|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
4-309 |
0e+00 |
|
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381381 [Multi-domain] Cd Length: 307 Bit Score: 567.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 4 TKFLTFNNGEKMPVIGIGTWQASDEEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKRWLDAGKVKREELFIVTKVPP 83
Cdd:cd19155 1 RNCVTFNNGEKMPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 84 VSNRPHEVEPTIKKSLEDLQLDYVDLYLVHTPFTININEDGSFKLDKEGLMEVDVTTNHAAIWVAMEALVEKGLTKSIGV 163
Cdd:cd19155 81 GGNRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLSKEDDSGKLDPTGEHKQDYTTDLLDIWKAMEAQVDQGLTRSIGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 164 SNFSKDQVARLLKNCKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGSKGIAKFNAGAG-IVRDLPDLMDIPEV 242
Cdd:cd19155 161 SNFNREQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPGAAHFSPGTGsPSGSSPDLLQDPVV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24644950 243 KEIAASHGKTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSSLDQNIRICDF 309
Cdd:cd19155 241 KAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIRGRTF 307
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
4-309 |
1.31e-131 |
|
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: 377.14 E-value: 1.31e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 4 TKFLTFNNGEKMPVIGIGTWQASDEEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKRWLDAGKVKREELFIVTKVPP 83
Cdd:cd19154 1 SASITLSNGVKMPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLWT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 84 VSNRPHEVEPTIKKSLEDLQLDYVDLYLVHTPFTININEDGSFKLDKEGLMEVDVttNHAAIWVAMEALVEKGLTKSIGV 163
Cdd:cd19154 81 HEHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGTMENGMSIHDAV--DVEDVWRGMEKVYDEGLTKAIGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 164 SNFSKDQVARLLKNCKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGSKGIAKFnAGAGIVRDLPDLMDIPEVK 243
Cdd:cd19154 159 SNFNNDQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSPGRANF-TKSTGVSPAPNLLQDPIVK 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24644950 244 EIAASHGKTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSSLDQNIRICDF 309
Cdd:cd19154 238 AIAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLRLFLF 303
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
12-309 |
3.50e-129 |
|
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: 370.29 E-value: 3.50e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 12 GEKMPVIGIGTWQASDEEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKRWLDAGKVKREELFIVTKVPPVSNRPHEV 91
Cdd:cd19111 1 GFPMPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLEFKDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 92 EPTIKKSLEDLQLDYVDLYLVHTPFTININEDGSFKLDkeglMEVDVTTnhaaIWVAMEALVEKGLTKSIGVSNFSKDQV 171
Cdd:cd19111 81 EKSLEKSLENLKLPYVDLYLIHHPCGFVNKKDKGEREL----ASSDVTS----VWRAMEALVSEGKVKSIGLSNFNPRQI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 172 ARLLKNCKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGSKGIAKFNAGAgivrDLPDLMDIPEVKEIAASHGK 251
Cdd:cd19111 153 NKILAYAKVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSPGRANQSLWP----DQPDLLEDPTVLAIAKELDK 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 24644950 252 TPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSSLDQNIRICDF 309
Cdd:cd19111 229 TPAQVLLRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMKYFDF 286
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
15-297 |
4.27e-129 |
|
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: 368.35 E-value: 4.27e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 15 MPVIGIGTWQASDEEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKRWLdagkVKREELFIVTKVPPVSNRPHEVEPT 94
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESG----VPREELFITTKLWPTDHGYERVREA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 95 IKKSLEDLQLDYVDLYLVHTPFTininedgsfkldkegLMEVDVTTNHAAIWVAMEALVEKGLTKSIGVSNFSKDQVARL 174
Cdd:cd19071 77 LEESLKDLGLDYLDLYLIHWPVP---------------GKEGGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEEL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 175 LKNCKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGSKGIakfnagagivrdlpDLMDIPEVKEIAASHGKTPA 254
Cdd:cd19071 142 LAAARIKPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRR--------------PLLDDPVLKEIAKKYGKTPA 207
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 24644950 255 QVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKL 297
Cdd:cd19071 208 QVLLRWALQRGVVVIPKSSNPERIKENLDVFDFELSEEDMAAI 250
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
11-306 |
5.63e-129 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 368.61 E-value: 5.63e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 11 NGEKMPVIGIGTWQASDEEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKRwldAGkVKREELFIVTKVPPVSNRPHE 90
Cdd:COG0656 1 NGVEIPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAA---SG-VPREELFVTTKVWNDNHGYDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 91 VEPTIKKSLEDLQLDYVDLYLVHTPFtininedgsfkldKEGLMEVdvttnhaaiWVAMEALVEKGLTKSIGVSNFSKDQ 170
Cdd:COG0656 77 TLAAFEESLERLGLDYLDLYLIHWPG-------------PGPYVET---------WRALEELYEEGLIRAIGVSNFDPEH 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 171 VARLLKNCKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGSkgiakfnagagivrdlPDLMDIPEVKEIAASHG 250
Cdd:COG0656 135 LEELLAETGVKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGR----------------GKLLDDPVLAEIAEKHG 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 24644950 251 KTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSSLDQNIRI 306
Cdd:COG0656 199 KTPAQVVLRWHLQRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRGERL 254
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
10-307 |
3.27e-126 |
|
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: 362.76 E-value: 3.27e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 10 NNGEKMPVIGIGTWQA-SDEEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKRWLDAGKVKREELFIVTKVPPVSNRP 88
Cdd:cd19116 6 NDGNEIPAIALGTWKLkDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLWNSYHER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 89 HEVEPTIKKSLEDLQLDYVDLYLVHTPFTININEDGSFKLDKEgLMEVDVTTnhaaIWVAMEALVEKGLTKSIGVSNFSK 168
Cdd:cd19116 86 EQVEPALRESLKRLGLDYVDLYLIHWPVAFKENNDSESNGDGS-LSDIDYLE----TWRGMEDLVKLGLTRSIGVSNFNS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 169 DQVARLLKNCKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGSKGIAKFnagagivRDLPDLMDIPEVKEIAAS 248
Cdd:cd19116 161 EQINRLLSNCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLVPRGQ-------TNPPPRLDDPTLVAIAKK 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 24644950 249 HGKTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSSLDQNIRIC 307
Cdd:cd19116 234 YGKTTAQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRVY 292
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
9-307 |
4.15e-117 |
|
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: 340.13 E-value: 4.15e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 9 FNNGEKMPVIGIGTWQASDEEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKRWLDAGK-VKREELFIVTKVPPVSNR 87
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPGKaVPREDLFVTSKLWNTKHH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 88 PHEVEPTIKKSLEDLQLDYVDLYLVHTPFTINiNEDGSFKLDKEGLMEVDvTTNHAAIWVAMEALVEKGLTKSIGVSNFS 167
Cdd:cd19106 81 PEDVEPALRKTLKDLQLDYLDLYLIHWPYAFE-RGDNPFPKNPDGTIRYD-STHYKETWKAMEKLVDKGLVKAIGLSNFN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 168 KDQVARLLKNCKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGS--KGIAKfnagagivRDLPDLMDIPEVKEI 245
Cdd:cd19106 159 SRQIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSpdRPWAK--------PDEPVLLEEPKVKAL 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24644950 246 AASHGKTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSSLDQNIRIC 307
Cdd:cd19106 231 AKKYNKSPAQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRYI 292
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
5-306 |
1.48e-115 |
|
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: 335.47 E-value: 1.48e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 5 KFLTFNNGEKMPVIGIGTWQASDEEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKRWLDAGKVKREELFIVTKVPPV 84
Cdd:cd19125 1 RFFKLNTGAKIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLWCT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 85 SNRPHEVEPTIKKSLEDLQLDYVDLYLVHTPFTIninEDGSFKLDKEGLMEVDVttnhAAIWVAMEALVEKGLTKSIGVS 164
Cdd:cd19125 81 DHAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRL---KKGAHMPEPEEVLPPDI----PSTWKAMEKLVDSGKVRAIGVS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 165 NFSKDQVARLLKNCKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGSKGIAKFNagagivrdlPDLMDIPEVKE 244
Cdd:cd19125 154 NFSVKKLEDLLAVARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGTTWVK---------KNVLKDPIVTK 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24644950 245 IAASHGKTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSSLDQNIRI 306
Cdd:cd19125 225 VAEKLGKTPAQVALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSIEQQRRV 286
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
5-305 |
2.66e-110 |
|
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: 322.82 E-value: 2.66e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 5 KFLTFNNGEKMPVIGIGTWQASDEEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKRWLDAGKVKREELFIVTKVPPV 84
Cdd:cd19123 2 KTLPLSNGDLIPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLWNN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 85 SNRPHEVEPTIKKSLEDLQLDYVDLYLVHTPftININEDGSFKLDKE---GLMEVDVttnhAAIWVAMEALVEKGLTKSI 161
Cdd:cd19123 82 SHAPEDVLPALEKTLADLQLDYLDLYLMHWP--VALKKGVGFPESGEdllSLSPIPL----EDTWRAMEELVDKGLCRHI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 162 GVSNFSKDQVARLLKNCKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGSKGIAKFNAGAgivrDLPDLMDIPE 241
Cdd:cd19123 156 GVSNFSVKKLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDRPAAMKAE----GEPVLLEDPV 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24644950 242 VKEIAASHGKTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSSLDQNIR 305
Cdd:cd19123 232 INKIAEKHGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHR 295
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
11-302 |
4.40e-106 |
|
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: 311.12 E-value: 4.40e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 11 NGEKMPVIGIGT--WQASDEEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKRWLDAGKVK-REELFIVTKVPPVSNR 87
Cdd:cd19124 1 SGQTMPVIGMGTasDPPSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKLWCSDAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 88 PHEVEPTIKKSLEDLQLDYVDLYLVHTPFTINiNEDGSFKLDKEGLMEVDVTtnhaAIWVAMEALVEKGLTKSIGVSNFS 167
Cdd:cd19124 81 PDLVLPALKKSLRNLQLEYVDLYLIHWPVSLK-PGKFSFPIEEEDFLPFDIK----GVWEAMEECQRLGLTKAIGVSNFS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 168 KDQVARLLKNCKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGSKGIAkfnAGAGIVrdlpdlMDIPEVKEIAA 247
Cdd:cd19124 156 CKKLQELLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTK---WGSNAV------MESDVLKEIAA 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 24644950 248 SHGKTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSSLDQ 302
Cdd:cd19124 227 AKGKTVAQVSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEIPQ 281
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
15-300 |
1.30e-103 |
|
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: 304.17 E-value: 1.30e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 15 MPVIGIGTWQASD-EEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKRWLDAGKVKREELFIVTKVPPVSNRPHEVEP 93
Cdd:cd19136 1 MPILGLGTFRLRGeEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 94 TIKKSLEDLQLDYVDLYLVHTPftininedGSFKLDKEGLMEVDvttNHAAIWVAMEALVEKGLTKSIGVSNFSKDQVAR 173
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWP--------GVQGLKPSDPRNAE---LRRESWRALEDLYKEGKLRAIGVSNYTVRHLEE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 174 LLKNCKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGSKGiakfnagagivrdlPDLMDIPEVKEIAASHGKTP 253
Cdd:cd19136 150 LLKYCEVPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGD--------------LRLLEDPTVLAIAKKYGRTP 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 24644950 254 AQVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSSL 300
Cdd:cd19136 216 AQVLLRWALQQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
12-327 |
1.34e-101 |
|
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: 300.87 E-value: 1.34e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 12 GEKMPVIGIGTWQASDEEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKRWLDAGKVKREELFIVTKVPPVSNRPHEV 91
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEKGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 92 EPTIKKSLEDLQLDYVDLYLVHTPFTININEDgSFKLDKEGlMEVDVTTNHAAIWVAMEALVEKGLTKSIGVSNFSKDQV 171
Cdd:cd19107 81 KGACQKTLSDLKLDYLDLYLIHWPTGFKPGKE-LFPLDESG-NVIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 172 ARLLKN--CKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGS--KGIAKfnagagivRDLPDLMDIPEVKEIAA 247
Cdd:cd19107 159 ERILNKpgLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSpdRPWAK--------PEDPSLLEDPKIKEIAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 248 SHGKTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSSLDQNIRICDFAFFhgvERHPEFTFKNQY 327
Cdd:cd19107 231 KHNKTTAQVLIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRACALLSC---SSHKDYPFHAEY 307
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
7-305 |
1.52e-101 |
|
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: 300.88 E-value: 1.52e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 7 LTFNNGEKMPVIGIGTWQASDEEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKRWLDAGKVKREELFIVTKVPPVSN 86
Cdd:cd19115 5 VKLNSGYDMPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLWNTFH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 87 RPHEVEPTIKKSLEDLQLDYVDLYLVHTPFTI-----NINEDGSFKLDKEGLMEVDVTtnHAAIWVAMEALVEKGLTKSI 161
Cdd:cd19115 85 DGERVEPICRKQLADWGIDYFDLFLIHFPIALkyvdpAVRYPPGWFYDGKKVEFSNAP--IQETWTAMEKLVDKGLARSI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 162 GVSNFSKDQVARLLKNCKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGSKGIAKFNAGAGivRDLPDLMDIPE 241
Cdd:cd19115 163 GVSNFSAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGPQSFLELDLPGA--KDTPPLFEHDV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24644950 242 VKEIAASHGKTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSSLDQNIR 305
Cdd:cd19115 241 IKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLR 304
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
10-300 |
2.25e-99 |
|
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: 294.32 E-value: 2.25e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 10 NNGEKMPVIGIGTWQASDEEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKRWLD-AGKVKREELFIVTKVPPVSNRP 88
Cdd:cd19118 2 NTGNKIPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKeEPGVKREDLFITSKLWNNSHRP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 89 HEVEPTIKKSLEDLQLDYVDLYLVHTP----FTININEDgSFKLDKEGLMEVDVTTNHAAIWVAMEALVEKGLTKSIGVS 164
Cdd:cd19118 82 EYVEPALDDTLKELGLDYLDLYLIHWPvafkPTGDLNPL-TAVPTNGGEVDLDLSVSLVDTWKAMVELKKTGKVKSIGVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 165 NFSKDQVARLLKNCKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGskgiakfNAGAGivrdLPDLMDIPEVKE 244
Cdd:cd19118 161 NFSIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLG-------NNLAG----LPLLVQHPEVKA 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 24644950 245 IAASHGKTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDvfDFELTAEEVAKLSSL 300
Cdd:cd19118 230 IAAKLGKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVTAL 283
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
7-305 |
6.37e-98 |
|
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: 291.70 E-value: 6.37e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 7 LTFNNGEKMPVIGIGTWQASDEEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKRWLDAGKVKREELFIVTKVppvSN 86
Cdd:cd19112 3 ITLNSGHKMPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKL---WN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 87 RPHE-VEPTIKKSLEDLQLDYVDLYLVHTPFTININEDGS--FKLDKEGLMEVDVTTNHAAIWVAMEALVEKGLTKSIGV 163
Cdd:cd19112 80 SDHGhVIEACKDSLKKLQLDYLDLYLVHFPVATKHTGVGTtgSALGEDGVLDIDVTISLETTWHAMEKLVSAGLVRSIGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 164 SNFSKDQVARLLKNCKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGskGIAKFNAGAGIVRDLPDlmdiPEVK 243
Cdd:cd19112 160 SNYDIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLG--GAAANAEWFGSVSPLDD----PVLK 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24644950 244 EIAASHGKTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSSLDQNIR 305
Cdd:cd19112 234 DLAKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYR 295
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
7-301 |
3.54e-96 |
|
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: 285.04 E-value: 3.54e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 7 LTFNNGEKMPVIGIGTWQASDEEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKrwldAGKVKREELFIVTKVppvSN 86
Cdd:cd19131 2 ITLNDGNTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIR----ASGVPREELFITTKL---WN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 87 RPHEVEPTIK---KSLEDLQLDYVDLYLVHTPftininedgsfkLDKEGLMevdVTTnhaaiWVAMEALVEKGLTKSIGV 163
Cdd:cd19131 75 SDQGYDSTLRafdESLRKLGLDYVDLYLIHWP------------VPAQDKY---VET-----WKALIELKKEGRVKSIGV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 164 SNFSKDQVARLLKNCKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGSKGiakfnagagivrdlpdLMDIPEVK 243
Cdd:cd19131 135 SNFTIEHLQRLIDETGVVPVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGG----------------LLSDPVIG 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 24644950 244 EIAASHGKTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSSLD 301
Cdd:cd19131 199 EIAEKHGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELDADDMQAIAGLD 256
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
7-301 |
1.50e-95 |
|
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: 283.70 E-value: 1.50e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 7 LTFNNGEKMPVIGIGTWQASD-EEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKRwldaGKVKREELFIVTKVPPVS 85
Cdd:cd19133 1 VTLNNGVEMPILGFGVFQIPDpEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKK----SGIPREELFITTKLWIQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 86 NRPHEVEPTIKKSLEDLQLDYVDLYLVHTPFTininedgsfkldkeglmevDVttnHAAiWVAMEALVEKGLTKSIGVSN 165
Cdd:cd19133 77 AGYEKAKKAFERSLKRLGLDYLDLYLIHQPFG-------------------DV---YGA-WRAMEELYKEGKIRAIGVSN 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 166 FSKDQVARLLKNCKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGskgiakfnagagivRDLPDLMDIPEVKEI 245
Cdd:cd19133 134 FYPDRLVDLILHNEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFA--------------EGRNNLFENPVLTEI 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 24644950 246 AASHGKTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSSLD 301
Cdd:cd19133 200 AEKYGKSVAQVILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAALD 255
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
10-305 |
4.25e-94 |
|
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: 281.43 E-value: 4.25e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 10 NNGEKMPVIGIGTWqASDE----EIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKRWLDAGKVKREELFIVTKVPPVS 85
Cdd:cd19108 6 NDGHFIPVLGFGTY-APEEvpksKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKLWCTF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 86 NRPHEVEPTIKKSLEDLQLDYVDLYLVHTPFTININEDgSFKLDKEGLMEVDvTTNHAAIWVAMEALVEKGLTKSIGVSN 165
Cdd:cd19108 85 HRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEE-LFPKDENGKLIFD-TVDLCATWEAMEKCKDAGLAKSIGVSN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 166 FSKDQVARLLKN--CKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGSKGIAKFnagagIVRDLPDLMDIPEVK 243
Cdd:cd19108 163 FNRRQLEMILNKpgLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQRDKEW-----VDQNSPVLLEDPVLC 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24644950 244 EIAASHGKTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSSLDQNIR 305
Cdd:cd19108 238 ALAKKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLR 299
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
13-327 |
8.83e-94 |
|
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: 280.69 E-value: 8.83e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 13 EKMPVIGIGTWQASDEEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKRWLDAGKVKREELFIVTKVPPVSNRPHEVE 92
Cdd:cd19110 2 EDIPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKSLVK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 93 PTIKKSLEDLQLDYVDLYLVHTPFTININEDgSFKLDKEGlMEVDVTTNHAAIWVAMEALVEKGLTKSIGVSNFSKDQVA 172
Cdd:cd19110 82 TACTRSLKALKLNYLDLYLIHWPMGFKPGEP-DLPLDRSG-MVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 173 RLLK--NCKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGSkgiakfnAGAGIvrdlpDLMDIPEVKEIAASHG 250
Cdd:cd19110 160 RLLNkpGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGG-------SCEGV-----DLIDDPVIQRIAKKHG 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24644950 251 KTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSSLDQNIRIcdfAFFHGVERHPEFTFKNQY 327
Cdd:cd19110 228 KSPAQILIRFQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRL---ATFPITENHKDYPFHIEY 301
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
7-308 |
2.00e-93 |
|
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: 280.10 E-value: 2.00e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 7 LTFNNGEKMPVIGIGTWQASDEEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKRWLDAGKVKREELFIVTKVPPVSN 86
Cdd:cd19113 3 IKLNSGYKMPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWNNFH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 87 RPHEVEPTIKKSLEDLQLDYVDLYLVHTPFT---ININED---GSFKLDKEGLMEVDVTTnhAAIWVAMEALVEKGLTKS 160
Cdd:cd19113 83 DPKNVETALNKTLSDLKLDYVDLFLIHFPIAfkfVPIEEKyppGFYCGDGDNFVYEDVPI--LDTWKALEKLVDAGKIKS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 161 IGVSNFSKDQVARLLKNCKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGSKGIAKFNAGAgiVRDLPDLMDIP 240
Cdd:cd19113 161 IGVSNFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGPQSFVELNQGR--ALNTPTLFEHD 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24644950 241 EVKEIAASHGKTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSSLDQNIRICD 308
Cdd:cd19113 239 TIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLRFND 306
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
12-298 |
2.32e-92 |
|
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: 276.04 E-value: 2.32e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 12 GEKMPVIGIGT---WQAS-----DEEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKRWLdagkVKREELFIVTKVPP 83
Cdd:cd19120 1 GSKIPAIAFGTgtaWYKSgdddiQRDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALKESG----VPREDLFITTKVSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 84 VSNRPHEvepTIKKSLEDLQLDYVDLYLVHTPFTininedgsfklDKEGlmevdvTTNHAAIWVAMEALVEKGLTKSIGV 163
Cdd:cd19120 77 GIKDPRE---ALRKSLAKLGVDYVDLYLIHSPFF-----------AKEG------GPTLAEAWAELEALKDAGLVRSIGV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 164 SNFSKDQVARLLKNCKIRPANNQIEHHVYL--QQRDLVDFCKSENITVTAYSPLGSkgiakfnagagIVRDLPDLMDiPE 241
Cdd:cd19120 137 SNFRIEDLEELLDTAKIKPAVNQIEFHPYLypQQPALLEYCREHGIVVSAYSPLSP-----------LTRDAGGPLD-PV 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 24644950 242 VKEIAASHGKTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLS 298
Cdd:cd19120 205 LEKIAEKYGVTPAQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEID 261
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
11-300 |
1.61e-90 |
|
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: 270.67 E-value: 1.61e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 11 NGEKMPVIGIGTWQASDEEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKRwldaGKVKREELFIVTKVPPVSNRPHE 90
Cdd:cd19140 4 NGVRIPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIAA----SGVPRDELFLTTKVWPDNYSPDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 91 VEPTIKKSLEDLQLDYVDLYLVHTPftiniNEDGSFK--LDkeglmevdvttnhaaiwvAMEALVEKGLTKSIGVSNFSK 168
Cdd:cd19140 80 FLASVEESLRKLRTDYVDLLLLHWP-----NKDVPLAetLG------------------ALNEAQEAGLARHIGVSNFTV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 169 DQVARLLKNCKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGSkgiakfnaGAgivrdlpdLMDIPEVKEIAAS 248
Cdd:cd19140 137 ALLREAVELSEAPLFTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLAR--------GE--------VLKDPVLQEIGRK 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 24644950 249 HGKTPAQVLLRWIID-TGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSSL 300
Cdd:cd19140 201 HGKTPAQVALRWLLQqEGVAAIPKATNPERLEENLDIFDFTLSDEEMARIAAL 253
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
4-300 |
6.39e-90 |
|
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: 270.52 E-value: 6.39e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 4 TKFLTFNNGEKMPVIGIGTWQASDEEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKrwlDAGkVKREELFIVTKVPp 83
Cdd:cd19117 3 SKTFKLNTGAEIPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIK---DSG-VPREEIFITTKLW- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 84 vSNRPHEVEPTIKKSLEDLQLDYVDLYLVHTPFTININEDGSFKLDKEGLMEVDVTTNHAAIWVAMEALVEKGLTKSIGV 163
Cdd:cd19117 78 -CTWHRRVEEALDQSLKKLGLDYVDLYLMHWPVPLDPDGNDFLFKKDDGTKDHEPDWDFIKTWELMQKLPATGKVKAIGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 164 SNFSKDQVARLLK--NCKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGSkgiakfnAGAGIVRDlpdlmdiPE 241
Cdd:cd19117 157 SNFSIKNLEKLLAspSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGS-------TNAPLLKE-------PV 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 24644950 242 VKEIAASHGKTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVfdFELTAEEVAKLSSL 300
Cdd:cd19117 223 IIKIAKKHGKTPAQVIISWGLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEIDEL 279
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
15-297 |
8.78e-90 |
|
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: 268.37 E-value: 8.78e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 15 MPVIGIGTWQASDEEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKrwldAGKVKREELFIVTKVPPVSNRPHEVEPT 94
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIA----ESGVPREDLFITTKVWRDHLRPEDLKKS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 95 IKKSLEDLQLDYVDLYLVHTP-FTININEdgSFKldkeglmevdvttnhaaiwvAMEALVEKGLTKSIGVSNFSKDQVAR 173
Cdd:cd19073 77 VDRSLEKLGTDYVDLLLIHWPnPTVPLEE--TLG--------------------ALKELKEAGKVKSIGVSNFTIELLEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 174 LLKNCKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLgskgiakfnAGAGIVRDlpdlmdiPEVKEIAASHGKTP 253
Cdd:cd19073 135 ALDISPLPIAVNQVEFHPFLYQAELLEYCRENDIVITAYSPL---------ARGEVLRD-------PVIQEIAEKYDKTP 198
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 24644950 254 AQVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKL 297
Cdd:cd19073 199 AQVALRWLVQKGIVVIPKASSEDHLKENLAIFDWELTSEDVAKI 242
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
5-300 |
9.75e-90 |
|
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: 269.79 E-value: 9.75e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 5 KFLTFNNGEKMPVIGIGTWQASDEEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKRWLDAGkVKREELFIVTKVPPV 84
Cdd:cd19121 2 TSFKLNTGASIPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAIAGG-VKREDLFVTTKLWST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 85 SNRphEVEPTIKKSLEDLQLDYVDLYLVHTPFTININ-EDGSFKLDKEGLMEVDVTTNHAAIWVAMEALVEKGLTKSIGV 163
Cdd:cd19121 81 YHR--RVELCLDRSLKSLGLDYVDLYLVHWPVLLNPNgNHDLFPTLPDGSRDLDWDWNHVDTWKQMEKVLKTGKTKAIGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 164 SNFSKDQVARLLKNCKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGSKGiakfnagagivrdlPDLMDIPEVK 243
Cdd:cd19121 159 SNYSIPYLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTG--------------SPLISDEPVV 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 24644950 244 EIAASHGKTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFelTAEEVAKLSSL 300
Cdd:cd19121 225 EIAKKHNVGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDL--DDEDMNKLNDI 279
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
16-300 |
4.40e-89 |
|
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: 267.85 E-value: 4.40e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 16 PVIGIGTWQASDEEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKRWLDAGKVKREELFIVTKVPPVSNRPHEVEPTI 95
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVKEQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 96 KKSLEDLQLDYVDLYLVHTPFTININEDGSFKLDKEGLMevDVTTNHAAIWVAMEALVEKGLTKSIGVSNFSKDQVARLL 175
Cdd:cd19128 82 LITLQDLQLEYLDLFLIHWPLAFDMDTDGDPRDDNQIQS--LSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 176 KNCKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGskgiAKFNAGAGIVrdlpdlMDIPEVKEIAASHGKTPAQ 255
Cdd:cd19128 160 NYCKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLG----GSYGDGNLTF------LNDSELKALATKYNTTPPQ 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 24644950 256 VLLRWIID---TGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSSL 300
Cdd:cd19128 230 VIIAWHLQkwpKNYSVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
7-301 |
2.68e-88 |
|
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: 265.07 E-value: 2.68e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 7 LTFNNGEKMPVIGIGTWQA-SDEEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKRwldAGkVKREELFIVTKVPPVS 85
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQTpDGDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRE---SG-VPREELFVTTKLWNDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 86 NRPHEVEPTIKKSLEDLQLDYVDLYLVHTPFtininedgsfkldKEGLMEVdvttnhaaiWVAMEALVEKGLTKSIGVSN 165
Cdd:cd19126 77 QRARRTEDAFQESLDRLGLDYVDLYLIHWPG-------------KDKFIDT---------WKALEKLYASGKVKAIGVSN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 166 FSKDQVARLLKNCKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGSKGiakfnagagivrdlpdLMDIPEVKEI 245
Cdd:cd19126 135 FQEHHLEELLAHADVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQGG----------------LLSNPVLAAI 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 24644950 246 AASHGKTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSSLD 301
Cdd:cd19126 199 GEKYGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAIDALN 254
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
9-302 |
1.77e-87 |
|
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: 262.98 E-value: 1.77e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 9 FNNGEKMPVIGIGTWQASDEEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKRwldaGKVKREELFIVTKVPPVSNRP 88
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRR----SGVPREELFVTTKLPGRHHGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 89 HEVEPTIKKSLEDLQLDYVDLYLVHTPftininedgsfkLDKEGLmevdvttnHAAIWVAMEALVEKGLTKSIGVSNFSK 168
Cdd:cd19132 77 EEALRTIEESLYRLGLDYVDLYLIHWP------------NPSRDL--------YVEAWQALIEAREEGLVRSIGVSNFLP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 169 DQVARLLKNCKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGSKGiakfnagagivrdlpDLMDIPEVKEIAAS 248
Cdd:cd19132 137 EHLDRLIDETGVTPAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLGRGS---------------GLLDEPVIKAIAEK 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 24644950 249 HGKTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSSLDQ 302
Cdd:cd19132 202 HGKTPAQVVLRWHVQLGVVPIPKSANPERQRENLAIFDFELSDEDMAAIAALDR 255
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
6-306 |
4.04e-86 |
|
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: 260.02 E-value: 4.04e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 6 FLTFNNGEKMPVIGIGTWQASD-EEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKrwldAGKVKREELFIVTKVppv 84
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEEgSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIK----ESGIPREELFITSKV--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 85 SNRPHEVEPTIK---KSLEDLQLDYVDLYLVHTPftininedgsfkldKEGLmevdvttNHAAiWVAMEALVEKGLTKSI 161
Cdd:cd19157 74 WNADQGYDSTLKafeASLERLGLDYLDLYLIHWP--------------VKGK-------YKET-WKALEKLYKDGRVRAI 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 162 GVSNFSKDQVARLLKNCKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLgSKGiakfnagagivrdlpDLMDIPE 241
Cdd:cd19157 132 GVSNFQVHHLEDLLADAEIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPL-MQG---------------QLLDNPV 195
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24644950 242 VKEIAASHGKTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSSLDQNIRI 306
Cdd:cd19157 196 LKEIAEKYNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNENLRV 260
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
7-301 |
5.21e-84 |
|
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: 254.64 E-value: 5.21e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 7 LTFNNGEKMPVIGIGTWQASDEEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKRwldaGKVKREELFIVTKVPPVSN 86
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRR----SGVDRSDIFVTTKLWISDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 87 RPHEVEPTIKKSLEDLQLDYVDLYLVHTPFTininedgsfkldkeglMEVDVTTnhaAIWVAMEALVEKGLTKSIGVSNF 166
Cdd:cd19127 77 GYDKALRGFDASLRRLGLDYVDLYLLHWPVP----------------NDFDRTI---QAYKALEKLLAEGRVRAIGVSNF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 167 SKDQVARLLKNCKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGskGIAKFNAGAGIVRdlPDLMDIPEVKEIA 246
Cdd:cd19127 138 TPEHLERLIDATTVVPAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIG--GVMRYGASGPTGP--GDVLQDPTITGLA 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 24644950 247 ASHGKTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSSLD 301
Cdd:cd19127 214 EKYGKTPAQIVLRWHLQNGVSAIPKSVHPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
4-300 |
2.67e-83 |
|
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: 252.63 E-value: 2.67e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 4 TKFLTFNNGEKMPVIGIGTWQASDEEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKrwldAGKVKREELFIVTKVPP 83
Cdd:cd19135 2 TPTVRLSNGVEMPILGLGTSHSGGYSHEAVVYALKECGYRHIDTAKRYGCEELLGKAIK----ESGVPREDLFLTTKLWP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 84 VSNRPHEVEPTIKKSLEDLQLDYVDLYLVHTPFTininedgsfkldkeGLMEVDVTTNHAAIWVAMEALVEKGLTKSIGV 163
Cdd:cd19135 78 SDYGYESTKQAFEASLKRLGVDYLDLYLLHWPDC--------------PSSGKNVKETRAETWRALEELYDEGLCRAIGV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 164 SNFSKDQVARLLKNCKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLgSKGIAkfnagagivrdlpdLMDiPEVK 243
Cdd:cd19135 144 SNFLIEHLEQLLEDCSVVPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPL-AKGKA--------------LEE-PTVT 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 24644950 244 EIAASHGKTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSSL 300
Cdd:cd19135 208 ELAKKYQKTPAQILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
1-306 |
8.47e-83 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 251.92 E-value: 8.47e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 1 MVNTKFLTFNNGEKMPVIGIGTWQASDEEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKrwldAGKVKREELFIVTK 80
Cdd:PRK11565 1 MANPTVIKLQDGNVMPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALK----EASVAREELFITTK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 81 VppVSNRPHEVEPTIKKSLEDLQLDYVDLYLVHTPftininedgsfkldkeglmeVDVTTNHAAIWVAMEALVEKGLTKS 160
Cdd:PRK11565 77 L--WNDDHKRPREALEESLKKLQLDYVDLYLMHWP--------------------VPAIDHYVEAWKGMIELQKEGLIKS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 161 IGVSNFSKDQVARLLKNCKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPL--GSKGIakfnagagivrdlpdlMD 238
Cdd:PRK11565 135 IGVCNFQIHHLQRLIDETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLaqGGKGV----------------FD 198
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24644950 239 IPEVKEIAASHGKTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSSLDQNIRI 306
Cdd:PRK11565 199 QKVIRDLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRLDKDELGEIAKLDQGKRL 266
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
4-300 |
9.08e-83 |
|
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: 252.42 E-value: 9.08e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 4 TKFLTFNNGEKMPVIGIGTWQASD--EEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKRWLDAGKVKREELFIVTKV 81
Cdd:cd19119 1 EISFKLNTGASIPALGLGTASPHEdrAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 82 PPVSNRphEVEPTIKKSLEDLQLDYVDLYLVHTPFTININEDGSFK----LDKEGLMEVDVTTNHAAIWVAMEALVEKGL 157
Cdd:cd19119 81 WPTFYD--EVERSLDESLKALGLDYVDLLLVHWPVCFEKDSDDSGKpftpVNDDGKTRYAASGDHITTYKQLEKIYLDGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 158 TKSIGVSNFSKDQVARLLKNCKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGSKGIAkfnagagivrdlpdLM 237
Cdd:cd19119 159 AKAIGVSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAP--------------NL 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24644950 238 DIPEVKEIAASHGKTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVfdFELTAEEVAKLSSL 300
Cdd:cd19119 225 KNPLVKKIAEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLDDI 285
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
7-306 |
1.50e-82 |
|
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: 250.90 E-value: 1.50e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 7 LTFNNGEKMPVIGIGTWQASD-EEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKrwldAGKVKREELFIVTKVppvS 85
Cdd:cd19156 1 VKLANGVEMPRLGLGVWRVQDgAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIR----ESGVPREEVFVTTKL---W 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 86 NRPHEVEPTIK---KSLEDLQLDYVDLYLVHTPFtinineDGSFKldkeglmevdvttnhaAIWVAMEALVEKGLTKSIG 162
Cdd:cd19156 74 NSDQGYESTLAafeESLEKLGLDYVDLYLIHWPV------KGKFK----------------DTWKAFEKLYKEKKVRAIG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 163 VSNFSKDQVARLLKNCKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGSKgiakfnagagivrdlpDLMDIPEV 242
Cdd:cd19156 132 VSNFHEHHLEELLKSCKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQG----------------KLLSNPVL 195
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24644950 243 KEIAASHGKTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSSLDQNIRI 306
Cdd:cd19156 196 KAIGKKYGKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTDHRY 259
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
12-323 |
7.69e-82 |
|
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: 250.49 E-value: 7.69e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 12 GEKMPVIGIGTWQASDE----EIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKRWLDAGKVKREELFIVTKVPPVSNR 87
Cdd:cd19109 1 GNSIPIIGLGTYSEPKTtpkgACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 88 PHEVEPTIKKSLEDLQLDYVDLYLVHTPFTIN-------INEDGSFKLDKeglmevdvtTNHAAIWVAMEALVEKGLTKS 160
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAFKpgdeiypRDENGKWLYHK---------TNLCATWEALEACKDAGLVKS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 161 IGVSNFSKDQVARLLKN--CKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGSKGiakfnAGAGIVRDLPDLMD 238
Cdd:cd19109 152 IGVSNFNRRQLELILNKpgLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCR-----DPIWVNVSSPPLLE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 239 IPEVKEIAASHGKTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSSLDQNIRICDFAFFhgvERH 318
Cdd:cd19109 227 DPLLNSIGKKYNKTAAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYVELLMW---RDH 303
|
....*
gi 24644950 319 PEFTF 323
Cdd:cd19109 304 PEYPF 308
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
7-306 |
2.08e-81 |
|
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: 247.85 E-value: 2.08e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 7 LTFNNGEKMPVIGIGTWQASDEEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKrwldAGKVKREELFIVTKvppVSN 86
Cdd:cd19134 3 VTLNDDNTMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIA----ASGIPRGELFVTTK---LAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 87 RPHEVEPTI---KKSLEDLQLDYVDLYLVHTPftinINEDGSFkldkeglmeVDVttnhaaiWVAMEALVEKGLTKSIGV 163
Cdd:cd19134 76 PDQGFTASQaacRASLERLGLDYVDLYLIHWP----AGREGKY---------VDS-------WGGLMKLREEGLARSIGV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 164 SNFSKDQVARLLKNCKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGskgiakfnagagivrdLPDLMDIPEVK 243
Cdd:cd19134 136 SNFTAEHLENLIDLTFFTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLG----------------VGRLLDNPAVT 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24644950 244 EIAASHGKTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSSLDQNIRI 306
Cdd:cd19134 200 AIAAAHGRTPAQVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDALDGLDDGTRF 262
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
12-308 |
7.54e-81 |
|
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: 247.86 E-value: 7.54e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 12 GEKMPVIGIGTWQASDEEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKRWLDAGKVKREELFIVTKVPPVSNRPHEV 91
Cdd:cd19114 1 GDKMPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGKDHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 92 EPTIKKSLEDLQLDYVDLYLVHTPFTI-------------NINEDGSFKLDKEGLMEVdvttnhaaiWVAMEALVEKGLT 158
Cdd:cd19114 81 REAFDRQLKDYGLDYIDLYLIHFPIPAayvdpaenypflwKDKELKKFPLEQSPMQEC---------WREMEKLVDAGLV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 159 KSIGVSNFSKDQVARLLKNCKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGSKGIAKFNAGAgivRDLPDLMD 238
Cdd:cd19114 152 RNIGIANFNVQLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAVYTKVTKHL---KHFTNLLE 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 239 IPEVKEIAASHGKTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSSLDQNIRICD 308
Cdd:cd19114 229 HPVVKKLADKHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANARFND 298
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
10-284 |
2.35e-76 |
|
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: 236.20 E-value: 2.35e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 10 NNGEKMPVIGIGTWQASDEEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKRWLDAGKVKREELFIVTKVPPVSNRPH 89
Cdd:cd19129 1 NGSGAIPALGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNHRPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 90 EVEPTIKKSLEDLQLDYVDLYLVHTPFTININEDGSFKlDKEGLMEVDVTTNHAAIWVAMEALVEKGLTKSIGVSNFSKD 169
Cdd:cd19129 81 RVKPAFEASLKRLQLDYLDLYLIHTPFAFQPGDEQDPR-DANGNVIYDDGVTLLDTWRAMERLVDEGRCKAIGLSDVSLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 170 QVARLLKNCKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGsKGIAkfnagagivrdlPDLMDIPEVKEIAASH 249
Cdd:cd19129 160 KLREIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLG-HGME------------PKLLEDPVITAIARRV 226
|
250 260 270
....*....|....*....|....*....|....*
gi 24644950 250 GKTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDV 284
Cdd:cd19129 227 NKTPAQVLLAWAIQRGTALLTTSKTPSRIRENFDI 261
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
12-298 |
1.60e-73 |
|
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: 227.50 E-value: 1.60e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 12 GEKMPVIGIGTW---------QASDEEIETAIDAALEAGYRHIDTAPVYGN---EKAIGRVLKrwldagKVKREELFIVT 79
Cdd:cd19072 1 GEEVPVLGLGTWgigggmskdYSDDKKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAIK------GFDREDLFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 80 KVPPVSNRPHEVEPTIKKSLEDLQLDYVDLYLVHTP-FTININEdgsfkldkeglmevdvttnhaaIWVAMEALVEKGLT 158
Cdd:cd19072 75 KVSPDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPnPSIPIEE----------------------TLRAMEELVEEGKI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 159 KSIGVSNFSKDQVAR---LLKNCKIrpANNQIEHHVYLQ--QRDLVDFCKSENITVTAYSPLGsKGiakfnagagivrDL 233
Cdd:cd19072 133 RYIGVSNFSLEELEEaqsYLKKGPI--VANQVEYNLFDReeESGLLPYCQKNGIAIIAYSPLE-KG------------KL 197
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24644950 234 PDLMDIPEVKEIAASHGKTPAQVLLRWII-DTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLS 298
Cdd:cd19072 198 SNAKGSPLLDEIAKKYGKTPAQIALNWLIsKPNVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
7-301 |
8.81e-72 |
|
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: 223.25 E-value: 8.81e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 7 LTFNNGEKMPVIGIGTWQASDEEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKrwldAGKVKREELFIVTKVPPVSN 86
Cdd:cd19130 2 IVLNDGNSIPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIA----ASGIPRDELFVTTKLWNDRH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 87 RPHEVEPTIKKSLEDLQLDYVDLYLVHTPftininedgsfkldkeglmeVDVTTNHAAIWVAMEALVEKGLTKSIGVSNF 166
Cdd:cd19130 78 DGDEPAAAFAESLAKLGLDQVDLYLVHWP--------------------TPAAGNYVHTWEAMIELRAAGRTRSIGVSNF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 167 SKDQVARLLKNCKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGSKgiakfnagagivrdlpDLMDIPEVKEIA 246
Cdd:cd19130 138 LPPHLERIVAATGVVPAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQG----------------KLLGDPPVGAIA 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 24644950 247 ASHGKTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSSLD 301
Cdd:cd19130 202 AAHGKTPAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAIDALD 256
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
15-300 |
5.63e-70 |
|
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: 217.99 E-value: 5.63e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 15 MPVIGIGTWQASDEEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKrwlDAGkVKREELFIVTKVPPVSNRPHEVEPT 94
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIA---ESG-VPRDELFITTKIWIDNLSKDKLLPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 95 IKKSLEDLQLDYVDLYLVHTPFTininedgsfkldkEGLMEVDVTTNhaaiwvAMEALVEKGLTKSIGVSNFSK---DQV 171
Cdd:cd19139 77 LEESLEKLRTDYVDLTLIHWPSP-------------NDEVPVEEYIG------ALAEAKEQGLTRHIGVSNFTIallDEA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 172 ARLLKNCKIrpANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGSkgiakfnagaGIVrdlpdlMDIPEVKEIAASHGK 251
Cdd:cd19139 138 IAVVGAGAI--ATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLAY----------GKV------LDDPVLAAIAERHGA 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 24644950 252 TPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSSL 300
Cdd:cd19139 200 TPAQIALAWAMARGYAVIPSSTKREHLRSNLLALDLTLDADDMAAIAAL 248
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
18-301 |
7.37e-70 |
|
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: 219.11 E-value: 7.37e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 18 IGIGTWQA-------SDEEIETAIDAALEAGYRHIDTAPVYG---NEKAIGRVLKRWldagKVKREELFIVTKVP----- 82
Cdd:pfam00248 1 IGLGTWQLgggwgpiSKEEALEALRAALEAGINFIDTAEVYGdgkSEELLGEALKDY----PVKRDKVVIATKVPdgdgp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 83 -PVSNRPHEVEPTIKKSLEDLQLDYVDLYLVHTPftininedgsfkldkeglmevDVTTNHAAIWVAMEALVEKGLTKSI 161
Cdd:pfam00248 77 wPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWP---------------------DPDTPIEETWDALEELKKEGKIRAI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 162 GVSNFSKDQVARLLKNCKIRPANNQIEHHVY--LQQRDLVDFCKSENITVTAYSPLGSKGIAKFNAGAGIVRD------- 232
Cdd:pfam00248 136 GVSNFDAEQIEKALTKGKIPIVAVQVEYNLLrrRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPgerrrll 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24644950 233 ---LPDLMD-IPEVKEIAASHGKTPAQVLLRWII--DTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSSLD 301
Cdd:pfam00248 216 kkgTPLNLEaLEALEEIAKEHGVSPAQVALRWALskPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
8-296 |
3.51e-66 |
|
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: 209.79 E-value: 3.51e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 8 TFNNGEKMPVIGIGTW--QASDEEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKRWL-DAGKVKREELFIVTKVPPV 84
Cdd:cd19122 2 TLNNGVKIPAVGFGTFanEGAKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLkENPSVKREDLFICTKVWNH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 85 SNRPHEVEPTIKKSLEDLQLDYVDLYLVHTPFTININEDGSFKLDKEG--LMEVDVTTNHAAIWVAMEALVEKGLTKSIG 162
Cdd:cd19122 82 LHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAEKNDQRSPKLGPDGkyVILKDLTENPEPTWRAMEEIYESGKAKAIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 163 VSNFSKDQVARLLKNCKIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGSKGiaKFNAGAGIVRDLPDLmdipev 242
Cdd:cd19122 162 VSNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQN--QVPSTGERVSENPTL------ 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 24644950 243 KEIAASHGKTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVF-----DFElTAEEVAK 296
Cdd:cd19122 234 NEVAEKGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIelsdeDFE-AINQVAK 291
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
7-297 |
1.23e-65 |
|
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: 207.49 E-value: 1.23e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 7 LTFNNGEKMPVIGIGTWQASD------EEIEtAIDAALEAGYRHIDTAPVYGN---EKAIGRVLKRwldagkvKREELFI 77
Cdd:cd19138 3 VTLPDGTKVPALGQGTWYMGEdpakraQEIE-ALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRG-------RRDKVFL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 78 VTKVPPVSNRPHEVEPTIKKSLEDLQLDYVDLYLVHTPFTININEdgsfkldkegLMEvdvttnhaaiwvAMEALVEKGL 157
Cdd:cd19138 75 VSKVLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWRGGVPLAE----------TVA------------AMEELKKEGK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 158 TKSIGVSNFSKDQVARLL-----KNCkirpANNQIEHHvyLQQR----DLVDFCKSENITVTAYSPLGSKGIAKfnagag 228
Cdd:cd19138 133 IRAWGVSNFDTDDMEELWavpggGNC----AANQVLYN--LGSRgieyDLLPWCREHGVPVMAYSPLAQGGLLR------ 200
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 229 ivrdlPDLMDIPEVKEIAASHGKTPAQVLLRWII-DTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKL 297
Cdd:cd19138 201 -----RGLLENPTLKEIAARHGATPAQVALAWVLrDGNVIAIPKSGSPEHARENAAAADLELTEEDLAEL 265
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
14-297 |
2.71e-64 |
|
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: 205.15 E-value: 2.71e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 14 KMPVIGIGTWQASD-----------EEIETAIDAALEAGYRHIDTAPVYGN---EKAIGRVLKRwldagKVKREELFIVT 79
Cdd:cd19093 1 EVSPLGLGTWQWGDrlwwgygeygdEDLQAAFDAALEAGVNLFDTAEVYGTgrsERLLGRFLKE-----LGDRDEVVIAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 80 KVPPVSNR--PHEVEPTIKKSLEDLQLDYVDLYLVHTPFTININEDgsfkldkeglmevdvttnhaAIWVAMEALVEKGL 157
Cdd:cd19093 76 KFAPLPWRltRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSQIE--------------------ALMDGLADAVEEGL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 158 TKSIGVSNFSKDQVAR---LLKNCKIRPANNQIEHHV---YLQQRDLVDFCKSENITVTAYSPLGsKGIA--KFNAGA-- 227
Cdd:cd19093 136 VRAVGVSNYSADQLRRahkALKERGVPLASNQVEYSLlyrDPEQNGLLPACDELGITLIAYSPLA-QGLLtgKYSPENpp 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24644950 228 -GIVRDLP---DLMDIPEV----KEIAASHGKTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKL 297
Cdd:cd19093 215 pGGRRRLFgrkNLEKVQPLldalEEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAEL 292
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
14-308 |
2.64e-62 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 199.09 E-value: 2.64e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 14 KMPVIGIGTWQASDEEIETAIDAALEAGYRHIDTAPVYGNEKAIGRVLKrwldAGKVKREELFIVTKVpPVSN-RPHEVE 92
Cdd:PRK11172 2 SIPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIA----ESGVPRDELFITTKI-WIDNlAKDKLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 93 PTIKKSLEDLQLDYVDLYLVHTPFTINinedgsfkldkeglmEVDVTtnhaaiwVAMEALVE---KGLTKSIGVSNFSKD 169
Cdd:PRK11172 77 PSLKESLQKLRTDYVDLTLIHWPSPND---------------EVSVE-------EFMQALLEakkQGLTREIGISNFTIA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 170 QVARLLKNC-KIRPANNQIEHHVYLQQRDLVDFCKSENITVTAYSPLgskgiakfnAGAGIVRDlpdlmdiPEVKEIAAS 248
Cdd:PRK11172 135 LMKQAIAAVgAENIATNQIELSPYLQNRKVVAFAKEHGIHVTSYMTL---------AYGKVLKD-------PVIARIAAK 198
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 249 HGKTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSSLDQNIRICD 308
Cdd:PRK11172 199 HNATPAQVILAWAMQLGYSVIPSSTKRENLASNLLAQDLQLDAEDMAAIAALDRNGRLVS 258
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
10-300 |
1.50e-59 |
|
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: 193.47 E-value: 1.50e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 10 NNGEKMPVIGIGTWQ-------ASDEEIETAIDAALEAGYRHIDTAPVYG---NEKAIGRVLKRWldagkvKREELFIVT 79
Cdd:COG0667 8 RSGLKVSRLGLGTMTfggpwggVDEAEAIAILDAALDAGINFFDTADVYGpgrSEELLGEALKGR------PRDDVVIAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 80 KV-PPVSNRPHEVEPT---IKKSLED----LQLDYVDLYLVHTPftininedgsfkldkeglmevDVTTNHAAIWVAMEA 151
Cdd:COG0667 82 KVgRRMGPGPNGRGLSrehIRRAVEAslrrLGTDYIDLYQLHRP---------------------DPDTPIEETLGALDE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 152 LVEKGLTKSIGVSNFSKDQVARLLKNCK--IRPANNQIEHHVyLQQR---DLVDFCKSENITVTAYSPLGS-------KG 219
Cdd:COG0667 141 LVREGKIRYIGVSNYSAEQLRRALAIAEglPPIVAVQNEYSL-LDRSaeeELLPAARELGVGVLAYSPLAGglltgkyRR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 220 IAKFNAGAGIVRDLPDLMDIPE-------VKEIAASHGKTPAQVLLRWIIDTG--VSAIPKSTNPARLKQNLDVFDFELT 290
Cdd:COG0667 220 GATFPEGDRAATNFVQGYLTERnlalvdaLRAIAAEHGVTPAQLALAWLLAQPgvTSVIPGARSPEQLEENLAAADLELS 299
|
330
....*....|
gi 24644950 291 AEEVAKLSSL 300
Cdd:COG0667 300 AEDLAALDAA 309
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
12-293 |
3.72e-58 |
|
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: 188.16 E-value: 3.72e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 12 GEKMPVIGIGTWQ---------ASDEEIETAIDAALEAGYRHIDTAPVYG---NEKAIGRVLKRWldagkvKREELFIVT 79
Cdd:cd19137 1 GEKIPALGLGTWGiggfltpdySRDEEMVELLKTAIELGYTHIDTAEMYGgghTEELVGKAIKDF------PREDLFIVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 80 KVPPVSNRPHEVEPTIKKSLEDLQLDYVDLYLVHTPfTININEDGSFKldkeglmevdvttnhaaiwvAMEALVEKGLTK 159
Cdd:cd19137 75 KVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWP-NPNIPLEETLS--------------------AMAEGVRQGLIR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 160 SIGVSNFSKDQVARLLKNCKIRPANNQIEHHVY---LQQRDLVDFCKSENITVTAYSPLgSKGIAKFNAgagivrdlpdl 236
Cdd:cd19137 134 YIGVSNFNRRLLEEAISKSQTPIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPL-RRGLEKTNR----------- 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 24644950 237 mdipEVKEIAASHGKTPAQVLLRWIIDT-GVSAIPKSTNPARLKQNLDVFDFELTAEE 293
Cdd:cd19137 202 ----TLEEIAKNYGKTIAQIALAWLIQKpNVVAIPKAGRVEHLKENLKATEIKLSEEE 255
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
16-299 |
1.96e-53 |
|
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: 177.01 E-value: 1.96e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 16 PVIGIGTWQ---------ASDEEIETAIDAALEAGYRHIDTAPVYGN---EKAIGRVLKRwldagkvKREELFIVTKVPP 83
Cdd:cd19085 2 SRLGLGCWQfgggywwgdQDDEESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKG-------RRDDVVIATKVSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 84 VSNRPHEVEPTIKKSLEDLQLDYVDLYLVHTPftininedgSFKLDKEGLMEvdvttnhaaiwvAMEALVEKGLTKSIGV 163
Cdd:cd19085 75 DNLTPEDVRKSCERSLKRLGTDYIDLYQIHWP---------SSDVPLEETME------------ALEKLKEEGKIRAIGV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 164 SNFSKDQVARLLKNCKIrpANNQIEHHvyLQQR----DLVDFCKSENITVTAYSPLGsKGI--AKFNAGAGIVRD----- 232
Cdd:cd19085 134 SNFGPAQLEEALDAGRI--DSNQLPYN--LLWRaieyEILPFCREHGIGVLAYSPLA-QGLltGKFSSAEDFPPGdartr 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24644950 233 LPDLMD----------IPEVKEIAASHGKTPAQVLLRWII--DTGVSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSS 299
Cdd:cd19085 209 LFRHFEpgaeeetfeaLEKLKEIADELGVTMAQLALAWVLqqPGVTSVIVGARNPEQLEENAAAVDLELSPSVLERLDE 287
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
12-297 |
8.10e-49 |
|
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: 165.01 E-value: 8.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 12 GEKMPVIGIGTWQ--------ASDEEIETAIDAALEAGYRHIDTAPVYGN---EKAIGRVLKRwldagkvKREELFIVTK 80
Cdd:cd19084 1 DLKVSRIGLGTWAiggtwwgeVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKG-------RRDDVVIATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 81 VPPVSNRPHEVEPTIKK---------SLEDLQLDYVDLYLVHTPftininedgsfkldkeglmevDVTTNHAAIWVAMEA 151
Cdd:cd19084 74 CGLRWDGGKGVTKDLSPesirkeveqSLRRLQTDYIDLYQIHWP---------------------DPNTPIEETAEALEK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 152 LVEKGLTKSIGVSNFSKDQVARLLKNCKIrpANNQIEHHVyLQQ---RDLVDFCKSENITVTAYSPLGsKGI--AKFNA- 225
Cdd:cd19084 133 LKKEGKIRYIGVSNFSVEQLEEARKYGPI--VSLQPPYSM-LEReieEELLPYCRENGIGVLPYGPLA-QGLltGKYKKe 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 226 ---GAGIVRDL------PDLMDIPEV----KEIAASHGKTPAQVLLRWIIDT-GV-SAIPKSTNPARLKQNLDVFDFELT 290
Cdd:cd19084 209 ptfPPDDRRSRfpffrgENFEKNLEIvdklKEIAEKYGKSLAQLAIAWTLAQpGVtSAIVGAKNPEQLEENAGALDWELT 288
|
....*..
gi 24644950 291 AEEVAKL 297
Cdd:cd19084 289 EEELKEI 295
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
16-283 |
5.36e-45 |
|
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: 153.44 E-value: 5.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 16 PVIGIGTWQ----ASDEEIETAIDAALEAGYRHIDTAPVYGN---EKAIGRVLKrwldaGKVKREELFIVTKV------- 81
Cdd:cd06660 1 SRLGLGTMTfggdGDEEEAFALLDAALEAGGNFFDTADVYGDgrsERLLGRWLK-----GRGNRDDVVIATKGghppggd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 82 -PPVSNRPHEVEPTIKKSLEDLQLDYVDLYLVHTPftininedgsfkldkeglmevDVTTNHAAIWVAMEALVEKGLTKS 160
Cdd:cd06660 76 pSRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRD---------------------DPSTPVEETLEALNELVREGKIRY 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 161 IGVSNFSKDQVARLL----KNCKIRPANNQIEHHVYLQQ---RDLVDFCKSENITVTAYSPLGSkGiakfnagagivrdl 233
Cdd:cd06660 135 IGVSNWSAERLAEALayakAHGLPGFAAVQPQYSLLDRSpmeEELLDWAEENGLPLLAYSPLAR-G-------------- 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 24644950 234 pdlmdipevkeiaashgktPAQVLLRWII--DTGVSAIPKSTNPARLKQNLD 283
Cdd:cd06660 200 -------------------PAQLALAWLLsqPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-300 |
1.43e-44 |
|
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: 154.37 E-value: 1.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 17 VIGIGTW-------------QASDEEIEtAIDAALEAGYRHIDTAPVYG---NEKAIGRVLKRWldagkvkREELFIVTK 80
Cdd:cd19102 3 TIGLGTWaiggggwgggwgpQDDRDSIA-AIRAALDLGINWIDTAAVYGlghSEEVVGRALKGL-------RDRPIVATK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 81 VPPVSN---------RPHEVEPTIKKSLEDLQLDYVDLYLVHTP-FTINInEDGsfkldkeglmevdvttnhaaiWVAME 150
Cdd:cd19102 75 CGLLWDeegrirrslKPASIRAECEASLRRLGVDVIDLYQIHWPdPDEPI-EEA---------------------WGALA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 151 ALVEKGLTKSIGVSNFSKDQVARLLkncKIRP-ANNQ-----IEHHVylqQRDLVDFCKSENITVTAYSPLGSkGI---- 220
Cdd:cd19102 133 ELKEEGKVRAIGVSNFSVDQMKRCQ---AIHPiASLQppyslLRRGI---EAEILPFCAEHGIGVIVYSPMQS-GLltgk 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 221 -----------------AKFNAGAGIVRDLpDLMDipEVKEIAASHGKTPAQVLLRWII-DTGV-SAIPKSTNPARLKQN 281
Cdd:cd19102 206 mtpervaslpaddwrrrSPFFQEPNLARNL-ALVD--ALRPIAERHGRTVAQLAIAWVLrRPEVtSAIVGARRPDQIDET 282
|
330
....*....|....*....
gi 24644950 282 LDVFDFELTAEEVAKLSSL 300
Cdd:cd19102 283 VGAADLRLTPEELAEIEAL 301
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
10-293 |
4.03e-42 |
|
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: 147.32 E-value: 4.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 10 NNGEKMPVIGIGTW-----QASDEEIETAIDAALEAGYRHIDTAPVYGN---EKAIGRVLKRWldagKVKREELFIVTK- 80
Cdd:cd19092 1 PEGLEVSRLVLGCMrladwGESAEELLSLIEAALELGITTFDHADIYGGgkcEELFGEALALN----PGLREKIEIQTKc 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 81 --VPPVSNRPHEVEP----------TIKKSLEDLQLDYVDLYLVHTPFTininedgsfkldkegLMEVDVTTNhaaiwvA 148
Cdd:cd19092 77 giRLGDDPRPGRIKHydtskehilaSVEGSLKRLGTDYLDLLLLHRPDP---------------LMDPEEVAE------A 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 149 MEALVEKGLTKSIGVSNFSKDQVARLLKNCKIRPANNQIEH---HVYLQQRDLVDFCKSENITVTAYSPLGSKGIAKfna 225
Cdd:cd19092 136 FDELVKSGKVRYFGVSNFTPSQIELLQSYLDQPLVTNQIELsllHTEAIDDGTLDYCQLLDITPMAWSPLGGGRLFG--- 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 226 gaGIVRDLPDLMDipEVKEIAASHGKTPAQVLLRWIIDTGVSAIP--KSTNPARLKQNLDVFDFELTAEE 293
Cdd:cd19092 213 --GFDERFQRLRA--ALEELAEEYGVTIEAIALAWLLRHPARIQPilGTTNPERIRSAVKALDIELTREE 278
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
19-293 |
2.93e-41 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 145.68 E-value: 2.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 19 GIGTWQASDEEIETAIDAALEAGYRHIDTAPVYGN---EKAIGRVLKRWldagKVKREELFIVTK---VPPVSNRPHEVE 92
Cdd:COG4989 22 RLGEWDLSPAEAAALIEAALELGITTFDHADIYGGytcEALFGEALKLS----PSLREKIELQTKcgiRLPSEARDNRVK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 93 P----------TIKKSLEDLQLDYVDLYLVHTPFTininedgsfkldkegLMEVDVTtnhAAiwvAMEALVEKGLTKSIG 162
Cdd:COG4989 98 HydtskehiiaSVEGSLRRLGTDYLDLLLLHRPDP---------------LMDPEEV---AE---AFDELKASGKVRHFG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 163 VSNFSKDQVARLLKNCKIRPANNQIE----HHVYLQQRDLvDFCKSENITVTAYSPLGSKGIAK-FNAGAGIVRDLpdlm 237
Cdd:COG4989 157 VSNFTPSQFELLQSALDQPLVTNQIElsllHTDAFDDGTL-DYCQLNGITPMAWSPLAGGRLFGgFDEQFPRLRAA---- 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 24644950 238 dipeVKEIAASHGKTPAQVLLRWIIDTGVSAIP--KSTNPARLKQNLDVFDFELTAEE 293
Cdd:COG4989 232 ----LDELAEKYGVSPEAIALAWLLRHPAGIQPviGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
10-297 |
2.74e-37 |
|
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: 135.40 E-value: 2.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 10 NNGEKMPVIGIGT----------WQASDEEIETAIDAALEAGYRHIDTAPVYGN---EKAIGRVLKRWLdagkvKREELF 76
Cdd:cd19079 7 NSGLKVSRLCLGCmsfgdpkwrpWVLDEEESRPIIKRALDLGINFFDTANVYSGgasEEILGRALKEFA-----PRDEVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 77 IVTKV-PPVSNRP--------HeVEPTIKKSLEDLQLDYVDLYLVH-----TPFtininedgsfkldkEGLMEvdvttnh 142
Cdd:cd19079 82 IATKVyFPMGDGPngrglsrkH-IMAEVDASLKRLGTDYIDLYQIHrwdyeTPI--------------EETLE------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 143 aaiwvAMEALVEKGLTKSIGVSNFSKDQVARLL----KNCKIRPANNQiEHHVYLQQ---RDLVDFCKSENITVTAYSPL 215
Cdd:cd19079 140 -----ALHDVVKSGKVRYIGASSMYAWQFAKALhlaeKNGWTKFVSMQ-NHYNLLYReeeREMIPLCEEEGIGVIPWSPL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 216 G----SKGIAKFNAGAGIVRDLPDLMD----------IPEVKEIAASHGKTPAQVLLRWIIDTGVSAIP--KSTNPARLK 279
Cdd:cd19079 214 ArgrlARPWGDTTERRRSTTDTAKLKYdyfteadkeiVDRVEEVAKERGVSMAQVALAWLLSKPGVTAPivGATKLEHLE 293
|
330
....*....|....*...
gi 24644950 280 QNLDVFDFELTAEEVAKL 297
Cdd:cd19079 294 DAVAALDIKLSEEEIKYL 311
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
10-305 |
2.87e-37 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 136.49 E-value: 2.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 10 NNGEKMPVIGIGTW--QASDEE--IETaIDAALEAGYRHIDTAPVYGN-EKAIGRVLKRWldagkvkREELFIVTKVPPV 84
Cdd:COG1453 8 KTGLEVSVLGFGGMrlPRKDEEeaEAL-IRRAIDNGINYIDTARGYGDsEEFLGKALKGP-------RDKVILATKLPPW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 85 SNRPHEVEPTIKKSLEDLQLDYVDLYLVHtpftiNINEDGSFK--LDKEGLMEvdvttnhaaiwvAMEALVEKGLTKSIG 162
Cdd:COG1453 80 VRDPEDMRKDLEESLKRLQTDYIDLYLIH-----GLNTEEDLEkvLKPGGALE------------ALEKAKAEGKIRHIG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 163 VSNFSKDQVARLLknckirpannqIE---------HHVYLQQR-----DLVDFCKSENITVTAYSPLgskgiakfnAGAG 228
Cdd:COG1453 143 FSTHGSLEVIKEA-----------IDtgdfdfvqlQYNYLDQDnqageEALEAAAEKGIGVIIMKPL---------KGGR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 229 IVRDLPDLMDIPEVKeiaashgKTPAQVLLRWII-DTGVS-AIPKSTNPARLKQNLDVFD-FE-LTAEEVAKLSSLDQNI 304
Cdd:COG1453 203 LANPPEKLVELLCPP-------LSPAEWALRFLLsHPEVTtVLSGMSTPEQLDENLKTADnLEpLTEEELAILERLAEEL 275
|
.
gi 24644950 305 R 305
Cdd:COG1453 276 G 276
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
12-292 |
4.06e-36 |
|
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: 131.95 E-value: 4.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 12 GEKMPVIGIGTW-----QASDEEIETAIDAALEAGYRHIDTAPVYGN---EKAIGRVLKRWldagkvKREELFIVTKV-- 81
Cdd:cd19074 1 GLKVSELSLGTWltfggQVDDEDAKACVRKAYDLGINFFDTADVYAAgqaEEVLGKALKGW------PRESYVISTKVfw 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 82 --PPVSN-----RPHEVEpTIKKSLEDLQLDYVDLYLVHTPftininedgsfklDKEGLMEVDVTtnhaaiwvAMEALVE 154
Cdd:cd19074 75 ptGPGPNdrglsRKHIFE-SIHASLKRLQLDYVDIYYCHRY-------------DPETPLEETVR--------AMDDLIR 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 155 KGLTKSIGVSNFSKDQVARLLKNCK----IRPANNQIEHHvYLQQR---DLVDFCKSENITVTAYSPL------------ 215
Cdd:cd19074 133 QGKILYWGTSEWSAEQIAEAHDLARqfglIPPVVEQPQYN-MLWREieeEVIPLCEKNGIGLVVWSPLaqglltgkyrdg 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 216 ---GSKGIAKFNAGAGIVRDL--PDLMD-IPEVKEIAASHGKTPAQVLLRWII--DTGVSAIPKSTNPARLKQNLDVFDF 287
Cdd:cd19074 212 ippPSRSRATDEDNRDKKRRLltDENLEkVKKLKPIADELGLTLAQLALAWCLrnPAVSSAIIGASRPEQLEENVKASGV 291
|
....*
gi 24644950 288 ELTAE 292
Cdd:cd19074 292 KLSPE 296
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
16-290 |
6.96e-36 |
|
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: 130.03 E-value: 6.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 16 PVIGIGTWQAS-----------DEEIETaIDAALEAGYRHIDTAPVYG---NEKAIGRVLKRWldagkvkREELFIVTKV 81
Cdd:cd19088 2 SRLGYGAMRLTgpgiwgppadrEEAIAV-LRRALELGVNFIDTADSYGpdvNERLIAEALHPY-------PDDVVIATKG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 82 ---------PPVSNRPHEVEPTIKKSLEDLQLDYVDLYLVHTPFTinineDGSFkldkeglmevdvttnhAAIWVAMEAL 152
Cdd:cd19088 74 glvrtgpgwWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDP-----KVPF----------------EEQLGALAEL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 153 VEKGLTKSIGVSNFSKDQVARLLKNCKIrpANNQIEHHVYLQQ-RDLVDFCKSENITVTAYSPLGSKGIAKfnagagivr 231
Cdd:cd19088 133 QDEGLIRHIGLSNVTVAQIEEARAIVRI--VSVQNRYNLANRDdEGVLDYCEAAGIAFIPWFPLGGGDLAQ--------- 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24644950 232 dlpdlmDIPEVKEIAASHGKTPAQVLLRWIIDTG--VSAIPKSTNPARLKQNLDVFDFELT 290
Cdd:cd19088 202 ------PGGLLAEVAARLGATPAQVALAWLLARSpvMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
7-300 |
2.05e-34 |
|
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: 128.11 E-value: 2.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 7 LTFNNGEKMPvigiGTWQASD-EEIETAIDAALEAGYRHIDTAPVYGN---EKAIGRVLKRwldagkvKREELFIVTKVP 82
Cdd:cd19091 21 MTFGGGGGFF----GAWGGVDqEEADRLVDIALDAGINFFDTADVYSEgesEEILGKALKG-------RRDDVLIATKVR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 83 -PVSNRPHEVEPT-------IKKSLEDLQLDYVDLYLVH-----TPFtininedgsfkldkEGLMEvdvttnhaaiwvAM 149
Cdd:cd19091 90 gRMGEGPNDVGLSrhhiiraVEASLKRLGTDYIDLYQLHgfdalTPL--------------EETLR------------AL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 150 EALVEKGLTKSIGVSNFSKDQVARLLKNCK----IRPANNQIehHVYLQQRD----LVDFCKSENITVTAYSPLGsKGI- 220
Cdd:cd19091 144 DDLVRQGKVRYIGVSNFSAWQIMKALGISErrglARFVALQA--YYSLLGRDleheLMPLALDQGVGLLVWSPLA-GGLl 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 221 -AKFNAGAGIVR---------DLPDLMD------IPEVKEIAASHGKTPAQVLLRWII--DTGVSAIPKSTNPARLKQNL 282
Cdd:cd19091 221 sGKYRRGQPAPEgsrlrrtgfDFPPVDRergydvVDALREIAKETGATPAQVALAWLLsrPTVSSVIIGARNEEQLEDNL 300
|
330
....*....|....*...
gi 24644950 283 DVFDFELTAEEVAKLSSL 300
Cdd:cd19091 301 GAAGLSLTPEEIARLDKV 318
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
18-297 |
4.33e-34 |
|
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: 126.95 E-value: 4.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 18 IGIGTWQ---ASDEEIETAI-DAALEAGYRHIDTAPVYGN----------EKAIGRvlkrWLdAGKVKREELFIVTKV-- 81
Cdd:cd19081 12 LCLGTMVfgwTADEETSFALlDAFVDAGGNFIDTADVYSAwvpgnaggesETIIGR----WL-KSRGKRDRVVIATKVgf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 82 PPVSNRP----HEVEPTIKKSLEDLQLDYVDLYLVHTPftininedgsfkldkeglmevDVTTNHAAIWVAMEALVEKGL 157
Cdd:cd19081 87 PMGPNGPglsrKHIRRAVEASLRRLQTDYIDLYQAHWD---------------------DPATPLEETLGALNDLIRQGK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 158 TKSIGVSNFSKDQVARLLKNCK---------IRPANNQIEHHVYlqQRDLVDFCKSENITVTAYSPLGS----------K 218
Cdd:cd19081 146 VRYIGASNYSAWRLQEALELSRqhglpryvsLQPEYNLVDRESF--EGELLPLCREEGIGVIPYSPLAGgfltgkyrseA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 219 GIAKFNAGAGIVRDL---PDLMDIPEVKEIAASHGKTPAQVLLRWIIDT-GVSA-IPKSTNPARLKQNLDVFDFELTAEE 293
Cdd:cd19081 224 DLPGSTRRGEAAKRYlneRGLRILDALDEVAAEHGATPAQVALAWLLARpGVTApIAGARTVEQLEDLLAAAGLRLTDEE 303
|
....
gi 24644950 294 VAKL 297
Cdd:cd19081 304 VARL 307
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
10-314 |
7.82e-34 |
|
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: 126.40 E-value: 7.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 10 NNGEKMPVIGIGTWQAS--------DEEIETAIDAALEAGYRHIDTAPVYG-NEKAIGRvlkrWLDAGKVKREELFIVTK 80
Cdd:cd19144 8 RNGPSVPALGFGAMGLSafygppkpDEERFAVLDAAFELGCTFWDTADIYGdSEELIGR----WFKQNPGKREKIFLATK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 81 V----------PPVSNRPHEVEPTIKKSLEDLQLDYVDLYLVHtpftininedgsfkldkeglmEVDVTTNHAAIWVAME 150
Cdd:cd19144 84 FgieknvetgeYSVDGSPEYVKKACETSLKRLGVDYIDLYYQH---------------------RVDGKTPIEKTVAAMA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 151 ALVEKGLTKSIGVSNFSKDQVARLlknCKIRP-ANNQIEHHVYL-----QQRDLVDFCKSENITVTAYSPLG-------- 216
Cdd:cd19144 143 ELVQEGKIKHIGLSECSAETLRRA---HAVHPiAAVQIEYSPFSldierPEIGVLDTCRELGVAIVAYSPLGrgfltgai 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 217 -----------SKGIAKFNAgagivRDLPDLMD-IPEVKEIAASHGKTPAQVLLRWIIDTG--VSAIPKSTNPARLKQNL 282
Cdd:cd19144 220 rspddfeegdfRRMAPRFQA-----ENFPKNLElVDKIKAIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLEENL 294
|
330 340 350
....*....|....*....|....*....|..
gi 24644950 283 DVFDFELTAEEVAKLSsldqniRICDFAFFHG 314
Cdd:cd19144 295 GALKVKLTEEEEKEIR------EIAEEAEVVG 320
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
25-297 |
1.74e-33 |
|
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: 125.02 E-value: 1.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 25 ASDEEIETAIDAALEAGYRHIDTAPVYG---NEKAIGRVLKRWldagkvkREELFIVTKVPP----------VSNRPHEV 91
Cdd:cd19076 29 ADEEESIATLHRALELGVTFLDTADMYGpgtNEELLGKALKDR-------RDEVVIATKFGIvrdpgsgfrgVDGRPEYV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 92 EPTIKKSLEDLQLDYVDLYLVHtpftininedgsfkldkeglmEVDVTTNHAAIWVAMEALVEKGLTKSIGVSNFSKDQV 171
Cdd:cd19076 102 RAACEASLKRLGTDVIDLYYQH---------------------RVDPNVPIEETVGAMAELVEEGKVRYIGLSEASADTI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 172 ARLLKNCKIrpANNQIEHHvyLQQRD----LVDFCKSENITVTAYSPLGsKGiakFNAGAGIVRDLPDLMD--------- 238
Cdd:cd19076 161 RRAHAVHPI--TAVQSEYS--LWTRDiedeVLPTCRELGIGFVAYSPLG-RG---FLTGAIKSPEDLPEDDfrrnnprfq 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24644950 239 ----------IPEVKEIAASHGKTPAQVLLRWIIDTG--VSAIPKSTNPARLKQNLDVFDFELTAEEVAKL 297
Cdd:cd19076 233 genfdknlklVEKLEAIAAEKGCTPAQLALAWVLAQGddIVPIPGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-300 |
9.48e-33 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 123.21 E-value: 9.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 14 KMPVIGIGTW---------------QASDEEIETAIDAALEAGYRHIDTAPVYG---NEKAIGRVLKRwldagkVKREEL 75
Cdd:cd19103 3 KLPKIALGTWswgsggaggdqvfgnHLDEDTLKAVFDKAMAAGLNLWDTAAVYGmgaSEKILGEFLKR------YPREDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 76 FIVTKVPP--VSNRPHEVEPTIKKSLEDLQLDYVDLYLVHTPftininedgsfkldkeglMEVDVTTNHAAiwvameALV 153
Cdd:cd19103 77 IISTKFTPqiAGQSADPVADMLEGSLARLGTDYIDIYWIHNP------------------ADVERWTPELI------PLL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 154 EKGLTKSIGVSNFSKDQVAR---LLKNCKIRPAnnQIEHHVYLQQRD-----LVDFCKSENITVTAYS------------ 213
Cdd:cd19103 133 KSGKVKHVGVSNHNLAEIKRaneILAKAGVSLS--AVQNHYSLLYRSseeagILDYCKENGITFFAYMvleqgalsgkyd 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 214 -----PLGSKGIAKFNagaGIVRDLPDLMDIpeVKEIAASHGKTPAQVLLRWIIDTGVSAIPKSTNPARLKQNLDVFDFE 288
Cdd:cd19103 211 tkhplPEGSGRAETYN---PLLPQLEELTAV--MAEIGAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASIT 285
|
330
....*....|..
gi 24644950 289 LTAEEVAKLSSL 300
Cdd:cd19103 286 LTDDEIKELEQL 297
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
16-284 |
5.21e-32 |
|
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: 120.03 E-value: 5.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 16 PVIGIGTWQ-------ASDEEIETAIDAALEAGYRHIDTAPVYGN-EKAIGRVLKrwldagKVKREELFIVTKV------ 81
Cdd:cd19095 1 SVLGLGTSGigrvwgvPSEAEAARLLNTALDLGINLIDTAPAYGRsEERLGRALA------GLRRDDLFIATKVgthgeg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 82 --PPVSNRPHEVEPTIKKSLEDLQLDYVDLYLVHTPFTININEDgsfkldkegLMEvdvttnhaaiwvAMEALVEKGLTK 159
Cdd:cd19095 75 grDRKDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGE---------VLE------------TLEDLKAAGKVR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 160 SIGVSNFSKDqVARLLKnckirpANN----QIEHHVYLQ-QRDLVDFCKSENITVTAYSPLGSkgiakfNAGAGIVRDLP 234
Cdd:cd19095 134 YIGVSGDGEE-LEAAIA------SGVfdvvQLPYNVLDReEEELLPLAAEAGLGVIVNRPLAN------GRLRRRVRRRP 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 24644950 235 DLMDIPEVKEIAASHG-KTPAQVLLRWIIDT-GV-SAIPKSTNPARLKQNLDV 284
Cdd:cd19095 201 LYADYARRPEFAAEIGgATWAQAALRFVLSHpGVsSAIVGTTNPEHLEENLAA 253
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-284 |
6.53e-32 |
|
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: 119.61 E-value: 6.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 10 NNGEKMPVIGIGTWQASDEEIETaIDAALEAGYRHIDTAPVYGN---EKAIGRVLKRwldagkVKREELFIVTKV--PPV 84
Cdd:cd19105 8 KTGLKVSRLGFGGGGLPRESPEL-LRRALDLGINYFDTAEGYGNgnsEEIIGEALKG------LRRDKVFLATKAspRLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 85 SNRPHEVEPTIKKSLEDLQLDYVDLYLVHTPftininEDGSFKLDKEGLMEvdvttnhaaiwvAMEALVEKGLTKSIGVS 164
Cdd:cd19105 81 KKDKAELLKSVEESLKRLQTDYIDIYQLHGV------DTPEERLLNEELLE------------ALEKLKKEGKVRFIGFS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 165 --NFSKDQVARLLKnCK----IRPANNQIEHHVYLQqrDLVDFCKSENITVTAYSPLGSkgiakfnagagivrdlpdLMD 238
Cdd:cd19105 143 thDNMAEVLQAAIE-SGwfdvIMVAYNFLNQPAELE--EALAAAAEKGIGVVAMKTLAG------------------GYL 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 24644950 239 IPEVKEIAASHGKTPAQVLLRWI-----IDTGVSAIpksTNPARLKQNLDV 284
Cdd:cd19105 202 QPALLSVLKAKGFSLPQAALKWVlsnprVDTVVPGM---RNFAELEENLAA 249
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
17-284 |
4.50e-31 |
|
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase YqkF is a founding member of aldo-keto reductase family 11 member C1 (AKR11C1). It may function as oxidoreductase. This family also includes Bacillus halodurans AKR11C1, an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase.
Pssm-ID: 381312 [Multi-domain] Cd Length: 238 Bit Score: 116.81 E-value: 4.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 17 VIGIGTWQ--------ASDEEIETAIDAALEAGYRHIDTAPVYGN---EKAIGRVLKRwldagkvKREELFIVTKVPPVs 85
Cdd:cd19086 5 EIGFGTWGlggdwwgdVDDAEAIRALRAALDLGINFFDTADVYGDghsERLLGKALKG-------RRDKVVIATKFGNR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 86 NRPHEVEPT------IKKSLED----LQLDYVDLYLVHTPFTININEDgsfkldkeglmevdvttnhaAIWVAMEALVEK 155
Cdd:cd19086 77 FDGGPERPQdfspeyIREAVEAslkrLGTDYIDLYQLHNPPDEVLDND--------------------ELFEALEKLKQE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 156 GLTKSIGVSNFSKDQVARLLKNCKIRPAnnQIEHHVYLQQ--RDLVDFCKSENITVTAYSPLGSKGIAkfnagagivrdl 233
Cdd:cd19086 137 GKIRAYGVSVGDPEEALAALRRGGIDVV--QVIYNLLDQRpeEELFPLAEEHGVGVIARVPLASGLLT------------ 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 24644950 234 pdlmdipevkeiaashGKtPAQVLLRWIIDT-GVS-AIPKSTNPARLKQNLDV 284
Cdd:cd19086 203 ----------------GK-LAQAALRFILSHpAVStVIPGARSPEQVEENAAA 238
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
10-299 |
1.06e-30 |
|
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: 118.14 E-value: 1.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 10 NNGEKMPVIGIGTW---------QASDEEIETAIDAALEAGYRHIDTAPVYGN---EKAIGRVLKRwldagkvKREELFI 77
Cdd:cd19149 6 KSGIEASVIGLGTWaigggpwwgGSDDNESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKG-------RRDKVVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 78 VTK------------------VPPVSN-RPHEVEPTIKKSLEDLQLDYVDLYLVHTPftininedgsfkldkeglmevDV 138
Cdd:cd19149 79 ATKcglrwdreggsfffvrdgVTVYKNlSPESIREEVEQSLKRLGTDYIDLYQTHWQ---------------------DV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 139 TTNHAAIWVAMEALVEKGLTKSIGVSNFSKDQVARLLKNCKIrpANNQ---------IEhhvylqqRDLVDFCKSENITV 209
Cdd:cd19149 138 ETPIEETMEALEELKRQGKIRAIGASNVSVEQIKEYVKAGQL--DIIQekysmldrgIE-------KELLPYCKKNNIAF 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 210 TAYSPLGsKGI--------AKFNAG---AGIVRDLPD-LMDIPEVKE----IAASHGKTPAQVLLRWIIDTG--VSAIPK 271
Cdd:cd19149 209 QAYSPLE-QGLltgkitpdREFDAGdarSGIPWFSPEnREKVLALLEkwkpLCEKYGCTLAQLVIAWTLAQPgiTSALCG 287
|
330 340
....*....|....*....|....*...
gi 24644950 272 STNPARLKQNLDVFDFELTAEEVAKLSS 299
Cdd:cd19149 288 ARKPEQAEENAKAGDIRLSAEDIATMRS 315
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
18-293 |
8.46e-30 |
|
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: 115.10 E-value: 8.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 18 IGIGTWQ-------ASDEE--IETaIDAALEAGYRHIDTAPVYG---NEKAIGRVLKrwldaGKVKREELFIVTKV---- 81
Cdd:cd19148 7 IALGTWAiggwmwgGTDEKeaIET-IHKALDLGINLIDTAPVYGfglSEEIVGKALK-----EYGKRDRVVIATKVglew 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 82 ----PPVSN-RPHEVEPTIKKSLEDLQLDYVDLYLVHTPFTininedgsfkldkegLMEVDVTtnhAAiwvAMEALVEKG 156
Cdd:cd19148 81 deggEVVRNsSPARIRKEVEDSLRRLQTDYIDLYQVHWPDP---------------LVPIEET---AE---ALKELLDEG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 157 LTKSIGVSNFSKDQVARLLKNCKI---RPANNQIEHHVylqQRDLVDFCKSENITVTAYSPLgSKGI--AKFNA-----G 226
Cdd:cd19148 140 KIRAIGVSNFSPEQMETFRKVAPLhtvQPPYNLFEREI---EKDVLPYARKHNIVTLAYGAL-CRGLlsGKMTKdtkfeG 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24644950 227 AGIVRDLPD---------LMDIPEVKEIAASH-GKTPAQVLLRWIIDTGVSAIP--KSTNPARLKQNLDVFDFELTAEE 293
Cdd:cd19148 216 DDLRRTDPKfqeprfsqyLAAVEELDKLAQERyGKSVIHLAVRWLLDQPGVSIAlwGARKPEQLDAVDEVFGWSLNDED 294
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
27-300 |
1.02e-28 |
|
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: 112.51 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 27 DEEIETAIDAALEAGYRHIDTAPVYG---NEKAIGRVLKRWldagkvKREELFIVTKVP--------PVSNRPHEVEPTI 95
Cdd:cd19083 32 EEEGKDLVREALDNGVNLLDTAFIYGlgrSEELVGEVLKEY------NRNEVVIATKGAhkfggdgsVLNNSPEFLRSAV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 96 KKSLEDLQLDYVDLYLVHTPftininedgsfklDKEGLMEVDVTtnhaaiwvAMEALVEKGLTKSIGVSNFSKDQvarlL 175
Cdd:cd19083 106 EKSLKRLNTDYIDLYYIHFP-------------DGETPKAEAVG--------ALQELKDEGKIRAIGVSNFSLEQ----L 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 176 KNCKIRPANNQIEHHVYLQQRD----LVDFCKSENITVTAYSPLGSKGIA-------KFNAGaGIVRDLPD--------- 235
Cdd:cd19083 161 KEANKDGYVDVLQGEYNLLQREaeedILPYCVENNISFIPYFPLASGLLAgkytkdtKFPDN-DLRNDKPLfkgerfsen 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24644950 236 LMDIPEVKEIAASHGKTPAQVLLRWII-DTGVSA-IPKSTNPARLKQNLDVFDFELTAEEVAKLSSL 300
Cdd:cd19083 240 LDKVDKLKSIADEKGVTVAHLALAWYLtRPAIDVvIPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
18-283 |
3.99e-28 |
|
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: 110.87 E-value: 3.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 18 IGIGTWQ-----ASDEEIETAIDAALEAGYRHIDTAPVYGN---EKAIGRVLKRWLDAGKVKREELFIVTK--------- 80
Cdd:cd19099 6 LGLGTYRgdsddETDEEYREALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGIKRDEVVIVTKagyipgdgd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 81 -------------------VPPVSNRPHEVEPT-----IKKSLEDLQLDYVDLYLVHTPftininEDGSFKLDKEGLMEv 136
Cdd:cd19099 86 eplrplkyleeklgrglidVADSAGLRHCISPAyledqIERSLKRLGLDTIDLYLLHNP------EEQLLELGEEEFYD- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 137 dvttNHAAIWVAMEALVEKGLTKSIGVS--NFSK-----DQVARLLKNCKIRPANNQIEHHVYLQQ-------------- 195
Cdd:cd19099 159 ----RLEEAFEALEEAVAEGKIRYYGIStwDGFRappalPGHLSLEKLVAAAEEVGGDNHHFKVIQlplnllepealtek 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 196 -------RDLVDFCKSENITVTAYSPLgskgiakfNAGAGIVRdlpdlmdIPEVKEIAASHGKTPAQVLLRWIIDT-GV- 266
Cdd:cd19099 235 ntvkgeaLSLLEAAKELGLGVIASRPL--------NQGQLLGE-------LRLADLLALPGGATLAQRALQFARSTpGVd 299
|
330
....*....|....*..
gi 24644950 267 SAIPKSTNPARLKQNLD 283
Cdd:cd19099 300 SALVGMRRPEHVDENLA 316
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
26-300 |
2.18e-27 |
|
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: 108.81 E-value: 2.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 26 SDEEIETAI-DAALEAGYRHIDTAPVYGN---EKAIGRVLKRwldagkvKREELFIVTKV-PPVSNRPHE-------VEP 93
Cdd:cd19087 27 TDEETSFAImDRALDAGINFFDTADVYGGgrsEEIIGRWIAG-------RRDDIVLATKVfGPMGDDPNDrglsrrhIRR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 94 TIKKSLEDLQLDYVDLYLVHTPftininedgsfkldkeglmevDVTTNHAAIWVAMEALVEKGLTKSIGVSNFSKDQVAR 173
Cdd:cd19087 100 AVEASLRRLQTDYIDLYQMHHF---------------------DRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQIAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 174 LLKNCKIRPANNQI-EHHVY-LQQR----DLVDFCKSENITVTAYSPLG--------------SKGIAKFNAGAGIVRDL 233
Cdd:cd19087 159 AQGIAARRGLLRFVsEQPMYnLLKRqaelEILPAARAYGLGVIPYSPLAgglltgkygkgkrpESGRLVERARYQARYGL 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 234 PDLMDIPE-VKEIAASHGKTPAQVLLRWII-DTGV-SAIPKSTNPARLKQNLDVFDFELTAEEVAKLSSL 300
Cdd:cd19087 239 EEYRDIAErFEALAAEAGLTPASLALAWVLsHPAVtSPIIGPRTLEQLEDSLAALEITLTPELLAEIDEL 308
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
17-283 |
8.71e-27 |
|
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: 107.26 E-value: 8.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 17 VIGIGTW-----QASDEEIETAIDAALEAGYRHIDTAPVYGN---EKAIGRVlkrwldagKVKREELFIVTKVPPV---S 85
Cdd:cd19075 4 ILGTMTFgsqgrFTTAEAAAELLDAFLERGHTEIDTARVYPDgtsEELLGEL--------GLGERGFKIDTKANPGvggG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 86 NRPHEVEPTIKKSLEDLQLDYVDLYLVHTPftininedgsfkldkeglmevDVTTNHAAIWVAMEALVEKGLTKSIGVSN 165
Cdd:cd19075 76 LSPENVRKQLETSLKRLKVDKVDVFYLHAP---------------------DRSTPLEETLAAIDELYKEGKFKEFGLSN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 166 FSKDQVARLLKNCK----IRPAnnqiehhVY---------LQQRDLVDFCKSENITVTAYSPLG----SKGIAKF----- 223
Cdd:cd19075 135 YSAWEVAEIVEICKengwVLPT-------VYqgmynaitrQVETELFPCLRKLGIRFYAYSPLAggflTGKYKYSedkag 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 224 -------NAGAGIVRDL---PDLMD-IPEVKEIAASHGKTPAQVLLRWII----------DT---GVSaipkstNPARLK 279
Cdd:cd19075 208 ggrfdpnNALGKLYRDRywkPSYFEaLEKVEEAAEKEGISLAEAALRWLYhhsaldgekgDGvilGAS------SLEQLE 281
|
....
gi 24644950 280 QNLD 283
Cdd:cd19075 282 ENLA 285
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
12-283 |
2.54e-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: 381326 [Multi-domain] Cd Length: 238 Bit Score: 104.49 E-value: 2.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 12 GEKMPVIGIGT---WQASDEEIETAIDAALEAGYRHIDTAPVYGN-EKAIGRVLKRwldagkvKREELFIVTKVPPVSnr 87
Cdd:cd19100 8 GLKVSRLGFGGgplGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKG-------RRDKVFLATKTGARD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 88 PHEVEPTIKKSLEDLQLDYVDLYLVHtpftiNIN--EDGSFKLDKEGLMEvdvttnhaaiwvAMEALVEKGLTKSIGVSN 165
Cdd:cd19100 79 YEGAKRDLERSLKRLGTDYIDLYQLH-----AVDteEDLDQVFGPGGALE------------ALLEAKEEGKIRFIGISG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 166 FSKDQVARLLKN-------CKIrpanNQIEHHVYLQQRDLVDFCKSENITVTAYSPLGskgiakfnAGAgivrdlpdlmd 238
Cdd:cd19100 142 HSPEVLLRALETgefdvvlFPI----NPAGDHIDSFREELLPLAREKGVGVIAMKVLA--------GGR----------- 198
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 24644950 239 ipevkeIAASHGKTPAQvLLRWIIDTG--VSAIPKSTNPARLKQNLD 283
Cdd:cd19100 199 ------LLSGDPLDPEQ-ALRYALSLPpvDVVIVGMDSPEELDENLA 238
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
27-299 |
5.11e-26 |
|
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: 105.01 E-value: 5.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 27 DEEIETaIDAALEAGYRHIDTAPVYG---NEKAIGRVLKRwldagkvKREELFIVTK----------VPPVSN-RPHEVE 92
Cdd:cd19078 25 EEMIEL-IRKAVELGITFFDTAEVYGpytNEELVGEALKP-------FRDQVVIATKfgfkidggkpGPLGLDsRPEHIR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 93 PTIKKSLEDLQLDYVDLYLVHtpftininedgsfkldkeglmEVDVTTNHAAIWVAMEALVEKGLTKSIGVSNFSKDQVA 172
Cdd:cd19078 97 KAVEGSLKRLQTDYIDLYYQH---------------------RVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETIR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 173 RLLKNCKIrpANNQIEHHVYLQ--QRDLVDFCKSENITVTAYSPLGsKGI--------AKFNAG---AGIVRDLP----- 234
Cdd:cd19078 156 RAHAVCPV--TAVQSEYSMMWRepEKEVLPTLEELGIGFVPFSPLG-KGFltgkidenTKFDEGddrASLPRFTPealea 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24644950 235 --DLMDIpeVKEIAASHGKTPAQVLLRWIIDTG--VSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSS 299
Cdd:cd19078 233 nqALVDL--LKEFAEEKGATPAQIALAWLLAKKpwIVPIPGTTKLSRLEENIGAADIELTPEELREIED 299
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
18-286 |
8.26e-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: 381323 [Multi-domain] Cd Length: 267 Bit Score: 103.76 E-value: 8.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 18 IGIGTWQ-------------ASDEEIETAIDAALEAGYRHIDTAPVYGN-EKAIGRVLKRWldagkvkrEELFIVTKVPP 83
Cdd:cd19097 3 LALGTAQfgldygianksgkPSEKEAKKILEYALKAGINTLDTAPAYGDsEKVLGKFLKRL--------DKFKIITKLPP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 84 VSNRPHEVEPTI----KKSLEDLQLDYVDLYLVHTPftininedgsfkldkeglmeVDVTTNHAAIWVAMEALVEKGLTK 159
Cdd:cd19097 75 LKEDKKEDEAAIeasvEASLKRLKVDSLDGLLLHNP--------------------DDLLKHGGKLVEALLELKKEGLIR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 160 SIGVSNFSKDQVARLLKNCKIR----PANnqiehhvYLQQR----DLVDFCKSENITVTAYSPL--------GSKGIAKF 223
Cdd:cd19097 135 KIGVSVYSPEELEKALESFKIDiiqlPFN-------ILDQRflksGLLAKLKKKGIEIHARSVFlqglllmePDKLPAKF 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24644950 224 NAGAGIVRDLpdlmdipevKEIAASHGKTPAQVLLRWI-----IDT---GVsaipksTNPARLKQNLDVFD 286
Cdd:cd19097 208 APAKPLLKKL---------HELAKKLGLSPLELALGFVlslpeIDKivvGV------DSLEQLKEIIAAFK 263
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
11-297 |
8.54e-26 |
|
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: 104.24 E-value: 8.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 11 NGEKMPVIGIG----TWQA---SDEEIETAIDAALEAGYRHIDTAPVYGNEKAIG--RVLKRWLDAGKVKREELFIVTKV 81
Cdd:cd19077 1 NGKLVGPIGLGlmglTWRPnptPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHAnlKLLARFFRKYPEYADKVVLSVKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 82 -------PPVSnRPHEVEPTIKKSLEDL-QLDYVDLYlvhtpftininedGSFKLDKEGLMEVDVTtnhaaiwvAMEALV 153
Cdd:cd19077 81 gldpdtlRPDG-SPEAVRKSIENILRALgGTKKIDIF-------------EPARVDPNVPIEETIK--------ALKELV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 154 EKGLTKSIGVSNFSKDQVARLLKNCKIrpANNQIEHHVYLQ---QRDLVDFCKSENITVTAYSPLGsKGIakfnagagIV 230
Cdd:cd19077 139 KEGKIRGIGLSEVSAETIRRAHAVHPI--AAVEVEYSLFSReieENGVLETCAELGIPIIAYSPLG-RGL--------LT 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 231 RDLPDLMDIPE------------------------VKEIAASHGKTPAQVLLRWIIDTG---VSAIPKSTNPARLKQNLD 283
Cdd:cd19077 208 GRIKSLADIPEgdfrrhldrfngenfeknlklvdaLQELAEKKGCTPAQLALAWILAQSgpkIIPIPGSTTLERVEENLK 287
|
330
....*....|....
gi 24644950 284 VFDFELTAEEVAKL 297
Cdd:cd19077 288 AANVELTDEELKEI 301
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-299 |
1.60e-25 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 103.83 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 15 MPVIGIGTWQASD--------EEIETAIDAALEAGYRHIDTAPVYGN-EKAIGRVLKRWLDAGKVkREELFIVTKVPPVS 85
Cdd:cd19101 2 ISRVINGMWQLSGghggirdeDAAVRAMAAYVDAGLTTFDCADIYGPaEELIGEFRKRLRRERDA-ADDVQIHTKWVPDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 86 NR----PHEVEPTIKKSLEDLQLDYVDLYLVHTpftininedgsFKLDKEGLMEvdvttnhAAIWvaMEALVEKGLTKSI 161
Cdd:cd19101 81 GEltmtRAYVEAAIDRSLKRLGVDRLDLVQFHW-----------WDYSDPGYLD-------AAKH--LAELQEEGKIRHL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 162 GVSNFSKDQVARLLKNcKIRPANNQIEHHVyLQQR---DLVDFCKSENITVTAYSPLG-------------SKGIAKFNA 225
Cdd:cd19101 141 GLTNFDTERLREILDA-GVPIVSNQVQYSL-LDRRpenGMAALCEDHGIKLLAYGTLAggllsekylgvpePTGPALETR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 226 -------------GAGIVRDLPDLMdipevKEIAASHGKTPAQVLLRWIID-TGV-SAIPKSTNPARLKQNLDVFDFELT 290
Cdd:cd19101 219 slqkyklmidewgGWDLFQELLRTL-----KAIADKHGVSIANVAVRWVLDqPGVaGVIVGARNSEHIDDNVRAFSFRLD 293
|
....*....
gi 24644950 291 AEEVAKLSS 299
Cdd:cd19101 294 DEDRAAIDA 302
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
16-292 |
2.08e-25 |
|
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: 102.63 E-value: 2.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 16 PVIGIGT-------WQASDEEIETAIDAALEAGYRHIDTAPVYGN-EKAIGRVLKRWldagkvKREELFIVTKVPPVSNR 87
Cdd:cd19090 1 SALGLGTaglggvfGGVDDDEAVATIRAALDLGINYIDTAPAYGDsEERLGLALAEL------PREPLVLSTKVGRLPED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 88 PH-----EVEPTIKKSLEDLQLDYVDLYLVHTPftininEDGSFK--LDKEGLMEvdvttnhaaiwvAMEALVEKGLTKS 160
Cdd:cd19090 75 TAdysadRVRRSVEESLERLGRDRIDLLMIHDP------ERVPWVdiLAPGGALE------------ALLELKEEGLIKH 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 161 IGVSNFSKDQVARLLKNCK---IRPANNqiehhvY--LQQ---RDLVDFCKSENITVTAYSPLGSkGI--AKFNAGAGIV 230
Cdd:cd19090 137 IGLGGGPPDLLRRAIETGDfdvVLTANR------YtlLDQsaaDELLPAAARHGVGVINASPLGM-GLlaGRPPERVRYT 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24644950 231 RD--LPDLMD-IPEVKEIAASHGKTPAQVLLRWII-DTGVSA-IPKSTNPARLKQNLDVFDFELTAE 292
Cdd:cd19090 210 YRwlSPELLDrAKRLYELCDEHGVPLPALALRFLLrDPRISTvLVGASSPEELEQNVAAAEGPLPEE 276
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
23-297 |
6.18e-25 |
|
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: 102.30 E-value: 6.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 23 WQASDEEIETAIDAALEAGYRHIDTAPVYGN---EKAIGRVLKRwldagkvKREELFIVTKVppvSNRPHEVEPT----- 94
Cdd:cd19080 26 WGADREEARAMFDAYVEAGGNFIDTANNYTNgtsERLLGEFIAG-------NRDRIVLATKY---TMNRRPGDPNaggnh 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 95 -------IKKSLEDLQLDYVDLYLVHTPftininedgsfkldkeglmevDVTTNHAAIWVAMEALVEKGLTKSIGVSNFS 167
Cdd:cd19080 96 rknlrrsVEASLRRLQTDYIDLLYVHAW---------------------DFTTPVEEVMRALDDLVRAGKVLYVGISDTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 168 KDQVARLLKNCKIR----PANNQIEHHVyLQ---QRDLVDFCKSENITVTAYSPLGS------KGIAKFNAGAGIVRDLP 234
Cdd:cd19080 155 AWVVARANTLAELRgwspFVALQIEYSL-LErtpERELLPMARALGLGVTPWSPLGGglltgkYQRGEEGRAGEAKGVTV 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24644950 235 DLMDIPE--------VKEIAASHGKTPAQVLLRWIIDTGVSAIP--KSTNPARLKQNLDVFDFELTAEEVAKL 297
Cdd:cd19080 234 GFGKLTErnwaivdvVAAVAEELGRSAAQVALAWVRQKPGVVIPiiGARTLEQLKDNLGALDLTLSPEQLARL 306
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
16-286 |
6.82e-25 |
|
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: 100.71 E-value: 6.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 16 PVIGIGT------WQAS-DEE--IETaIDAALEAGYRHIDTAPVYGN---EKAIGRVLKRWldagkvKREELFIVTKVPP 83
Cdd:cd19096 1 SVLGFGTmrlpesDDDSiDEEkaIEM-IRYAIDAGINYFDTAYGYGGgksEEILGEALKEG------PREKFYLATKLPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 84 VSNRPHE-VEPTIKKSLEDLQLDYVDLYLVHtpftiNINEDGSF-KLDKEGLMEvdvttnhaaiwvAMEALVEKGLTKSI 161
Cdd:cd19096 74 WSVKSAEdFRRILEESLKRLGVDYIDFYLLH-----GLNSPEWLeKARKGGLLE------------FLEKAKKEGLIRHI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 162 GVSnfSKDQvARLLKncKIRPAN----NQIEHHV----YLQQRDLVDFCKSENITVTAYSPLGskgiakfnaGAGIVRDL 233
Cdd:cd19096 137 GFS--FHDS-PELLK--EILDSYdfdfVQLQYNYldqeNQAGRPGIEYAAKKGMGVIIMEPLK---------GGGLANNP 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 24644950 234 pdlmdiPEVKEIAASHGKTPAQVLLRWI-----IDTGVSAIpksTNPARLKQNLDVFD 286
Cdd:cd19096 203 ------PEALAILCGAPLSPAEWALRFLlshpeVTTVLSGM---STPEQLDENIAAAD 251
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-283 |
1.01e-24 |
|
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: 101.25 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 16 PVIGIGTWQ----ASDEEIETAIDAALEAGYRHIDTAPVYG--NEKAIG----RVLKRWLDAGKVkREELFIVTKV---P 82
Cdd:cd19752 1 SELCLGTMYfgtrTDEETSFAILDRYVAAGGNFLDTANNYAfwTEGGVGgeseRLIGRWLKDRGN-RDDVVIATKVgagP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 83 PVSNRPHE---------VEPTIKKSLEDLQLDYVDLYLVH-----TPFtininedgsfkldkEGLMEvdvttnhaaiwvA 148
Cdd:cd19752 80 RDPDGGPEspeglsaetIEQEIDKSLRRLGTDYIDLYYAHvddrdTPL--------------EETLE------------A 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 149 MEALVEKGLTKSIGVSNFSKDQVARLLKNCKIR--PANNQIE-HHVYLQQR-------------DLVDFCKSE-NITVTA 211
Cdd:cd19752 134 FNELVKAGKVRAIGASNFAAWRLERARQIARQQgwAEFSAIQqRHSYLRPRpgadfgvqrivtdELLDYASSRpDLTLLA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 212 YSPLGSKGIAKFNagagivRDLPDLMDIPE-------VKEIAASHGKTPAQVLLRWIIDTGVSAIP--KSTNPARLKQNL 282
Cdd:cd19752 214 YSPLLSGAYTRPD------RPLPEQYDGPDsdarlavLEEVAGELGATPNQVVLAWLLHRTPAIIPllGASTVEQLEENL 287
|
.
gi 24644950 283 D 283
Cdd:cd19752 288 A 288
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
18-292 |
2.49e-24 |
|
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: 100.72 E-value: 2.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 18 IGIGT--W--QASDEEIETAIDAALEAGYRHIDTA---PV------YG-NEKAIGRvlkrWLdAGKVKREELFIVTKVPP 83
Cdd:cd19094 4 ICLGTmtWgeQNTEAEAHEQLDYAFDEGVNFIDTAemyPVppspetQGrTEEIIGS----WL-KKKGNRDKVVLATKVAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 84 VSNR------------PHEVEPTIKKSLEDLQLDYVDLYLVHTP--FTININEDGSFKLDKEGlmevdVTTNHAAIWVAM 149
Cdd:cd19094 79 PGEGitwprgggtrldRENIREAVEGSLKRLGTDYIDLYQLHWPdrYTPLFGGGYYTEPSEEE-----DSVSFEEQLEAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 150 EALVEKGLTKSIGVSNFSKDQVARLLKNCKI----RPANNQiehHVY--LQQRDLVDF---CKSENITVTAYSPLG---- 216
Cdd:cd19094 154 GELVKAGKIRHIGLSNETPWGVMKFLELAEQlglpRIVSIQ---NPYslLNRNFEEGLaeaCHRENVGLLAYSPLAggvl 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 217 ---------SKGIAKFNAGAGIV---RDLPDLMDIPEVKEIAASHGKTPAQVLLRWIID-TGV-SAIPKSTNPARLKQNL 282
Cdd:cd19094 231 tgkyldgaaRPEGGRLNLFPGYMaryRSPQALEAVAEYVKLARKHGLSPAQLALAWVRSrPFVtSTIIGATTLEQLKENI 310
|
330
....*....|
gi 24644950 283 DVFDFELTAE 292
Cdd:cd19094 311 DAFDVPLSDE 320
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
16-286 |
1.04e-23 |
|
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: 98.39 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 16 PVIGIGT----WQASDEEIETAIDAALEAGYRHIDTAPVYGNEKAIG---RVLKRWLdAGKVKREELFIVTK------VP 82
Cdd:cd19082 1 SRIVLGTadfgTRIDEEEAFALLDAFVELGGNFIDTARVYGDWVERGaseRVIGEWL-KSRGNRDKVVIATKgghpdlED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 83 PVSNR--PHEVEPTIKKSLEDLQLDYVDLYLVH-----TPFtininedgsfkldkEGLMEVdvttnhaaiwvaMEALVEK 155
Cdd:cd19082 80 MSRSRlsPEDIRADLEESLERLGTDYIDLYFLHrddpsVPV--------------GEIVDT------------LNELVRA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 156 GLTKSIGVSNFSkdqVARllknckIRPANNqiehhvYLQQRDLVDFCKSEN----------------------------- 206
Cdd:cd19082 134 GKIRAFGASNWS---TER------IAEANA------YAKAHGLPGFAASSPqwslarpneppwpgptlvamdeemrawhe 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 207 ---ITVTAYSPLGsKGiakFNAGAgIVRDLPDLMDIPE-------------VKEIAASHGKTPAQVLLRWIIDTGVSAIP 270
Cdd:cd19082 199 enqLPVFAYSSQA-RG---FFSKR-AAGGAEDDSELRRvyyseenferlerAKELAEEKGVSPTQIALAYVLNQPFPTVP 273
|
330
....*....|....*...
gi 24644950 271 --KSTNPARLKQNLDVFD 286
Cdd:cd19082 274 iiGPRTPEQLRDSLAAAD 291
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
7-300 |
3.47e-23 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 97.72 E-value: 3.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 7 LTFNNGekmpviGIG-TW-QASDEEIETAIDAALEAGYRHIDTAPVYGN---EKAIGRVLKRwldagkvKREELFIVTKV 81
Cdd:cd19104 15 LTFGGG------GIGgLMgRTTREEQIAAVRRALDLGINFFDTAPSYGDgksEENLGRALKG-------LPAGPYITTKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 82 ----PPVSNRPHEVEPTIKKSLEDLQLDYVDLYLVHTPFTiniNEDGSFKLDKEGLMEVDVTtnhAAIWVAMEALVEKGL 157
Cdd:cd19104 82 rldpDDLGDIGGQIERSVEKSLKRLKRDSVDLLQLHNRIG---DERDKPVGGTLSTTDVLGL---GGVADAFERLRSEGK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 158 TKSIGVS---------------NFSKDQVARLLKNckiRPANNQ-IEHHVYLQQRDLVDFCKSENITVTAYSPLGSKGIA 221
Cdd:cd19104 156 IRFIGITglgnppairelldsgKFDAVQVYYNLLN---PSAAEArPRGWSAQDYGGIIDAAAEHGVGVMGIRVLAAGALT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 222 -KFNAG--AGIVRDLPDLMDI---PEVKEIAASHGKTPAQVLLRWIIDT-GVS-AIPKSTNPARLKQNLDVFDF-ELTAE 292
Cdd:cd19104 233 tSLDRGreAPPTSDSDVAIDFrraAAFRALAREWGETLAQLAHRFALSNpGVStVLVGVKNREELEEAVAAEAAgPLPAE 312
|
....*...
gi 24644950 293 EVAKLSSL 300
Cdd:cd19104 313 NLARLEAL 320
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
10-295 |
1.06e-21 |
|
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: 93.09 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 10 NNGEKMPVIGIGTWQ--ASDEEIETA---IDAALEAGYRHIDTAPVYGN-----EKAIGRVLKRWLDAgkvKREELFIVT 79
Cdd:cd19089 6 RSGLHLPAISLGLWHnfGDYTSPEEArelLRTAFDLGITHFDLANNYGPppgsaEENFGRILKRDLRP---YRDELVIST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 80 KV------PPV---SNRPHEVEpTIKKSLEDLQLDYVDLYLVHTPftininedgsfklDKEGLMEvdvttnhaaiwVAME 150
Cdd:cd19089 83 KAgygmwpGPYgdgGSRKYLLA-SLDQSLKRMGLDYVDIFYHHRY-------------DPDTPLE-----------ETMT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 151 AL---VEKGLTKSIGVSNFSKDQVARLLKNC---KIRPANNQIEHHVYLQQ--RDLVDFCKSENITVTAYSPLG------ 216
Cdd:cd19089 138 ALadaVRSGKALYVGISNYPGAKARRAIALLrelGVPLIIHQPRYSLLDRWaeDGLLEVLEEAGIGFIAFSPLAqglltd 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 217 --SKGIAKFNAGAGIVRDLPDLMDIPEVKE-------IAASHGKTPAQVLLRWII-DTGV-SAIPKSTNPARLKQNLDVF 285
Cdd:cd19089 218 kyLNGIPPDSRRAAESKFLTEEALTPEKLEqlrklnkIAAKRGQSLAQLALSWVLrDPRVtSVLIGASSPSQLEDNVAAL 297
|
330
....*....|.
gi 24644950 286 D-FELTAEEVA 295
Cdd:cd19089 298 KnLDFSEEELA 308
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
26-297 |
5.84e-21 |
|
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381371 [Multi-domain] Cd Length: 304 Bit Score: 91.34 E-value: 5.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 26 SDEEIETAIDAALEAGYRHIDTAPVYG---NEKAIGRVLKrwldaGKVkREELFIVTKV---------PPVSNRPHEVEP 93
Cdd:cd19145 31 PEEEGIALIHHAFNSGVTFLDTSDIYGpntNEVLLGKALK-----DGP-REKVQLATKFgiheiggsgVEVRGDPAYVRA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 94 TIKKSLEDLQLDYVDLYLVHtpftininedgsfKLDKEGLMEVDVTtnhaaiwvAMEALVEKGLTKSIGVSNFSKDQVAR 173
Cdd:cd19145 105 ACEASLKRLDVDYIDLYYQH-------------RIDTTVPIEITMG--------ELKKLVEEGKIKYIGLSEASADTIRR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 174 LLKnckIRPANN-QIEHHVYLQ--QRDLVDFCKSENITVTAYSPLGsKGiakFNAGAGIVRDLPDLMDIPE--------- 241
Cdd:cd19145 164 AHA---VHPITAvQLEWSLWTRdiEEEIIPTCRELGIGIVPYSPLG-RG---FFAGKAKLEELLENSDVRKshprfqgen 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24644950 242 ----------VKEIAASHGKTPAQVLLRWIIDTG--VSAIPKSTNPARLKQNLDVFDFELTAEEVAKL 297
Cdd:cd19145 237 leknkvlyerVEALAKKKGCTPAQLALAWVLHQGedVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
10-295 |
1.14e-18 |
|
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: 84.53 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 10 NNGEKMPVIGIGT-------WQASDEEIETAIDAALEAGYRHIDTAPVYGN---EKAIGRVLKrwldagKVKREELFIVT 79
Cdd:cd19163 8 KTGLKVSKLGFGAsplggvfGPVDEEEAIRTVHEALDSGINYIDTAPWYGQgrsETVLGKALK------GIPRDSYYLAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 80 KV----PPVSN----RPHEVEPTIKKSLEDLQLDYVDLYLVHtpftinineDGSFKLDK-----EGLmevdvttnhaaiw 146
Cdd:cd19163 82 KVgrygLDPDKmfdfSAERITKSVEESLKRLGLDYIDIIQVH---------DIEFAPSLdqilnETL------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 147 VAMEALVEKGLTKSIGVSNFSKDQVARLLKNCKirpanNQIE------HHVYLQQR--DLVDFCKSENITVTAYSPLGS- 217
Cdd:cd19163 140 PALQKLKEEGKVRFIGITGYPLDVLKEVLERSP-----VKIDtvlsycHYTLNDTSllELLPFFKEKGVGVINASPLSMg 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 218 ----KGIAKFNAGAgivrdlpdlmdiPEVKEIAA-------SHGKTPAQVLLRWIIDT--GVSAIPKSTNPARLKQNLDV 284
Cdd:cd19163 215 llteRGPPDWHPAS------------PEIKEACAkaaayckSRGVDISKLALQFALSNpdIATTLVGTASPENLRKNLEA 282
|
330
....*....|.
gi 24644950 285 FDFELTAEEVA 295
Cdd:cd19163 283 AEEPLDAHLLA 293
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
10-297 |
4.68e-18 |
|
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: 83.03 E-value: 4.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 10 NNGEKMPVIGIGTW-----QASDEEIETAIDAALEAGYRHIDTAPVYGN---EKAIGRVLKRwldaGKVKREELFIVTKV 81
Cdd:cd19143 8 RSGLKVSALSFGSWvtfgnQVDVDEAKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIKE----LGWPRSDYVVSTKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 82 -------PPVS---NRPHEVEPTiKKSLEDLQLDYVDLYLVHTPftininedgsfklDKEGLMEVDVTtnhaaiwvAMEA 151
Cdd:cd19143 84 fwggggpPPNDrglSRKHIVEGT-KASLKRLQLDYVDLVFCHRP-------------DPATPIEETVR--------AMND 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 152 LVEKGLTKSIGVSNFSKDQ------VARLLKncKIRPANNQIEHHVYLQQRDLVDF---CKSENITVTAYSPLGSkGI-- 220
Cdd:cd19143 142 LIDQGKAFYWGTSEWSAQQieeaheIADRLG--LIPPVMEQPQYNLFHRERVEVEYaplYEKYGLGTTTWSPLAS-GLlt 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 221 AKFNAG--AGIVRDLPD---------------LMDIPEVKEIAASHGKTPAQVLLRWII-DTGVS-AIPKSTNPARLKQN 281
Cdd:cd19143 219 GKYNNGipEGSRLALPGyewlkdrkeelgqekIEKVRKLKPIAEELGCSLAQLAIAWCLkNPNVStVITGATKVEQLEEN 298
|
330
....*....|....*....
gi 24644950 282 ---LDVFDfELTAEEVAKL 297
Cdd:cd19143 299 lkaLEVLP-KLTPEVMEKI 316
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
16-222 |
6.49e-16 |
|
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: 76.63 E-value: 6.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 16 PVIGIGTWQ------ASDEEIETAIDAALEAGYRHIDTAPVYG---NEKAIGRVLKRWLdagkvkREELFIVTKV----- 81
Cdd:cd19162 1 PRLGLGAASlgnlarAGEDEAAATLDAAWDAGIRYFDTAPLYGlglSERRLGAALARHP------RAEYVVSTKVgrlle 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 82 PPVSNRPHEVEP-----------TIKKSLEDLQLDYVDLYLVHtpftininedgsfklDKEGLMEVDVTTNhaaiWVAME 150
Cdd:cd19162 75 PGAAGRPAGADRrfdfsadgirrSIEASLERLGLDRLDLVFLH---------------DPDRHLLQALTDA----FPALE 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24644950 151 ALVEKGLTKSIGVSNFSKDQVARLLKNCK---IRPANNqiehHVYLQQR---DLVDFCKSENITVTAYSPLGSKGIAK 222
Cdd:cd19162 136 ELRAEGVVGAIGVGVTDWAALLRAARRADvdvVMVAGR----YTLLDRRaatELLPLCAAKGVAVVAAGVFNSGILAT 209
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
25-182 |
3.60e-14 |
|
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: 71.80 E-value: 3.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 25 ASDEEIETaIDAALEAGYRHIDTAPVYGNEKAiGRVLKRWLDAGKVKREELFIVTKVPPVSNRPHE-----VEPTIKKSL 99
Cdd:cd19153 31 EQDEAVAI-VAEAFAAGINHFDTSPYYGAESS-EAVLGKALAALQVPRSSYTVATKVGRYRDSEFDysaerVRASVATSL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 100 EDLQLDYVDLYLVHtpftinineDGSFkldkeglmeVDVTTNHAAIWVAMEALVEKGLTKSIGVSNFSKDQVARLLKNCK 179
Cdd:cd19153 109 ERLHTTYLDVVYLH---------DIEF---------VDYDTLVDEALPALRTLKDEGVIKRIGIAGYPLDTLTRATRRCS 170
|
...
gi 24644950 180 IRP 182
Cdd:cd19153 171 PGS 173
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
11-196 |
5.87e-14 |
|
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: 71.34 E-value: 5.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 11 NGEKMPVIGIGTWQA-----SDEEIETAIDAALEAGYRHIDTAPVYGNEKA---IGRVLKR--WldagkvKREELFIVTK 80
Cdd:cd19142 9 SGLRVSNVGLGTWSTfstaiSEEQAEEIVTLAYENGINYFDTSDAFTSGQAeteLGRILKKkgW------KRSSYIVSTK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 81 V----PPVS---NRPHEVEpTIKKSLEDLQLDYVDLYLVHtpftininedgsfKLDKEGLMEVDVTtnhaaiwvAMEALV 153
Cdd:cd19142 83 IywsyGSEErglSRKHIIE-SVRASLRRLQLDYIDIVIIH-------------KADPMCPMEEVVR--------AMSYLI 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 24644950 154 EKGLTKSIGVSNFSKDQVARLLKNCK----IRPANNQIEHHVYLQQR 196
Cdd:cd19142 141 DNGLIMYWGTSRWSPVEIMEAFSIARqfncPTPICEQSEYHMFCREK 187
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
37-300 |
3.02e-13 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 68.84 E-value: 3.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 37 ALEAGYRHIDTAPVYG----NEkaigrvLKRwlDAGKVKREELFIVTKV----------PPvSNRPHEVEPTIKKSLEDL 102
Cdd:PRK10376 49 AVALGVNHIDTSDFYGphvtNQ------LIR--EALHPYPDDLTIVTKVgarrgedgswLP-AFSPAELRRAVHDNLRNL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 103 QLDYVDLylvhtpftININEDGSFKLDKEGlmevdvttnhaAIWVAMEALVE---KGLTKSIGVSNFSKDQVARLLKNCK 179
Cdd:PRK10376 120 GLDVLDV--------VNLRLMGDGHGPAEG-----------SIEEPLTVLAElqrQGLVRHIGLSNVTPTQVAEARKIAE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 180 IRPANNqiehHVYLQQRD---LVDFCKSENITVTAYSPLGskGIAKFNAGAgivrdlpdlmdipeVKEIAASHGKTPAQV 256
Cdd:PRK10376 181 IVCVQN----HYNLAHRAddaLIDALARDGIAYVPFFPLG--GFTPLQSST--------------LSDVAASLGATPMQV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 24644950 257 LLRWIIDTG--VSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSSL 300
Cdd:PRK10376 241 ALAWLLQRSpnILLIPGTSSVAHLRENLAAAELVLSEEVLAELDGI 286
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
12-215 |
7.90e-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: 67.86 E-value: 7.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 12 GEKMPVIGIGTW-----QASDEEIETAIDAALEAGYRHIDTAPVYGNEKA---IGRVLKR--WldagkvKREELFIVTKV 81
Cdd:cd19141 9 GLRVSCLGLGTWvtfgsQISDEVAEELVTLAYENGINLFDTAEVYAAGKAeivLGKILKKkgW------RRSSYVITTKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 82 --------PPVSNRPHEVEpTIKKSLEDLQLDYVDLYLVHTPftininedgsfkldkeglmevDVTTNHAAIWVAMEALV 153
Cdd:cd19141 83 fwggkaetERGLSRKHIIE-GLKASLERLQLEYVDIVFANRP---------------------DPNTPMEEIVRAFTHVI 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24644950 154 EKGLTKSIGVSNFSKDQVARLLKNCK----IRPANNQIEHHVYlqQRDLVDFCKSE-----NITVTAYSPL 215
Cdd:cd19141 141 NQGMAMYWGTSRWSAMEIMEAYSVARqfnlIPPIVEQAEYHLF--QREKVEMQLPElfhkiGVGAMTWSPL 209
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
17-302 |
2.47e-12 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 66.80 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 17 VIGIGTW----QASDEEIETAIDAALEAGYRHIDTAPVYG----------NEKAIGRvlkrWLdAGKVKREELFIVTKVP 82
Cdd:PRK10625 15 TLGLGTMtfgeQNSEADAHAQLDYAVAQGINLIDVAEMYPvpprpetqglTETYIGN----WL-AKRGSREKLIIASKVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 83 -PVSNRPHEVEP-------TIKKSLED----LQLDYVDLYLVHTPftinINEDGSF-KLDKEGLMEVDVTTnhaaIWVAM 149
Cdd:PRK10625 90 gPSRNNDKGIRPnqaldrkNIREALHDslkrLQTDYLDLYQVHWP----QRPTNCFgKLGYSWTDSAPAVS----LLETL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 150 EALVEK---GLTKSIGVSNFSKDQVARLLKNCKIR--PANNQIEHHVYLQQRD----LVDFCKSENITVTAYSPLGSKGI 220
Cdd:PRK10625 162 DALAEQqraGKIRYIGVSNETAFGVMRYLHLAEKHdlPRIVTIQNPYSLLNRSfevgLAEVSQYEGVELLAYSCLAFGTL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 221 A-KFNAGAGIVRDLPDLMD-------------IPEVKEIAASHGKTPAQVLLRWIIDTG--VSAIPKSTNPARLKQNLDV 284
Cdd:PRK10625 242 TgKYLNGAKPAGARNTLFSrftrysgeqtqkaVAAYVDIAKRHGLDPAQMALAFVRRQPfvASTLLGATTMEQLKTNIES 321
|
330
....*....|....*...
gi 24644950 285 FDFELTAEEVAKLSSLDQ 302
Cdd:PRK10625 322 LHLTLSEEVLAEIEAVHQ 339
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
33-286 |
3.25e-12 |
|
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: 66.15 E-value: 3.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 33 AIDAALEAGYRHIDTAPVYGN-EKAIGRVLKRwlDAGKVKREELFIVTKVPPVSNR-----PHEVEPTIKKSLEDLQLDY 106
Cdd:cd19164 39 IVRRALELGIRAFDTSPYYGPsEIILGRALKA--LRDEFPRDTYFIITKVGRYGPDdfdysPEWIRASVERSLRRLHTDY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 107 VDLYLVHtpftinineDGSFKLDKEglmevdvttnhaaIWVAMEALVE---KGLTKSIGVSNFSKD---QVARLLKNCKI 180
Cdd:cd19164 117 LDLVYLH---------DVEFVADEE-------------VLEALKELFKlkdEGKIRNVGISGYPLPvllRLAELARTTAG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 181 RP-------ANNQIEHHVYLQQRDLVdFCKSENITVTAYSPLG-----SKGIAKFNAGAGIVRDLPDlmdipEVKEIAAS 248
Cdd:cd19164 175 RPldavlsyCHYTLQNTTLLAYIPKF-LAAAGVKVVLNASPLSmgllrSQGPPEWHPASPELRAAAA-----KAAEYCQA 248
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 24644950 249 HGKTPAQVLLRWIIDTGVSAIPK---STNPARLKQNLDVFD 286
Cdd:cd19164 249 KGTDLADVALRYALREWGGEGPTvvgCSNVDELEEAVEAYW 289
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
11-304 |
4.00e-12 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 66.17 E-value: 4.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 11 NGEKMPVIGIGTW------QASDEEiETAIDAALEAGYRHIDTAPVYG-----NEKAIGRVLKrwlDAGKVKREELFIVT 79
Cdd:PRK09912 21 SGLRLPALSLGLWhnfghvNALESQ-RAILRKAFDLGITHFDLANNYGpppgsAEENFGRLLR---EDFAAYRDELIIST 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 80 KV-------PPVSNRPHE-VEPTIKKSLEDLQLDYVDLYLVHtpftininedgsfKLDKEGLMEVDVTtnhaaiwvAMEA 151
Cdd:PRK09912 97 KAgydmwpgPYGSGGSRKyLLASLDQSLKRMGLEYVDIFYSH-------------RVDENTPMEETAS--------ALAH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 152 LVEKGLTKSIGVSNFSKDQVAR---LLKNCKI-----RPANNQIEHhvYLQQRDLVDFCKSENITVTAYSPLGS------ 217
Cdd:PRK09912 156 AVQSGKALYVGISSYSPERTQKmveLLREWKIpllihQPSYNLLNR--WVDKSGLLDTLQNNGVGCIAFTPLAQglltgk 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 218 --KGI---AKFNAGAGIVRDLPDLM-------DIPEVKEIAASHGKTPAQVLLRWII-DTGV-SAIPKSTNPARLKQNLD 283
Cdd:PRK09912 234 ylNGIpqdSRMHREGNKVRGLTPKMlteanlnSLRLLNEMAQQRGQSMAQMALSWLLkDERVtSVLIGASRAEQLEENVQ 313
|
330 340
....*....|....*....|..
gi 24644950 284 VF-DFELTAEEvakLSSLDQNI 304
Cdd:PRK09912 314 ALnNLTFSTEE---LAQIDQHI 332
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
10-295 |
6.97e-12 |
|
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: 65.12 E-value: 6.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 10 NNGEKMPVIGIGTW---------QASDEEIETAIDAaleaGYRHIDTAPVYG-----NEKAIGRVLKRWLdagKVKREEL 75
Cdd:cd19151 7 RSGLKLPAISLGLWhnfgdvdryENSRAMLRRAFDL----GITHFDLANNYGpppgsAEENFGRILKEDL---KPYRDEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 76 FIVTKVP------PVSN---RPHEVEpTIKKSLEDLQLDYVDLYLVHTPftininedgsfklDKEGLMEVDVTtnhaaiw 146
Cdd:cd19151 80 IISTKAGytmwpgPYGDwgsKKYLIA-SLDQSLKRMGLDYVDIFYHHRP-------------DPETPLEETMG------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 147 vAMEALVEKGLTKSIGVSNFSKDQV---ARLLKN----CKI-RPANNQIEHHVylqQRDLVDFCKSENITVTAYSPLGS- 217
Cdd:cd19151 139 -ALDQIVRQGKALYVGISNYPPEEAreaAAILKDlgtpCLIhQPKYSMFNRWV---EEGLLDVLEEEGIGCIAFSPLAQg 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 218 -------KGIAKFNAGAGIVRDL------PDLMD-IPEVKEIAASHGKTPAQVLLRWII--DTGVSAIPKSTNPARLKQN 281
Cdd:cd19151 215 lltdrylNGIPEDSRAAKGSSFLkpeqitEEKLAkVRRLNEIAQARGQKLAQMALAWVLrnKRVTSVLIGASKPSQIEDA 294
|
330
....*....|....*
gi 24644950 282 LDVFD-FELTAEEVA 295
Cdd:cd19151 295 VGALDnREFSEEELA 309
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
16-292 |
1.67e-11 |
|
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381378 [Multi-domain] Cd Length: 308 Bit Score: 64.17 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 16 PVIGIGT-------WQASDEEIETAIDAALEAGYRHIDTAPVYGN---EKAIGRVLKRwldagkVKREELFIVTKV---- 81
Cdd:cd19152 1 PKLGFGTaplgnlyEAVSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALRE------LGREDYVISTKVgrll 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 82 ------------PPVSNRPHEVE-----PTIKKSLED----LQLDYVDLYLVHTPftininedgsfklDKEGLMEVDVTT 140
Cdd:cd19152 75 vplqeveptfepGFWNPLPFDAVfdysyDGILRSIEDslqrLGLSRIDLLSIHDP-------------DEDLAGAESDEH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 141 NHAAI---WVAMEALVEKGLTKSIGV-SNFSkDQVARLLKNCK---IRPAN--NQIEHHvylQQRDLVDFCKSENITVTA 211
Cdd:cd19152 142 FAQAIkgaFRALEELREEGVIKAIGLgVNDW-EVILRILEEADldwVMLAGryTLLDHS---AARELLPECEKRGVKVVN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 212 YSPLGSkGI------AKFNAGAGIVRDLPDLMDipEVKEIAASHGKTPAQVLLRWIID-TGVSA-IPKSTNPARLKQNLD 283
Cdd:cd19152 218 AGPFNS-GFlaggdnFDYYEYGPAPPELIARRD--RIEALCEQHGVSLAAAALQFALApPAVASvAPGASSPERVEENVA 294
|
....*....
gi 24644950 284 VFDFELTAE 292
Cdd:cd19152 295 LLATEIPAA 303
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
12-295 |
3.01e-11 |
|
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: 63.24 E-value: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 12 GEKMPVIGIGTWQ--ASDEEIETA---IDAALEAGYRHIDTAPVYG-----NEKAIGRVLKRWLDAgkvKREELFIVTKV 81
Cdd:cd19150 9 GLKLPALSLGLWHnfGDDTPLETQraiLRTAFDLGITHFDLANNYGpppgsAEENFGRILREDFAG---YRDELIISTKA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 82 P------PVS---NRPHeVEPTIKKSLEDLQLDYVDLYLVHtpftininedgsfKLDKEGLMEvdvTTNHaaiwvAMEAL 152
Cdd:cd19150 86 GydmwpgPYGewgSRKY-LLASLDQSLKRMGLDYVDIFYSH-------------RFDPDTPLE---ETMG-----ALDHA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 153 VEKGLTKSIGVSNFSKD---QVARLLKNCKI-----RPANNQIEHhvYLQQRDLVDFCKSENITVTAYSPLGS------- 217
Cdd:cd19150 144 VRSGKALYVGISSYSPErtrEAAAILRELGTpllihQPSYNMLNR--WVEESGLLDTLQELGVGCIAFTPLAQglltdky 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 218 -KGI---AKFNAGAGIVRDLPDLMDIPEVK---EIAASHGKTPAQVLLRWIIDTGV--SAIPKSTNPARLKQNLDVFD-F 287
Cdd:cd19150 222 lNGIpegSRASKERSLSPKMLTEANLNSIRalnEIAQKRGQSLAQMALAWVLRDGRvtSALIGASRPEQLEENVGALDnL 301
|
....*...
gi 24644950 288 ELTAEEVA 295
Cdd:cd19150 302 TFSADELA 309
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
11-200 |
3.68e-11 |
|
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: 63.08 E-value: 3.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 11 NGEKMPVIGIGTW-----QASDEEIETAIDAALEAGYRHIDTAPVYGN---EKAIGRVLKR--WldagkvKREELFIVTK 80
Cdd:cd19160 11 SGLRVSCLGLGTWvtfgsQISDETAEDLLTVAYEHGVNLFDTAEVYAAgkaERTLGNILKSkgW------RRSSYVVTTK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 81 V--------PPVSNRPHEVEpTIKKSLEDLQLDYVDLYLVHtpftininedgsfKLDKEGLMEvdvttnhaAIWVAMEAL 152
Cdd:cd19160 85 IywggqaetERGLSRKHIIE-GLRGSLDRLQLEYVDIVFAN-------------RSDPNSPME--------EIVRAMTYV 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 24644950 153 VEKGLTKSIGVSNFSKDQVARLLKNCK----IRPANNQIEHHVYlqQRDLVD 200
Cdd:cd19160 143 INQGMAMYWGTSRWSAMEIMEAYSVARqfnlIPPVCEQAEYHLF--QREKVE 192
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
11-282 |
4.71e-11 |
|
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: 62.75 E-value: 4.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 11 NGEKMPVIGIGTW-----QASDEEIETAIDAALEAGYRHIDTAPVYGNEKA---IGRVLKR--WldagkvKREELFIVTK 80
Cdd:cd19159 9 SGLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAeviLGSIIKKkgW------RRSSLVITTK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 81 V--------PPVSNRPHEVEpTIKKSLEDLQLDYVDLYLVHTPftininedgsfkldkeglmevDVTTNHAAIWVAMEAL 152
Cdd:cd19159 83 LywggkaetERGLSRKHIIE-GLKGSLQRLQLEYVDVVFANRP---------------------DSNTPMEEIVRAMTHV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 153 VEKGLTKSIGVSNFSKDQVARLLKNCK----IRPANNQIEHHVYlqQRDLVDFCKSE---NITVTA--YSPLGSkGIAKF 223
Cdd:cd19159 141 INQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLF--QREKVEVQLPElyhKIGVGAmtWSPLAC-GIISG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 224 NAGAGIvrdlPD-----------LMD-------------IPEVKEIAASHGKTPAQVLLRWII-DTGVSAI-PKSTNPAR 277
Cdd:cd19159 218 KYGNGV----PEssraslkcyqwLKErivseegrkqqnkLKDLSPIAERLGCTLPQLAVAWCLrNEGVSSVlLGSSTPEQ 293
|
....*
gi 24644950 278 LKQNL 282
Cdd:cd19159 294 LIENL 298
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
11-282 |
6.16e-10 |
|
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.
Pssm-ID: 381384 [Multi-domain] Cd Length: 324 Bit Score: 59.33 E-value: 6.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 11 NGEKMPVIGIGTW-----QASDEEIETAIDAALEAGYRHIDTAPVYGNEKA---IGRVLKR--WldagkvKREELFIVTK 80
Cdd:cd19158 9 SGLRVSCLGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAevvLGNIIKKkgW------RRSSLVITTK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 81 V--------PPVSNRPHEVEpTIKKSLEDLQLDYVDLYLVHTPftininedgsfklDKEGLMEVDVTtnhaaiwvAMEAL 152
Cdd:cd19158 83 IfwggkaetERGLSRKHIIE-GLKASLERLQLEYVDVVFANRP-------------DPNTPMEETVR--------AMTHV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 153 VEKGLTKSIGVSNFSKDQVARLLKNCK----IRPANNQIEHHVYlqQRDLVDFCKSE-----NITVTAYSPLGSKGIA-K 222
Cdd:cd19158 141 INQGMAMYWGTSRWSSMEIMEAYSVARqfnlIPPICEQAEYHMF--QREKVEVQLPElfhkiGVGAMTWSPLACGIVSgK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 223 FNAGA-----GIVRDLPDLMD-------------IPEVKEIAASHGKTPAQVLLRWII-DTGVSAI-PKSTNPARLKQNL 282
Cdd:cd19158 219 YDSGIppysrASLKGYQWLKDkilseegrrqqakLKELQAIAERLGCTLPQLAIAWCLrNEGVSSVlLGASNAEQLMENI 298
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
26-286 |
9.50e-10 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 58.88 E-value: 9.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 26 SDEEIETAIDAALEAGYRHIDTAPVYGNEKA---IGRVLKRwldagkVKREELFIVTKV---------PPVSNRPHEVEP 93
Cdd:cd19161 18 SNADADATLDAAWDSGIRYFDTAPMYGHGLAehrLGDFLRE------KPRDEFVLSTKVgrllkpareGSVPDPNGFVDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 94 T------------IKKSLED----LQLDYVDLYLVH--TPFTI-NINEDGSFKLDKEGLMEvdvttnhaaiwvAMEALVE 154
Cdd:cd19161 92 LpfeivydysydgIMRSFEDslqrLGLNRIDILYVHdiGVYTHgDRKERHHFAQLMSGGFK------------ALEELKK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 155 KGLTKSIGVSNFSKDQVARLLKNCKIRPANNQIEHHVyLQQRDLVDF---CKSENITVTAYSPL-------GSKGIAKFN 224
Cdd:cd19161 160 AGVIKAFGLGVNEVQICLEALDEADLDCFLLAGRYSL-LDQSAEEEFlprCEQRGTSLVIGGVFnsgilatGTKSGAKFN 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24644950 225 AGAGIvrdlPDLMD-IPEVKEIAASHGKTPAQVLLRWII-DTGVSAI-PKSTNPARLKQNLDVFD 286
Cdd:cd19161 239 YGDAP----AEIISrVMEIEKICDAYNVPLAAAALQFPLrHPAVASVlTGARNPAQLRQNVEAFQ 299
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
31-299 |
5.55e-07 |
|
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins; Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis.
Pssm-ID: 381372 [Multi-domain] Cd Length: 326 Bit Score: 50.50 E-value: 5.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 31 ETA---IDAALEAGYRHIDTAPVY---GNEKAIGRvlkrWLdAGKVKREELFIVTKVPpVSNRPHEVEP----------- 93
Cdd:cd19146 35 ETAfklLDAFYEQGGNFIDTANNYqgeESERWVGE----WM-ASRGNRDEMVLATKYT-TGYRRGGPIKiksnyqgnhak 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 94 ----TIKKSLEDLQLDYVDLYLVHT-PFTININEdgsfkldkegLMEvdvttnhaaiwvAMEALVEKGLTKSIGVSnfsk 168
Cdd:cd19146 109 slrlSVEASLKKLQTSYIDILYVHWwDYTTSIPE----------LMQ------------SLNHLVAAGKVLYLGVS---- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 169 DQVARLLKNCkirpaNNQIEHHVYLQ---------------QRDLVDFCKSENItvtAYSPLGSKGIAKFNAGAGIVRDL 233
Cdd:cd19146 163 DTPAWVVSKA-----NAYARAHGLTQfvvyqghwsaafrdfERDILPMCEAEGM---ALAPWGVLGQGQFRTEEEFKRRG 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24644950 234 PDLMDI-----PEVK------EIAASHGKTPAQVLLRWIIDTG--VSAIPKSTNPARLKQNLDVFDFELTAEEVAKLSS 299
Cdd:cd19146 235 RSGRKGgpqteKERKvsekleKVAEEKGTAITSVALAYVMHKApyVFPIVGGRKVEHLKGNIEALGISLSDEEIQEIED 313
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
31-113 |
4.93e-06 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 47.47 E-value: 4.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 31 ETAIDAALEA---GYRHIDTAPVYGN---EKAIGRVLKrwldAGKVKREELFIVTKVPPVSN----RPHEVEPTIKKSLE 100
Cdd:PLN02587 31 EDAIASVREAfrlGINFFDTSPYYGGtlsEKVLGKALK----ALGIPREKYVVSTKCGRYGEgfdfSAERVTKSVDESLA 106
|
90
....*....|...
gi 24644950 101 DLQLDYVDLYLVH 113
Cdd:PLN02587 107 RLQLDYVDILHCH 119
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
35-302 |
3.61e-04 |
|
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: 381324 [Multi-domain] Cd Length: 318 Bit Score: 41.56 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 35 DAALEAGYRHIDTAPVYGNEKAIgrvLKRWLDAGKVKREELFIVTKVP-------PVSNRPHEVE----PTIKKSL-EDL 102
Cdd:cd19098 42 DAAWAAGVRYFDAARSYGRAEEF---LGSWLRSRNIAPDAVFVGSKWGytytadwQVDAAVHEVKdhslARLLKQWeETR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 103 QL--DYVDLYLVHtpftininedgSFKLDkEGLMEvdvttnHAAIWVAMEALVEKGLtkSIGVSNFSKDQVARLLKNCKI 180
Cdd:cd19098 119 SLlgKHLDLYQIH-----------SATLE-SGVLE------DADVLAALAELKAEGV--KIGLSLSGPQQAETLRRALEI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 181 RPannqiehhvylQQRDLVDFCKSeniTVTAYSPLGSKGIAK-FNAGAGIV--------RdLPDLMDIPEV-------KE 244
Cdd:cd19098 179 EI-----------DGARLFDSVQA---TWNLLEQSAGEALEEaHEAGMGVIvkealangR-LTDRNPSPELaplmavlKA 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 245 IAASHGKTPAQVLLRWIIDTGVSAIPKS--TNPARLKQNLDVFDFELTAEEVAKLSSLDQ 302
Cdd:cd19098 244 VADRLGVTPDALALAAVLAQPFVDVVLSgaATPEQLRSNLRALDVSLDLELLAALADLAE 303
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
34-297 |
6.62e-04 |
|
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; Phanerochaete chrysosporium ADD (EC1.1.1.91) is a founding member of aldo-keto reductase family 9 member A3. It is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). This family also includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381373 [Multi-domain] Cd Length: 319 Bit Score: 40.96 E-value: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 34 IDAALEAGYRHIDTAPVYGNEKA---IGRvlkrWLdAGKVKREELFIVTKVPPVSNRPHEVEP---------------TI 95
Cdd:cd19147 40 LDAFYEAGGNFIDTANNYQDEQSetwIGE----WM-KSRKNRDQIVIATKFTTDYKAYEVGKGkavnycgnhkrslhvSV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 96 KKSLEDLQLDYVDLYLVHT-PFTININEdgsfkldkegLMEvdvttnhaaiwvAMEALVEKGLTKSIGVSNFSKDQVArl 174
Cdd:cd19147 115 RDSLRKLQTDWIDILYVHWwDYTTSIEE----------VMD------------SLHILVQQGKVLYLGVSDTPAWVVS-- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644950 175 lknckirPANNQIEHH------VYLQQ---------RDLVDFCKSENITVTAYSPLGSkgiAKFNA----------GAGI 229
Cdd:cd19147 171 -------AANYYATAHgktpfsVYQGRwnvlnrdfeRDIIPMARHFGMALAPWDVLGG---GKFQSkkaveerkknGEGL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24644950 230 VRDL-PDLMDIPEVK------EIAASHG-KTPAQVLLRWIIDTGVSAIP--KSTNPARLKQNLDVFDFELTAEEVAKL 297
Cdd:cd19147 241 RSFVgGTEQTPEEVKisealeKVAEEHGtESVTAIALAYVRSKAPNVFPlvGGRKIEHLKDNIEALSIKLTPEEIEYL 318
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