAFkenNDSESNGDGSLSDidylETWRGMEDLVKLGLTRSIGVSNFNSE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 159 QISRALALGLT-PVHNsQVELHLYFPQHDHVDFCKKHNISVTSYATLGSPGRVNFTLPtgqkldwapaPSDLQDQNVLAL 237
Cdd:cd19116 162 QINRLLSNCNIkPAVN-QIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLVPRGQTNP----------PPRLDDPTLVAI 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17550248 238 AEKTHKTPAQVLLRYALDRGCAILPKSIQENRIKENFEVFDFSLTEEDIAKLEESKNSQRLF 299
Cdd:cd19116 231 AKKYGKTTAQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRVY 292
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
12-299 |
5.90e-110 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 319.69 E-value: 5.90e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 12 NGVEMPVIGLGTWQSSPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKELleeGvVKREELFITTKAWTHELAPGK 91
Cdd:COG0656 1 NGVEIPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAAS---G-VPREELFVTTKVWNDNHGYDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 92 LEGGLRESLKKLQLEYVDLYLAHMPAafnddmsehiASPVEDVWRQFDAVYKAGLAKAVGVSNWNNDQISRALAL-GLTP 170
Cdd:COG0656 77 TLAAFEESLERLGLDYLDLYLIHWPG----------PGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAEtGVKP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 171 VHNsQVELHLYFPQHDHVDFCKKHNISVTSYATLGSpGRVnftlptgqkldwapapsdLQDQNVLALAEKTHKTPAQVLL 250
Cdd:COG0656 147 AVN-QVELHPYLQQRELLAFCREHGIVVEAYSPLGR-GKL------------------LDDPVLAEIAEKHGKTPAQVVL 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 17550248 251 RYALDRGCAILPKSIQENRIKENFEVFDFSLTEEDIAKLEESKNSQRLF 299
Cdd:COG0656 207 RWHLQRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRGERLG 255
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
9-298 |
8.92e-105 |
|
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: 307.74 E-value: 8.92e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 9 KLSNGVEMPVIGLGTWQSSPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKELLEEGVVKREELFITTKAWTHELA 88
Cdd:cd19125 4 KLNTGAKIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLWCTDHA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 89 PGKLEGGLRESLKKLQLEYVDLYLAHMPAAFNDDMS-----EHIASPVEDVWRQFDAVYKAGLAKAVGVSNWNNDQISRA 163
Cdd:cd19125 84 PEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKGAHmpepeEVLPPDIPSTWKAMEKLVDSGKVRAIGVSNFSVKKLEDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 164 LALGLTPVHNSQVELHLYFPQHDHVDFCKKHNISVTSYATLGSPGRVNFTLPTgqkldwapapsdLQDQNVLALAEKTHK 243
Cdd:cd19125 164 LAVARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGTTWVKKNV------------LKDPIVTKVAEKLGK 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 17550248 244 TPAQVLLRYALDRGCAILPKSIQENRIKENFEVFDFSLTEEDIAKLEESKNSQRL 298
Cdd:cd19125 232 TPAQVALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSIEQQRRV 286
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
5-299 |
1.47e-103 |
|
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: 305.60 E-value: 1.47e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 5 TASIKLSNGVEMPVIGLGTWQSSPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKELLEEGVVKREELFITTKAWT 84
Cdd:cd19155 1 RNCVTFNNGEKMPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 85 HELAPGKLEGGLRESLKKLQLEYVDLYLAHMPAAFN---DD---------MSEHIASPVEDVWRQFDAVYKAGLAKAVGV 152
Cdd:cd19155 81 GGNRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLskeDDsgkldptgeHKQDYTTDLLDIWKAMEAQVDQGLTRSIGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 153 SNWNNDQISRALALGLTPVHNSQVELHLYFPQHDHVDFCKKHNISVTSYATLGSPGRVNFTLPTGQKLDWAPAPsdLQDQ 232
Cdd:cd19155 161 SNFNREQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPGAAHFSPGTGSPSGSSPDL--LQDP 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17550248 233 NVLALAEKTHKTPAQVLLRYALDRGCAILPKSIQENRIKENFEVFDFSLTEEDIAKLEESKNSQRLF 299
Cdd:cd19155 239 VVKAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIRGR 305
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
10-300 |
3.10e-97 |
|
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: 289.28 E-value: 3.10e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 10 LSNGVEMPVIGLGTWQSSPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKELLEEG-VVKREELFITTKAWTHELA 88
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPGkAVPREDLFVTSKLWNTKHH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 89 PGKLEGGLRESLKKLQLEYVDLYLAHMPAAF---------NDDMS-EHIASPVEDVWRQFDAVYKAGLAKAVGVSNWNND 158
Cdd:cd19106 81 PEDVEPALRKTLKDLQLDYLDLYLIHWPYAFergdnpfpkNPDGTiRYDSTHYKETWKAMEKLVDKGLVKAIGLSNFNSR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 159 QISRALALG-LTPVHNsQVELHLYFPQHDHVDFCKKHNISVTSYATLGSPGRVnftlptgqkldWAPA--PSDLQDQNVL 235
Cdd:cd19106 161 QIDDILSVArIKPAVL-QVECHPYLAQNELIAHCKARGLVVTAYSPLGSPDRP-----------WAKPdePVLLEEPKVK 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17550248 236 ALAEKTHKTPAQVLLRYALDRGCAILPKSIQENRIKENFEVFDFSLTEEDIAKLEESKNSQRLFL 300
Cdd:cd19106 229 ALAKKYNKSPAQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRYIV 293
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
6-299 |
1.82e-93 |
|
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: 279.30 E-value: 1.82e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 6 ASIKLSNGVEMPVIGLGTWQSSPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKELLEEGVVKREELFITTKAWTH 85
Cdd:cd19123 2 KTLPLSNGDLIPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLWNN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 86 ELAPGKLEGGLRESLKKLQLEYVDLYLAHMPAAF---------NDDMSEHIASPVEDVWRQFDAVYKAGLAKAVGVSNWN 156
Cdd:cd19123 82 SHAPEDVLPALEKTLADLQLDYLDLYLMHWPVALkkgvgfpesGEDLLSLSPIPLEDTWRAMEELVDKGLCRHIGVSNFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 157 NDQISRALALG-LTPVHNsQVELHLYFPQHDHVDFCKKHNISVTSYATLGSPGRvnftlPTGQKLdwAPAPSDLQDQNVL 235
Cdd:cd19123 162 VKKLEDLLATArIKPAVN-QVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDR-----PAAMKA--EGEPVLLEDPVIN 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17550248 236 ALAEKTHKTPAQVLLRYALDRGCAILPKSIQENRIKENFEVFDFSLTEEDIAKLEESKNSQRLF 299
Cdd:cd19123 234 KIAEKHGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHRYV 297
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
16-289 |
1.91e-89 |
|
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like protein is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase similar to Bacillus subtilis glyoxal reductase (YvgN) that reduces glyoxal and methylglyoxal (2-oxopropanal).
Pssm-ID: 381362 [Multi-domain] Cd Length: 262 Bit Score: 267.96 E-value: 1.91e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 16 MPVIGLGTWQ-SSPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKELLEEGVVKREELFITTKAWTHELAPGKLEG 94
Cdd:cd19136 1 MPILGLGTFRlRGEEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 95 GLRESLKKLQLEYVDLYLAHMPAAFNDDMS--EHIASPVEdVWRQFDAVYKAGLAKAVGVSNWNNDQISRALALGLTPVH 172
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWPGVQGLKPSdpRNAELRRE-SWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYCEVPPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 173 NSQVELHLYFPQHDHVDFCKKHNISVTSYATLGSPGrvnftlptgqkldwapaPSDLQDQNVLALAEKTHKTPAQVLLRY 252
Cdd:cd19136 160 VNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGD-----------------LRLLEDPTVLAIAKKYGRTPAQVLLRW 222
|
250 260 270
....*....|....*....|....*....|....*..
gi 17550248 253 ALDRGCAILPKSIQENRIKENFEVFDFSLTEEDIAKL 289
Cdd:cd19136 223 ALQQGIGVIPKSTNPERIAENIKVFDFELSEEDMAEL 259
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
13-315 |
3.35e-86 |
|
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: 261.20 E-value: 3.35e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 13 GVEMPVIGLGTWQSSPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKELLEEGVVKREELFITTKAWTHELAPGKL 92
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEKGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 93 EGGLRESLKKLQLEYVDLYLAHMPAAFN--------DDMSEHIASPVE--DVWRQFDAVYKAGLAKAVGVSNWNNDQISR 162
Cdd:cd19107 81 KGACQKTLSDLKLDYLDLYLIHWPTGFKpgkelfplDESGNVIPSDTTflDTWEAMEELVDEGLVKAIGVSNFNHLQIER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 163 AL---ALGLTPVHNsQVELHLYFPQHDHVDFCKKHNISVTSYATLGSPGRvnftlptgqklDWAPA--PSDLQDQNVLAL 237
Cdd:cd19107 161 ILnkpGLKYKPAVN-QIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDR-----------PWAKPedPSLLEDPKIKEI 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17550248 238 AEKTHKTPAQVLLRYALDRGCAILPKSIQENRIKENFEVFDFSLTEEDIAKLEESKNSQRLFLQDFMTGHPEDAFAAE 315
Cdd:cd19107 229 AAKHNKTTAQVLIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRACALLSCSSHKDYPFHAE 306
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
7-290 |
7.70e-86 |
|
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: 258.46 E-value: 7.70e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 7 SIKLSNGVEMPVIGLGTWQSSPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKelleEGVVKREELFITTKAWTHE 86
Cdd:cd19131 1 TITLNDGNTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIR----ASGVPREELFITTKLWNSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 87 LAPGKLEGGLRESLKKLQLEYVDLYLAHMPAAFNDDMSEhiaspvedVWRQFDAVYKAGLAKAVGVSNWNNDQISRAL-A 165
Cdd:cd19131 77 QGYDSTLRAFDESLRKLGLDYVDLYLIHWPVPAQDKYVE--------TWKALIELKKEGRVKSIGVSNFTIEHLQRLIdE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 166 LGLTPVHNsQVELHLYFPQHDHVDFCKKHNISVTSYATLGSpGRVnftlptgqkldwapapsdLQDQNVLALAEKTHKTP 245
Cdd:cd19131 149 TGVVPVVN-QIELHPRFQQRELRAFHAKHGIQTESWSPLGQ-GGL------------------LSDPVIGEIAEKHGKTP 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 17550248 246 AQVLLRYALDRGCAILPKSIQENRIKENFEVFDFSLTEEDIAKLE 290
Cdd:cd19131 209 AQVVIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELDADDMQAIA 253
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
8-289 |
1.50e-84 |
|
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: 255.19 E-value: 1.50e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 8 IKLSNGVEMPVIGLGTWQ-SSPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKElleeGVVKREELFITTKAWTHE 86
Cdd:cd19133 1 VTLNNGVEMPILGFGVFQiPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKK----SGIPREELFITTKLWIQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 87 LAPGKLEGGLRESLKKLQLEYVDLYLAHMPaaFNDdmsehiaspVEDVWRQFDAVYKAGLAKAVGVSNWNNDQISRALAL 166
Cdd:cd19133 77 AGYEKAKKAFERSLKRLGLDYLDLYLIHQP--FGD---------VYGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLILH 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 167 G-LTPVHNsQVELHLYFPQHDHVDFCKKHNISVTSYATLGSpGRVNFtlptgqkldwapapsdLQDQNVLALAEKTHKTP 245
Cdd:cd19133 146 NeVKPAVN-QIETHPFNQQIEAVEFLKKYGVQIEAWGPFAE-GRNNL----------------FENPVLTEIAEKYGKSV 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 17550248 246 AQVLLRYALDRGCAILPKSIQENRIKENFEVFDFSLTEEDIAKL 289
Cdd:cd19133 208 AQVILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAI 251
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
7-290 |
4.46e-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: 250.61 E-value: 4.46e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 7 SIKLSNGVEMPVIGLGTWQssPAEV-----ITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKELLEEGVVKREELFITTK 81
Cdd:cd19108 2 RVKLNDGHFIPVLGFGTYA--PEEVpkskaLEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 82 AWTHELAPGKLEGGLRESLKKLQLEYVDLYLAHMPAAFN--DDM---SEH---IASPVE--DVWRQFDAVYKAGLAKAVG 151
Cdd:cd19108 80 LWCTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKpgEELfpkDENgklIFDTVDlcATWEAMEKCKDAGLAKSIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 152 VSNWNNDQISRAL---ALGLTPVHNsQVELHLYFPQHDHVDFCKKHNISVTSYATLGSpgrvnftlptgQKL-DW--APA 225
Cdd:cd19108 160 VSNFNRRQLEMILnkpGLKYKPVCN-QVECHPYLNQSKLLDFCKSKDIVLVAYSALGS-----------QRDkEWvdQNS 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17550248 226 PSDLQDQNVLALAEKTHKTPAQVLLRYALDRGCAILPKSIQENRIKENFEVFDFSLTEEDIAKLE 290
Cdd:cd19108 228 PVLLEDPVLCALAKKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALD 292
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
10-291 |
6.60e-82 |
|
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: 249.25 E-value: 6.60e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 10 LSNGVEMPVIGLGTWQSSPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKELL-EEGVVKREELFITTKAWTHELA 88
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLkEEPGVKREDLFITSKLWNNSHR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 89 PGKLEGGLRESLKKLQLEYVDLYLAHMPAAFNDDMSEHIASPVE---------------DVWRQFDAVYKAGLAKAVGVS 153
Cdd:cd19118 81 PEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTGDLNPLTAVPtnggevdldlsvslvDTWKAMVELKKTGKVKSIGVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 154 NWNNDQISRAL-ALGLTPVHNsQVELHLYFPQHDHVDFCKKHNISVTSYATLGSpgrvnftlptgqklDWAPAPSDLQDQ 232
Cdd:cd19118 161 NFSIDHLQAIIeETGVVPAVN-QIEAHPLLLQDELVDYCKSKNIHITAYSPLGN--------------NLAGLPLLVQHP 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 17550248 233 NVLALAEKTHKTPAQVLLRYALDRGCAILPKSIQENRIKENFEvfDFSLTEEDIAKLEE 291
Cdd:cd19118 226 EVKAIAAKLGKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVTA 282
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
16-290 |
1.19e-80 |
|
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: 244.87 E-value: 1.19e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 16 MPVIGLGTWQSSPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKELleegVVKREELFITTKAWTHELAPGKLEGG 95
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAES----GVPREDLFITTKVWRDHLRPEDLKKS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 96 LRESLKKLQLEYVDLYLAHMPAAfnddmsehiASPVEDVWRQFDAVYKAGLAKAVGVSNWNNDQISRALALGLTPVHNSQ 175
Cdd:cd19073 77 VDRSLEKLGTDYVDLLLIHWPNP---------TVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPLPIAVNQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 176 VELHLYFPQHDHVDFCKKHNISVTSYATLGSpGRVnftlptgqkldwapapsdLQDQNVLALAEKTHKTPAQVLLRYALD 255
Cdd:cd19073 148 VEFHPFLYQAELLEYCRENDIVITAYSPLAR-GEV------------------LRDPVIQEIAEKYDKTPAQVALRWLVQ 208
|
250 260 270
....*....|....*....|....*....|....*
gi 17550248 256 RGCAILPKSIQENRIKENFEVFDFSLTEEDIAKLE 290
Cdd:cd19073 209 KGIVVIPKASSEDHLKENLAIFDWELTSEDVAKID 243
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
7-291 |
5.06e-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: 244.36 E-value: 5.06e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 7 SIKLSNGVEMPVIGLGTWQSSPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKELLeEGVVKREELFITTKAW-TH 85
Cdd:cd19121 3 SFKLNTGASIPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAI-AGGVKREDLFVTTKLWsTY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 86 ElapGKLEGGLRESLKKLQLEYVDLYLAHMPAAFNDDMSEHIASPVED-------------VWRQFDAVYKAGLAKAVGV 152
Cdd:cd19121 82 H---RRVELCLDRSLKSLGLDYVDLYLVHWPVLLNPNGNHDLFPTLPDgsrdldwdwnhvdTWKQMEKVLKTGKTKAIGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 153 SNWNNDQISRALALG-LTPVHNsQVELHLYFPQHDHVDFCKKHNISVTSYATLGSpgrvnftlpTGQKLdwapapsdLQD 231
Cdd:cd19121 159 SNYSIPYLEELLKHAtVVPAVN-QVENHPYLPQQELVDFCKEKGILIEAYSPLGS---------TGSPL--------ISD 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 232 QNVLALAEKTHKTPAQVLLRYALDRGCAILPKSIQENRIKENFEVFDFslTEEDIAKLEE 291
Cdd:cd19121 221 EPVVEIAKKHNVGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDL--DDEDMNKLND 278
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
12-291 |
5.32e-79 |
|
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: 241.79 E-value: 5.32e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 12 NGVEMPVIGLGT--WQSSPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKELLEEGVVK-REELFITTKAWTHELA 88
Cdd:cd19124 1 SGQTMPVIGMGTasDPPSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKLWCSDAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 89 PGKLEGGLRESLKKLQLEYVDLYLAHMPA-----AFNDDMSEHIASP--VEDVWRQFDAVYKAGLAKAVGVSNWNNDQIS 161
Cdd:cd19124 81 PDLVLPALKKSLRNLQLEYVDLYLIHWPVslkpgKFSFPIEEEDFLPfdIKGVWEAMEECQRLGLTKAIGVSNFSCKKLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 162 RALALGLTPVHNSQVELHLYFPQHDHVDFCKKHNISVTSYATLGSPGRVnftlptgqkldWAPaPSDLQDQNVLALAEKT 241
Cdd:cd19124 161 ELLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTK-----------WGS-NAVMESDVLKEIAAAK 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 17550248 242 HKTPAQVLLRYALDRGCAILPKSIQENRIKENFEVFDFSLTEEDIAKLEE 291
Cdd:cd19124 229 GKTVAQVSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISE 278
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
6-297 |
1.43e-78 |
|
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: 241.62 E-value: 1.43e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 6 ASIKLSNGVEMPVIGLGTWQSSPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKELLEEGVVKREELFITTKAWTH 85
Cdd:cd19112 1 STITLNSGHKMPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLWNS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 86 ElaPGKLEGGLRESLKKLQLEYVDLYLAHMPAA------------FNDD--MSEHIASPVEDVWRQFDAVYKAGLAKAVG 151
Cdd:cd19112 81 D--HGHVIEACKDSLKKLQLDYLDLYLVHFPVAtkhtgvgttgsaLGEDgvLDIDVTISLETTWHAMEKLVSAGLVRSIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 152 VSNWNNDQISRALALGLTPVHNSQVELHLYFPQHDHVDFCKKHNISVTSYATLGSpGRVNftlptgqkLDWAPAPSDLQD 231
Cdd:cd19112 159 ISNYDIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGG-AAAN--------AEWFGSVSPLDD 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17550248 232 QNVLALAEKTHKTPAQVLLRYALDRGCAILPKSIQENRIKENFEVFDFSLTEEDIAKLEESKNSQR 297
Cdd:cd19112 230 PVLKDLAKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYR 295
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
8-291 |
1.98e-78 |
|
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: 240.00 E-value: 1.98e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 8 IKLSNGVEMPVIGLGTWQSSPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKelleEGVVKREELFITTKAWTHEL 87
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIR----RSGVDRSDIFVTTKLWISDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 88 APGKLEGGLRESLKKLQLEYVDLYLAHMPAAfnDDMSEHIASpvedvWRQFDAVYKAGLAKAVGVSNWNNDQISRAL-AL 166
Cdd:cd19127 77 GYDKALRGFDASLRRLGLDYVDLYLLHWPVP--NDFDRTIQA-----YKALEKLLAEGRVRAIGVSNFTPEHLERLIdAT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 167 GLTPVHNsQVELHLYFPQHDHVDFCKKHNISVTSYATLGspgrvnftlptGQKLDWAPAPSD----LQDQNVLALAEKTH 242
Cdd:cd19127 150 TVVPAVN-QVELHPYFSQKDLRAFHRRLGIVTQAWSPIG-----------GVMRYGASGPTGpgdvLQDPTITGLAEKYG 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 17550248 243 KTPAQVLLRYALDRGCAILPKSIQENRIKENFEVFDFSLTEEDIAKLEE 291
Cdd:cd19127 218 KTPAQIVLRWHLQNGVSAIPKSVHPERIAENIDIFDFALSAEDMAAIDA 266
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
8-289 |
4.46e-78 |
|
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: 238.49 E-value: 4.46e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 8 IKLSNGVEMPVIGLGTWQ-SSPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKElleeGVVKREELFITTKAWTHE 86
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQtPDGDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRE----SGVPREELFVTTKLWNDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 87 LAPGKLEGGLRESLKKLQLEYVDLYLAHMPAAfnddmsEHIAspveDVWRQFDAVYKAGLAKAVGVSNWNNDQISRALAL 166
Cdd:cd19126 77 QRARRTEDAFQESLDRLGLDYVDLYLIHWPGK------DKFI----DTWKALEKLYASGKVKAIGVSNFQEHHLEELLAH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 167 G-LTPVHNsQVELHLYFPQHDHVDFCKKHNISVTSYATLGSpgrvnftlptGQKLDwapapsdlqDQNVLALAEKTHKTP 245
Cdd:cd19126 147 AdVVPAVN-QVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQ----------GGLLS---------NPVLAAIGEKYGKSA 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 17550248 246 AQVLLRYALDRGCAILPKSIQENRIKENFEVFDFSLTEEDIAKL 289
Cdd:cd19126 207 AQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAI 250
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
5-291 |
1.17e-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: 238.55 E-value: 1.17e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 5 TASIKLSNGVEMPVIGLGTWQSSPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKelleEGVVKREELFITTKAW- 83
Cdd:cd19117 3 SKTFKLNTGAEIPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIK----DSGVPREEIFITTKLWc 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 84 THELAPgklEGGLRESLKKLQLEYVDLYLAHMPAAFNDDMSEHIASP------------VEDVWRQFDAVYKAGLAKAVG 151
Cdd:cd19117 79 TWHRRV---EEALDQSLKKLGLDYVDLYLMHWPVPLDPDGNDFLFKKddgtkdhepdwdFIKTWELMQKLPATGKVKAIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 152 VSNWNNDQISRALALG---LTPVHNsQVELHLYFPQHDHVDFCKKHNISVTSYATLGSPGrvnftlptgqkldwAPApsd 228
Cdd:cd19117 156 VSNFSIKNLEKLLASPsakIVPAVN-QIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTN--------------APL--- 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17550248 229 LQDQNVLALAEKTHKTPAQVLLRYALDRGCAILPKSIQENRIKENFEVfdFSLTEEDIAKLEE 291
Cdd:cd19117 218 LKEPVIIKIAKKHGKTPAQVIISWGLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEIDE 278
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
7-299 |
1.19e-77 |
|
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: 238.06 E-value: 1.19e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 7 SIKLSNGVEMPVIGLGTWQSSPA-EVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKElleeGVVKREELFITTKAWTH 85
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEEGsEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKE----SGIPREELFITSKVWNA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 86 ELAPGKLEGGLRESLKKLQLEYVDLYLAHMPaafnddmsehIASPVEDVWRQFDAVYKAGLAKAVGVSNWNNDQISRALA 165
Cdd:cd19157 77 DQGYDSTLKAFEASLERLGLDYLDLYLIHWP----------VKGKYKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 166 LG-LTPVHNsQVELHLYFPQHDHVDFCKKHNISVTSYatlgSPgrvnftLPTGQKLDwapapsdlqDQNVLALAEKTHKT 244
Cdd:cd19157 147 DAeIVPMVN-QVEFHPRLTQKELRDYCKKQGIQLEAW----SP------LMQGQLLD---------NPVLKEIAEKYNKS 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 17550248 245 PAQVLLRYALDRGCAILPKSIQENRIKENFEVFDFSLTEEDIAKLEESKNSQRLF 299
Cdd:cd19157 207 VAQVILRWDLQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNENLRVG 261
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
4-289 |
3.90e-76 |
|
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381361 [Multi-domain] Cd Length: 265 Bit Score: 234.14 E-value: 3.90e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 4 ATASIKLSNGVEMPVIGLGTWQS---SPAEVITAVKtavKAGYRLIDTASVYQNEEAIGTAIKElleEGVvKREELFITT 80
Cdd:cd19135 1 GTPTVRLSNGVEMPILGLGTSHSggySHEAVVYALK---ECGYRHIDTAKRYGCEELLGKAIKE---SGV-PREDLFLTT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 81 KAWTHELAPGKLEGGLRESLKKLQLEYVDLYLAHMPAAfnDDMSEHIASPVEDVWRQFDAVYKAGLAKAVGVSNWNNDQI 160
Cdd:cd19135 74 KLWPSDYGYESTKQAFEASLKRLGVDYLDLYLLHWPDC--PSSGKNVKETRAETWRALEELYDEGLCRAIGVSNFLIEHL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 161 SRALALGLTPVHNSQVELHLYFPQHDHVDFCKKHNISVTSYATLgSPGRVnftlptgqkldwapapsdLQDQNVLALAEK 240
Cdd:cd19135 152 EQLLEDCSVVPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPL-AKGKA------------------LEEPTVTELAKK 212
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 17550248 241 THKTPAQVLLRYALDRGCAILPKSIQENRIKENFEVFDFSLTEEDIAKL 289
Cdd:cd19135 213 YQKTPAQILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATL 261
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
11-291 |
1.17e-75 |
|
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381366 [Multi-domain] Cd Length: 253 Bit Score: 232.53 E-value: 1.17e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 11 SNGVEMPVIGLGTWQSSPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKelleEGVVKREELFITTKAWTHELAPG 90
Cdd:cd19140 3 VNGVRIPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIA----ASGVPRDELFLTTKVWPDNYSPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 91 KLEGGLRESLKKLQLEYVDLYLAHMPaafNDDMsehiasPVEDVWRQFDAVYKAGLAKAVGVSNWNNDQISRALALGLTP 170
Cdd:cd19140 79 DFLASVEESLRKLRTDYVDLLLLHWP---NKDV------PLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSEAP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 171 VHNSQVELHLYFPQHDHVDFCKKHNISVTSYATLGSpGRVnftlptgqkldwapapsdLQDQNVLALAEKTHKTPAQVLL 250
Cdd:cd19140 150 LFTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLAR-GEV------------------LKDPVLQEIGRKHGKTPAQVAL 210
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 17550248 251 RYALDR-GCAILPKSIQENRIKENFEVFDFSLTEEDIAKLEE 291
Cdd:cd19140 211 RWLLQQeGVAAIPKATNPERLEENLDIFDFTLSDEEMARIAA 252
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
8-298 |
2.68e-75 |
|
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from Leishmania major and Trypanosoma brucei are founding members of aldo-keto reductase family 5 member A1 (AKR5A1) and A2 (AKR5A2), respectively. PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity toward the synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde.
Pssm-ID: 381382 [Multi-domain] Cd Length: 266 Bit Score: 232.02 E-value: 2.68e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 8 IKLSNGVEMPVIGLGTWQSSP-AEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKElleeGVVKREELFITTKAWTHE 86
Cdd:cd19156 1 VKLANGVEMPRLGLGVWRVQDgAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRE----SGVPREEVFVTTKLWNSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 87 LAPGKLEGGLRESLKKLQLEYVDLYLAHMPaafnddmsehIASPVEDVWRQFDAVYKAGLAKAVGVSNWNNDQISRALAL 166
Cdd:cd19156 77 QGYESTLAAFEESLEKLGLDYVDLYLIHWP----------VKGKFKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 167 G-LTPVHNsQVELHLYFPQHDHVDFCKKHNISVTSYATLGSpGRVnftlptgqkldwapapsdLQDQNVLALAEKTHKTP 245
Cdd:cd19156 147 CkVAPMVN-QIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQ-GKL------------------LSNPVLKAIGKKYGKSA 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 17550248 246 AQVLLRYALDRGCAILPKSIQENRIKENFEVFDFSLTEEDIAKLEESKNSQRL 298
Cdd:cd19156 207 AQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTDHRY 259
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
8-293 |
4.46e-75 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 231.50 E-value: 4.46e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 8 IKLSNGVEMPVIGLGTWQSSPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAikelLEEGVVKREELFITTKAWTHE- 86
Cdd:PRK11565 7 IKLQDGNVMPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKA----LKEASVAREELFITTKLWNDDh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 87 LAPGKlegGLRESLKKLQLEYVDLYLAHMPAAFNDDMSehiaspveDVWRQFDAVYKAGLAKAVGVSNWNNDQISRAL-A 165
Cdd:PRK11565 83 KRPRE---ALEESLKKLQLDYVDLYLMHWPVPAIDHYV--------EAWKGMIELQKEGLIKSIGVCNFQIHHLQRLIdE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 166 LGLTPVHNsQVELHLYFPQHDHVDFCKKHNISVTSYATLGSPGRVNFtlptgqkldwapapsdlqDQNVL-ALAEKTHKT 244
Cdd:PRK11565 152 TGVTPVIN-QIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGKGVF------------------DQKVIrDLADKYGKT 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 17550248 245 PAQVLLRYALDRGCAILPKSIQENRIKENFEVFDFSLTEED---IAKLEESK 293
Cdd:PRK11565 213 PAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRLDKDElgeIAKLDQGK 264
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
13-312 |
1.92e-74 |
|
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: 231.23 E-value: 1.92e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 13 GVEMPVIGLGTWQSS----PAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKELLEEGVVKREELFITTKAWTHELA 88
Cdd:cd19109 1 GNSIPIIGLGTYSEPkttpKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 89 PGKLEGGLRESLKKLQLEYVDLYLAHMPAAFNDdmSEHIASPVED------------VWRQFDAVYKAGLAKAVGVSNWN 156
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAFKP--GDEIYPRDENgkwlyhktnlcaTWEALEACKDAGLVKSIGVSNFN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 157 NDQISRAL---ALGLTPVHNsQVELHLYFPQHDHVDFCKKHNISVTSYATLGSPGR---VNFTLPtgqkldwaPApsdLQ 230
Cdd:cd19109 159 RRQLELILnkpGLKHKPVSN-QVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDpiwVNVSSP--------PL---LE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 231 DQNVLALAEKTHKTPAQVLLRYALDRGCAILPKSIQENRIKENFEVFDFSLTEEDIAKLEESKNSQRlFLQDFM-TGHPE 309
Cdd:cd19109 227 DPLLNSIGKKYNKTAAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVR-YVELLMwRDHPE 305
|
...
gi 17550248 310 DAF 312
Cdd:cd19109 306 YPF 308
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
15-315 |
7.22e-74 |
|
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: 229.46 E-value: 7.22e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 15 EMPVIGLGTWQSSPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKELLEEGVVKREELFITTKAWTHELAPGKLEG 94
Cdd:cd19110 3 DIPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKSLVKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 95 GLRESLKKLQLEYVDLYLAHMPAAFN--------DDMSEHIASPVE--DVWRQFDAVYKAGLAKAVGVSNWNNDQISRAL 164
Cdd:cd19110 83 ACTRSLKALKLNYLDLYLIHWPMGFKpgepdlplDRSGMVIPSDTDflDTWEAMEDLVIEGLVKNIGVSNFNHEQLERLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 165 ---ALGLTPVHNsQVELHLYFPQHDHVDFCKKHNISVTSYATLGSPGRvnftlptGQKLdwapapsdLQDQNVLALAEKT 241
Cdd:cd19110 163 nkpGLRVKPVTN-QIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSCE-------GVDL--------IDDPVIQRIAKKH 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17550248 242 HKTPAQVLLRYALDRGCAILPKSIQENRIKENFEVFDFSLTEEDIAKLEESKNSQRLFLQDFMTGHPEDAFAAE 315
Cdd:cd19110 227 GKSPAQILIRFQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFPITENHKDYPFHIE 300
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
13-291 |
5.81e-71 |
|
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: 220.95 E-value: 5.81e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 13 GVEMPVIGLGT---WQSSPA-----EVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKELLeegvVKREELFITTKAWT 84
Cdd:cd19120 1 GSKIPAIAFGTgtaWYKSGDddiqrDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALKESG----VPREDLFITTKVSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 85 helAPGKLEGGLRESLKKLQLEYVDLYLAHMPAAFNDDmsehiASPVEDVWRQFDAVYKAGLAKAVGVSNWNNDQISRAL 164
Cdd:cd19120 77 ---GIKDPREALRKSLAKLGVDYVDLYLIHSPFFAKEG-----GPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 165 ALG-LTPVHNsQVELH--LYFPQHDHVDFCKKHNISVTSYATLgspgrvnftLPTGQKldwapAPSDLqDQNVLALAEKT 241
Cdd:cd19120 149 DTAkIKPAVN-QIEFHpyLYPQQPALLEYCREHGIVVSAYSPL---------SPLTRD-----AGGPL-DPVLEKIAEKY 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 17550248 242 HKTPAQVLLRYALDRGCAILPKSIQENRIKENFEVFDFSLTEEDIAKLEE 291
Cdd:cd19120 213 GVTPAQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEIDK 262
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
4-291 |
6.42e-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: 217.29 E-value: 6.42e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 4 ATASIKLSNGVEMPVIGLGTWQSSPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKELLEEGVVKREELFITTKAW 83
Cdd:cd19115 1 ASPTVKLNSGYDMPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 84 THELAPGKLEGGLRESLKKLQLEYVDLYLAHMPAA-------------FNDDMSEHIAS--PVEDVWRQFDAVYKAGLAK 148
Cdd:cd19115 81 NTFHDGERVEPICRKQLADWGIDYFDLFLIHFPIAlkyvdpavryppgWFYDGKKVEFSnaPIQETWTAMEKLVDKGLAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 149 AVGVSNWNNDQISRALALGLTPVHNSQVELHLYFPQHDHVDFCKKHNISVTSYATLGSPGRVNFTLPTGQKldwapAPSD 228
Cdd:cd19115 161 SIGVSNFSAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGPQSFLELDLPGAKD-----TPPL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17550248 229 LQDQNVLALAEKTHKTPAQVLLRYALDRGCAILPKSIQENRIKENFEVFDFSLTEEDIAKLEE 291
Cdd:cd19115 236 FEHDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISA 298
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
17-286 |
3.54e-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: 3.54e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 17 PVIGLGTWQSSPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKELLEEGVVKREELFITTKAWTHELAPGKLEGGL 96
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVKEQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 97 RESLKKLQLEYVDLYLAHMPAAF--NDDMSEHIAS--------PVEDVWRQFDAVYKAGLAKAVGVSNWNNDQISRALAL 166
Cdd:cd19128 82 LITLQDLQLEYLDLFLIHWPLAFdmDTDGDPRDDNqiqslskkPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLNY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 167 GLTPVHNSQVELHLYFPQHDHVDFCKKHNISVTSYATLGspgrvnftlptGQKLDWAPAPsdLQDQNVLALAEKTHKTPA 246
Cdd:cd19128 162 CKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLG-----------GSYGDGNLTF--LNDSELKALATKYNTTPP 228
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 17550248 247 QVLLRYALDR---GCAILPKSIQENRIKENFEVFDFSLTEEDI 286
Cdd:cd19128 229 QVIIAWHLQKwpkNYSVIPKSANKSRCQQNFDINDLALTKEDM 271
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
10-290 |
7.28e-68 |
|
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: 212.52 E-value: 7.28e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 10 LSNGVEMPVIGLGTWQSSPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKElleeGVVKREELFITTKAwthelaP 89
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRR----SGVPREELFVTTKL------P 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 90 GKLEG------GLRESLKKLQLEYVDLYLAHMPAAFNDDMSEhiaspvedVWRQFDAVYKAGLAKAVGVSNWNNDQISRA 163
Cdd:cd19132 71 GRHHGyeealrTIEESLYRLGLDYVDLYLIHWPNPSRDLYVE--------AWQALIEAREEGLVRSIGVSNFLPEHLDRL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 164 L-ALGLTPVHNsQVELHLYFPQHDHVDFCKKHNISVTSYATLGSPGRVnftlptgqkldwapapsdLQDQNVLALAEKTH 242
Cdd:cd19132 143 IdETGVTPAVN-QIELHPYFPQAEQRAYHREHGIVTQSWSPLGRGSGL------------------LDEPVIKAIAEKHG 203
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 17550248 243 KTPAQVLLRYALDRGCAILPKSIQENRIKENFEVFDFSLTEEDIAKLE 290
Cdd:cd19132 204 KTPAQVVLRWHVQLGVVPIPKSANPERQRENLAIFDFELSDEDMAAIA 251
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
5-291 |
6.85e-67 |
|
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: 211.20 E-value: 6.85e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 5 TASIKLSNGVEMPVIGLGTW--QSSPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKELLEEGVVKREELFITTKA 82
Cdd:cd19119 1 EISFKLNTGASIPALGLGTAspHEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 83 WthelaP---GKLEGGLRESLKKLQLEYVDLYLAHMPAAF---NDDM------------------SEHIaspveDVWRQF 138
Cdd:cd19119 81 W-----PtfyDEVERSLDESLKALGLDYVDLLLVHWPVCFekdSDDSgkpftpvnddgktryaasGDHI-----TTYKQL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 139 DAVYKAGLAKAVGVSNWNNDQISRAL-ALGLTPVHNsQVELHLYFPQHDHVDFCKKHNISVTSYATLGSPGrvnftlptg 217
Cdd:cd19119 151 EKIYLDGRAKAIGVSNYSIVYLERLIkECKVVPAVN-QVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHG--------- 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17550248 218 qkldwAPApsdLQDQNVLALAEKTHKTPAQVLLRYALDRGCAILPKSIQENRIKENFEVfdFSLTEEDIAKLEE 291
Cdd:cd19119 221 -----APN---LKNPLVKKIAEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLDD 284
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
16-289 |
8.65e-67 |
|
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: 209.52 E-value: 8.65e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 16 MPVIGLGTWQSSPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIkellEEGVVKREELFITTKAWTHELAPGKLEGG 95
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAI----AESGVPRDELFITTKIWIDNLSKDKLLPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 96 LRESLKKLQLEYVDLYLAHMPAAFNddmsehiASPVEDVWRQFDAVYKAGLAKAVGVSNWNNDQISRALA-LGLTPVHNS 174
Cdd:cd19139 77 LEESLEKLRTDYVDLTLIHWPSPND-------EVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAvVGAGAIATN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 175 QVELHLYFPQHDHVDFCKKHNISVTSYATLGSpGRVnftlptgqkldwapapsdLQDQNVLALAEKTHKTPAQVLLRYAL 254
Cdd:cd19139 150 QIELSPYLQNRKLVAHCKQHGIHVTSYMTLAY-GKV------------------LDDPVLAAIAERHGATPAQIALAWAM 210
|
250 260 270
....*....|....*....|....*....|....*
gi 17550248 255 DRGCAILPKSIQENRIKENFEVFDFSLTEEDIAKL 289
Cdd:cd19139 211 ARGYAVIPSSTKREHLRSNLLALDLTLDADDMAAI 245
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
7-290 |
1.40e-66 |
|
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: 211.15 E-value: 1.40e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 7 SIKLSNGVEMPVIGLGTWQSSPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKELLEEGVVKREELFITTKAWTHE 86
Cdd:cd19113 2 DIKLNSGYKMPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWNNF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 87 LAPGKLEGGLRESLKKLQLEYVDLYLAHMPAAF----------------NDDMSEHIASPVEDVWRQFDAVYKAGLAKAV 150
Cdd:cd19113 82 HDPKNVETALNKTLSDLKLDYVDLFLIHFPIAFkfvpieekyppgfycgDGDNFVYEDVPILDTWKALEKLVDAGKIKSI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 151 GVSNWNNDQISRAL-ALGLTPVhNSQVELHLYFPQHDHVDFCKKHNISVTSYATLGSPGRVNFTLPTGQKldwapAPSDL 229
Cdd:cd19113 162 GVSNFPGALILDLLrGATIKPA-VLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGPQSFVELNQGRALN-----TPTLF 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17550248 230 QDQNVLALAEKTHKTPAQVLLRYALDRGCAILPKSIQENRIKENFEVFDFSLTEED---IAKLE 290
Cdd:cd19113 236 EHDTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDfeeIAKLD 299
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
11-308 |
7.43e-64 |
|
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: 203.46 E-value: 7.43e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 11 SNGVEMPVIGLGTWQSSPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKELLEEGVVKREELFITTKAWTHELAPG 90
Cdd:cd19129 1 NGSGAIPALGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNHRPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 91 KLEGGLRESLKKLQLEYVDLYLAHMPAAFN--DDMSEHIAS---------PVEDVWRQFDAVYKAGLAKAVGVSNWNNDQ 159
Cdd:cd19129 81 RVKPAFEASLKRLQLDYLDLYLIHTPFAFQpgDEQDPRDANgnviyddgvTLLDTWRAMERLVDEGRCKAIGLSDVSLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 160 ISRALALGLTPVHNSQVELHLYFPQHDHVDFCKKHNISVTSYATLGSPGRvnftlptgqkldwapaPSDLQDQNVLALAE 239
Cdd:cd19129 161 LREIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGME----------------PKLLEDPVITAIAR 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17550248 240 KTHKTPAQVLLRYALDRGCAILPKSIQENRIKENFEVfdFSLTEEDIAKLEESKNSQRLFLQDFMTGHP 308
Cdd:cd19129 225 RVNKTPAQVLLAWAIQRGTALLTTSKTPSRIRENFDI--STLPEDAMREINEGIKTRYRFNSVVETGVP 291
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
16-290 |
4.51e-63 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 200.64 E-value: 4.51e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 16 MPVIGLGTWQSSPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIkellEEGVVKREELFITTKAWTHELAPGKLEGG 95
Cdd:PRK11172 3 IPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAI----AESGVPRDELFITTKIWIDNLAKDKLIPS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 96 LRESLKKLQLEYVDLYLAHMPAAFNddmsehiASPVEDVWRQFDAVYKAGLAKAVGVSNWNNDQISRAL-ALGLTPVHNS 174
Cdd:PRK11172 79 LKESLQKLRTDYVDLTLIHWPSPND-------EVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQAIaAVGAENIATN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 175 QVELHLYFPQHDHVDFCKKHNISVTSYATLGSpGRVnftlptgqkldwapapsdLQDQNVLALAEKTHKTPAQVLLRYAL 254
Cdd:PRK11172 152 QIELSPYLQNRKVVAFAKEHGIHVTSYMTLAY-GKV------------------LKDPVIARIAAKHNATPAQVILAWAM 212
|
250 260 270
....*....|....*....|....*....|....*....
gi 17550248 255 DRGCAILPKSIQENRIKENFEVFDFSLTEED---IAKLE 290
Cdd:PRK11172 213 QLGYSVIPSSTKRENLASNLLAQDLQLDAEDmaaIAALD 251
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
7-298 |
1.70e-62 |
|
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: 198.93 E-value: 1.70e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 7 SIKLSNGVEMPVIGLGTWQSSPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKelleEGVVKREELFITTKAWTHE 86
Cdd:cd19134 2 TVTLNDDNTMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIA----ASGIPRGELFVTTKLATPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 87 LAPGKLEGGLRESLKKLQLEYVDLYLAHMPAAfndDMSEHIaspveDVWRQFDAVYKAGLAKAVGVSNWNNDQISRALAL 166
Cdd:cd19134 78 QGFTASQAACRASLERLGLDYVDLYLIHWPAG---REGKYV-----DSWGGLMKLREEGLARSIGVSNFTAEHLENLIDL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 167 -GLTPVHNsQVELHLYFPQHDHVDFCKKHNISVTSYATLGspgrvnftlpTGQKLDwAPApsdlqdqnVLALAEKTHKTP 245
Cdd:cd19134 150 tFFTPAVN-QIELHPLLNQAELRKVNAQHGIVTQAYSPLG----------VGRLLD-NPA--------VTAIAAAHGRTP 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 17550248 246 AQVLLRYALDRGCAILPKSIQENRIKENFEVFDFSLTEEDIAKLEESKNSQRL 298
Cdd:cd19134 210 AQVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDALDGLDDGTRF 262
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
13-297 |
9.65e-62 |
|
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: 198.55 E-value: 9.65e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 13 GVEMPVIGLGTWQSSPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKELLEEGVVKREELFITTKAWTHELAPGKL 92
Cdd:cd19114 1 GDKMPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGKDHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 93 EGGLRESLKKLQLEYVDLYLAHMP-------------AAFNDDMSEHIA---SPVEDVWRQFDAVYKAGLAKAVGVSNWN 156
Cdd:cd19114 81 REAFDRQLKDYGLDYIDLYLIHFPipaayvdpaenypFLWKDKELKKFPleqSPMQECWREMEKLVDAGLVRNIGIANFN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 157 NDQISRALALGLTPVHNSQVELHLYFPQHDHVDFCKKHNISVTSYATLGSPGRVNFTlptgQKLdwAPAPSDLQDQNVLA 236
Cdd:cd19114 161 VQLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAVYTKVT----KHL--KHFTNLLEHPVVKK 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17550248 237 LAEKTHKTPAQVLLRYALDRGCAILPKSIQENRIKENFEVFDFSLTEEDIAKLEESKNSQR 297
Cdd:cd19114 235 LADKHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANAR 295
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
13-290 |
7.52e-58 |
|
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: 187.05 E-value: 7.52e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 13 GVEMPVIGLGTW-----QSSPA----EVITAVKTAVKAGYRLIDTASVYQN---EEAIGTAIKElleegvVKREELFITT 80
Cdd:cd19072 1 GEEVPVLGLGTWgigggMSKDYsddkKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAIKG------FDREDLFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 81 KAWTHELAPGKLEGGLRESLKKLQLEYVDLYLAHMPaafNDdmsehiASPVEDVWRQFDAVYKAGLAKAVGVSNWNNDQI 160
Cdd:cd19072 75 KVSPDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWP---NP------SIPIEETLRAMEELVEEGKIRYIGVSNFSLEEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 161 SRALA-LGLTPVHNSQVELHLYFP--QHDHVDFCKKHNISVTSYATLGSpGRVNFtlptgqkldwAPAPSDLQDqnvlaL 237
Cdd:cd19072 146 EEAQSyLKKGPIVANQVEYNLFDReeESGLLPYCQKNGIAIIAYSPLEK-GKLSN----------AKGSPLLDE-----I 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 17550248 238 AEKTHKTPAQVLLRYALDRGCAI-LPKSIQENRIKENFEVFDFSLTEEDIAKLE 290
Cdd:cd19072 210 AKKYGKTPAQIALNWLISKPNVIaIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
9-280 |
1.76e-57 |
|
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: 187.06 E-value: 1.76e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 9 KLSNGVEMPVIGLGTWQS--SPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKELLEEG-VVKREELFITTKAWTH 85
Cdd:cd19122 2 TLNNGVKIPAVGFGTFANegAKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKVWNH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 86 ELAPGKLEGGLRESLKKLQLEYVDLYLAHMP-AAFNDD-------------MSEHIASPVEDVWRQFDAVYKAGLAKAVG 151
Cdd:cd19122 82 LHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPiAAEKNDqrspklgpdgkyvILKDLTENPEPTWRAMEEIYESGKAKAIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 152 VSNWNNDQISRALALGLTPVHNSQVELHLYFPQHDHVDFCKKHNISVTSYATLGSPGRVNftlPTGQKLDwapapsdlQD 231
Cdd:cd19122 162 VSNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQVP---STGERVS--------EN 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 17550248 232 QNVLALAEKTHKTPAQVLLRYALDRGCAILPKSIQENRIKENFEVFDFS 280
Cdd:cd19122 231 PTLNEVAEKGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIELS 279
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
19-291 |
3.71e-54 |
|
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: 178.27 E-value: 3.71e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 19 IGLGTWQ-------SSPAEVITAVKTAVKAGYRLIDTASVY---QNEEAIGTAIKELleegVVKREELFITTKAWT--HE 86
Cdd:pfam00248 1 IGLGTWQlgggwgpISKEEALEALRAALEAGINFIDTAEVYgdgKSEELLGEALKDY----PVKRDKVVIATKVPDgdGP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 87 LAPGKLEGGLR----ESLKKLQLEYVDLYLAHMPaafndDMSehiaSPVEDVWRQFDAVYKAGLAKAVGVSNWNNDQISR 162
Cdd:pfam00248 77 WPSGGSKENIRksleESLKRLGTDYIDLYYLHWP-----DPD----TPIEETWDALEELKKEGKIRAIGVSNFDAEQIEK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 163 ALALGLTPVHNSQVELHLYFPQHDH--VDFCKKHNISVTSYATLGS---------PGRVNFTLPTGQKLDWAPAPSDLqD 231
Cdd:pfam00248 148 ALTKGKIPIVAVQVEYNLLRRRQEEelLEYCKKNGIPLIAYSPLGGglltgkytrDPDKGPGERRRLLKKGTPLNLEA-L 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17550248 232 QNVLALAEKTHKTPAQVLLRYAL--DRGCAILPKSIQENRIKENFEVFDFSLTEEDIAKLEE 291
Cdd:pfam00248 227 EALEEIAKEHGVSPAQVALRWALskPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDE 288
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
7-290 |
5.28e-53 |
|
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: 174.33 E-value: 5.28e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 7 SIKLSNGVEMPVIGLGTWQSSPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTAIKelleEGVVKREELFITTKAWTHE 86
Cdd:cd19130 1 SIVLNDGNSIPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIA----ASGIPRDELFVTTKLWNDR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 87 LAPGKLEGGLRESLKKLQLEYVDLYLAHMPAAFNDDMSEhiaspvedVWRQFDAVYKAGLAKAVGVSNWNNDQISR-ALA 165
Cdd:cd19130 77 HDGDEPAAAFAESLAKLGLDQVDLYLVHWPTPAAGNYVH--------TWEAMIELRAAGRTRSIGVSNFLPPHLERiVAA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 166 LGLTPVHNsQVELHLYFPQHDHVDFCKKHNISVTSYATLGSpgrvnftlptGQKLDwapapsdlqDQNVLALAEKTHKTP 245
Cdd:cd19130 149 TGVVPAVN-QIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQ----------GKLLG---------DPPVGAIAAAHGKTP 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 17550248 246 AQVLLRYALDRGCAILPKSIQENRIKENFEVFDFSLTEEDIAKLE 290
Cdd:cd19130 209 AQIVLRWHLQKGHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAID 253
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
13-291 |
4.10e-51 |
|
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme transport and metabolism, General function prediction only];
Pssm-ID: 440431 [Multi-domain] Cd Length: 316 Bit Score: 171.13 E-value: 4.10e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 13 GVEMPVIGLGTWQ-------SSPAEVITAVKTAVKAGYRLIDTASVY---QNEEAIGTAIKELleegvvKREELFITTKa 82
Cdd:COG0667 10 GLKVSRLGLGTMTfggpwggVDEAEAIAILDAALDAGINFFDTADVYgpgRSEELLGEALKGR------PRDDVVIATK- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 83 WTHELAPGKLEGGLR---------ESLKKLQLEYVDLYLAHMPaafnDDmsehiASPVEDVWRQFDAVYKAGLAKAVGVS 153
Cdd:COG0667 83 VGRRMGPGPNGRGLSrehirraveASLRRLGTDYIDLYQLHRP----DP-----DTPIEETLGALDELVREGKIRYIGVS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 154 NWNNDQISRALAL--GLTPVHNSQVELHLYF--PQHDHVDFCKKHNISVTSYATLGS-----PGRVNFTLPTG--QKLDW 222
Cdd:COG0667 154 NYSAEQLRRALAIaeGLPPIVAVQNEYSLLDrsAEEELLPAARELGVGVLAYSPLAGglltgKYRRGATFPEGdrAATNF 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17550248 223 APAPSDLQDQNVL----ALAEKTHKTPAQVLLRYALDRGCAILP----KSIQenRIKENFEVFDFSLTEEDIAKLEE 291
Cdd:COG0667 234 VQGYLTERNLALVdalrAIAAEHGVTPAQLALAWLLAQPGVTSVipgaRSPE--QLEENLAAADLELSAEDLAALDA 308
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
8-290 |
5.99e-48 |
|
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: 161.65 E-value: 5.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 8 IKLSNGVEMPVIGLGTWQ-----SSPAEVITAVKTAVKAGYRLIDTASVYQN---EEAIGTAIKELleegvvkREELFIT 79
Cdd:cd19138 3 VTLPDGTKVPALGQGTWYmgedpAKRAQEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR-------RDKVFLV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 80 TKAWTHELAPGKLEGGLRESLKKLQLEYVDLYLAHMPAAFnddmsehiasPVEDVWRQFDAVYKAGLAKAVGVSNWNNDQ 159
Cdd:cd19138 76 SKVLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWRGGV----------PLAETVAAMEELKKEGKIRAWGVSNFDTDD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 160 ISRALAL--GLTPVHNsQVELHLYF--PQHDHVDFCKKHNISVTSYATLGSPGRvnftlptgqkldwaPAPSDLQDQNVL 235
Cdd:cd19138 146 MEELWAVpgGGNCAAN-QVLYNLGSrgIEYDLLPWCREHGVPVMAYSPLAQGGL--------------LRRGLLENPTLK 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 17550248 236 ALAEKTHKTPAQVLLRYALDRGCAI-LPKSIQENRIKENFEVFDFSLTEEDIAKLE 290
Cdd:cd19138 211 EIAARHGATPAQVALAWVLRDGNVIaIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
15-290 |
4.49e-44 |
|
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: 152.38 E-value: 4.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 15 EMPVIGLGTWQ-----------SSPAEVITAVKTAVKAGYRLIDTASVY---QNEEAIGTAIKELLEegvvkREELFITT 80
Cdd:cd19093 1 EVSPLGLGTWQwgdrlwwgygeYGDEDLQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFLKELGD-----RDEVVIAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 81 K----AWTHelAPGKLEGGLRESLKKLQLEYVDLYLAHMPAAFNddmsehiaSPVEDVWRQFDAVYKAGLAKAVGVSNWN 156
Cdd:cd19093 76 KfaplPWRL--TRRSVVKALKASLERLGLDSIDLYQLHWPGPWY--------SQIEALMDGLADAVEEGLVRAVGVSNYS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 157 NDQISRALAL----GLTPVHNsQVELHL--YFP-QHDHVDFCKKHNISVTSYATLGS---PGRVNFTLPTGQKLDWAPAP 226
Cdd:cd19093 146 ADQLRRAHKAlkerGVPLASN-QVEYSLlyRDPeQNGLLPACDELGITLIAYSPLAQgllTGKYSPENPPPGGRRRLFGR 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17550248 227 SDL-QDQNVL----ALAEKTHKTPAQVLLRYALDRGCAILPKSIQENRIKENFEVFDFSLTEEDIAKLE 290
Cdd:cd19093 225 KNLeKVQPLLdaleEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
13-290 |
1.70e-41 |
|
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381363 [Multi-domain] Cd Length: 260 Bit Score: 144.64 E-value: 1.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 13 GVEMPVIGLGTWQ---------SSPAEVITAVKTAVKAGYRLIDTASVY---QNEEAIGTAIKELleegvvKREELFITT 80
Cdd:cd19137 1 GEKIPALGLGTWGiggfltpdySRDEEMVELLKTAIELGYTHIDTAEMYgggHTEELVGKAIKDF------PREDLFIVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 81 KAWTHELAPGKLEGGLRESLKKLQLEYVDLYLAHMPaafNDDMsehiasPVEDVWRQFDAVYKAGLAKAVGVSNWNNDQI 160
Cdd:cd19137 75 KVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWP---NPNI------PLEETLSAMAEGVRQGLIRYIGVSNFNRRLL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 161 SRALALGLTPVHNSQVELHLY---FPQHDHVDFCKKHNISVTSYATLGSPgrvnfTLPTGQKLDwapapsdlqdqnvlAL 237
Cdd:cd19137 146 EEAISKSQTPIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPLRRG-----LEKTNRTLE--------------EI 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 17550248 238 AEKTHKTPAQVLLRYALDRGCAI-LPKSIQENRIKENFEVFDFSLTEEDIAKLE 290
Cdd:cd19137 207 AKNYGKTIAQIALAWLIQKPNVVaIPKAGRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
13-290 |
4.76e-41 |
|
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: 144.59 E-value: 4.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 13 GVEMPVIGLGTWQSSP--------AEVITAVKTAVKAGYRLIDTASVYQN---EEAIGTAIKElleegvvKREELFITTK 81
Cdd:cd19084 1 DLKVSRIGLGTWAIGGtwwgevddQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKG-------RRDDVVIATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 82 A---W------THELAPGKLEGGLRESLKKLQLEYVDLYLAHMPaafnDDmsehiASPVEDVWRQFDAVYKAGLAKAVGV 152
Cdd:cd19084 74 CglrWdggkgvTKDLSPESIRKEVEQSLRRLQTDYIDLYQIHWP----DP-----NTPIEETAEALEKLKKEGKIRYIGV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 153 SNWNNDQISRALALGltPVHNSQVELHLYFPQH--DHVDFCKKHNISVTSYATLG--------------SPGRVNFTLPT 216
Cdd:cd19084 145 SNFSVEQLEEARKYG--PIVSLQPPYSMLEREIeeELLPYCRENGIGVLPYGPLAqglltgkykkeptfPPDDRRSRFPF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 217 GQKLDWAPApsdlqdQNVLA----LAEKTHKTPAQVLLRYALDR---GCAIL-PKSIQEnrIKENFEVFDFSLTEEDIAK 288
Cdd:cd19084 223 FRGENFEKN------LEIVDklkeIAEKYGKSLAQLAIAWTLAQpgvTSAIVgAKNPEQ--LEENAGALDWELTEEELKE 294
|
..
gi 17550248 289 LE 290
Cdd:cd19084 295 ID 296
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
17-206 |
3.87e-39 |
|
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: 137.65 E-value: 3.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 17 PVIGLGTWQ----SSPAEVITAVKTAVKAGYRLIDTASVY---QNEEAIGTAIKElleegVVKREELFITTKA------- 82
Cdd:cd06660 1 SRLGLGTMTfggdGDEEEAFALLDAALEAGGNFFDTADVYgdgRSERLLGRWLKG-----RGNRDDVVIATKGghppggd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 83 -WTHELAPGKLEGGLRESLKKLQLEYVDLYLAHmpaafNDDmsehIASPVEDVWRQFDAVYKAGLAKAVGVSNWNNDQIS 161
Cdd:cd06660 76 pSRSRLSPEHIRRDLEESLRRLGTDYIDLYYLH-----RDD----PSTPVEETLEALNELVREGKIRYIGVSNWSAERLA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17550248 162 RALAL----GLTPVHNSQVELHLYFPQHDH---VDFCKKHNISVTSYATLGS 206
Cdd:cd06660 147 EALAYakahGLPGFAAVQPQYSLLDRSPMEeelLDWAEENGLPLLAYSPLAR 198
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
18-291 |
6.23e-35 |
|
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: 128.56 E-value: 6.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 18 VIGLGTW-------------QSSpAEVITAVKTAVKAGYRLIDTASVY---QNEEAIGTAIKELleegvvkREELFITTK 81
Cdd:cd19102 3 TIGLGTWaiggggwgggwgpQDD-RDSIAAIRAALDLGINWIDTAAVYglgHSEEVVGRALKGL-------RDRPIVATK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 82 ---AW------THELAPGKLEGGLRESLKKLQLEYVDLYLAHMPAafNDDmsehiasPVEDVWRQFDAVYKAGLAKAVGV 152
Cdd:cd19102 75 cglLWdeegriRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPD--PDE-------PIEEAWGALAELKEEGKVRAIGV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 153 SNWNNDQISRALALGltPVHNSQVELHLYFP--QHDHVDFCKKHNISVTSYATLGS--------PGRVnFTLPTGqklDW 222
Cdd:cd19102 146 SNFSVDQMKRCQAIH--PIASLQPPYSLLRRgiEAEILPFCAEHGIGVIVYSPMQSglltgkmtPERV-ASLPAD---DW 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 223 APAPSDLQDQNV---LAL-------AEKTHKTPAQVLLRYALDRG---CAIlPKSIQENRIKENFEVFDFSLTEEDIAKL 289
Cdd:cd19102 220 RRRSPFFQEPNLarnLALvdalrpiAERHGRTVAQLAIAWVLRRPevtSAI-VGARRPDQIDETVGAADLRLTPEELAEI 298
|
..
gi 17550248 290 EE 291
Cdd:cd19102 299 EA 300
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
17-291 |
4.44e-34 |
|
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: 126.16 E-value: 4.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 17 PVIGLGTWQ---------SSPAEVITAVKTAVKAGYRLIDTASVYQN---EEAIGTAIKElleegvvKREELFITTKAWT 84
Cdd:cd19085 2 SRLGLGCWQfgggywwgdQDDEESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKG-------RRDDVVIATKVSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 85 HELAPGKLEGGLRESLKKLQLEYVDLYLAHMPaafnddmSEHIasPVEDVWRQFDAVYKAGLAKAVGVSNWNNDQISRAL 164
Cdd:cd19085 75 DNLTPEDVRKSCERSLKRLGTDYIDLYQIHWP-------SSDV--PLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 165 ALGltPVHNSQVELHLYF--PQHDHVDFCKKHNISVTSYATLGSpGrvnftLPTGQ-KLDWAPAPSDLQDQNVL------ 235
Cdd:cd19085 146 DAG--RIDSNQLPYNLLWraIEYEILPFCREHGIGVLAYSPLAQ-G-----LLTGKfSSAEDFPPGDARTRLFRhfepga 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17550248 236 ------------ALAEKTHKTPAQVLLRYALDRG---CAILPKSiQENRIKENFEVFDFSLTEEDIAKLEE 291
Cdd:cd19085 218 eeetfealeklkEIADELGVTMAQLALAWVLQQPgvtSVIVGAR-NPEQLEENAAAVDLELSPSVLERLDE 287
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
8-290 |
1.16e-31 |
|
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: 120.00 E-value: 1.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 8 IKLSN-GVEMPVIGLGT----------WQSSPAEVITAVKTAVKAGYRLIDTASVYQN---EEAIGTAIKELLeegvvKR 73
Cdd:cd19079 3 VRLGNsGLKVSRLCLGCmsfgdpkwrpWVLDEEESRPIIKRALDLGINFFDTANVYSGgasEEILGRALKEFA-----PR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 74 EELFITTKAWtHELAPGKLEGGL---------RESLKKLQLEYVDLYLAHMPaafnDDmsehiASPVEDVWRQFDAVYKA 144
Cdd:cd19079 78 DEVVIATKVY-FPMGDGPNGRGLsrkhimaevDASLKRLGTDYIDLYQIHRW----DY-----ETPIEETLEALHDVVKS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 145 GLAKAVGVSN---WnndQISRALAL----GLTPVHNSQVELHLYF--PQHDHVDFCKKHNISVTSYATL----------G 205
Cdd:cd19079 148 GKVRYIGASSmyaW---QFAKALHLaeknGWTKFVSMQNHYNLLYreEEREMIPLCEEEGIGVIPWSPLargrlarpwgD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 206 SPGRVNFTLPTGQKLDWAPAPSDLQDQN-VLALAEKTHKTPAQVLLRYALDRGCAILPksI----QENRIKENFEVFDFS 280
Cdd:cd19079 225 TTERRRSTTDTAKLKYDYFTEADKEIVDrVEEVAKERGVSMAQVALAWLLSKPGVTAP--IvgatKLEHLEDAVAALDIK 302
|
330
....*....|
gi 17550248 281 LTEEDIAKLE 290
Cdd:cd19079 303 LSEEEIKYLE 312
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
21-290 |
8.77e-27 |
|
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: 106.92 E-value: 8.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 21 LGT--------WQSSPAEVITAVKTAVKAGYRLIDTASVYQN---EEAIGTAIKElleegvvKREELFITTKaWTHELAP 89
Cdd:cd19080 15 LGTmtfgtewgWGADREEARAMFDAYVEAGGNFIDTANNYTNgtsERLLGEFIAG-------NRDRIVLATK-YTMNRRP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 90 GKLEGG----------LRESLKKLQLEYVDLYLAHMPaafndDMSehiaSPVEDVWRQFDAVYKAGLAKAVGVSN---Wn 156
Cdd:cd19080 87 GDPNAGgnhrknlrrsVEASLRRLQTDYIDLLYVHAW-----DFT----TPVEEVMRALDDLVRAGKVLYVGISDtpaW- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 157 ndQISRALAL----GLTPVHNSQVELHLYF--PQHDHVDFCKKHNISVTSYATLGS--------PGRVNftlPTGQKLDW 222
Cdd:cd19080 157 --VVARANTLaelrGWSPFVALQIEYSLLErtPERELLPMARALGLGVTPWSPLGGglltgkyqRGEEG---RAGEAKGV 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17550248 223 APAPSDLQDQN------VLALAEKTHKTPAQVLLRYALDRGCAILPksIQENR----IKENFEVFDFSLTEEDIAKLE 290
Cdd:cd19080 232 TVGFGKLTERNwaivdvVAAVAEELGRSAAQVALAWVRQKPGVVIP--IIGARtleqLKDNLGALDLTLSPEQLARLD 307
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
13-284 |
1.54e-26 |
|
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: 106.14 E-value: 1.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 13 GVEMPVIGLGTW-----QSSPAEVITAVKTAVKAGYRLIDTASVY---QNEEAIGTAIKELleegvvKREELFITTKAWt 84
Cdd:cd19074 1 GLKVSELSLGTWltfggQVDDEDAKACVRKAYDLGINFFDTADVYaagQAEEVLGKALKGW------PRESYVISTKVF- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 85 HELAPGKLEGGL---------RESLKKLQLEYVDLYLAHMPaafnDDMsehiaSPVEDVWRQFDAVYKAGLAKAVGVSNW 155
Cdd:cd19074 74 WPTGPGPNDRGLsrkhifesiHASLKRLQLDYVDIYYCHRY----DPE-----TPLEETVRAMDDLIRQGKILYWGTSEW 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 156 NNDQISRALAL----GLTPVHNSQVELHLYFPQHDH--VDFCKKHNISVTSYATLgSPGrvnftLPTGQKLDWAPAPS-- 227
Cdd:cd19074 145 SAEQIAEAHDLarqfGLIPPVVEQPQYNMLWREIEEevIPLCEKNGIGLVVWSPL-AQG-----LLTGKYRDGIPPPSrs 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17550248 228 -------------DLQDQNV------LALAEKTHKTPAQVLLRYALDR---GCAILPKSIQEnRIKENFEVFDFSLTEE 284
Cdd:cd19074 219 ratdednrdkkrrLLTDENLekvkklKPIADELGLTLAQLALAWCLRNpavSSAIIGASRPE-QLEENVKASGVKLSPE 296
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-276 |
7.84e-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: 103.05 E-value: 7.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 13 GVEMPVIGLGTwQSSPAEVITAVKTAVKAGYRLIDTASVYQN---EEAIGTAIKElleegvVKREELFITTKAWTH--EL 87
Cdd:cd19105 10 GLKVSRLGFGG-GGLPRESPELLRRALDLGINYFDTAEGYGNgnsEEIIGEALKG------LRRDKVFLATKASPRldKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 88 APGKLEGGLRESLKKLQLEYVDLYLAHMPaafnDDMSEHIASpvEDVWRQFDAVYKAGLAKAVGVS--NWNNDQISRALA 165
Cdd:cd19105 83 DKAELLKSVEESLKRLQTDYIDIYQLHGV----DTPEERLLN--EELLEALEKLKKEGKVRFIGFSthDNMAEVLQAAIE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 166 LG----LTPVHNsqvelhlYFPQHDH----VDFCKKHNISVTSYATLGSPGRVNFTLPTGQKLDWapapsdlqdqnvlal 237
Cdd:cd19105 157 SGwfdvIMVAYN-------FLNQPAEleeaLAAAAEKGIGVVAMKTLAGGYLQPALLSVLKAKGF--------------- 214
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 17550248 238 aekthkTPAQVLLRYAL--DRGCAILP--KSIQEnrIKENFEV 276
Cdd:cd19105 215 ------SLPQAALKWVLsnPRVDTVVPgmRNFAE--LEENLAA 249
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
35-290 |
1.01e-25 |
|
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: 104.04 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 35 VKTAVKAGYRLIDTASVY---QNEEAIGTAIKELleegvvKREELFITTKAwTHEL---------APGKLEGGLRESLKK 102
Cdd:cd19083 39 VREALDNGVNLLDTAFIYglgRSEELVGEVLKEY------NRNEVVIATKG-AHKFggdgsvlnnSPEFLRSAVEKSLKR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 103 LQLEYVDLYLAHMPaafnDDmsehiASPVEDVWRQFDAVYKAGLAKAVGVSNWNNDQISRALALGLTPVHNSQVELHLYF 182
Cdd:cd19083 112 LNTDYIDLYYIHFP----DG-----ETPKAEAVGALQELKDEGKIRAIGVSNFSLEQLKEANKDGYVDVLQGEYNLLQRE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 183 PQHDHVDFCKKHNISVTSYATLGS---PGRV--NFTLPTGqklDWAPAPSDLQDQ----------NVLALAEKTHKTPAQ 247
Cdd:cd19083 183 AEEDILPYCVENNISFIPYFPLASgllAGKYtkDTKFPDN---DLRNDKPLFKGErfsenldkvdKLKSIADEKGVTVAH 259
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 17550248 248 VLLRYALDRGC--AILPKSIQENRIKENFEVFDFSLTEEDIAKLE 290
Cdd:cd19083 260 LALAWYLTRPAidVVIPGAKRAEQVIDNLKALDVTLTEEEIAFID 304
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
18-198 |
3.62e-25 |
|
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: 101.01 E-value: 3.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 18 VIGLGTWQ--------SSPAEVITAVKTAVKAGYRLIDTASVYQN---EEAIGTAIKElleegvvKREELFITTKA---- 82
Cdd:cd19086 5 EIGFGTWGlggdwwgdVDDAEAIRALRAALDLGINFFDTADVYGDghsERLLGKALKG-------RRDKVVIATKFgnrf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 83 -----WTHELAPGKLEGGLRESLKKLQLEYVDLYLAHMP--AAFNDDmsehiaspveDVWRQFDAVYKAGLAKAVGVSNW 155
Cdd:cd19086 78 dggpeRPQDFSPEYIREAVEASLKRLGTDYIDLYQLHNPpdEVLDND----------ELFEALEKLKQEGKIRAYGVSVG 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17550248 156 NNDQISRALALGLtpVHNSQVELHLYF--PQHDHVDFCKKHNISV 198
Cdd:cd19086 148 DPEEALAALRRGG--IDVVQVIYNLLDqrPEEELFPLAEEHGVGV 190
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
12-306 |
4.34e-25 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 103.36 E-value: 4.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 12 NGVEMPVIGLGTW---QSSPAEVITAVKTAVKAGYRLIDTASVY-QNEEAIGTAIKELleegvvkREELFITTK--AWTH 85
Cdd:COG1453 9 TGLEVSVLGFGGMrlpRKDEEEAEALIRRAIDNGINYIDTARGYgDSEEFLGKALKGP-------RDKVILATKlpPWVR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 86 ElaPGKLEGGLRESLKKLQLEYVDLYLAHMPaafndDMSEHIASPVED--VWRQFDAVYKAGLAKAVGVSNWNN-DQISR 162
Cdd:COG1453 82 D--PEDMRKDLEESLKRLQTDYIDLYLIHGL-----NTEEDLEKVLKPggALEALEKAKAEGKIRHIGFSTHGSlEVIKE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 163 ALALGLTPVhnsqVELHLYFPQHDH------VDFCKKHNISVTSYATLGspgrvnftlptGQKLdwAPAPSDLQDqnvla 236
Cdd:COG1453 155 AIDTGDFDF----VQLQYNYLDQDNqageeaLEAAAEKGIGVIIMKPLK-----------GGRL--ANPPEKLVE----- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 237 lAEKTHKTPAQVLLRYALDR--------GCAilpkSIQEnrIKENFEVFD--FSLTEEDIAKLEESKNSQRLFLQDFMTG 306
Cdd:COG1453 213 -LLCPPLSPAEWALRFLLSHpevttvlsGMS----TPEQ--LDENLKTADnlEPLTEEELAILERLAEELGELLKDFCTG 285
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
11-289 |
1.07e-22 |
|
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: 95.75 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 11 SNGVEMPVIGLG----TW---QSSPAEVITAVKTAVKAGYRLIDTASVYQ---NEEAIGTAIKElleegvvKREELFITT 80
Cdd:cd19076 7 TQGLEVSALGLGcmgmSAfygPADEEESIATLHRALELGVTFLDTADMYGpgtNEELLGKALKD-------RRDEVVIAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 81 KaWTHELAPGKLEGGLR-----------ESLKKLQLEYVDLYLAHMPaafnDDmsehiASPVEDVWRQFDAVYKAGLAKA 149
Cdd:cd19076 80 K-FGIVRDPGSGFRGVDgrpeyvraaceASLKRLGTDVIDLYYQHRV----DP-----NVPIEETVGAMAELVEEGKVRY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 150 VGVSNWNNDQISRALAlgLTPVHNSQVELHLYF--PQHDHVDFCKKHNISVTSYATLG--------------SPGRVNFT 213
Cdd:cd19076 150 IGLSEASADTIRRAHA--VHPITAVQSEYSLWTrdIEDEVLPTCRELGIGFVAYSPLGrgfltgaikspedlPEDDFRRN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 214 LPTGQKLDWApapSDLQD-QNVLALAEKTHKTPAQVLLRYALDRGCAILP----KSIQenRIKENFEVFDFSLTEEDIAK 288
Cdd:cd19076 228 NPRFQGENFD---KNLKLvEKLEAIAAEKGCTPAQLALAWVLAQGDDIVPipgtKRIK--YLEENVGALDVVLTPEELAE 302
|
.
gi 17550248 289 L 289
Cdd:cd19076 303 I 303
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
17-262 |
2.31e-22 |
|
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: 93.82 E-value: 2.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 17 PVIGLGTWQSS----------PAEVITAVKTAVKAGYRLIDTASVY---QNEEAIGTAIKElleegvvKREELFITTKA- 82
Cdd:cd19088 2 SRLGYGAMRLTgpgiwgppadREEAIAVLRRALELGVNFIDTADSYgpdVNERLIAEALHP-------YPDDVVIATKGg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 83 --------WTHELAPGKLEGGLRESLKKLQLEYVDLYLAHMPAAFnddmsehiaSPVEDVWRQFDAVYKAGLAKAVGVSN 154
Cdd:cd19088 75 lvrtgpgwWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPK---------VPFEEQLGALAELQDEGLIRHIGLSN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 155 WNNDQISRALAlgLTPVHNSQVELHLYFPQHDHV-DFCKKHNISVTSYATLGSpgrvnFTLPTGQKLdwapapsdlqdqn 233
Cdd:cd19088 146 VTVAQIEEARA--IVRIVSVQNRYNLANRDDEGVlDYCEAAGIAFIPWFPLGG-----GDLAQPGGL------------- 205
|
250 260
....*....|....*....|....*....
gi 17550248 234 VLALAEKTHKTPAQVLLRYALDRGCAILP 262
Cdd:cd19088 206 LAEVAARLGATPAQVALAWLLARSPVMLP 234
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
17-268 |
3.07e-22 |
|
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381321 [Multi-domain] Cd Length: 253 Bit Score: 93.45 E-value: 3.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 17 PVIGLGTWQ-------SSPAEVITAVKTAVKAGYRLIDTASVYQN-EEAIGTAIKELLeegvvkREELFITTKAWTH--- 85
Cdd:cd19095 1 SVLGLGTSGigrvwgvPSEAEAARLLNTALDLGINLIDTAPAYGRsEERLGRALAGLR------RDDLFIATKVGTHgeg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 86 -----ELAPGKLEGGLRESLKKLQLEYVDLYLAHMPAAfNDDMSEHIASPVEdvWRQfdavykAGLAKAVGVSNWNNDqI 160
Cdd:cd19095 75 grdrkDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSD-DELTGEVLETLED--LKA------AGKVRYIGVSGDGEE-L 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 161 SRALALGLTPVhnSQVELHLYFPQHDHV-DFCKKHNISVTSYATLGSPGRVNFTLPTGQKLDWAPAPSDLQDQNVlalae 239
Cdd:cd19095 145 EAAIASGVFDV--VQLPYNVLDREEEELlPLAAEAGLGVIVNRPLANGRLRRRVRRRPLYADYARRPEFAAEIGG----- 217
|
250 260 270
....*....|....*....|....*....|....*.
gi 17550248 240 kthKTPAQVLLRYALDR---GCAIL----PKSIQEN 268
Cdd:cd19095 218 ---ATWAQAALRFVLSHpgvSSAIVgttnPEHLEEN 250
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
13-291 |
3.68e-22 |
|
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli aldehyde reductase (AKR13C1) and Thermotoga maritima aldo-keto reductase (AKR13C2). Aldehyde reductase (EC 1.1.1.21), also called aldose reductase, is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides.
Pssm-ID: 381304 [Multi-domain] Cd Length: 301 Bit Score: 94.22 E-value: 3.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 13 GVEMPVIGLG----TWQSSPA----EVITAVKTAVKAGYRLIDTASVY---QNEEAIGTAIKElleegvvKREELFITTK 81
Cdd:cd19078 1 GLEVSAIGLGcmgmSHGYGPPpdkeEMIELIRKAVELGITFFDTAEVYgpyTNEELVGEALKP-------FRDQVVIATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 82 aWTHELAPGKLEGG------------LRESLKKLQLEYVDLYLAHMpaaFNDDmsehiaSPVEDVWRQFDAVYKAGLAKA 149
Cdd:cd19078 74 -FGFKIDGGKPGPLgldsrpehirkaVEGSLKRLQTDYIDLYYQHR---VDPN------VPIEEVAGTMKELIKEGKIRH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 150 VGVSNWNNDQISRALAlgLTPVHNSQVELHLYF--PQHDHVDFCKKHNISVTSYATLGS---PGRV--NFTLPTGQKLDW 222
Cdd:cd19078 144 WGLSEAGVETIRRAHA--VCPVTAVQSEYSMMWrePEKEVLPTLEELGIGFVPFSPLGKgflTGKIdeNTKFDEGDDRAS 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17550248 223 AP--APSDL-QDQNVLAL----AEKTHKTPAQVLLRYALDRGCAI--LPKSIQENRIKENFEVFDFSLTEEDIAKLEE 291
Cdd:cd19078 222 LPrfTPEALeANQALVDLlkefAEEKGATPAQIALAWLLAKKPWIvpIPGTTKLSRLEENIGAADIELTPEELREIED 299
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-268 |
7.38e-22 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 93.54 E-value: 7.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 19 IGLGTWQSSP-----AEVITAVKTAVKAGYRLIDTASVYQN---EEAIGTAIKELLEEGVVKREELFITTKA-------- 82
Cdd:cd19099 6 LGLGTYRGDSddetdEEYREALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGIKRDEVVIVTKAgyipgdgd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 83 -------WT------------------HELAPGKLEGGLRESLKKLQLEYVDLYLAHMPAAFNDDMSEhiaspvEDVWRQ 137
Cdd:cd19099 86 eplrplkYLeeklgrglidvadsaglrHCISPAYLEDQIERSLKRLGLDTIDLYLLHNPEEQLLELGE------EEFYDR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 138 FDAVYKAgLAKAV--------GVSNWNNDQISRALA--LGLTPVHNS--------------QVELHLYFPQHDH------ 187
Cdd:cd19099 160 LEEAFEA-LEEAVaegkiryyGISTWDGFRAPPALPghLSLEKLVAAaeevggdnhhfkviQLPLNLLEPEALTekntvk 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 188 ------VDFCKKHNISVTSYATLGSPGrvnftLPTGQKLDWAPAPSDLqdqnvlalaekthKTPAQVLLRYALDR---GC 258
Cdd:cd19099 239 gealslLEAAKELGLGVIASRPLNQGQ-----LLGELRLADLLALPGG-------------ATLAQRALQFARSTpgvDS 300
|
330
....*....|....
gi 17550248 259 AIL----PKSIQEN 268
Cdd:cd19099 301 ALVgmrrPEHVDEN 314
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
19-204 |
7.62e-22 |
|
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: 93.14 E-value: 7.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 19 IGLGTWQ--------SSPAEVITAVKTAVKAGYRLIDTASVY---QNEEAIGTAIKELleegvVKREELFITTKA---WT 84
Cdd:cd19148 7 IALGTWAiggwmwggTDEKEAIETIHKALDLGINLIDTAPVYgfgLSEEIVGKALKEY-----GKRDRVVIATKVgleWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 85 HE------LAPGKLEGGLRESLKKLQLEYVDLYLAHMPaafnDDMsehiaSPVEDVWRQFDAVYKAGLAKAVGVSNWNND 158
Cdd:cd19148 82 EGgevvrnSSPARIRKEVEDSLRRLQTDYIDLYQVHWP----DPL-----VPIEETAEALKELLDEGKIRAIGVSNFSPE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17550248 159 QIS--RALAlgltPVHNSQVELHLYFPQ--HDHVDFCKKHNISVTSYATL 204
Cdd:cd19148 153 QMEtfRKVA----PLHTVQPPYNLFEREieKDVLPYARKHNIVTLAYGAL 198
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
8-291 |
1.15e-21 |
|
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381375 [Multi-domain] Cd Length: 315 Bit Score: 93.11 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 8 IKLSN-GVEMPVIGLGTW---------QSSPAEVITAVKTAVKAGYRLIDTASVYQN---EEAIGTAIKElleegvvKRE 74
Cdd:cd19149 2 RKLGKsGIEASVIGLGTWaigggpwwgGSDDNESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKG-------RRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 75 ELFITTKA---WTHE----------------LAPGKLEGGLRESLKKLQLEYVDLYLAHMPAafnddmsehIASPVEDVW 135
Cdd:cd19149 75 KVVLATKCglrWDREggsfffvrdgvtvyknLSPESIREEVEQSLKRLGTDYIDLYQTHWQD---------VETPIEETM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 136 RQFDAVYKAGLAKAVGVSNWNNDQISRALALGltPVHNSQVELHLYFPQH--DHVDFCKKHNISVTSYATLGSpgrvnfT 213
Cdd:cd19149 146 EALEELKRQGKIRAIGASNVSVEQIKEYVKAG--QLDIIQEKYSMLDRGIekELLPYCKKNNIAFQAYSPLEQ------G 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 214 LPTGQ-KLDWAPAPSDLQDQN----------VLA-------LAEKTHKTPAQVLLRYALDRG--CAILPKSIQENRIKEN 273
Cdd:cd19149 218 LLTGKiTPDREFDAGDARSGIpwfspenrekVLAllekwkpLCEKYGCTLAQLVIAWTLAQPgiTSALCGARKPEQAEEN 297
|
330
....*....|....*...
gi 17550248 274 FEVFDFSLTEEDIAKLEE 291
Cdd:cd19149 298 AKAGDIRLSAEDIATMRS 315
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
12-291 |
1.87e-21 |
|
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: 92.51 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 12 NGVEMPVIGLGTW--------QSSPAEVITAVKTAVKAGYRLIDTASVYQ-NEEAIGTAIKelLEEGvvKREELFITTK- 81
Cdd:cd19144 9 NGPSVPALGFGAMglsafygpPKPDEERFAVLDAAFELGCTFWDTADIYGdSEELIGRWFK--QNPG--KREKIFLATKf 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 82 ----------AWTHElAPGKLEGGLRESLKKLQLEYVDLYLAHMPAAfnddmsehiASPVEDVWRQFDAVYKAGLAKAVG 151
Cdd:cd19144 85 gieknvetgeYSVDG-SPEYVKKACETSLKRLGVDYIDLYYQHRVDG---------KTPIEKTVAAMAELVQEGKIKHIG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 152 VSNWNNDQISRALALglTPVHNSQVE-----LHLYFPQHDHVDFCKKHNISVTSYATLG--------------SPGRVNF 212
Cdd:cd19144 155 LSECSAETLRRAHAV--HPIAAVQIEyspfsLDIERPEIGVLDTCRELGVAIVAYSPLGrgfltgairspddfEEGDFRR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 213 TLPTGQKLDWaPAPSDLQDQnVLALAEKTHKTPAQVLLRYALDRGCAIL--PKSIQENRIKENFEVFDFSLTEEDIAKLE 290
Cdd:cd19144 233 MAPRFQAENF-PKNLELVDK-IKAIAKKKNVTAGQLTLAWLLAQGDDIIpiPGTTKLKRLEENLGALKVKLTEEEEKEIR 310
|
.
gi 17550248 291 E 291
Cdd:cd19144 311 E 311
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
13-291 |
1.32e-20 |
|
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: 89.98 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 13 GVEMPVIGLGT-------------WQSSPAEVITAVKTAVKAGYRLIDTASVY---QNEEAIGTAIKElleegvvKREEL 76
Cdd:cd19091 10 GLKVSELALGTmtfgggggffgawGGVDQEEADRLVDIALDAGINFFDTADVYsegESEEILGKALKG-------RRDDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 77 FITTKAwTHELAPGKLEGGL---------RESLKKLQLEYVDLYLAHMPAAfnddmsehiASPVEDVWRQFDAVYKAGLA 147
Cdd:cd19091 83 LIATKV-RGRMGEGPNDVGLsrhhiiravEASLKRLGTDYIDLYQLHGFDA---------LTPLEETLRALDDLVRQGKV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 148 KAVGVSNWNNDQISRALAL----GLTPVhnsqVELHLYFP------QHDHVDFCKKHNISVTSYATLGS---PGRVNFTL 214
Cdd:cd19091 153 RYIGVSNFSAWQIMKALGIserrGLARF----VALQAYYSllgrdlEHELMPLALDQGVGLLVWSPLAGgllSGKYRRGQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 215 P----TGQKLDWAPAPS-------DLQDQnVLALAEKTHKTPAQVLLRYALDR--GCAILPKSIQENRIKENFEVFDFSL 281
Cdd:cd19091 229 PapegSRLRRTGFDFPPvdrergyDVVDA-LREIAKETGATPAQVALAWLLSRptVSSVIIGARNEEQLEDNLGAAGLSL 307
|
330
....*....|
gi 17550248 282 TEEDIAKLEE 291
Cdd:cd19091 308 TPEEIARLDK 317
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-291 |
3.77e-20 |
|
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: 88.81 E-value: 3.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 15 EMPVIGLGTWQ--------SSPAEVITAVKTAVKAGYRLIDTASVYQN-EEAIGTAIKELLEEGVVKREELFIT------ 79
Cdd:cd19101 1 TISRVINGMWQlsgghggiRDEDAAVRAMAAYVDAGLTTFDCADIYGPaEELIGEFRKRLRRERDAADDVQIHTkwvpdp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 80 -----TKAWThelapgklEGGLRESLKKLQLEYVDL------------YLahmpaafnddmsehiaspveDVWRQFDAVY 142
Cdd:cd19101 81 geltmTRAYV--------EAAIDRSLKRLGVDRLDLvqfhwwdysdpgYL--------------------DAAKHLAELQ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 143 KAGLAKAVGVSNWNNDQISRALALGLTPVHNsQVELHLY--FPQHDHVDFCKKHNISVTSYATLG------------SPG 208
Cdd:cd19101 133 EEGKIRHLGLTNFDTERLREILDAGVPIVSN-QVQYSLLdrRPENGMAALCEDHGIKLLAYGTLAggllsekylgvpEPT 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 209 RVNFTLPTGQK--------LDWapapsDLQdQNVLAL----AEKTHKTPAQVLLRYALDR---GCAILPKSIQEnRIKEN 273
Cdd:cd19101 212 GPALETRSLQKyklmidewGGW-----DLF-QELLRTlkaiADKHGVSIANVAVRWVLDQpgvAGVIVGARNSE-HIDDN 284
|
330
....*....|....*...
gi 17550248 274 FEVFDFSLTEEDIAKLEE 291
Cdd:cd19101 285 VRAFSFRLDDEDRAAIDA 302
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
39-256 |
5.62e-20 |
|
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: 88.04 E-value: 5.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 39 VKAGYRLIDTASVY----------QNEEAIGTAIKELLeegvvKREELFITTKAWTHE------LAPGKLEGGLRESLKK 102
Cdd:cd19081 36 VDAGGNFIDTADVYsawvpgnaggESETIIGRWLKSRG-----KRDRVVIATKVGFPMgpngpgLSRKHIRRAVEASLRR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 103 LQLEYVDLYLAHMPaafnDDmsehiASPVEDVWRQFDAVYKAGLAKAVGVSNWNNDQISRALAL----GLTPVHNSQVEL 178
Cdd:cd19081 111 LQTDYIDLYQAHWD----DP-----ATPLEETLGALNDLIRQGKVRYIGASNYSAWRLQEALELsrqhGLPRYVSLQPEY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 179 HLYFPQH---DHVDFCKKHNISVTSYATLGS---PGRVNftlpTGQKLDWAPAPSDLQDQ-------NVLA----LAEKT 241
Cdd:cd19081 182 NLVDRESfegELLPLCREEGIGVIPYSPLAGgflTGKYR----SEADLPGSTRRGEAAKRylnerglRILDaldeVAAEH 257
|
250
....*....|....*
gi 17550248 242 HKTPAQVLLRYALDR 256
Cdd:cd19081 258 GATPAQVALAWLLAR 272
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-291 |
2.84e-19 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 86.23 E-value: 2.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 16 MPVIGLGTW---------------QSSPAEVITAVKTAVKAGYRLIDTASVY---QNEEAIGTAIKElleegvVKREELF 77
Cdd:cd19103 4 LPKIALGTWswgsggaggdqvfgnHLDEDTLKAVFDKAMAAGLNLWDTAAVYgmgASEKILGEFLKR------YPREDYI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 78 ITTKaWTHELA---PGKLEGGLRESLKKLQLEYVDLYLAHMPAafnddmsehiaspveDVWR---QFDAVYKAGLAKAVG 151
Cdd:cd19103 78 ISTK-FTPQIAgqsADPVADMLEGSLARLGTDYIDIYWIHNPA---------------DVERwtpELIPLLKSGKVKHVG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 152 VSNWNNDQISRALA-LGLTPVHNSQVELHLYFPQHDH-----VDFCKKHNISVTSYATL--GS-PGRVNFTLPTGQKLDW 222
Cdd:cd19103 142 VSNHNLAEIKRANEiLAKAGVSLSAVQNHYSLLYRSSeeagiLDYCKENGITFFAYMVLeqGAlSGKYDTKHPLPEGSGR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 223 APAPSDLQDQ-----NVLA-LAEKTHKTPAQVLLRYALDRGcaILP-----KSIQenrIKENFEVFDFSLTEEDIAKLEE 291
Cdd:cd19103 222 AETYNPLLPQleeltAVMAeIGAKHGASIAQVAIAWAIAKG--TTPiigvtKPHH---VEDAARAASITLTDDEIKELEQ 296
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
12-290 |
4.73e-19 |
|
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: 85.37 E-value: 4.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 12 NGVEMPVIGLG----TW---QSSPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTA--IKELLEEGVVKREELFITTK- 81
Cdd:cd19077 1 NGKLVGPIGLGlmglTWrpnPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHANLklLARFFRKYPEYADKVVLSVKg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 82 AW-THELAP-GKLEG---GLRESLKKL-QLEYVDLYlahMPAAFNDDMsehiasPVEDVWRQFDAVYKAGLAKAVGVSNW 155
Cdd:cd19077 81 GLdPDTLRPdGSPEAvrkSIENILRALgGTKKIDIF---EPARVDPNV------PIEETIKALKELVKEGKIRGIGLSEV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 156 NNDQISRALALglTPVHNSQVELHLYF---PQHDHVDFCKKHNISVTSYATLGSpGrvnftLPTGQKLDWAPAPSD---- 228
Cdd:cd19077 152 SAETIRRAHAV--HPIAAVEVEYSLFSreiEENGVLETCAELGIPIIAYSPLGR-G-----LLTGRIKSLADIPEGdfrr 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17550248 229 ----LQDQNV---LALAEKTHK-------TPAQVLLRY--ALDRGCAI-LPKSIQENRIKENFEVFDFSLTEEDIAKLE 290
Cdd:cd19077 224 hldrFNGENFeknLKLVDALQElaekkgcTPAQLALAWilAQSGPKIIpIPGSTTLERVEENLKAANVELTDEELKEIN 302
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
13-291 |
8.84e-19 |
|
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: 84.96 E-value: 8.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 13 GVEMPVIGLGTW-----QSSPAEVITAVKTAVKAGYRLIDTASVYQN---EEAIGTAIKELleegVVKREELFITTKA-W 83
Cdd:cd19143 10 GLKVSALSFGSWvtfgnQVDVDEAKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIKEL----GWPRSDYVVSTKIfW 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 84 THELAPGKLEG--------GLRESLKKLQLEYVDLYLAHMPaafnDdmsehIASPVEDVWRQFDAVYKAGLAKAVGVSNW 155
Cdd:cd19143 86 GGGGPPPNDRGlsrkhiveGTKASLKRLQLDYVDLVFCHRP----D-----PATPIEETVRAMNDLIDQGKAFYWGTSEW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 156 NNDQISRALA----LGLTPVHNSQVELHLYFPQHDHVDF---CKKHNISVTSYATLGS---PGRVNFTLPTGQKL----- 220
Cdd:cd19143 157 SAQQIEEAHEiadrLGLIPPVMEQPQYNLFHRERVEVEYaplYEKYGLGTTTWSPLASgllTGKYNNGIPEGSRLalpgy 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 221 DWAPAPSDLQDQNVLA-------LAEKTHKTPAQVLLRYAL---DRGCAILPKSiQENRIKENFEVFDF--SLTEEDIAK 288
Cdd:cd19143 237 EWLKDRKEELGQEKIEkvrklkpIAEELGCSLAQLAIAWCLknpNVSTVITGAT-KVEQLEENLKALEVlpKLTPEVMEK 315
|
...
gi 17550248 289 LEE 291
Cdd:cd19143 316 IEA 318
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
37-254 |
2.19e-18 |
|
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: 83.37 E-value: 2.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 37 TAVKAGYRLIDTASVYQN-------EEAIGTAIKELleegvVKREELFITTK--------AWTHELAPGKLEGGLRESLK 101
Cdd:cd19082 25 AFVELGGNFIDTARVYGDwvergasERVIGEWLKSR-----GNRDKVVIATKgghpdledMSRSRLSPEDIRADLEESLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 102 KLQLEYVDLYLAHMpaafnDDMSEhiasPVEDVWRQFDAVYKAGLAKAVGVSNWNNDQISRALAL----GLTPVHNSQVE 177
Cdd:cd19082 100 RLGTDYIDLYFLHR-----DDPSV----PVGEIVDTLNELVRAGKIRAFGASNWSTERIAEANAYakahGLPGFAASSPQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 178 LHLYFPQHDHV-------------DFCKKHNISVTSYAtlgSPGRVNFTLPTGQKLDWAPAPSDLQD--------QNVLA 236
Cdd:cd19082 171 WSLARPNEPPWpgptlvamdeemrAWHEENQLPVFAYS---SQARGFFSKRAAGGAEDDSELRRVYYseenferlERAKE 247
|
250
....*....|....*...
gi 17550248 237 LAEKTHKTPAQVLLRYAL 254
Cdd:cd19082 248 LAEEKGVSPTQIALAYVL 265
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-275 |
4.07e-18 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 81.76 E-value: 4.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 13 GVEMPVIGLGT---WQSSPAEVITAVKTAVKAGYRLIDTASVYQN-EEAIGTAIKElleegvvKREELFITTKawTHELA 88
Cdd:cd19100 8 GLKVSRLGFGGgplGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKG-------RRDKVFLATK--TGARD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 89 PGKLEGGLRESLKKLQLEYVDLYLAHM---PAAFNDDMSEHIAspvedvwrqFDAVYKA---GLAKAVGVSNWNNDQISR 162
Cdd:cd19100 79 YEGAKRDLERSLKRLGTDYIDLYQLHAvdtEEDLDQVFGPGGA---------LEALLEAkeeGKIRFIGISGHSPEVLLR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 163 ALALG-----LTPVhnSQVELHLYFPQHDHVDFCKKHNISVTSYATLGSpGRvnftlptgqkldwapapsdlqdqnvlaL 237
Cdd:cd19100 150 ALETGefdvvLFPI--NPAGDHIDSFREELLPLAREKGVGVIAMKVLAG-GR---------------------------L 199
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 17550248 238 AEKTHKTPAQvLLRYALDRGC--AILP--KSIQEnrIKENFE 275
Cdd:cd19100 200 LSGDPLDPEQ-ALRYALSLPPvdVVIVgmDSPEE--LDENLA 238
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
11-285 |
5.18e-18 |
|
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: 82.22 E-value: 5.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 11 SNGVEMPVIGLGTW-----QSSPAEVITAVKTAVKAGYRLIDTASVYQN---EEAIGTAIKELLEegvvKREELFITTKA 82
Cdd:cd19092 1 PEGLEVSRLVLGCMrladwGESAEELLSLIEAALELGITTFDHADIYGGgkcEELFGEALALNPG----LREKIEIQTKC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 83 wthELAPGKLEGGLR----------------ESLKKLQLEYVDLYLAHMPAAFNDdmsehiaspVEDVWRQFDAVYKAGL 146
Cdd:cd19092 77 ---GIRLGDDPRPGRikhydtskehilasveGSLKRLGTDYLDLLLLHRPDPLMD---------PEEVAEAFDELVKSGK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 147 AKAVGVSNWNNDQISrAL--ALGLTPVHNsQVELHLYFPQHDH---VDFCKKHNISVTSYATLGSpGRVnFTlptgqkld 221
Cdd:cd19092 145 VRYFGVSNFTPSQIE-LLqsYLDQPLVTN-QIELSLLHTEAIDdgtLDYCQLLDITPMAWSPLGG-GRL-FG-------- 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 222 wapaPSDLQDQNVLA----LAEKTHKTPAQVLLRYALDRGCAILP--KSIQENRIKENFEVFDFSLTEED 285
Cdd:cd19092 213 ----GFDERFQRLRAaleeLAEEYGVTIEAIALAWLLRHPARIQPilGTTNPERIRSAVKALDIELTREE 278
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
8-289 |
5.82e-18 |
|
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: 82.48 E-value: 5.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 8 IKL-SNGVEMPVIGLG-----TWQSSP---AEVITAVKTAVKAGYRLIDTASVY---QNEEAIGTAIKELLeegvvkREE 75
Cdd:cd19145 3 VKLgSQGLEVSAQGLGcmglsGDYGAPkpeEEGIALIHHAFNSGVTFLDTSDIYgpnTNEVLLGKALKDGP------REK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 76 LFITTKAWTHELAPGKLE---------GGLRESLKKLQLEYVDLYLAHmpaafNDDMSehiaSPVEDVWRQFDAVYKAGL 146
Cdd:cd19145 77 VQLATKFGIHEIGGSGVEvrgdpayvrAACEASLKRLDVDYIDLYYQH-----RIDTT----VPIEITMGELKKLVEEGK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 147 AKAVGVSNWNNDQISRALAlgLTPVHNSQVELHLYF--PQHDHVDFCKKHNISVTSYATLgspGRVNFTlpTGQKLDWAP 224
Cdd:cd19145 148 IKYIGLSEASADTIRRAHA--VHPITAVQLEWSLWTrdIEEEIIPTCRELGIGIVPYSPL---GRGFFA--GKAKLEELL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 225 APSDL-------QDQN----------VLALAEKTHKTPAQVLLRYALDRG---CAIlPKSIQENRIKENFEVFDFSLTEE 284
Cdd:cd19145 221 ENSDVrkshprfQGENleknkvlyerVEALAKKKGCTPAQLALAWVLHQGedvVPI-PGTTKIKNLNQNIGALSVKLTKE 299
|
....*
gi 17550248 285 DIAKL 289
Cdd:cd19145 300 DLKEI 304
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
22-254 |
1.14e-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: 81.93 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 22 GTW-QSSPAEVITAVKTAVKAGYRLIDTASVY---QNEEAIGTAIKELleegvvkREELFITTK----AWTHELAPGKLE 93
Cdd:cd19104 24 GLMgRTTREEQIAAVRRALDLGINFFDTAPSYgdgKSEENLGRALKGL-------PAGPYITTKvrldPDDLGDIGGQIE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 94 GGLRESLKKLQLEYVDLYLAHMPAAFNDDMSEHIASPVED------VWRQFDAVYKAGLAKAVGVSNWNN-DQISRALAL 166
Cdd:cd19104 97 RSVEKSLKRLKRDSVDLLQLHNRIGDERDKPVGGTLSTTDvlglggVADAFERLRSEGKIRFIGITGLGNpPAIRELLDS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 167 GltPVHNSQVELHL-----------YFPQHDH---VDFCKKHNISVTSYATLGSpGRVNFTL---PTGQKLDWAPAPSDL 229
Cdd:cd19104 177 G--KFDAVQVYYNLlnpsaaearprGWSAQDYggiIDAAAEHGVGVMGIRVLAA-GALTTSLdrgREAPPTSDSDVAIDF 253
|
250 260
....*....|....*....|....*.
gi 17550248 230 Q-DQNVLALAEKTHKTPAQVLLRYAL 254
Cdd:cd19104 254 RrAAAFRALAREWGETLAQLAHRFAL 279
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
17-254 |
8.55e-17 |
|
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: 78.75 E-value: 8.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 17 PVIGLGT------WQS-SPAEVITAVKTAVKAGYRLIDTASVYQN-EEAIGTAIKElleegvVKREELFITTKAWTHE-- 86
Cdd:cd19090 1 SALGLGTaglggvFGGvDDDEAVATIRAALDLGINYIDTAPAYGDsEERLGLALAE------LPREPLVLSTKVGRLPed 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 87 ---LAPGKLEGGLRESLKKLQLEYVDLYLAHMPAAFNDDMSEHIASPVEdvwrQFDAVYKAGLAKAVGVSNWNNDQISRA 163
Cdd:cd19090 75 tadYSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILAPGGALE----ALLELKEEGLIKHIGLGGGPPDLLRRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 164 L----------ALGLTPVhNSQVELHLyfpqhdhVDFCKKHNISV---TSYAT-LGSPGRVNFTLPTGqklDWAPAPSDL 229
Cdd:cd19090 151 IetgdfdvvltANRYTLL-DQSAADEL-------LPAAARHGVGVinaSPLGMgLLAGRPPERVRYTY---RWLSPELLD 219
|
250 260
....*....|....*....|....*
gi 17550248 230 QDQNVLALAEKTHKTPAQVLLRYAL 254
Cdd:cd19090 220 RAKRLYELCDEHGVPLPALALRFLL 244
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
18-160 |
1.87e-16 |
|
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: 78.37 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 18 VIGLGTW-----QSSPAEVITAVKTAVKAGYRLIDTASVYQN---EEAIGTAikELLEEGVVkreelfITTKA---WTHE 86
Cdd:cd19075 4 ILGTMTFgsqgrFTTAEAAAELLDAFLERGHTEIDTARVYPDgtsEELLGEL--GLGERGFK------IDTKAnpgVGGG 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17550248 87 LAPGKLEGGLRESLKKLQLEYVDLYLAHMPaafndDMSehiaSPVEDVWRQFDAVYKAGLAKAVGVSNWNNDQI 160
Cdd:cd19075 76 LSPENVRKQLETSLKRLKVDKVDVFYLHAP-----DRS----TPLEETLAAIDELYKEGKFKEFGLSNYSAWEV 140
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
21-166 |
9.63e-16 |
|
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, Saccharopolyspora erythraea EryBII, and Streptomyces avermitilis aveBVIII are founding members of aldo-keto reductase family 12 member A1 (AKR12A1), B1 (AKR12B1), and C1(AKR12C1), respectively. TylCII acts as a NDP-hexose 2,3-enoyl reductase. EryBII is a mycarose/desosamine reductase involved in L-mycarose and D-desosamine production. aveBVIII functions as a dTDP-4-keto-6-deoxy-L-hexose-2,3-reductase.
Pssm-ID: 381313 [Multi-domain] Cd Length: 310 Bit Score: 76.07 E-value: 9.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 21 LGTW----QSSPAEVITAVKTAVKAGYRLIDTASVYQN---EEAIGTAIKElleegvvKREELFITTKAwTHELAPGKLE 93
Cdd:cd19087 18 LGTMnfggRTDEETSFAIMDRALDAGINFFDTADVYGGgrsEEIIGRWIAG-------RRDDIVLATKV-FGPMGDDPND 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 94 GGL---------RESLKKLQLEYVDLYLAHmpaafNDDMSehiaSPVEDVWRQFDAVYKAGLAKAVGVSNWNNDQISRAL 164
Cdd:cd19087 90 RGLsrrhirravEASLRRLQTDYIDLYQMH-----HFDRD----TPLEETLRALDDLVRQGKIRYIGVSNFAAWQIAKAQ 160
|
..
gi 17550248 165 AL 166
Cdd:cd19087 161 GI 162
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
19-291 |
2.48e-15 |
|
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: 75.29 E-value: 2.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 19 IGLGT--W--QSSPAEVITAVKTAVKAGYRLIDTASVY----------QNEEAIGTAIKelleeGVVKREELFITTKA-- 82
Cdd:cd19094 4 ICLGTmtWgeQNTEAEAHEQLDYAFDEGVNFIDTAEMYpvppspetqgRTEEIIGSWLK-----KKGNRDKVVLATKVag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 83 ----WTHELAPG------KLEGGLRESLKKLQLEYVDLYLAHMPA---------AFNDDMSEHIASPVEDVWRQFDAVYK 143
Cdd:cd19094 79 pgegITWPRGGGtrldreNIREAVEGSLKRLGTDYIDLYQLHWPDrytplfgggYYTEPSEEEDSVSFEEQLEALGELVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 144 AGLAKAVGVSNWNNDQISRAL----ALGLTPVHNSQVELHLYFPQH--DHVDFCKKHNISVTSYATLGspgrvnFTLPTG 217
Cdd:cd19094 159 AGKIRHIGLSNETPWGVMKFLelaeQLGLPRIVSIQNPYSLLNRNFeeGLAEACHRENVGLLAYSPLA------GGVLTG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 218 QKLDWAPAPSD-------------LQDQNVLA------LAEKTHKTPAQVLLRYALDR---GCAIL-PKSIQEnrIKENF 274
Cdd:cd19094 233 KYLDGAARPEGgrlnlfpgymaryRSPQALEAvaeyvkLARKHGLSPAQLALAWVRSRpfvTSTIIgATTLEQ--LKENI 310
|
330
....*....|....*..
gi 17550248 275 EVFDFSLTEEDIAKLEE 291
Cdd:cd19094 311 DAFDVPLSDELLAEIDA 327
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
17-278 |
2.10e-14 |
|
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381322 [Multi-domain] Cd Length: 255 Bit Score: 71.82 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 17 PVIGLGT------WQSS--PAEVITAVKTAVKAGYRLIDTASVY---QNEEAIGTAIKELleegvvKREELFITTK-AWT 84
Cdd:cd19096 1 SVLGFGTmrlpesDDDSidEEKAIEMIRYAIDAGINYFDTAYGYgggKSEEILGEALKEG------PREKFYLATKlPPW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 85 HELAPGKLEGGLRESLKKLQLEYVDLYLAHmpaAFNDDMSEHIASPvEDVWRQFDAVYKAGLAKAVGVS-NWNNDQISRA 163
Cdd:cd19096 75 SVKSAEDFRRILEESLKRLGVDYIDFYLLH---GLNSPEWLEKARK-GGLLEFLEKAKKEGLIRHIGFSfHDSPELLKEI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 164 LALGltPVHNSQVELHLYFPQHDH----VDFCKKHNISVtsYATlgSPgrvnftLPTGQKLDWAPApsdlqdqnVLALAE 239
Cdd:cd19096 151 LDSY--DFDFVQLQYNYLDQENQAgrpgIEYAAKKGMGV--IIM--EP------LKGGGLANNPPE--------ALAILC 210
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 17550248 240 KTHKTPAQVLLRYALDRG---CAIL-PKSIQEnrIKENFEVFD 278
Cdd:cd19096 211 GAPLSPAEWALRFLLSHPevtTVLSgMSTPEQ--LDENIAAAD 251
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
12-189 |
1.42e-13 |
|
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: 70.01 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 12 NGVEMPVIGLGTW-----QSSPAEVITAVKTAVKAGYRLIDTASVYQNEEAIGTaIKELLEEGVVKREELFITTKA-WTH 85
Cdd:cd19160 11 SGLRVSCLGLGTWvtfgsQISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERT-LGNILKSKGWRRSSYVVTTKIyWGG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 86 E------LAPGKLEGGLRESLKKLQLEYVDLYLAHMPAAfnddmsehiASPVEDVWRQFDAVYKAGLAKAVGVSNWNNDQ 159
Cdd:cd19160 90 QaetergLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDP---------NSPMEEIVRAMTYVINQGMAMYWGTSRWSAME 160
|
170 180 190
....*....|....*....|....*....|....
gi 17550248 160 ISRALALG----LTPVHNSQVELHLYfpQHDHVD 189
Cdd:cd19160 161 IMEAYSVArqfnLIPPVCEQAEYHLF--QREKVE 192
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
39-262 |
1.98e-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: 381391 [Multi-domain] Cd Length: 291 Bit Score: 69.28 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 39 VKAGYRLIDTASVY----------QNEEAIGtaiKELLEEGVvkREELFITTK---------AWTHE---LAPGKLEGGL 96
Cdd:cd19752 27 VAAGGNFLDTANNYafwteggvggESERLIG---RWLKDRGN--RDDVVIATKvgagprdpdGGPESpegLSAETIEQEI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 97 RESLKKLQLEYVDLYLAHMpaafnDDMsehiASPVEDVWRQFDAVYKAGLAKAVGVSNWNNDQISRALAL----GLTPVH 172
Cdd:cd19752 102 DKSLRRLGTDYIDLYYAHV-----DDR----DTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERARQIarqqGWAEFS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 173 NSQVELHLYFPQH------------DHVDFCKKH-NISVTSYATL--GSPGRVNFTLPTgqklDWAPAPSDLQDQNVLAL 237
Cdd:cd19752 173 AIQQRHSYLRPRPgadfgvqrivtdELLDYASSRpDLTLLAYSPLlsGAYTRPDRPLPE----QYDGPDSDARLAVLEEV 248
|
250 260
....*....|....*....|....*
gi 17550248 238 AEKTHKTPAQVLLRYALDRGCAILP 262
Cdd:cd19752 249 AGELGATPNQVVLAWLLHRTPAIIP 273
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
12-181 |
3.91e-13 |
|
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: 68.91 E-value: 3.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 12 NGVEMPVIGLGTWQSSPAEVITAV-----KTAVKAGYRLIDTASVY---QNEEAIGTAIKElleeGVVKREELFITTKAW 83
Cdd:cd19159 9 SGLRVSCLGLGTWVTFGGQISDEVaerlmTIAYESGVNLFDTAEVYaagKAEVILGSIIKK----KGWRRSSLVITTKLY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 84 -------THELAPGKLEGGLRESLKKLQLEYVDLYLAHMPAAfnddmsehiASPVEDVWRQFDAVYKAGLAKAVGVSNWN 156
Cdd:cd19159 85 wggkaetERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDS---------NTPMEEIVRAMTHVINQGMAMYWGTSRWS 155
|
170 180
....*....|....*....|....*....
gi 17550248 157 NDQISRALALG----LTPVHNSQVELHLY 181
Cdd:cd19159 156 AMEIMEAYSVArqfnMIPPVCEQAEYHLF 184
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
13-181 |
5.39e-13 |
|
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: 68.24 E-value: 5.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 13 GVEMPVIGLGTW-----QSS---PAEVITAvktAVKAGYRLIDTASVYQNEEAiGTAIKELLEEGVVKREELFITTKA-W 83
Cdd:cd19141 9 GLRVSCLGLGTWvtfgsQISdevAEELVTL---AYENGINLFDTAEVYAAGKA-EIVLGKILKKKGWRRSSYVITTKIfW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 84 ThelapGKLEG-----------GLRESLKKLQLEYVDLYLAHMPaafnDDMsehiaSPVEDVWRQFDAVYKAGLAKAVGV 152
Cdd:cd19141 85 G-----GKAETerglsrkhiieGLKASLERLQLEYVDIVFANRP----DPN-----TPMEEIVRAFTHVINQGMAMYWGT 150
|
170 180 190
....*....|....*....|....*....|...
gi 17550248 153 SNWNNDQISRALALG----LTPVHNSQVELHLY 181
Cdd:cd19141 151 SRWSAMEIMEAYSVArqfnLIPPIVEQAEYHLF 183
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-167 |
7.00e-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: 67.55 E-value: 7.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 19 IGLGTWQ-------------SSPAEVITAVKTAVKAGYRLIDTASVYQN-EEAIGTAIKELleegvvkrEELFITTK--- 81
Cdd:cd19097 3 LALGTAQfgldygianksgkPSEKEAKKILEYALKAGINTLDTAPAYGDsEKVLGKFLKRL--------DKFKIITKlpp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 82 -AWTHELAPGKLEGGLRESLKKLQLEYVDLYLAHMPAAFNDDMsehiaspvEDVWRQFDAVYKAGLAKAVGVSNWNNDQI 160
Cdd:cd19097 75 lKEDKKEDEAAIEASVEASLKRLKVDSLDGLLLHNPDDLLKHG--------GKLVEALLELKKEGLIRKIGVSVYSPEEL 146
|
....*..
gi 17550248 161 SRALALG 167
Cdd:cd19097 147 EKALESF 153
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
13-166 |
2.02e-12 |
|
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: 66.51 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 13 GVEMPVIGLGTWQ-----SSPAEVITAVKTAVKAGYRLIDTASVY-----QNEEAIGTAIKELLEEgvvKREELFITTKA 82
Cdd:cd19089 8 GLHLPAISLGLWHnfgdyTSPEEARELLRTAFDLGITHFDLANNYgpppgSAEENFGRILKRDLRP---YRDELVISTKA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 83 wTHELAPGKLEGG---------LRESLKKLQLEYVDLYLAHMPaafndDMSehiaSPVEDVWRQFDAVYKAGLAKAVGVS 153
Cdd:cd19089 85 -GYGMWPGPYGDGgsrkyllasLDQSLKRMGLDYVDIFYHHRY-----DPD----TPLEETMTALADAVRSGKALYVGIS 154
|
170
....*....|...
gi 17550248 154 NWNNDQISRALAL 166
Cdd:cd19089 155 NYPGAKARRAIAL 167
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
12-181 |
1.80e-11 |
|
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: 63.95 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 12 NGVEMPVIGLGTWQSSPAEVITAV-----KTAVKAGYRLIDTASVY---QNEEAIGTAIKElleEGVvKREELFITTKAW 83
Cdd:cd19158 9 SGLRVSCLGLGTWVTFGGQITDEMaehlmTLAYDNGINLFDTAEVYaagKAEVVLGNIIKK---KGW-RRSSLVITTKIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 84 -------THELAPGKLEGGLRESLKKLQLEYVDLYLAHMPAAfnddmsehiASPVEDVWRQFDAVYKAGLAKAVGVSNWN 156
Cdd:cd19158 85 wggkaetERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDP---------NTPMEETVRAMTHVINQGMAMYWGTSRWS 155
|
170 180
....*....|....*....|....*....
gi 17550248 157 NDQISRALALG----LTPVHNSQVELHLY 181
Cdd:cd19158 156 SMEIMEAYSVArqfnLIPPICEQAEYHMF 184
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
9-284 |
4.39e-11 |
|
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: 62.57 E-value: 4.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 9 KLSN-GVEMPVIGLGT-------WQSSPAEVITAVKTAVKAGYRLIDTASVY---QNEEAIGTAIKElleegvVKREELF 77
Cdd:cd19163 5 KLGKtGLKVSKLGFGAsplggvfGPVDEEEAIRTVHEALDSGINYIDTAPWYgqgRSETVLGKALKG------IPRDSYY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 78 ITTKAWTHELAPG--------KLEGGLRESLKKLQLEYVDLYLAHMPaAFNDDMSEHIAS--PVedvwrqFDAVYKAGLA 147
Cdd:cd19163 79 LATKVGRYGLDPDkmfdfsaeRITKSVEESLKRLGLDYIDIIQVHDI-EFAPSLDQILNEtlPA------LQKLKEEGKV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 148 KAVGVSNWNNDQISRALALGLTPV-----------HNSQVElhlyfpqhDHVDFCKKHNISVTSYATLGSPGRVNFTLPt 216
Cdd:cd19163 152 RFIGITGYPLDVLKEVLERSPVKIdtvlsychytlNDTSLL--------ELLPFFKEKGVGVINASPLSMGLLTERGPP- 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17550248 217 gqklDWAPAPSDLQD--QNVLALAEKTHKTPAQVLLRYALDR--------GCAilpksiQENRIKENFEVFDFSLTEE 284
Cdd:cd19163 223 ----DWHPASPEIKEacAKAAAYCKSRGVDISKLALQFALSNpdiattlvGTA------SPENLRKNLEAAEEPLDAH 290
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
12-163 |
8.61e-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: 61.71 E-value: 8.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 12 NGVEMPVIGLGTWQS-SP------AEVItaVKTAVKAGYRLIDTASVYQNEEAiGTAIKELLEEGVVKREELFITTKAWT 84
Cdd:cd19142 9 SGLRVSNVGLGTWSTfSTaiseeqAEEI--VTLAYENGINYFDTSDAFTSGQA-ETELGRILKKKGWKRSSYIVSTKIYW 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 85 HElapGKLEGGL---------RESLKKLQLEYVDLYLAHMpaafNDDMsehiaSPVEDVWRQFDAVYKAGLAKAVGVSNW 155
Cdd:cd19142 86 SY---GSEERGLsrkhiiesvRASLRRLQLDYIDIVIIHK----ADPM-----CPMEEVVRAMSYLIDNGLIMYWGTSRW 153
|
....*...
gi 17550248 156 NNDQISRA 163
Cdd:cd19142 154 SPVEIMEA 161
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
13-166 |
2.52e-10 |
|
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: 60.49 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 13 GVEMPVIGLGTW---------QSSPAevitAVKTAVKAGYRLIDTASVY-----QNEEAIGTAIKELLEEgvvKREELFI 78
Cdd:cd19151 9 GLKLPAISLGLWhnfgdvdryENSRA----MLRRAFDLGITHFDLANNYgpppgSAEENFGRILKEDLKP---YRDELII 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 79 TTKAwTHELAPGK---------LEGGLRESLKKLQLEYVDLYLAHMPAAfnddmsehiASPVEDVWRQFDAVYKAGLAKA 149
Cdd:cd19151 82 STKA-GYTMWPGPygdwgskkyLIASLDQSLKRMGLDYVDIFYHHRPDP---------ETPLEETMGALDQIVRQGKALY 151
|
170
....*....|....*..
gi 17550248 150 VGVSNWNNDQISRALAL 166
Cdd:cd19151 152 VGISNYPPEEAREAAAI 168
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
13-166 |
8.80e-10 |
|
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
Pssm-ID: 381376 [Multi-domain] Cd Length: 309 Bit Score: 58.62 E-value: 8.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 13 GVEMPVIGLGTWQS----SPAEVITAV-KTAVKAGYRLIDTASVY-----QNEEAIGTAIKELLEEgvvKREELFITTKA 82
Cdd:cd19150 9 GLKLPALSLGLWHNfgddTPLETQRAIlRTAFDLGITHFDLANNYgpppgSAEENFGRILREDFAG---YRDELIISTKA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 83 wTHELAPGKL-EGGLR--------ESLKKLQLEYVDLYLAHMpaaFNDDmsehiaSPVEDVWRQFDAVYKAGLAKAVGVS 153
Cdd:cd19150 86 -GYDMWPGPYgEWGSRkyllasldQSLKRMGLDYVDIFYSHR---FDPD------TPLEETMGALDHAVRSGKALYVGIS 155
|
170
....*....|...
gi 17550248 154 NWNNDQISRALAL 166
Cdd:cd19150 156 SYSPERTREAAAI 168
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
12-291 |
5.56e-09 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 56.54 E-value: 5.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 12 NGVEMPVIGLGTWQS----SPAEVITAV-KTAVKAGYRLIDTASVY-----QNEEAIGtaiKELLEEGVVKREELFITTK 81
Cdd:PRK09912 21 SGLRLPALSLGLWHNfghvNALESQRAIlRKAFDLGITHFDLANNYgpppgSAEENFG---RLLREDFAAYRDELIISTK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 82 AwTHELAPGKLEGG---------LRESLKKLQLEYVDLYLAHMpaafnddMSEHiaSPVEDVWRQFDAVYKAGLAKAVGV 152
Cdd:PRK09912 98 A-GYDMWPGPYGSGgsrkyllasLDQSLKRMGLEYVDIFYSHR-------VDEN--TPMEETASALAHAVQSGKALYVGI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 153 SNWNNDQISRALALgltpVHNSQVELHLYFPQHDHVD-FCKKHNISVTSYATlgSPGRVNFT-----LPTGQKLDWAPAP 226
Cdd:PRK09912 168 SSYSPERTQKMVEL----LREWKIPLLIHQPSYNLLNrWVDKSGLLDTLQNN--GVGCIAFTplaqgLLTGKYLNGIPQD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 227 SDLQ---------DQNVLA------------LAEKTHKTPAQVLLRYAL--DRGCAILPKSIQENRIKENFEVF-DFSLT 282
Cdd:PRK09912 242 SRMHregnkvrglTPKMLTeanlnslrllneMAQQRGQSMAQMALSWLLkdERVTSVLIGASRAEQLEENVQALnNLTFS 321
|
....*....
gi 17550248 283 EEDIAKLEE 291
Cdd:PRK09912 322 TEELAQIDQ 330
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
34-281 |
2.05e-08 |
|
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: 54.59 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 34 AVKTAVKAGYRLIDTASVYQNEEAI-GTAIKELLEEgvVKREELFITTKA-----WTHELAPGKLEGGLRESLKKLQLEY 107
Cdd:cd19164 39 IVRRALELGIRAFDTSPYYGPSEIIlGRALKALRDE--FPRDTYFIITKVgrygpDDFDYSPEWIRASVERSLRRLHTDY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 108 VDLYLAHmPAAFNDDmsehiaspvEDVWRQFDAVYK---AGLAKAVGVSNWNNDQISRALALGLTPVHNSqVELHLYFPQ 184
Cdd:cd19164 117 LDLVYLH-DVEFVAD---------EEVLEALKELFKlkdEGKIRNVGISGYPLPVLLRLAELARTTAGRP-LDAVLSYCH 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 185 HDhvdfckKHNISVTSY-ATLGSPGRVNFTL---PTGQKL-------DWAPAPSDLQD--QNVLALAEKTHKTPAQVLLR 251
Cdd:cd19164 186 YT------LQNTTLLAYiPKFLAAAGVKVVLnasPLSMGLlrsqgppEWHPASPELRAaaAKAAEYCQAKGTDLADVALR 259
|
250 260 270
....*....|....*....|....*....|....*
gi 17550248 252 YALDRGCAILP-----KSIQEnrIKENFEVFDFSL 281
Cdd:cd19164 260 YALREWGGEGPtvvgcSNVDE--LEEAVEAYWSVL 292
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
12-164 |
1.35e-07 |
|
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: 52.15 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 12 NGVEMPVIGLGTWQSSPAEVITA---VKTAVKAGYRLIDTASVYQNEEA---IGTAIKELleegVVKREELFITTK---- 81
Cdd:cd19153 13 SPVGLGTAALGGVYGDGLEQDEAvaiVAEAFAAGINHFDTSPYYGAESSeavLGKALAAL----QVPRSSYTVATKvgry 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 82 -AWTHELAPGKLEGGLRESLKKLQLEYVDLYLAHMPAAFNDDMSEHIASPVEDVWRQfdavykAGLAKAVGVSNWNNDQI 160
Cdd:cd19153 89 rDSEFDYSAERVRASVATSLERLHTTYLDVVYLHDIEFVDYDTLVDEALPALRTLKD------EGVIKRIGIAGYPLDTL 162
|
....
gi 17550248 161 SRAL 164
Cdd:cd19153 163 TRAT 166
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
14-291 |
2.24e-07 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 51.78 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 14 VEMPVIGLGTW----QSSPAEVITAVKTAVKAGYRLIDTASVYQ----------NEEAIGTAIKElleEGvvKREELFIT 79
Cdd:PRK10625 11 LEVSTLGLGTMtfgeQNSEADAHAQLDYAVAQGINLIDVAEMYPvpprpetqglTETYIGNWLAK---RG--SREKLIIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 80 TKAW------------THELAPGKLEGGLRESLKKLQLEYVDLYLAHMP-------AAFNDDMSEhiASPVEDVWRQFDA 140
Cdd:PRK10625 86 SKVSgpsrnndkgirpNQALDRKNIREALHDSLKRLQTDYLDLYQVHWPqrptncfGKLGYSWTD--SAPAVSLLETLDA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 141 V---YKAGLAKAVGVSNWNNDQISRALALG-------LTPVHNSQVELHLYF-------PQHDHVDfckkhnisVTSYAT 203
Cdd:PRK10625 164 LaeqQRAGKIRYIGVSNETAFGVMRYLHLAekhdlprIVTIQNPYSLLNRSFevglaevSQYEGVE--------LLAYSC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 204 LGspgrvnFTLPTGQKLDWA-PAP------------SDLQDQNVLA----LAEKTHKTPAQVLLRYALDRG--CAILPKS 264
Cdd:PRK10625 236 LA------FGTLTGKYLNGAkPAGarntlfsrftrySGEQTQKAVAayvdIAKRHGLDPAQMALAFVRRQPfvASTLLGA 309
|
330 340
....*....|....*....|....*..
gi 17550248 265 IQENRIKENFEVFDFSLTEEDIAKLEE 291
Cdd:PRK10625 310 TTMEQLKTNIESLHLTLSEEVLAEIEA 336
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
17-167 |
8.74e-07 |
|
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381388 [Multi-domain] Cd Length: 290 Bit Score: 49.66 E-value: 8.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 17 PVIGLGTWQ------SSPAEVITAVKTAVKAGYRLIDTASVY---QNEEAIGTAIKELLeegvvkREELFITTKA----- 82
Cdd:cd19162 1 PRLGLGAASlgnlarAGEDEAAATLDAAWDAGIRYFDTAPLYglgLSERRLGAALARHP------RAEYVVSTKVgrlle 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 83 -------WTHELAPGKLEGGLR----ESLKKLQLEYVDLYLAHmpaafndDMSEHIASPVEDVWRQFDAVYKAGLAKAVG 151
Cdd:cd19162 75 pgaagrpAGADRRFDFSADGIRrsieASLERLGLDRLDLVFLH-------DPDRHLLQALTDAFPALEELRAEGVVGAIG 147
|
170
....*....|....*.
gi 17550248 152 VSNWNNDQISRALALG 167
Cdd:cd19162 148 VGVTDWAALLRAARRA 163
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
3-290 |
8.55e-06 |
|
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: 46.74 E-value: 8.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 3 SATASIKLSNGV--EMPvIGlGTWQS-----SPAEVITAVKTAVKAGYRLIDTASVYQNEEA---IGTAIKELleegvVK 72
Cdd:cd19147 3 SKTAGIRVSPLIlgAMS-IG-DAWSGfmgsmDKEQAFELLDAFYEAGGNFIDTANNYQDEQSetwIGEWMKSR-----KN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 73 REELFITTKAWT----HELAPGK-----------LEGGLRESLKKLQLEYVDLYLAHmpaaFNDDMSEhiaspVEDVWRQ 137
Cdd:cd19147 76 RDQIVIATKFTTdykaYEVGKGKavnycgnhkrsLHVSVRDSLRKLQTDWIDILYVH----WWDYTTS-----IEEVMDS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 138 FDAVYKAGLAKAVGVSNWNNDQISR----ALALGLTP--VHNSQVELHLYFPQHDHVDFCKKHNISVTSYATLG-----S 206
Cdd:cd19147 147 LHILVQQGKVLYLGVSDTPAWVVSAanyyATAHGKTPfsVYQGRWNVLNRDFERDIIPMARHFGMALAPWDVLGggkfqS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 207 PGRVNFTLPTGQKLDWAPAPSDLQDQNV-----LALAEKTHKTPA--QVLLRYALDRGCAILP----KSIQEnrIKENFE 275
Cdd:cd19147 227 KKAVEERKKNGEGLRSFVGGTEQTPEEVkiseaLEKVAEEHGTESvtAIALAYVRSKAPNVFPlvggRKIEH--LKDNIE 304
|
330
....*....|....*
gi 17550248 276 VFDFSLTEEDIAKLE 290
Cdd:cd19147 305 ALSIKLTPEEIEYLE 319
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
3-290 |
4.18e-05 |
|
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: 44.72 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 3 SATASIKLSngvemPvIGLGT------WQSSPAEVI--TAVK---TAVKAGYRLIDTASVYQNEEAigtaiKELLEEGVV 71
Cdd:cd19146 4 SPTAGVRVS-----P-LCLGAmsfgeaWKSMMGECDkeTAFKlldAFYEQGGNFIDTANNYQGEES-----ERWVGEWMA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 72 KR---EELFITTKAWT----HELAPGK----------LEGGLRESLKKLQLEYVDLYLAHMPaafndDMSehiaSPVEDV 134
Cdd:cd19146 73 SRgnrDEMVLATKYTTgyrrGGPIKIKsnyqgnhaksLRLSVEASLKKLQTSYIDILYVHWW-----DYT----TSIPEL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 135 WRQFDAVYKAGLAKAVGVSN---W----NNDQisrALALGLTPVHNSQVELHLYFP--QHDHVDFCKKHNISVTSYATLg 205
Cdd:cd19146 144 MQSLNHLVAAGKVLYLGVSDtpaWvvskANAY---ARAHGLTQFVVYQGHWSAAFRdfERDILPMCEAEGMALAPWGVL- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 206 spGRVNFTLPTGQKLDWAPA----PSDLQDQNVLA----LAEKTHKTPAQVLLRYALDRGCAILP----KSIQEnrIKEN 273
Cdd:cd19146 220 --GQGQFRTEEEFKRRGRSGrkggPQTEKERKVSEklekVAEEKGTAITSVALAYVMHKAPYVFPivggRKVEH--LKGN 295
|
330
....*....|....*..
gi 17550248 274 FEVFDFSLTEEDIAKLE 290
Cdd:cd19146 296 IEALGISLSDEEIQEIE 312
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
11-114 |
7.58e-04 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 40.53 E-value: 7.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550248 11 SNGVEMPVIGLGtwqSSP----------AEVITAVKTAVKAGYRLIDTASVYQN---EEAIGTAIKELleegVVKREELF 77
Cdd:PLN02587 6 STGLKVSSVGFG---ASPlgsvfgpvseEDAIASVREAFRLGINFFDTSPYYGGtlsEKVLGKALKAL----GIPREKYV 78
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 17550248 78 ITTKAWTH----ELAPGKLEGGLRESLKKLQLEYVDLYLAH 114
Cdd:PLN02587 79 VSTKCGRYgegfDFSAERVTKSVDESLARLQLDYVDILHCH 119
|
|
| |
