|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
2-309 |
0e+00 |
|
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: 520.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 2 STITLNNGFEMPVIGLGLWRLEKEELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAEAIQSGLVKREELFITSKVWNS 81
Cdd:cd19112 1 STITLNSGHKMPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLWNS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 82 DHGHVVEACKNSLKKLQLDYLDLYLVHYPLATKHSGVGTTASLLDENKVLDIDVTVSLETTWHDMEKTVSLGLVRSIGLS 161
Cdd:cd19112 81 DHGHVIEACKDSLKKLQLDYLDLYLVHFPVATKHTGVGTTGSALGEDGVLDIDVTISLETTWHAMEKLVSAGLVRSIGIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 162 NYELFLTRDCLSYAKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLGGATANVKAFGSISPLEDPVLIGLAKKYQ 241
Cdd:cd19112 161 NYDIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGGAAANAEWFGSVSPLDDPVLKDLAKKYG 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
7S5I_A 242 KSVAQIALRWNIERGTPVIPKSSKVERLKENLEVLNFKLEKEDIELINTIDKKFRTTLPSLSWGVDVY 309
Cdd:cd19112 241 KSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYRTNQPAKFWGIDLY 308
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
12-289 |
1.57e-104 |
|
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: 305.56 E-value: 1.57e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 12 MPVIGLGLWRLEKEELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAEAIqsglVKREELFITSKVWNSDHG--HVVEA 89
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESG----VPREELFITTKLWPTDHGyeRVREA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 90 CKNSLKKLQLDYLDLYLVHYPLATKHsgvgttaslldenkvldIDVTVSLETTWHDMEKTVSLGLVRSIGLSNYELFLTR 169
Cdd:cd19071 77 LEESLKDLGLDYLDLYLIHWPVPGKE-----------------GGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 170 DCLSYAKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLGGatanvkafGSISPLEDPVLIGLAKKYQKSVAQIAL 249
Cdd:cd19071 140 ELLAAARIKPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGR--------GRRPLLDDPVLKEIAKKYGKTPAQVLL 211
|
250 260 270 280
....*....|....*....|....*....|....*....|
7S5I_A 250 RWNIERGTPVIPKSSKVERLKENLEVLNFKLEKEDIELIN 289
Cdd:cd19071 212 RWALQRGVVVIPKSSNPERIKENLDVFDFELSEEDMAAID 251
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
3-297 |
4.33e-103 |
|
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: 303.43 E-value: 4.33e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 3 TITLNNGFEMPVIGLGLWRL-EKEELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAEAIQSGLVKREELFITSKVWNS 81
Cdd:cd19116 2 TIKLNDGNEIPAIALGTWKLkDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLWNS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 82 DHGH--VVEACKNSLKKLQLDYLDLYLVHYPLATKHSGVGTTASLLDenkVLDIDVtvsLETtWHDMEKTVSLGLVRSIG 159
Cdd:cd19116 82 YHEReqVEPALRESLKRLGLDYVDLYLIHWPVAFKENNDSESNGDGS---LSDIDY---LET-WRGMEDLVKLGLTRSIG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 160 LSNYELFLTRDCLSYAKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLGgatANVKAFGSISP--LEDPVLIGLA 237
Cdd:cd19116 155 VSNFNSEQINRLLSNCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFG---RLVPRGQTNPPprLDDPTLVAIA 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 238 KKYQKSVAQIALRWNIERGTPVIPKSSKVERLKENLEVLNFKLEKEDIELINTIDKKFRT 297
Cdd:cd19116 232 KKYGKTTAQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRV 291
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
8-297 |
5.98e-99 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 291.57 E-value: 5.98e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 8 NGFEMPVIGLGLWRLEKEELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAEaiqSGlVKREELFITSKVWNSDHG--H 85
Cdd:COG0656 1 NGVEIPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAA---SG-VPREELFVTTKVWNDNHGydD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 86 VVEACKNSLKKlqldyldlylvhyplatkhsgvgttaslldenkvLDID----------VTVSLETTWHDMEKTVSLGLV 155
Cdd:COG0656 77 TLAAFEESLER----------------------------------LGLDyldlylihwpGPGPYVETWRALEELYEEGLI 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 156 RSIGLSNYELFLTRDCLSYAKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLGGatanvkafGSIspLEDPVLIG 235
Cdd:COG0656 123 RAIGVSNFDPEHLEELLAETGVKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGR--------GKL--LDDPVLAE 192
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
7S5I_A 236 LAKKYQKSVAQIALRWNIERGTPVIPKSSKVERLKENLEVLNFKLEKEDIELINTIDKKFRT 297
Cdd:COG0656 193 IAEKHGKTPAQVVLRWHLQRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRGERL 254
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
2-296 |
3.45e-94 |
|
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: 281.22 E-value: 3.45e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 2 STITLNNGFEMPVIGLGLWRLEKEELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAEAIQSGLVKREELFITSKVWNS 81
Cdd:cd19154 2 ASITLSNGVKMPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLWTH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 82 DH--GHVVEACKNSLKKLQLDYLDLYLVHYPLATKHSgvgTTASLLDENKvLDIDVTVSLETTWHDMEKTVSLGLVRSIG 159
Cdd:cd19154 82 EHapEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDD---EGESGTMENG-MSIHDAVDVEDVWRGMEKVYDEGLTKAIG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 160 LSNYELFLTRDCLSYAKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLG--GATANVKAFGSI---SPLEDPVLI 234
Cdd:cd19154 158 VSNFNNDQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGspGRANFTKSTGVSpapNLLQDPIVK 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
7S5I_A 235 GLAKKYQKSVAQIALRWNIERGTPVIPKSSKVERLKENLEVLNFKLEKEDIELINTIDKKFR 296
Cdd:cd19154 238 AIAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLR 299
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
8-291 |
1.75e-91 |
|
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: 273.37 E-value: 1.75e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 8 NGFEMPVIGLG--LWRLEKEELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAEAIQSGLVK-REELFITSKVWNSDH- 83
Cdd:cd19124 1 SGQTMPVIGMGtaSDPPSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKLWCSDAh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 84 -GHVVEACKNSLKKLQLDYLDLYLVHYPLATKHsgvGTTASLLDENKVLDIDvtvsLETTWHDMEKTVSLGLVRSIGLSN 162
Cdd:cd19124 81 pDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKP---GKFSFPIEEEDFLPFD----IKGVWEAMEECQRLGLTKAIGVSN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 163 YELFLTRDCLSYAKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLGGATAnvkAFGSISPLEDPVLIGLAKKYQK 242
Cdd:cd19124 154 FSCKKLQELLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGT---KWGSNAVMESDVLKEIAAAKGK 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
7S5I_A 243 SVAQIALRWNIERGTPVIPKSSKVERLKENLEVLNFKLEKEDIELINTI 291
Cdd:cd19124 231 TVAQVSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
6-302 |
2.02e-91 |
|
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: 274.26 E-value: 2.02e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 6 LNNGFEMPVIGLGLWRLEKEELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAEAIQSGL-VKREELFITSKVWNSDHg 84
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPGKaVPREDLFVTSKLWNTKH- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 85 H---VVEACKNSLKKLQLDYLDLYLVHYPLATKHsgvGTTASLLDENKVLDIDVTVSLETtWHDMEKTVSLGLVRSIGLS 161
Cdd:cd19106 80 HpedVEPALRKTLKDLQLDYLDLYLIHWPYAFER---GDNPFPKNPDGTIRYDSTHYKET-WKAMEKLVDKGLVKAIGLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 162 NYELFLTRDCLSYAKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLGGATANVKAFGSISPLEDPVLIGLAKKYQ 241
Cdd:cd19106 156 NFNSRQIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPDRPWAKPDEPVLLEEPKVKALAKKYN 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
7S5I_A 242 KSVAQIALRWNIERGTPVIPKSSKVERLKENLEVLNFKLEKEDIELINTIDKKFRTTLPSL 302
Cdd:cd19106 236 KSPAQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRYIVPMI 296
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
3-296 |
1.04e-90 |
|
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: 272.76 E-value: 1.04e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 3 TITLNNGFEMPVIGLGLWRLEKEELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAEAIQSGLVKREELFITSKVWNSD 82
Cdd:cd19115 4 TVKLNSGYDMPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLWNTF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 83 HG--HVVEACKNSLKKLQLDYLDLYLVHYPLATKH--SGVGTTASLLDENKVLDIDvTVSLETTWHDMEKTVSLGLVRSI 158
Cdd:cd19115 84 HDgeRVEPICRKQLADWGIDYFDLFLIHFPIALKYvdPAVRYPPGWFYDGKKVEFS-NAPIQETWTAMEKLVDKGLARSI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 159 GLSNYELFLTRDCLSYAKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHT---PLGGATANVKAFGSISPL-EDPVLI 234
Cdd:cd19115 163 GVSNFSAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSsfgPQSFLELDLPGAKDTPPLfEHDVIK 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
7S5I_A 235 GLAKKYQKSVAQIALRWNIERGTPVIPKSSKVERLKENLEVLNFKLEKEDIELINTIDKKFR 296
Cdd:cd19115 243 SIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLR 304
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
1-296 |
1.41e-90 |
|
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: 271.59 E-value: 1.41e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 1 MSTITLNNGFEMPVIGLGLWRLEKEELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAEAIQSGLVKREELFITSKVWN 80
Cdd:cd19123 1 MKTLPLSNGDLIPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 81 SDHG--HVVEACKNSLKKLQLDYLDLYLVHYPLATKHsGVGTTASLLDENKVLDIdvtvSLETTWHDMEKTVSLGLVRSI 158
Cdd:cd19123 81 NSHApeDVLPALEKTLADLQLDYLDLYLMHWPVALKK-GVGFPESGEDLLSLSPI----PLEDTWRAMEELVDKGLCRHI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 159 GLSNYELFLTRDCLSYAKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLG--GATANVKAFGSISPLEDPVLIGL 236
Cdd:cd19123 156 GVSNFSVKKLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGsgDRPAAMKAEGEPVLLEDPVINKI 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 237 AKKYQKSVAQIALRWNIERGTPVIPKSSKVERLKENLEVLNFKLEKEDIELINTIDKKFR 296
Cdd:cd19123 236 AEKHGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHR 295
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
5-291 |
5.55e-86 |
|
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: 259.59 E-value: 5.55e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 5 TLNNGFEMPVIGLGLWRLEKEELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAEAIQSGLVKREELFITSKVWNSDHG 84
Cdd:cd19125 4 KLNTGAKIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLWCTDHA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 85 --HVVEACKNSLKKLQLDYLDLYLVHYPLATKHSGVGTTASlldenKVLDIDVtvslETTWHDMEKTVSLGLVRSIGLSN 162
Cdd:cd19125 84 peDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKGAHMPEPE-----EVLPPDI----PSTWKAMEKLVDSGKVRAIGVSN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 163 YELFLTRDCLSYAKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLGGATAnvkAFGSISPLEDPVLIGLAKKYQK 242
Cdd:cd19125 155 FSVKKLEDLLAVARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGT---TWVKKNVLKDPIVTKVAEKLGK 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
7S5I_A 243 SVAQIALRWNIERGTPVIPKSSKVERLKENLEVLNFKLEKEDIELINTI 291
Cdd:cd19125 232 TPAQVALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSI 280
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
13-291 |
1.18e-79 |
|
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: 243.20 E-value: 1.18e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 13 PVIGLGLWRLEKEELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAEAIQSGLVKREELFITSKVWNSDH--GHVVEAC 90
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHqpENVKEQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 91 KNSLKKLQLDYLDLYLVHYPLATKHSGVGTTAslldENKVLDIDVTVSLETTWHDMEKTVSLGLVRSIGLSNYELFLTRD 170
Cdd:cd19128 82 LITLQDLQLEYLDLFLIHWPLAFDMDTDGDPR----DDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 171 CLSYAKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLGGAtanvKAFGSISPLEDPVLIGLAKKYQKSVAQIALR 250
Cdd:cd19128 158 LLNYCKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGS----YGDGNLTFLNDSELKALATKYNTTPPQVIIA 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....
7S5I_A 251 WNIERGT---PVIPKSSKVERLKENLEVLNFKLEKEDIELINTI 291
Cdd:cd19128 234 WHLQKWPknySVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
4-292 |
2.35e-79 |
|
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: 241.71 E-value: 2.35e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 4 ITLNNGFEMPVIGLGLWRLE-KEELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAEAIqsglVKREELFITSKVWNSD 82
Cdd:cd19133 1 VTLNNGVEMPILGFGVFQIPdPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKSG----IPREELFITTKLWIQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 83 HGHvvEACKN----SLKKLQLDYLDLYLVHYPLATKHSgvgttaslldenkvldidvtvsletTWHDMEKTVSLGLVRSI 158
Cdd:cd19133 77 AGY--EKAKKaferSLKRLGLDYLDLYLIHQPFGDVYG-------------------------AWRAMEELYKEGKIRAI 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 159 GLSNYELFLTRDCLSYAKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLGGATANVkafgsispLEDPVLIGLAK 238
Cdd:cd19133 130 GVSNFYPDRLVDLILHNEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAEGRNNL--------FENPVLTEIAE 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
7S5I_A 239 KYQKSVAQIALRWNIERGTPVIPKSSKVERLKENLEVLNFKLEKEDIELINTID 292
Cdd:cd19133 202 KYGKSVAQVILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAALD 255
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
12-291 |
2.28e-78 |
|
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: 239.46 E-value: 2.28e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 12 MPVIGLGLWRL-EKEELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAEAIQSGLVKREELFITSKVWNSDHGH--VVE 88
Cdd:cd19136 1 MPILGLGTFRLrGEEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGYekARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 89 ACKNSLKKLQLDYLDLYLVHYPLATKHSGVGTtaslldENKVLDIDvtvsletTWHDMEKTVSLGLVRSIGLSNYELFLT 168
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWPGVQGLKPSDP------RNAELRRE-------SWRALEDLYKEGKLRAIGVSNYTVRHL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 169 RDCLSYAKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLGGatanvkafGSISPLEDPVLIGLAKKYQKSVAQIA 248
Cdd:cd19136 148 EELLKYCEVPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGS--------GDLRLLEDPTVLAIAKKYGRTPAQVL 219
|
250 260 270 280
....*....|....*....|....*....|....*....|...
7S5I_A 249 LRWNIERGTPVIPKSSKVERLKENLEVLNFKLEKEDIELINTI 291
Cdd:cd19136 220 LRWALQQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
9-296 |
1.08e-77 |
|
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: 239.00 E-value: 1.08e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 9 GFEMPVIGLGLWRLEKEELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAEAIQSGLVKREELFITSKVWNSDHG--HV 86
Cdd:cd19114 1 GDKMPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGkdHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 87 VEACKNSLKKLQLDYLDLYLVHYPLATKH---SGVGTTASLLDENKVLDIDvTVSLETTWHDMEKTVSLGLVRSIGLSNY 163
Cdd:cd19114 81 REAFDRQLKDYGLDYIDLYLIHFPIPAAYvdpAENYPFLWKDKELKKFPLE-QSPMQECWREMEKLVDAGLVRNIGIANF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 164 ELFLTRDCLSYAKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLGGA-----TANVKAFGSIspLEDPVLIGLAK 238
Cdd:cd19114 160 NVQLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAvytkvTKHLKHFTNL--LEHPVVKKLAD 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
7S5I_A 239 KYQKSVAQIALRWNIERGTPVIPKSSKVERLKENLEVLNFKLEKEDIELINTIDKKFR 296
Cdd:cd19114 238 KHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANAR 295
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
2-296 |
7.49e-77 |
|
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: 237.34 E-value: 7.49e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 2 STITLNNGFEMPVIGLGLWRLEKEELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAEAIQSGLVKREELFITSKVWNS 81
Cdd:cd19113 1 PDIKLNSGYKMPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 82 DHG--HVVEACKNSLKKLQLDYLDLYLVHYPLATK------------HSGvgttasllDENKVLDIDvtVSLETTWHDME 147
Cdd:cd19113 81 FHDpkNVETALNKTLSDLKLDYVDLFLIHFPIAFKfvpieekyppgfYCG--------DGDNFVYED--VPILDTWKALE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 148 KTVSLGLVRSIGLSNYELFLTRDCLSYAKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLGGAT----ANVKAFG 223
Cdd:cd19113 151 KLVDAGKIKSIGVSNFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGPQSfvelNQGRALN 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
7S5I_A 224 SISPLEDPVLIGLAKKYQKSVAQIALRWNIERGTPVIPKSSKVERLKENLEVLNFKLEKEDIELINTIDKKFR 296
Cdd:cd19113 231 TPTLFEHDTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLR 303
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
3-296 |
2.22e-76 |
|
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 234.21 E-value: 2.22e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 3 TITLNNGFEMPVIGLGLWRLEK-EELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAEaiqsGLVKREELFITSKVWNS 81
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEEgSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKE----SGIPREELFITSKVWNA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 82 DHGH--VVEACKNSLKKLQLDYLDLYLVHYPLATKHsgvgttaslldenkvldidvtvslETTWHDMEKTVSLGLVRSIG 159
Cdd:cd19157 77 DQGYdsTLKAFEASLERLGLDYLDLYLIHWPVKGKY------------------------KETWKALEKLYKDGRVRAIG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 160 LSNYELFLTRDCLSYAKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLggatanvkAFGSIspLEDPVLIGLAKK 239
Cdd:cd19157 133 VSNFQVHHLEDLLADAEIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPL--------MQGQL--LDNPVLKEIAEK 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
7S5I_A 240 YQKSVAQIALRWNIERGTPVIPKSSKVERLKENLEVLNFKLEKEDIELINTIDKKFR 296
Cdd:cd19157 203 YNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNENLR 259
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
9-296 |
1.76e-75 |
|
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: 232.77 E-value: 1.76e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 9 GFEMPVIGLGLWRLEKEELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAEAIQSGLVKREELFITSKVWNSDH--GHV 86
Cdd:cd19111 1 GFPMPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLefKDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 87 VEACKNSLKKLQLDYLDLYLVHYPLATKHsgvgttasllDENKVLDIDVTVSLETTWHDMEKTVSLGLVRSIGLSNYELF 166
Cdd:cd19111 81 EKSLEKSLENLKLPYVDLYLIHHPCGFVN----------KKDKGERELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 167 LTRDCLSYAKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLGGAT-ANVKAFGSI-SPLEDPVLIGLAKKYQKSV 244
Cdd:cd19111 151 QINKILAYAKVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSPGrANQSLWPDQpDLLEDPTVLAIAKELDKTP 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
7S5I_A 245 AQIALRWNIERGTPVIPKSSKVERLKENLEVLNFKLEKEDIELINTIDKKFR 296
Cdd:cd19111 231 AQVLLRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMK 282
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
4-292 |
4.24e-75 |
|
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes prostaglandin F2-alpha synthase (PGFS) from Leishmania major (AKR5A1) and Trypanosoma brucei (AKR5A2). PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity for synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde. The AKR5G family of AKR includes Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase, which corresponds to aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381352 [Multi-domain] Cd Length: 254 Bit Score: 230.79 E-value: 4.24e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 4 ITLNNGFEMPVIGLGLWRLEK-EELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAEaiqSGlVKREELFITSKVWNSD 82
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQTPDgDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRE---SG-VPREELFVTTKLWNDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 83 HGH--VVEACKNSLKKLQLDYLDLYLVHYPLATKhsgvgttaslldenkvldidvtvsLETTWHDMEKTVSLGLVRSIGL 160
Cdd:cd19126 77 QRArrTEDAFQESLDRLGLDYVDLYLIHWPGKDK------------------------FIDTWKALEKLYASGKVKAIGV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 161 SNYELFLTRDCLSYAKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLGGATAnvkafgsispLEDPVLIGLAKKY 240
Cdd:cd19126 133 SNFQEHHLEELLAHADVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQGGL----------LSNPVLAAIGEKY 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
7S5I_A 241 QKSVAQIALRWNIERGTPVIPKSSKVERLKENLEVLNFKLEKEDIELINTID 292
Cdd:cd19126 203 GKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAIDALN 254
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
2-296 |
6.57e-74 |
|
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: 229.72 E-value: 6.57e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 2 STITLNNGFEMPVIGLGLWRLEKEELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAEAIQSGLVKREELFITSKV-WN 80
Cdd:cd19155 2 NCVTFNNGEKMPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLpPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 81 SDHGHVVEAC-KNSLKKLQLDYLDLYLVHYPLATKHSGVGTTasLLDENKVLDIDVTVSLETTWHDMEKTVSLGLVRSIG 159
Cdd:cd19155 82 GNRREKVEKFlLKSLEKLQLDYVDLYLIHFPVGSLSKEDDSG--KLDPTGEHKQDYTTDLLDIWKAMEAQVDQGLTRSIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 160 LSNYELFLTRDCLSYAKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLG--GATANVKAFGSIS-----PLEDPV 232
Cdd:cd19155 160 LSNFNREQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGspGAAHFSPGTGSPSgsspdLLQDPV 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
7S5I_A 233 LIGLAKKYQKSVAQIALRWNIERGTPVIPKSSKVERLKENLEVLNFKLEKEDIELINTIDKKFR 296
Cdd:cd19155 240 VKAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIR 303
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
1-291 |
5.27e-73 |
|
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: 225.67 E-value: 5.27e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 1 MSTITLNNGFEMPVIGLGLWRLEKEElRSAILNAIK-LGYRHFDAAAHYKTEIDVGNAIAEaiqSGlVKREELFITSKVW 79
Cdd:cd19135 2 TPTVRLSNGVEMPILGLGTSHSGGYS-HEAVVYALKeCGYRHIDTAKRYGCEELLGKAIKE---SG-VPREDLFLTTKLW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 80 NSDHGH--VVEACKNSLKKLQLDYLDLYLVHYPLAtkHSGVGTTASLLDEnkvldidvtvsletTWHDMEKTVSLGLVRS 157
Cdd:cd19135 77 PSDYGYesTKQAFEASLKRLGVDYLDLYLLHWPDC--PSSGKNVKETRAE--------------TWRALEELYDEGLCRA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 158 IGLSNYELFLTRDCLSYAKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLGGAtanvkafgsiSPLEDPVLIGLA 237
Cdd:cd19135 141 IGVSNFLIEHLEQLLEDCSVVPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAKG----------KALEEPTVTELA 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
7S5I_A 238 KKYQKSVAQIALRWNIERGTPVIPKSSKVERLKENLEVLNFKLEKEDIELINTI 291
Cdd:cd19135 211 KKYQKTPAQILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
3-292 |
5.66e-72 |
|
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: 222.63 E-value: 5.66e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 3 TITLNNGFEMPVIGLGLWRLEKEELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAEaiqSGlVKREELFITSKVWNSD 82
Cdd:cd19131 1 TITLNDGNTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRA---SG-VPREELFITTKLWNSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 83 HGH--VVEACKNSLKKLQLDYLDLYLVHYPLATKhsgvgttaslldeNKVLDidvtvsletTWHDMEKTVSLGLVRSIGL 160
Cdd:cd19131 77 QGYdsTLRAFDESLRKLGLDYVDLYLIHWPVPAQ-------------DKYVE---------TWKALIELKKEGRVKSIGV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 161 SNYELFLTRDCLSYAKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLGGATAnvkafgsispLEDPVLIGLAKKY 240
Cdd:cd19131 135 SNFTIEHLQRLIDETGVVPVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGGL----------LSDPVIGEIAEKH 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
7S5I_A 241 QKSVAQIALRWNIERGTPVIPKSSKVERLKENLEVLNFKLEKEDIELINTID 292
Cdd:cd19131 205 GKTPAQVVIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELDADDMQAIAGLD 256
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
4-292 |
1.21e-70 |
|
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: 219.97 E-value: 1.21e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 4 ITLNNGFEMPVIGLGLWRLEKEELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAeaiQSGlVKREELFITSKVWNSDH 83
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIR---RSG-VDRSDIFVTTKLWISDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 84 GH--VVEACKNSLKKLQLDYLDLYLVHYPLATkhsgvgttaslldenkvlDIDVTVSletTWHDMEKTVSLGLVRSIGLS 161
Cdd:cd19127 77 GYdkALRGFDASLRRLGLDYVDLYLLHWPVPN------------------DFDRTIQ---AYKALEKLLAEGRVRAIGVS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 162 NYELFLTRDCLSYAKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLGGATANVKAF--GSISPLEDPVLIGLAKK 239
Cdd:cd19127 136 NFTPEHLERLIDATTVVPAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGGVMRYGASGptGPGDVLQDPTITGLAEK 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
7S5I_A 240 YQKSVAQIALRWNIERGTPVIPKSSKVERLKENLEVLNFKLEKEDIELINTID 292
Cdd:cd19127 216 YGKTPAQIVLRWHLQNGVSAIPKSVHPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
1-291 |
5.19e-70 |
|
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: 218.55 E-value: 5.19e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 1 MSTITLNNGFEMPVIGLGLWRLEKEELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAEAIQSGlVKREELFITSKVWN 80
Cdd:cd19121 1 MTSFKLNTGASIPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAIAGG-VKREDLFVTTKLWS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 81 SDHGHVVEACKNSLKKLQLDYLDLYLVHYPLATKHSGVGTTASLLDENKvLDIDVTVSLETTWHDMEKTVSLGLVRSIGL 160
Cdd:cd19121 80 TYHRRVELCLDRSLKSLGLDYVDLYLVHWPVLLNPNGNHDLFPTLPDGS-RDLDWDWNHVDTWKQMEKVLKTGKTKAIGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 161 SNYELFLTRDCLSYAKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLGGATanvkafgsiSPL-EDPVLIGLAKK 239
Cdd:cd19121 159 SNYSIPYLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTG---------SPLiSDEPVVEIAKK 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
7S5I_A 240 YQKSVAQIALRWNIERGTPVIPKSSKVERLKENLEVLnfKLEKEDIELINTI 291
Cdd:cd19121 230 HNVGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEII--DLDDEDMNKLNDI 279
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
12-289 |
5.32e-70 |
|
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: 217.14 E-value: 5.32e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 12 MPVIGLGLWRLEKEELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAEAiqsgLVKREELFITSKVWNSDHGH--VVEA 89
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAES----GVPREDLFITTKVWRDHLRPedLKKS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 90 CKNSLKKLQLDYLDLYLVHYPlatkhsgvgttaslldenkvldiDVTVSLETTWHDMEKTVSLGLVRSIGLSNYELFLTR 169
Cdd:cd19073 77 VDRSLEKLGTDYVDLLLIHWP-----------------------NPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 170 DCLSYAKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLggatanvkAFGSIspLEDPVLIGLAKKYQKSVAQIAL 249
Cdd:cd19073 134 EALDISPLPIAVNQVEFHPFLYQAELLEYCRENDIVITAYSPL--------ARGEV--LRDPVIQEIAEKYDKTPAQVAL 203
|
250 260 270 280
....*....|....*....|....*....|....*....|
7S5I_A 250 RWNIERGTPVIPKSSKVERLKENLEVLNFKLEKEDIELIN 289
Cdd:cd19073 204 RWLVQKGIVVIPKASSEDHLKENLAIFDWELTSEDVAKID 243
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
9-296 |
3.66e-68 |
|
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: 214.97 E-value: 3.66e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 9 GFEMPVIGLGLWRLEKEELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAEAIQSGLVKREELFITSKVWNSDH--GHV 86
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHekGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 87 VEACKNSLKKLQLDYLDLYLVHYPLATKHsgvGTTASLLDEN-KVLDIDVTvsLETTWHDMEKTVSLGLVRSIGLSNY-- 163
Cdd:cd19107 81 KGACQKTLSDLKLDYLDLYLIHWPTGFKP---GKELFPLDESgNVIPSDTT--FLDTWEAMEELVDEGLVKAIGVSNFnh 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 164 ---ELFLTRDCLSYakiKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLGGATANVKAFGSISPLEDPVLIGLAKKY 240
Cdd:cd19107 156 lqiERILNKPGLKY---KPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPKIKEIAAKH 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
7S5I_A 241 QKSVAQIALRWNIERGTPVIPKSSKVERLKENLEVLNFKLEKEDIELINTIDKKFR 296
Cdd:cd19107 233 NKTTAQVLIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWR 288
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
3-296 |
9.17e-68 |
|
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: 213.63 E-value: 9.17e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 3 TITLNNGFEMPVIGLGLWRLE---KEELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAEAIQSGLVKREELFITSKVW 79
Cdd:cd19108 2 RVKLNDGHFIPVLGFGTYAPEevpKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 80 NSDHG-HVVEAC-KNSLKKLQLDYLDLYLVHYPLATKHsgvGTTASLLDENKVLDIDvTVSLETTWHDMEKTVSLGLVRS 157
Cdd:cd19108 82 CTFHRpELVRPAlEKSLKKLQLDYVDLYLIHFPVALKP---GEELFPKDENGKLIFD-TVDLCATWEAMEKCKDAGLAKS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 158 IGLSNY-----ELFLTRDCLSYakiKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLGgATANVKAFGSISP--LED 230
Cdd:cd19108 158 IGVSNFnrrqlEMILNKPGLKY---KPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALG-SQRDKEWVDQNSPvlLED 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
7S5I_A 231 PVLIGLAKKYQKSVAQIALRWNIERGTPVIPKSSKVERLKENLEVLNFKLEKEDIELINTIDKKFR 296
Cdd:cd19108 234 PVLCALAKKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLR 299
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
9-294 |
8.35e-67 |
|
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: 210.17 E-value: 8.35e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 9 GFEMPVIGLGL---WRLEK-----EELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAEAiqsgLVKREELFITSKVWN 80
Cdd:cd19120 1 GSKIPAIAFGTgtaWYKSGdddiqRDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALKES----GVPREDLFITTKVSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 81 SdHGHVVEACKNSLKKLQLDYLDLYLVHYPLATKhsgvgttaslldenkvldiDVTVSLETTWHDMEKTVSLGLVRSIGL 160
Cdd:cd19120 77 G-IKDPREALRKSLAKLGVDYVDLYLIHSPFFAK-------------------EGGPTLAEAWAELEALKDAGLVRSIGV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 161 SNYELFLTRDCLSYAKIKPQVSQFETHPYF--QRESLVRFCKKHGVVPMAHTPLggaTANVKAFGSisPLeDPVLIGLAK 238
Cdd:cd19120 137 SNFRIEDLEELLDTAKIKPAVNQIEFHPYLypQQPALLEYCREHGIVVSAYSPL---SPLTRDAGG--PL-DPVLEKIAE 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
7S5I_A 239 KYQKSVAQIALRWNIERGTPVIPKSSKVERLKENLEVLNFKLEKEDIELINTIDKK 294
Cdd:cd19120 211 KYGVTPAQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEIDKAGKQ 266
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
3-295 |
1.23e-66 |
|
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are founding members of aldo-keto reductase family 3 member A1 (AKR3A1) and A2 (AKR3A2), respectively. Gcy1p, also called galactose-inducible crystallin-like protein 1, is a glycerol dehydrogenase involved in glycerol catabolism under microaerobic conditions. It has mRNA binding activity. Ypr1p acts as a 2-methylbutyraldehyde reductase that displays high specific activity towards 2-methylbutyraldehyde, as well as other aldehydes such as hexanal.
Pssm-ID: 381343 [Multi-domain] Cd Length: 284 Bit Score: 210.05 E-value: 1.23e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 3 TITLNNGFEMPVIGLGLWRLEKEELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAEaiqSGlVKREELFITSKVWNSD 82
Cdd:cd19117 5 TFKLNTGAEIPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIKD---SG-VPREEIFITTKLWCTW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 83 HGHVVEACKNSLKKLQLDYLDLYLVHYPLATKHSGVgtTASLLDENKVLDIDVTVSLETTWHDMEKTVSLGLVRSIGLSN 162
Cdd:cd19117 81 HRRVEEALDQSLKKLGLDYVDLYLMHWPVPLDPDGN--DFLFKKDDGTKDHEPDWDFIKTWELMQKLPATGKVKAIGVSN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 163 YELFLTRDCLS--YAKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLGGATANVkafgsispLEDPVLIGLAKKY 240
Cdd:cd19117 159 FSIKNLEKLLAspSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTNAPL--------LKEPVIIKIAKKH 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
7S5I_A 241 QKSVAQIALRWNIERGTPVIPKSSKVERLKENLEVlnFKLEKEDIELINTIDKKF 295
Cdd:cd19117 231 GKTPAQVIISWGLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEIDELHKEY 283
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
4-297 |
2.03e-66 |
|
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: 208.91 E-value: 2.03e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 4 ITLNNGFEMPVIGLGLWRLEK-EELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAeaiQSGlVKREELFITSKVWNSD 82
Cdd:cd19156 1 VKLANGVEMPRLGLGVWRVQDgAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIR---ESG-VPREEVFVTTKLWNSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 83 HGH--VVEACKNSLKKLQLDYLDLYLVHYPLATKHsgvgttaslldenkvldIDvtvsletTWHDMEKTVSLGLVRSIGL 160
Cdd:cd19156 77 QGYesTLAAFEESLEKLGLDYVDLYLIHWPVKGKF-----------------KD-------TWKAFEKLYKEKKVRAIGV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 161 SNYELFLTRDCLSYAKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLGGatanvkafGSIspLEDPVLIGLAKKY 240
Cdd:cd19156 133 SNFHEHHLEELLKSCKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQ--------GKL--LSNPVLKAIGKKY 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
7S5I_A 241 QKSVAQIALRWNIERGTPVIPKSSKVERLKENLEVLNFKLEKEDIELINTIDKKFRT 297
Cdd:cd19156 203 GKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTDHRY 259
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
6-291 |
2.20e-66 |
|
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: 209.57 E-value: 2.20e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 6 LNNGFEMPVIGLGLWRLEKEELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAEAIQS-GLVKREELFITSKVWNSDHG 84
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEePGVKREDLFITSKLWNNSHR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 85 --HVVEACKNSLKKLQLDYLDLYLVHYPLATKHSG--VGTTASLLDENKVlDIDVTVSLETTWHDMEKTVSLGLVRSIGL 160
Cdd:cd19118 81 peYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTGdlNPLTAVPTNGGEV-DLDLSVSLVDTWKAMVELKKTGKVKSIGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 161 SNYELFLTRDCLSYAKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLGGATAnvkafGSISPLEDPVLIGLAKKY 240
Cdd:cd19118 160 SNFSIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGNNLA-----GLPLLVQHPEVKAIAAKL 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
7S5I_A 241 QKSVAQIALRWNIERGTPVIPKSSKVERLKENLEVlnFKLEKEDIELINTI 291
Cdd:cd19118 235 GKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFEQ--VELSDDEFNAVTAL 283
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
6-295 |
2.82e-66 |
|
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: 209.66 E-value: 2.82e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 6 LNNGFEMPVIGLGLW--RLEKEELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAEAIQSGLVKREELFITSKVWNSDH 83
Cdd:cd19119 6 LNTGASIPALGLGTAspHEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVWPTFY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 84 GHVVEACKNSLKKLQLDYLDLYLVHYPLATK--HSGVGTTASLLDENKVLDIDVTVSLETTWHDMEKTVSLGLVRSIGLS 161
Cdd:cd19119 86 DEVERSLDESLKALGLDYVDLLLVHWPVCFEkdSDDSGKPFTPVNDDGKTRYAASGDHITTYKQLEKIYLDGRAKAIGVS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 162 NYELFLTRDCLSYAKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLGGATANVkafgsispLEDPVLIGLAKKYQ 241
Cdd:cd19119 166 NYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAPN--------LKNPLVKKIAEKYN 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
7S5I_A 242 KSVAQIALRWNIERGTPVIPKSSKVERLKENLEVLNfkLEKEDIELINTIDKKF 295
Cdd:cd19119 238 VSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKIVS--LTKEDLQKLDDIGEKY 289
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
9-296 |
3.06e-65 |
|
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: 207.34 E-value: 3.06e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 9 GFEMPVIGLGLWRLEKEELRSAILNAIKL----GYRHFDAAAHYKTEIDVGNAIAEAIQSGLVKREELFITSKVWNSDHG 84
Cdd:cd19109 1 GNSIPIIGLGTYSEPKTTPKGACAEAVKVaidtGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 85 -HVVE-ACKNSLKKLQLDYLDLYLVHYPLATKHsgvGTTASLLDENKVLDIDVTvSLETTWHDMEKTVSLGLVRSIGLSN 162
Cdd:cd19109 81 pELVRpTLERTLKVLQLDYVDLYIIEMPMAFKP---GDEIYPRDENGKWLYHKT-NLCATWEALEACKDAGLVKSIGVSN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 163 Y-----ELFLTRDCLSYakiKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLGGATANVKAFGSISPL-EDPVLIGL 236
Cdd:cd19109 157 FnrrqlELILNKPGLKH---KPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDPIWVNVSSPPLlEDPLLNSI 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 237 AKKYQKSVAQIALRWNIERGTPVIPKSSKVERLKENLEVLNFKLEKEDIELINTIDKKFR 296
Cdd:cd19109 234 GKKYNKTAAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVR 293
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
11-296 |
9.07e-65 |
|
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: 205.96 E-value: 9.07e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 11 EMPVIGLGLWRLEKEELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAEAIQSGLVKREELFITSKVWNSDHGH--VVE 88
Cdd:cd19110 3 DIPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKslVKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 89 ACKNSLKKLQLDYLDLYLVHYPLATKHsgvGTTASLLDENKVLdIDVTVSLETTWHDMEKTVSLGLVRSIGLSNY----- 163
Cdd:cd19110 83 ACTRSLKALKLNYLDLYLIHWPMGFKP---GEPDLPLDRSGMV-IPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFnheql 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 164 ELFLTRDCLsyaKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLGGATanvkafGSISPLEDPVLIGLAKKYQKS 243
Cdd:cd19110 159 ERLLNKPGL---RVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSC------EGVDLIDDPVIQRIAKKHGKS 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
7S5I_A 244 VAQIALRWNIERGTPVIPKSSKVERLKENLEVLNFKLEKEDIELINTIDKKFR 296
Cdd:cd19110 230 PAQILIRFQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLR 282
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
7-293 |
1.74e-62 |
|
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: 199.99 E-value: 1.74e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 7 NNGFEMPVIGLGLWRLEKEELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAEAIQSGLVKREELFITSKVWNSDH--G 84
Cdd:cd19129 1 NGSGAIPALGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNHrpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 85 HVVEACKNSLKKLQLDYLDLYLVHYPLATKHsgvGTTASLLDENKVLDIDVTVSLETTWHDMEKTVSLGLVRSIGLSNYE 164
Cdd:cd19129 81 RVKPAFEASLKRLQLDYLDLYLIHTPFAFQP---GDEQDPRDANGNVIYDDGVTLLDTWRAMERLVDEGRCKAIGLSDVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 165 LFLTRDCLSYAKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLGGATanvkafgSISPLEDPVLIGLAKKYQKSV 244
Cdd:cd19129 158 LEKLREIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGM-------EPKLLEDPVITAIARRVNKTP 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
7S5I_A 245 AQIALRWNIERGTPVIPKSSKVERLKENLEVLnfKLEKEDIELINTIDK 293
Cdd:cd19129 231 AQVLLAWAIQRGTALLTTSKTPSRIRENFDIS--TLPEDAMREINEGIK 277
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
6-292 |
4.26e-62 |
|
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: 197.49 E-value: 4.26e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 6 LNNGFEMPVIGLGLWRLEKEELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAeaiQSGlVKREELFITSKVWNSDHGH 85
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVR---RSG-VPREELFVTTKLPGRHHGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 86 --VVEACKNSLKKLQLDYLDLYLVHYPLATKhsgvgttaslldeNKVLDidvtvsletTWHDMEKTVSLGLVRSIGLSNY 163
Cdd:cd19132 77 eeALRTIEESLYRLGLDYVDLYLIHWPNPSR-------------DLYVE---------AWQALIEAREEGLVRSIGVSNF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 164 ELFLTRDCLSYAKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLGGATANvkafgsispLEDPVLIGLAKKYQKS 243
Cdd:cd19132 135 LPEHLDRLIDETGVTPAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLGRGSGL---------LDEPVIKAIAEKHGKT 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
7S5I_A 244 VAQIALRWNIERGTPVIPKSSKVERLKENLEVLNFKLEKEDIELINTID 292
Cdd:cd19132 206 PAQVVLRWHVQLGVVPIPKSANPERQRENLAIFDFELSDEDMAAIAALD 254
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
4-296 |
7.73e-61 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 194.91 E-value: 7.73e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 4 ITLNNGFEMPVIGLGLWRLEKEELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAEAIqsglVKREELFITSKVWNSDH 83
Cdd:PRK11565 7 IKLQDGNVMPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKEAS----VAREELFITTKLWNDDH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 84 GHVVEACKNSLKKLQLDYLDLYLVHYPLATKHSGVGttaslldenkvldidvtvsletTWHDMEKTVSLGLVRSIGLSNY 163
Cdd:PRK11565 83 KRPREALEESLKKLQLDYVDLYLMHWPVPAIDHYVE----------------------AWKGMIELQKEGLIKSIGVCNF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 164 ELFLTRDCLSYAKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLGGATANVkafgsispLEDPVLIGLAKKYQKS 243
Cdd:PRK11565 141 QIHHLQRLIDETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGKGV--------FDQKVIRDLADKYGKT 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
7S5I_A 244 VAQIALRWNIERGTPVIPKSSKVERLKENLEVLNFKLEKEDIELINTIDKKFR 296
Cdd:PRK11565 213 PAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRLDKDELGEIAKLDQGKR 265
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
3-296 |
4.13e-60 |
|
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: 192.76 E-value: 4.13e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 3 TITLNNGFEMPVIGLGLWRLEKEELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAeaiQSGlVKREELFITSKVWNSD 82
Cdd:cd19134 2 TVTLNDDNTMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIA---ASG-IPRGELFVTTKLATPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 83 HGHV--VEACKNSLKKLQLDYLDLYLVHYPLAtkhsgvgttasllDENKVLDidvtvsletTWHDMEKTVSLGLVRSIGL 160
Cdd:cd19134 78 QGFTasQAACRASLERLGLDYVDLYLIHWPAG-------------REGKYVD---------SWGGLMKLREEGLARSIGV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 161 SNYELFLTRDCLSYAKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLGGATAnvkafgsispLEDPVLIGLAKKY 240
Cdd:cd19134 136 SNFTAEHLENLIDLTFFTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGRL----------LDNPAVTAIAAAH 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
7S5I_A 241 QKSVAQIALRWNIERGTPVIPKSSKVERLKENLEVLNFKLEKEDIELINTIDKKFR 296
Cdd:cd19134 206 GRTPAQVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDALDGLDDGTR 261
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
8-289 |
1.71e-59 |
|
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: 190.55 E-value: 1.71e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 8 NGFEMPVIGLGLWRLEKEELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAEaiqSGlVKREELFITSKVWNSD--HGH 85
Cdd:cd19140 4 NGVRIPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIAA---SG-VPRDELFLTTKVWPDNysPDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 86 VVEACKNSLKKLQLDYLDLYLVHYPlatkhsgvgttaslldeNKvldidvTVSLETTWHDMEKTVSLGLVRSIGLSNYEL 165
Cdd:cd19140 80 FLASVEESLRKLRTDYVDLLLLHWP-----------------NK------DVPLAETLGALNEAQEAGLARHIGVSNFTV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 166 FLTRDCLSYAKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLggatanvkAFGSIspLEDPVLIGLAKKYQKSVA 245
Cdd:cd19140 137 ALLREAVELSEAPLFTNQVEYHPYLDQRKLLDAAREHGIALTAYSPL--------ARGEV--LKDPVLQEIGRKHGKTPA 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
7S5I_A 246 QIALRWNIER-GTPVIPKSSKVERLKENLEVLNFKLEKEDIELIN 289
Cdd:cd19140 207 QVALRWLLQQeGVAAIPKATNPERLEENLDIFDFTLSDEEMARIA 251
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
5-293 |
1.78e-58 |
|
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis.
Pssm-ID: 381348 [Multi-domain] Cd Length: 291 Bit Score: 189.37 E-value: 1.78e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 5 TLNNGFEMPVIGLGLWRLE--KEELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAEAI-QSGLVKREELFITSKVWNS 81
Cdd:cd19122 2 TLNNGVKIPAVGFGTFANEgaKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLkENPSVKREDLFICTKVWNH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 82 DHGH--VVEACKNSLKKLQLDYLDLYLVHYPLATKHSGVGTTASLLDENKVLDIDVTVSLETTWHDMEKTVSLGLVRSIG 159
Cdd:cd19122 82 LHEPedVKWSIDNSLKNLKLDYIDLFLVHWPIAAEKNDQRSPKLGPDGKYVILKDLTENPEPTWRAMEEIYESGKAKAIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 160 LSNYELFLTRDCLSYAKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLGGATANVKAFGSISplEDPVLIGLAKK 239
Cdd:cd19122 162 VSNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQVPSTGERVS--ENPTLNEVAEK 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
7S5I_A 240 YQKSVAQIALRWNIERGTPVIPKSSKVERLKENLEVLnfKLEKEDIELINTIDK 293
Cdd:cd19122 240 GGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSI--ELSDEDFEAINQVAK 291
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
12-288 |
4.12e-57 |
|
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: 184.48 E-value: 4.12e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 12 MPVIGLGLWRLEKEELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAeaiQSGlVKREELFITSKVW--NSDHGHVVEA 89
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIA---ESG-VPRDELFITTKIWidNLSKDKLLPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 90 CKNSLKKLQLDYLDLYLVHYPlatkhsgvgttaslldenkvlDIDVTVSLETTWHDMEKTVSLGLVRSIGLSNYELFLTR 169
Cdd:cd19139 77 LEESLEKLRTDYVDLTLIHWP---------------------SPNDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 170 DCLS-YAKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLggatanvkAFGSIspLEDPVLIGLAKKYQKSVAQIA 248
Cdd:cd19139 136 EAIAvVGAGAIATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTL--------AYGKV--LDDPVLAAIAERHGATPAQIA 205
|
250 260 270 280
....*....|....*....|....*....|....*....|
7S5I_A 249 LRWNIERGTPVIPKSSKVERLKENLEVLNFKLEKEDIELI 288
Cdd:cd19139 206 LAWAMARGYAVIPSSTKREHLRSNLLALDLTLDADDMAAI 245
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
4-292 |
7.79e-51 |
|
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: 168.55 E-value: 7.79e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 4 ITLNNGFEMPVIGLGLWRLEKEELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAeaiQSGLvKREELFITSKVWNSDH 83
Cdd:cd19130 2 IVLNDGNSIPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIA---ASGI-PRDELFVTTKLWNDRH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 84 GH--VVEACKNSLKKLQLDYLDLYLVHYPLATKHSGVgttaslldenkvldidvtvsleTTWHDMEKTVSLGLVRSIGLS 161
Cdd:cd19130 78 DGdePAAAFAESLAKLGLDQVDLYLVHWPTPAAGNYV----------------------HTWEAMIELRAAGRTRSIGVS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 162 NYELFLTRDCLSYAKIKPQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLGGatanvkafGSIspLEDPVLIGLAKKYQ 241
Cdd:cd19130 136 NFLPPHLERIVAATGVVPAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQ--------GKL--LGDPPVGAIAAAHG 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
7S5I_A 242 KSVAQIALRWNIERGTPVIPKSSKVERLKENLEVLNFKLEKEDIELINTID 292
Cdd:cd19130 206 KTPAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAIDALD 256
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
12-300 |
3.33e-50 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 167.12 E-value: 3.33e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 12 MPVIGLGLWRLEKEELRSAILNAIKLGYRHFDAAAHYKTEIDVGNAIAEaiqSGlVKREELFITSKVW--NSDHGHVVEA 89
Cdd:PRK11172 3 IPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAE---SG-VPRDELFITTKIWidNLAKDKLIPS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 90 CKNSLKKLQLDYLDLYLVHYPLATKHSGVGTTASLLDENKvldidvtvslettwhdmektvSLGLVRSIGLSNYELFLTR 169
Cdd:PRK11172 79 LKESLQKLRTDYVDLTLIHWPSPNDEVSVEEFMQALLEAK---------------------KQGLTREIGISNFTIALMK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 170 ---DCLSYAKIKPQvsQFETHPYFQRESLVRFCKKHGVVPMAHTPLggatanvkAFGSIspLEDPVLIGLAKKYQKSVAQ 246
Cdd:PRK11172 138 qaiAAVGAENIATN--QIELSPYLQNRKVVAFAKEHGIHVTSYMTL--------AYGKV--LKDPVIARIAAKHNATPAQ 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
7S5I_A 247 IALRWNIERGTPVIPKSSKVERLKENLEVLNFKLEKEDIELINTIDKKFRTTLP 300
Cdd:PRK11172 206 VILAWAMQLGYSVIPSSTKRENLASNLLAQDLQLDAEDMAAIAALDRNGRLVSP 259
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
9-289 |
4.29e-47 |
|
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: 158.93 E-value: 4.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 9 GFEMPVIGLGLWRL---------EKEELRSAILNAIKLGYRHFDAAAHYK---TEIDVGNAIAEaiqsglVKREELFITS 76
Cdd:cd19072 1 GEEVPVLGLGTWGIgggmskdysDDKKAIEALRYAIELGINLIDTAEMYGgghAEELVGKAIKG------FDREDLFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 77 KVWnSDHGH---VVEACKNSLKKLQLDYLDLYLVHYPlatkhsgvgttaslldenkvldiDVTVSLETTWHDMEKTVSLG 153
Cdd:cd19072 75 KVS-PDHLKyddVIKAAKESLKRLGTDYIDLYLIHWP-----------------------NPSIPIEETLRAMEELVEEG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 154 LVRSIGLSNYELFLTRDCLSYAKIKPQVS-QFETHPYFQRE--SLVRFCKKHGVVPMAHTPLGGATANVKAfgsisplED 230
Cdd:cd19072 131 KIRYIGVSNFSLEELEEAQSYLKKGPIVAnQVEYNLFDREEesGLLPYCQKNGIAIIAYSPLEKGKLSNAK-------GS 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 231 PVLIGLAKKYQKSVAQIALRWNIER-GTPVIPKSSKVERLKENLEVLNFKLEKEDIELIN 289
Cdd:cd19072 204 PLLDEIAKKYGKTPAQIALNWLISKpNVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
15-292 |
2.75e-42 |
|
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: 147.46 E-value: 2.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 15 IGLGLWRLE-------KEELRSAILNAIKLGYRHFDAAAHYKTEIdVGNAIAEAIQSGLVKREELFITSKVWNSDHGH-- 85
Cdd:pfam00248 1 IGLGTWQLGggwgpisKEEALEALRAALEAGINFIDTAEVYGDGK-SEELLGEALKDYPVKRDKVVIATKVPDGDGPWps 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 86 ------VVEACKNSLKKLQLDYLDLYLVHYPlatkhsgvgttaslldenkvldiDVTVSLETTWHDMEKTVSLGLVRSIG 159
Cdd:pfam00248 80 ggskenIRKSLEESLKRLGTDYIDLYYLHWP-----------------------DPDTPIEETWDALEELKKEGKIRAIG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 160 LSNYELFLTRDCLSYAKIKPQVSQFETHPYFQRES--LVRFCKKHGVVPMAHTPLGG---ATANVKAFGSISPLEDPVLI 234
Cdd:pfam00248 137 VSNFDAEQIEKALTKGKIPIVAVQVEYNLLRRRQEeeLLEYCKKNGIPLIAYSPLGGgllTGKYTRDPDKGPGERRRLLK 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
7S5I_A 235 G--------------LAKKYQKSVAQIALRW--NIERGTPVIPKSSKVERLKENLEVLNFKLEKEDIELINTID 292
Cdd:pfam00248 217 KgtplnlealealeeIAKEHGVSPAQVALRWalSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
3-289 |
7.47e-39 |
|
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: 137.77 E-value: 7.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 3 TITLNNGFEMPVIGLGLWRLE-----KEELRSAILNAIKLGYRHFDAAAHY---KTEIDVGNAIAEaiqsglvKREELFI 74
Cdd:cd19138 2 TVTLPDGTKVPALGQGTWYMGedpakRAQEIEALRAGIDLGMTLIDTAEMYgdgGSEELVGEAIRG-------RRDKVFL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 75 TSKV--WNSDHGHVVEACKNSLKKlqldyldlylvhypLATKHsgvgttaslldenkvldIDV-------TVSLETTWHD 145
Cdd:cd19138 75 VSKVlpSNASRQGTVRACERSLRR--------------LGTDY-----------------LDLyllhwrgGVPLAETVAA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 146 MEKTVSLGLVRSIGLSNYELFLTRDCLSYAKIKP-QVSQFETHpYFQRE---SLVRFCKKHGVVPMAHTPLGGAtanvkA 221
Cdd:cd19138 124 MEELKKEGKIRAWGVSNFDTDDMEELWAVPGGGNcAANQVLYN-LGSRGieyDLLPWCREHGVPVMAYSPLAQG-----G 197
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
7S5I_A 222 FGSISPLEDPVLIGLAKKYQKSVAQIALRWNIERG-TPVIPKSSKVERLKENLEVLNFKLEKEDIELIN 289
Cdd:cd19138 198 LLRRGLLENPTLKEIAARHGATPAQVALAWVLRDGnVIAIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
9-289 |
2.85e-37 |
|
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: 133.46 E-value: 2.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 9 GFEMPVIGLGLWRL---------EKEELRSAILNAIKLGYRHFDAAAHY---KTEIDVGNAIAEaiqsglVKREELFITS 76
Cdd:cd19137 1 GEKIPALGLGTWGIggfltpdysRDEEMVELLKTAIELGYTHIDTAEMYgggHTEELVGKAIKD------FPREDLFIVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 77 KVW--NSDHGHVVEACKNSLKKLQLDYLDLYLVHYPlatkhsgvgttaslldeNKvldidvTVSLETTWHDMEKTVSLGL 154
Cdd:cd19137 75 KVWptNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWP-----------------NP------NIPLEETLSAMAEGVRQGL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 155 VRSIGLSNYELFLTRDCLSYAKIKPQVSQFETHPY---FQRESLVRFCKKHGVVPMAHTPLGGatanvkafgSISPLEDp 231
Cdd:cd19137 132 IRYIGVSNFNRRLLEEAISKSQTPIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPLRR---------GLEKTNR- 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
7S5I_A 232 VLIGLAKKYQKSVAQIALRWNIERGTPV-IPKSSKVERLKENLEVLNFKLEKEDIELIN 289
Cdd:cd19137 202 TLEEIAKNYGKTIAQIALAWLIQKPNVVaIPKAGRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
11-289 |
8.43e-34 |
|
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: 125.03 E-value: 8.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 11 EMPVIGLGLW-----------RLEKEELRSAILNAIKLGYRHFDAAAHYKTeidvGNA---IAEAIQsGLVKREELFITS 76
Cdd:cd19093 1 EVSPLGLGTWqwgdrlwwgygEYGDEDLQAAFDAALEAGVNLFDTAEVYGT----GRSerlLGRFLK-ELGDRDEVVIAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 77 KV----WNSDHGHVVEACKNSLKKLQLDYLDLYLVHYPlaTKHSGvgttaslldenkvldidvtvSLETTWHDMEKTVSL 152
Cdd:cd19093 76 KFaplpWRLTRRSVVKALKASLERLGLDSIDLYQLHWP--GPWYS--------------------QIEALMDGLADAVEE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 153 GLVRSIGLSNYELFLTRDCLSYAK---IKPQVSQFE---THPYFQRESLVRFCKKHGVVPMAHTPLG------------- 213
Cdd:cd19093 134 GLVRAVGVSNYSADQLRRAHKALKergVPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAqglltgkyspenp 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 214 -----GATANVKAFGSISPLEDpVLIGLAKKYQKSVAQIALRWNIERGTPVIPKSSKVERLKENLEVLNFKLEKEDIELI 288
Cdd:cd19093 214 ppggrRRLFGRKNLEKVQPLLD-ALEEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAEL 292
|
.
7S5I_A 289 N 289
Cdd:cd19093 293 D 293
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
9-289 |
3.71e-28 |
|
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: 110.31 E-value: 3.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 9 GFEMPVIGLGLW--------RLEKEELRSAILNAIKLGYRHFDAAAHY---KTEIDVGNAIAEaiqsglvKREELFITSK 77
Cdd:cd19084 1 DLKVSRIGLGTWaiggtwwgEVDDQESIEAIKAAIDLGINFFDTAPVYgfgHSEEILGKALKG-------RRDDVVIATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 78 V---WNSDHG--------HVVEACKNSLKKLQLDYLDLYLVHYPlatkhsgvgttaslldenkvldiDVTVSLETTWHDM 146
Cdd:cd19084 74 CglrWDGGKGvtkdlspeSIRKEVEQSLRRLQTDYIDLYQIHWP-----------------------DPNTPIEETAEAL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 147 EKTVSLGLVRSIGLSNYELFLTRDCLSYAKI---KPQVSQFETHPyfqRESLVRFCKKHGVVPMAHTPLGGA--TANVKA 221
Cdd:cd19084 131 EKLKKEGKIRYIGVSNFSVEQLEEARKYGPIvslQPPYSMLEREI---EEELLPYCRENGIGVLPYGPLAQGllTGKYKK 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 222 FGSISP----LEDPVLIG---------------LAKKYQKSVAQIALRWNIER--GTPVIPKSSKVERLKENLEVLNFKL 280
Cdd:cd19084 208 EPTFPPddrrSRFPFFRGenfeknleivdklkeIAEKYGKSLAQLAIAWTLAQpgVTSAIVGAKNPEQLEENAGALDWEL 287
|
....*....
7S5I_A 281 EKEDIELIN 289
Cdd:cd19084 288 TEEELKEID 296
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-291 |
3.61e-25 |
|
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: 102.56 E-value: 3.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 1 MSTITL-NNGFEMPVIGLGLWRL-------EKEELRSAILNAIKLGYRHFDAAAHY---KTEIDVGNAIAEaiqsglVKR 69
Cdd:COG0667 1 MEYRRLgRSGLKVSRLGLGTMTFggpwggvDEAEAIAILDAALDAGINFFDTADVYgpgRSEELLGEALKG------RPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 70 EELFITSKV----------WNSDHGHVVEACKNSLKKLQLDYLDLYLVHYPlatkhsgvgttaslldenkvldiDVTVSL 139
Cdd:COG0667 75 DDVVIATKVgrrmgpgpngRGLSREHIRRAVEASLRRLGTDYIDLYQLHRP-----------------------DPDTPI 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 140 ETTWHDMEKTVSLGLVRSIGLSNYELFLTRDCLSYAKIKPQVS--QFEthpY--FQRES---LVRFCKKHGVVPMAHTPL 212
Cdd:COG0667 132 EETLGALDELVREGKIRYIGVSNYSAEQLRRALAIAEGLPPIVavQNE---YslLDRSAeeeLLPAARELGVGVLAYSPL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 213 GG-------------ATANVKAFGSISPLEDP-------VLIGLAKKYQKSVAQIALRWNIERG--TPVIPKSSKVERLK 270
Cdd:COG0667 209 AGglltgkyrrgatfPEGDRAATNFVQGYLTErnlalvdALRAIAAEHGVTPAQLALAWLLAQPgvTSVIPGARSPEQLE 288
|
330 340
....*....|....*....|.
7S5I_A 271 ENLEVLNFKLEKEDIELINTI 291
Cdd:COG0667 289 ENLAAADLELSAEDLAALDAA 309
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
13-295 |
1.10e-22 |
|
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: 95.35 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 13 PVIGLGLWRL---------EKEELRSAILNAIKLGYRHFDAAAHY---KTEIDVGNAIAEaiqsglvKREELFITSKVW- 79
Cdd:cd19085 2 SRLGLGCWQFgggywwgdqDDEESIATIHAALDAGINFFDTAEAYgdgHSEEVLGKALKG-------RRDDVVIATKVSp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 80 -NSDHGHVVEACKNSLKKLQLDYLDLYLVHYPLAtkhsgvgttaslldenkvlDIDVTVSLETtwhdMEKTVSLGLVRSI 158
Cdd:cd19085 75 dNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSS-------------------DVPLEETMEA----LEKLKEEGKIRAI 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 159 GLSNYELFLTRDCLSYAKIkpQVSQFethPY--FQRE---SLVRFCKKHGVVPMAHTP-----LGGATANV--------- 219
Cdd:cd19085 132 GVSNFGPAQLEEALDAGRI--DSNQL---PYnlLWRAieyEILPFCREHGIGVLAYSPlaqglLTGKFSSAedfppgdar 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 220 -------------KAFGSISPLEDpvligLAKKYQKSVAQIALRWNIERG--TPVIPKSSKVERLKENLEVLNFKLEKED 284
Cdd:cd19085 207 trlfrhfepgaeeETFEALEKLKE-----IADELGVTMAQLALAWVLQQPgvTSVIVGARNPEQLEENAAAVDLELSPSV 281
|
330
....*....|.
7S5I_A 285 IELINTIDKKF 295
Cdd:cd19085 282 LERLDEISDPL 292
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
13-274 |
1.81e-19 |
|
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: 85.26 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 13 PVIGLGLWRL----EKEELRSAILNAIKLGYRHFDAAAHY---KTEIDVGNAIAEaiqsgLVKREELFITSKV------- 78
Cdd:cd06660 1 SRLGLGTMTFggdgDEEEAFALLDAALEAGGNFFDTADVYgdgRSERLLGRWLKG-----RGNRDDVVIATKGghppggd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 79 ---WNSDHGHVVEACKNSLKKLQLDYLDLYLVHYPlatkhsgvgttaslldenkvldiDVTVSLETTWHDMEKTVSLGLV 155
Cdd:cd06660 76 psrSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRD-----------------------DPSTPVEETLEALNELVREGKI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 156 RSIGLSNYELFLTRDCLSYAK----IKPQVSQFE---THPYFQRESLVRFCKKHGVVPMAHTPLGGatanvkafgsispl 228
Cdd:cd06660 133 RYIGVSNWSAERLAEALAYAKahglPGFAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPLAR-------------- 198
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
7S5I_A 229 edpvliGLakkyqksvAQIALRW--NIERGTPVIPKSSKVERLKENLE 274
Cdd:cd06660 199 ------GP--------AQLALAWllSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
7-284 |
4.16e-19 |
|
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: 85.30 E-value: 4.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 7 NNGFEMPVIGLGLWRL-----EKEELRSAILNAIKLGYRHFDAA---AHYKTEIDVGNAIAEaiQSGLvkREELFITSKV 78
Cdd:cd19092 1 PEGLEVSRLVLGCMRLadwgeSAEELLSLIEAALELGITTFDHAdiyGGGKCEELFGEALAL--NPGL--REKIEIQTKC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 79 ---------------WNSDHGHVVEACKNSLKKlqldyldlylvhypLATKHsgvgttaslldenkvLDI------DVTV 137
Cdd:cd19092 77 girlgddprpgrikhYDTSKEHILASVEGSLKR--------------LGTDY---------------LDLlllhrpDPLM 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 138 SLETTWHDMEKTVSLGLVRSIGLSNY-----ELfLTrdclSYAKIKPQVSQFE---THPYFQRESLVRFCKKHGVVPMAH 209
Cdd:cd19092 128 DPEEVAEAFDELVKSGKVRYFGVSNFtpsqiEL-LQ----SYLDQPLVTNQIElslLHTEAIDDGTLDYCQLLDITPMAW 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 210 TPLGGAtanvKAFGSISPLEDPV---LIGLAKKYQKSVAQIALRWNIERGTPVIP--KSSKVERLKENLEVLNFKLEKED 284
Cdd:cd19092 203 SPLGGG----RLFGGFDERFQRLraaLEELAEEYGVTIEAIALAWLLRHPARIQPilGTTNPERIRSAVKALDIELTREE 278
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
14-283 |
2.22e-15 |
|
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: 74.94 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 14 VIGLGLW-----RLEKEELRSAILNAIKLGYRHFDAAAHY---KTEIDVGNAIAEaiqsglVKREELFITSKV------W 79
Cdd:cd19074 6 ELSLGTWltfggQVDDEDAKACVRKAYDLGINFFDTADVYaagQAEEVLGKALKG------WPRESYVISTKVfwptgpG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 80 NSDHG----HVVEACKNSLKKLQldyldlylvhyplaTKHsgvgttaslldenkvLDI------DVTVSLETTWHDMEKT 149
Cdd:cd19074 80 PNDRGlsrkHIFESIHASLKRLQ--------------LDY---------------VDIyychryDPETPLEETVRAMDDL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 150 VSLGLVRSIGLSNYELFLTRDCLSYAK----IKPQVSQFETHpYFQRES---LVRFCKKHGVVPMAHTPLG-----GATA 217
Cdd:cd19074 131 IRQGKILYWGTSEWSAEQIAEAHDLARqfglIPPVVEQPQYN-MLWREIeeeVIPLCEKNGIGLVVWSPLAqglltGKYR 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 218 NVKAFGSISPLEDPV-------------------LIGLAKKYQKSVAQIALRWNIER--GTPVIPKSSKVERLKENLEVL 276
Cdd:cd19074 210 DGIPPPSRSRATDEDnrdkkrrlltdenlekvkkLKPIADELGLTLAQLALAWCLRNpaVSSAIIGASRPEQLEENVKAS 289
|
....*..
7S5I_A 277 NFKLEKE 283
Cdd:cd19074 290 GVKLSPE 296
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
15-291 |
4.92e-15 |
|
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: 73.88 E-value: 4.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 15 IGLGLWRL--------EKEELRSAILNAIKLGYRHFDAAAHY---KTEIDVGNAIAEaiqsgLVKREELFITSKV---WN 80
Cdd:cd19148 7 IALGTWAIggwmwggtDEKEAIETIHKALDLGINLIDTAPVYgfgLSEEIVGKALKE-----YGKRDRVVIATKVgleWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 81 SDHGHVVEACK--------NSLKKLQLDYLDLYLVHYPlatkhsgvgttaslldenkvldiDVTVSLETTWHDMEKTVSL 152
Cdd:cd19148 82 EGGEVVRNSSParirkeveDSLRRLQTDYIDLYQVHWP-----------------------DPLVPIEETAEALKELLDE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 153 GLVRSIGLSNY-----ELFltRDCLSYAKIKPqvsqfethPY--FQRE---SLVRFCKKHGVVPMAHTPL------GGAT 216
Cdd:cd19148 139 GKIRAIGVSNFspeqmETF--RKVAPLHTVQP--------PYnlFEREiekDVLPYARKHNIVTLAYGALcrgllsGKMT 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 217 ANVKAFGSISPLEDPV---------------LIGLAKK-YQKSVAQIALRWNIERGTPVIP--KSSKVERLKENLEVLNF 278
Cdd:cd19148 209 KDTKFEGDDLRRTDPKfqeprfsqylaaveeLDKLAQErYGKSVIHLAVRWLLDQPGVSIAlwGARKPEQLDAVDEVFGW 288
|
330
....*....|...
7S5I_A 279 KLEKEDIELINTI 291
Cdd:cd19148 289 SLNDEDMKEIDAI 301
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
1-291 |
5.01e-14 |
|
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: 71.11 E-value: 5.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 1 MSTITL-NNGFEMPVIGLG-------------LWRLEKEELRSAILNAIKLGYRHFDAAAHY---KTEIDVGNAIAEaiq 63
Cdd:cd19091 1 MEYRTLgRSGLKVSELALGtmtfgggggffgaWGGVDQEEADRLVDIALDAGINFFDTADVYsegESEEILGKALKG--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 64 sglvKREELFITSKVWN----------SDHGHVVEACKNSLKKlqldyldlylvhypLATKHsgvgttaslLDENKVLDI 133
Cdd:cd19091 78 ----RRDDVLIATKVRGrmgegpndvgLSRHHIIRAVEASLKR--------------LGTDY---------IDLYQLHGF 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 134 DVTVSLETTWHDMEKTVSLGLVRSIGLSNYELFLTRDCLSYAKiKPQVSQFETHP--Y------FQREsLVRFCKKHGVV 205
Cdd:cd19091 131 DALTPLEETLRALDDLVRQGKVRYIGVSNFSAWQIMKALGISE-RRGLARFVALQayYsllgrdLEHE-LMPLALDQGVG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 206 PMAHTPLGG--------------ATANVKAFGSISPLEDP--------VLIGLAKKYQKSVAQIALRWNIER--GTPVIP 261
Cdd:cd19091 209 LLVWSPLAGgllsgkyrrgqpapEGSRLRRTGFDFPPVDRergydvvdALREIAKETGATPAQVALAWLLSRptVSSVII 288
|
330 340 350
....*....|....*....|....*....|
7S5I_A 262 KSSKVERLKENLEVLNFKLEKEDIELINTI 291
Cdd:cd19091 289 GARNEEQLEDNLGAAGLSLTPEEIARLDKV 318
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
7-300 |
1.76e-13 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 70.23 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 7 NNGFEMPVIGLGLWRL---EKEELRSAILNAIKLGYRHFDAAAHY-KTEIDVGNAIAEAiqsglvkREELFITSK--VWN 80
Cdd:COG1453 8 KTGLEVSVLGFGGMRLprkDEEEAEALIRRAIDNGINYIDTARGYgDSEEFLGKALKGP-------RDKVILATKlpPWV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 81 SDHGHVVEACKNSLKKLQLDYLDLYLVHyplatkhsGVGTTASL---LDENKVLDIdvtvslettwhdMEKTVSLGLVRS 157
Cdd:COG1453 81 RDPEDMRKDLEESLKRLQTDYIDLYLIH--------GLNTEEDLekvLKPGGALEA------------LEKAKAEGKIRH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 158 IGLS---NYELFLT---RDCLSYAKIkpQVSQFETHpYFQRESLVRFCKKH--GVVPMahTPLGGatanvkafGSISPLE 229
Cdd:COG1453 141 IGFSthgSLEVIKEaidTGDFDFVQL--QYNYLDQD-NQAGEEALEAAAEKgiGVIIM--KPLKG--------GRLANPP 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
7S5I_A 230 DPVLIGLAKKYqkSVAQIALR--WNIERGTPVIPKSSKVERLKENLEVLN--FKLEKEDIELINTIDKKFRTTLP 300
Cdd:COG1453 208 EKLVELLCPPL--SPAEWALRflLSHPEVTTVLSGMSTPEQLDENLKTADnlEPLTEEELAILERLAEELGELLK 280
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
7-288 |
7.09e-13 |
|
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: 68.07 E-value: 7.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 7 NNGFEMPVIGLGLW---------RLEKEELRSAILNAIKLGYRHFDAAAHY---KTEIDVGNAIAEaiqsglvKREELFI 74
Cdd:cd19149 6 KSGIEASVIGLGTWaigggpwwgGSDDNESIRTIHAALDLGINLIDTAPAYgfgHSEEIVGKAIKG-------RRDKVVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 75 TSK---VWNSDHGH------------------VVEACKNSLKKLQLDYLDLYLVHYPlatkhsgvgttaslldenkvldi 133
Cdd:cd19149 79 ATKcglRWDREGGSfffvrdgvtvyknlspesIREEVEQSLKRLGTDYIDLYQTHWQ----------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 134 DVTVSLETTWHDMEKTVSLGLVRSIGLSNYElflTRDCLSYAK------IKPQVSQFEThpyFQRESLVRFCKKHGVVPM 207
Cdd:cd19149 136 DVETPIEETMEALEELKRQGKIRAIGASNVS---VEQIKEYVKagqldiIQEKYSMLDR---GIEKELLPYCKKNNIAFQ 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 208 AHTPL-----------------GGATANVKAFgSISPLE-----DPVLIGLAKKYQKSVAQIALRWNIERG--TPVIPKS 263
Cdd:cd19149 210 AYSPLeqglltgkitpdrefdaGDARSGIPWF-SPENREkvlalLEKWKPLCEKYGCTLAQLVIAWTLAQPgiTSALCGA 288
|
330 340
....*....|....*....|....*
7S5I_A 264 SKVERLKENLEVLNFKLEKEDIELI 288
Cdd:cd19149 289 RKPEQAEENAKAGDIRLSAEDIATM 313
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
7-289 |
1.51e-12 |
|
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: 66.84 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 7 NNGFEMPVIGLGL----------WRLEKEELRSAILNAIKLGYRHFDAAAHYKT----EIdVGNAIAEaiqsgLVKREEL 72
Cdd:cd19079 7 NSGLKVSRLCLGCmsfgdpkwrpWVLDEEESRPIIKRALDLGINFFDTANVYSGgaseEI-LGRALKE-----FAPRDEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 73 FITSKVWN-SDHG---------HVVEACKNSLKKlqldyldlylvhypLATKHsgvgttaslldenkvldIDV------- 135
Cdd:cd19079 81 VIATKVYFpMGDGpngrglsrkHIMAEVDASLKR--------------LGTDY-----------------IDLyqihrwd 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 136 --TVSLET--TWHDMektVSLGLVRSIGLSNY------ELFLTRDCLSYAKIkpqVSQFETHPYFQRE---SLVRFCKKH 202
Cdd:cd19079 130 yeTPIEETleALHDV---VKSGKVRYIGASSMyawqfaKALHLAEKNGWTKF---VSMQNHYNLLYREeerEMIPLCEEE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 203 GVVPMAHTPLGG--------------ATANVKAFGSISPLED---PVLIG---LAKKYQKSVAQIALRWNIERGTPVIP- 261
Cdd:cd19079 204 GIGVIPWSPLARgrlarpwgdtterrRSTTDTAKLKYDYFTEadkEIVDRveeVAKERGVSMAQVALAWLLSKPGVTAPi 283
|
330 340
....*....|....*....|....*....
7S5I_A 262 -KSSKVERLKENLEVLNFKLEKEDIELIN 289
Cdd:cd19079 284 vGATKLEHLEDAVAALDIKLSEEEIKYLE 312
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
8-289 |
3.53e-12 |
|
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: 65.72 E-value: 3.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 8 NGFEMPVIGLGL----WR---LEKEELRSAILNAIKLGYRHFDAAAHYKTEIDVGN--AIAEAIQSGLVKREELFITSKV 78
Cdd:cd19077 1 NGKLVGPIGLGLmgltWRpnpTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHANlkLLARFFRKYPEYADKVVLSVKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 79 -WNSDHGHVV---EACKNSLKklqldyldlylvhyplatkhsgvgTTASLLDENKVLDI------DVTVSLETTWHDMEK 148
Cdd:cd19077 81 gLDPDTLRPDgspEAVRKSIE------------------------NILRALGGTKKIDIfeparvDPNVPIEETIKALKE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 149 TVSLGLVRSIGLSNyelfLTRDCLSYA-KIKPQVS-QFETHPyFQRESL----VRFCKKHGVVPMAHTPLG-----GATA 217
Cdd:cd19077 137 LVKEGKIRGIGLSE----VSAETIRRAhAVHPIAAvEVEYSL-FSREIEengvLETCAELGIPIIAYSPLGrglltGRIK 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 218 NV-----KAFGSISPLEDP-----------VLIGLAKKYQKSVAQIALRWNIERGTPVI---PKSSKVERLKENLEVLNF 278
Cdd:cd19077 212 SLadipeGDFRRHLDRFNGenfeknlklvdALQELAEKKGCTPAQLALAWILAQSGPKIipiPGSTTLERVEENLKAANV 291
|
330
....*....|.
7S5I_A 279 KLEKEDIELIN 289
Cdd:cd19077 292 ELTDEELKEIN 302
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-291 |
5.85e-12 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 65.00 E-value: 5.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 14 VIGLGLWRL-------------EKEELRsAILNAIKLGYRHFDAAAHYKT---EIDVGNAIAEaiqsglvKREELFITSK 77
Cdd:cd19102 3 TIGLGTWAIggggwgggwgpqdDRDSIA-AIRAALDLGINWIDTAAVYGLghsEEVVGRALKG-------LRDRPIVATK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 78 ---VWNSDhGHVV---------EACKNSLKKLQLDYLDLYLVHYPlatkhsgvgttaslldenkvldiDVTVSLETTWHD 145
Cdd:cd19102 75 cglLWDEE-GRIRrslkpasirAECEASLRRLGVDVIDLYQIHWP-----------------------DPDEPIEEAWGA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 146 MEKTVSLGLVRSIGLSNYELFLTRDCLSYAKI---KPQVSQFetHPYFQREsLVRFCKKHGVVPMAHTPLG-----GATA 217
Cdd:cd19102 131 LAELKEEGKVRAIGVSNFSVDQMKRCQAIHPIaslQPPYSLL--RRGIEAE-ILPFCAEHGIGVIVYSPMQsglltGKMT 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 218 NvkafGSISPLE-------DPVLIG---------------LAKKYQKSVAQIALRWNIERG--TPVIPKSSKVERLKENL 273
Cdd:cd19102 208 P----ERVASLPaddwrrrSPFFQEpnlarnlalvdalrpIAERHGRTVAQLAIAWVLRRPevTSAIVGARRPDQIDETV 283
|
330
....*....|....*...
7S5I_A 274 EVLNFKLEKEDIELINTI 291
Cdd:cd19102 284 GAADLRLTPEELAEIEAL 301
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
1-295 |
6.27e-12 |
|
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: 65.16 E-value: 6.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 1 MSTITL-NNGFEMPVIGLGLWRL-------EKEELRSAILN-AIKLGYRHFDAAAHYKteiDVGNAIAEAIQSGLVKREE 71
Cdd:cd19144 1 IPTRTLgRNGPSVPALGFGAMGLsafygppKPDEERFAVLDaAFELGCTFWDTADIYG---DSEELIGRWFKQNPGKREK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 72 LFITSKV-----------W-NSDHGHVVEACKNSLKKLqldyldlylvhyplatkhsGVGTtaslLDENKVLDIDVTVSL 139
Cdd:cd19144 78 IFLATKFgieknvetgeySvDGSPEYVKKACETSLKRL-------------------GVDY----IDLYYQHRVDGKTPI 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 140 ETTWHDMEKTVSLGLVRSIGLSNyelfLTRDCLSYA-KIKPQVS-QFETHPYF-----QRESLVRFCKKHGVVPMAHTPL 212
Cdd:cd19144 135 EKTVAAMAELVQEGKIKHIGLSE----CSAETLRRAhAVHPIAAvQIEYSPFSldierPEIGVLDTCRELGVAIVAYSPL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 213 GgatanvKAF--GSISPLED----------P---------------VLIGLAKKYQKSVAQIALRWNIERGTPV--IPKS 263
Cdd:cd19144 211 G------RGFltGAIRSPDDfeegdfrrmaPrfqaenfpknlelvdKIKAIAKKKNVTAGQLTLAWLLAQGDDIipIPGT 284
|
330 340 350
....*....|....*....|....*....|..
7S5I_A 264 SKVERLKENLEVLNFKLEKEDIELINTIDKKF 295
Cdd:cd19144 285 TKLKRLEENLGALKVKLTEEEEKEIREIAEEA 316
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
7-288 |
6.61e-12 |
|
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: 64.93 E-value: 6.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 7 NNGFEMPVIGLGLWRL-------EKEELRSAILNAIKLGYRHFDAAAHY---KTEIDVGNAIAEaiqsglvKREELFITS 76
Cdd:cd19076 7 TQGLEVSALGLGCMGMsafygpaDEEESIATLHRALELGVTFLDTADMYgpgTNEELLGKALKD-------RRDEVVIAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 77 K---VWNSDHG---------HVVEACKNSLKKlqldyldlylvhypLATKHsgvgttaslldenkvLD------IDVTVS 138
Cdd:cd19076 80 KfgiVRDPGSGfrgvdgrpeYVRAACEASLKR--------------LGTDV---------------IDlyyqhrVDPNVP 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 139 LETTWHDMEKTVSLGLVRSIGLSNyelfLTRDCLSYA-KIKP----QV--SQFETHPyfqRESLVRFCKKHGVVPMAHTP 211
Cdd:cd19076 131 IEETVGAMAELVEEGKVRYIGLSE----ASADTIRRAhAVHPitavQSeySLWTRDI---EDEVLPTCRELGIGFVAYSP 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 212 LG-----GATANVK-----AFGSISP------------LEDPVLiGLAKKYQKSVAQIALRWNIERGTPV--IPKSSKVE 267
Cdd:cd19076 204 LGrgfltGAIKSPEdlpedDFRRNNPrfqgenfdknlkLVEKLE-AIAAEKGCTPAQLALAWVLAQGDDIvpIPGTKRIK 282
|
330 340
....*....|....*....|.
7S5I_A 268 RLKENLEVLNFKLEKEDIELI 288
Cdd:cd19076 283 YLEENVGALDVVLTPEELAEI 303
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
13-281 |
9.35e-12 |
|
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: 63.78 E-value: 9.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 13 PVIGLGLWRLE----------KEELRSAILNAIKLGYRHFDAAAHYKteIDVGNA-IAEAIQSGlvkREELFITSKV--- 78
Cdd:cd19088 2 SRLGYGAMRLTgpgiwgppadREEAIAVLRRALELGVNFIDTADSYG--PDVNERlIAEALHPY---PDDVVIATKGglv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 79 ------WNSDH--GHVVEACKNSLKKLQLDYLDLYLVH-----YPLATKhsgVGTTASLLDEnkvldidvtvslettwhd 145
Cdd:cd19088 77 rtgpgwWGPDGspEYLRQAVEASLRRLGLDRIDLYQLHridpkVPFEEQ---LGALAELQDE------------------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 146 mektvslGLVRSIGLSNYELFLTRDCLSYAKIkpqVS-QFETHPYFQR-ESLVRFCKKHGVVPMAHTPLGGATanvkafg 223
Cdd:cd19088 136 -------GLIRHIGLSNVTVAQIEEARAIVRI---VSvQNRYNLANRDdEGVLDYCEAAGIAFIPWFPLGGGD------- 198
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
7S5I_A 224 sisPLEDPVLIG-LAKKYQKSVAQIALRWNIERGtPV---IPKSSKVERLKENLEVLNFKLE 281
Cdd:cd19088 199 ---LAQPGGLLAeVAARLGATPAQVALAWLLARS-PVmlpIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-78 |
6.15e-11 |
|
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: 62.34 E-value: 6.15e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
7S5I_A 15 IGLGLWRLE-----KEELRSAILNAIKLGYRHFDAAAHY---KTEIDVGNAIAEAIQSGLVKREELFITSKV 78
Cdd:cd19099 6 LGLGTYRGDsddetDEEYREALKAALDSGINVIDTAINYrggRSERLIGKALRELIEKGGIKRDEVVIVTKA 77
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
7-285 |
1.43e-10 |
|
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo. Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2). It catalyzes the conversion of 3-hydroxybutanal (3-HB) to 1,3-butanediol (1,3-BDO) by using NADPH as a cofactor.
Pssm-ID: 381315 [Multi-domain] Cd Length: 308 Bit Score: 61.12 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 7 NNGFEMPVIGLGLWRL-----EKEELRSAILNAIKLGYRHFDAAAHY-----KTEIDVGNAIAEAIQSglvKREELFITS 76
Cdd:cd19089 6 RSGLHLPAISLGLWHNfgdytSPEEARELLRTAFDLGITHFDLANNYgpppgSAEENFGRILKRDLRP---YRDELVIST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 77 KV----WNSDHG------HVVEACKNSLKKLQldyldlylvhyplatkhsgvgttaslLDenkVLDI------DVTVSLE 140
Cdd:cd19089 83 KAgygmWPGPYGdggsrkYLLASLDQSLKRMG--------------------------LD---YVDIfyhhryDPDTPLE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 141 TTWHDMEKTVSLGLVRSIGLSNYELFLTR---DCLSYAKIKPQVSQFethPY--FQR---ESLVRFCKKHGV-----VPM 207
Cdd:cd19089 134 ETMTALADAVRSGKALYVGISNYPGAKARraiALLRELGVPLIIHQP---RYslLDRwaeDGLLEVLEEAGIgfiafSPL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 208 AH-----TPLGGATANVKAFGSISPLEDPVLIG-----------LAKKYQKSVAQIALRWNI--ERGTPVIPKSSKVERL 269
Cdd:cd19089 211 AQglltdKYLNGIPPDSRRAAESKFLTEEALTPekleqlrklnkIAAKRGQSLAQLALSWVLrdPRVTSVLIGASSPSQL 290
|
330
....*....|....*..
7S5I_A 270 KENLEVL-NFKLEKEDI 285
Cdd:cd19089 291 EDNVAALkNLDFSEEEL 307
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
13-283 |
6.00e-10 |
|
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: 58.72 E-value: 6.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 13 PVIGLG------LWRLEKEEL-RSAILNAIKLGYRHFDAAAHY-KTEIDVGNAIAEaiqsglVKREELFITSKV------ 78
Cdd:cd19090 1 SALGLGtaglggVFGGVDDDEaVATIRAALDLGINYIDTAPAYgDSEERLGLALAE------LPREPLVLSTKVgrlped 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 79 -WNSDHGHVVEACKNSLKKLQLDYLDLYLVHYPlatkhsGVGTTASLLDENKVLDidvtvsletTWHDMEKTvslGLVRS 157
Cdd:cd19090 75 tADYSADRVRRSVEESLERLGRDRIDLLMIHDP------ERVPWVDILAPGGALE---------ALLELKEE---GLIKH 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 158 IGLSNYELFLTRDCLsyakikpQVSQFE---THPYF------QRESLVRFCKKHGVVPMAHTPLG-GATANvKAFGSISP 227
Cdd:cd19090 137 IGLGGGPPDLLRRAI-------ETGDFDvvlTANRYtlldqsAADELLPAAARHGVGVINASPLGmGLLAG-RPPERVRY 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
7S5I_A 228 LEDPV----------LIGLAKKYQKSVAQIALRW--NIERGTPVIPKSSKVERLKENLEVLNFKLEKE 283
Cdd:cd19090 209 TYRWLspelldrakrLYELCDEHGVPLPALALRFllRDPRISTVLVGASSPEELEQNVAAAEGPLPEE 276
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-276 |
3.81e-09 |
|
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: 56.05 E-value: 3.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 1 MSTITL-NNGFEMPVIGLGLWRLEKEELrSAILNAIKLGYRHFDAAAHY---KTEIDVGNAIAEaiqsglVKREELFITS 76
Cdd:cd19105 1 MPYRTLgKTGLKVSRLGFGGGGLPRESP-ELLRRALDLGINYFDTAEGYgngNSEEIIGEALKG------LRRDKVFLAT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 77 KVWN----SDHGHVVEACKNSLKKLQLDYLDLYLVHyplatkhsGVGTTASLLDENKVLDidvtvslettwhDMEKTVSL 152
Cdd:cd19105 74 KASPrldkKDKAELLKSVEESLKRLQTDYIDIYQLH--------GVDTPEERLLNEELLE------------ALEKLKKE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 153 GLVRSIGLSnyELFLTRDCLSYA-KIKP----QVSQFETHPYFQRESLVRFCKKH--GVVPMahtplggatanvKAFGSI 225
Cdd:cd19105 134 GKVRFIGFS--THDNMAEVLQAAiESGWfdviMVAYNFLNQPAELEEALAAAAEKgiGVVAM------------KTLAGG 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
7S5I_A 226 SPLEDPVLIGLAKKYqkSVAQIALRW--NIERGTPVIPKSSKVERLKENLEVL 276
Cdd:cd19105 200 YLQPALLSVLKAKGF--SLPQAALKWvlSNPRVDTVVPGMRNFAELEENLAAA 250
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
22-291 |
8.99e-09 |
|
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: 55.50 E-value: 8.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 22 LEKEELRSAILNAIKLGYRHFDAAAHY---KTEIDVGNAIAEAiqsglvKREELFITSK--VWNSDHGHVV--------E 88
Cdd:cd19083 30 LDEEEGKDLVREALDNGVNLLDTAFIYglgRSEELVGEVLKEY------NRNEVVIATKgaHKFGGDGSVLnnspeflrS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 89 ACKNSLKKLQLDYLDLYLVHYP--LATKHSGVGTTASLLDEnkvldidvtvslettwhdmektvslGLVRSIGLSNYELf 166
Cdd:cd19083 104 AVEKSLKRLNTDYIDLYYIHFPdgETPKAEAVGALQELKDE-------------------------GKIRAIGVSNFSL- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 167 ltrDCLSYAKIKPQVSQFEtHPY--FQRE---SLVRFCKKHGVV-----PMAHTPLGGA--------------------- 215
Cdd:cd19083 158 ---EQLKEANKDGYVDVLQ-GEYnlLQREaeeDILPYCVENNISfipyfPLASGLLAGKytkdtkfpdndlrndkplfkg 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 216 ---TANVKAFGSISPledpvligLAKKYQKSVAQIALRWNIERG--TPVIPKSSKVERLKENLEVLNFKLEKEDIELINT 290
Cdd:cd19083 234 erfSENLDKVDKLKS--------IADEKGVTVAHLALAWYLTRPaiDVVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDA 305
|
.
7S5I_A 291 I 291
Cdd:cd19083 306 L 306
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
7-289 |
1.40e-08 |
|
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: 54.91 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 7 NNGFEMPVIGLGLWRL--EKEELRS-AILNA-IKLGYRHFDAAAHY----------KTEIDVGNAIAeaiQSGlvKREEL 72
Cdd:cd19081 4 RTGLSVSPLCLGTMVFgwTADEETSfALLDAfVDAGGNFIDTADVYsawvpgnaggESETIIGRWLK---SRG--KRDRV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 73 FITSKV--WNSDHG------HVVEACKNSLKKlqldyldlylvhypLATKHsgvgttaslldenkvLDI------DVTVS 138
Cdd:cd19081 79 VIATKVgfPMGPNGpglsrkHIRRAVEASLRR--------------LQTDY---------------IDLyqahwdDPATP 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 139 LETTWHDMEKTVSLGLVRSIGLSNYELFLTRDCLSYAK---------IKPQVSQFETHPYfqRESLVRFCKKHGVVPMAH 209
Cdd:cd19081 130 LEETLGALNDLIRQGKVRYIGASNYSAWRLQEALELSRqhglpryvsLQPEYNLVDRESF--EGELLPLCREEGIGVIPY 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 210 TPLGG------------ATANVKAFGSISPLEDP-------VLIGLAKKYQKSVAQIALRWNIERG--TPVIPKSSKVER 268
Cdd:cd19081 208 SPLAGgfltgkyrseadLPGSTRRGEAAKRYLNErglrildALDEVAAEHGATPAQVALAWLLARPgvTAPIAGARTVEQ 287
|
330 340
....*....|....*....|.
7S5I_A 269 LKENLEVLNFKLEKEDIELIN 289
Cdd:cd19081 288 LEDLLAAAGLRLTDEEVARLD 308
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
7-277 |
1.90e-08 |
|
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: 54.72 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 7 NNGFEMPVIGLGLW-------RLEKEelRSAILNAIKLGYRHFDAAAHY-----KTEIDVGNAIAEAIQSglvKREELFI 74
Cdd:cd19151 7 RSGLKLPAISLGLWhnfgdvdRYENS--RAMLRRAFDLGITHFDLANNYgpppgSAEENFGRILKEDLKP---YRDELII 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 75 TSK----VWNS---DHG---HVVEACKNSLKKLQLDYLDLYLVHYPlatkhsgvgttaslldenkvldiDVTVSLETTWH 144
Cdd:cd19151 82 STKagytMWPGpygDWGskkYLIASLDQSLKRMGLDYVDIFYHHRP-----------------------DPETPLEETMG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 145 DMEKTVSLGLVRSIGLSNYELFLTRD-----------CLSYakiKPQVSQFETHPyfqRESLVRFCKKHGVVPMAHTPLG 213
Cdd:cd19151 139 ALDQIVRQGKALYVGISNYPPEEAREaaailkdlgtpCLIH---QPKYSMFNRWV---EEGLLDVLEEEGIGCIAFSPLA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 214 GATANVKAFGSI----------SPL-EDPV----------LIGLAKKYQKSVAQIALRWNIERG--TPVIPKSSKVERLK 270
Cdd:cd19151 213 QGLLTDRYLNGIpedsraakgsSFLkPEQIteeklakvrrLNEIAQARGQKLAQMALAWVLRNKrvTSVLIGASKPSQIE 292
|
....*..
7S5I_A 271 ENLEVLN 277
Cdd:cd19151 293 DAVGALD 299
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
14-275 |
2.57e-08 |
|
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: 53.64 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 14 VIGLGLWRL--------EKEELRSAILNAIKLGYRHFDAAAHY---KTEIDVGNAIAEaiqsglvKREELFITSKVWNSD 82
Cdd:cd19086 5 EIGFGTWGLggdwwgdvDDAEAIRALRAALDLGINFFDTADVYgdgHSERLLGKALKG-------RRDKVVIATKFGNRF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 83 HG-----------HVVEACKNSLKKLQLDYLDLYLVHYPlatkhsgvgtTASLLDENKVLDIdvtvslettwhdMEKTVS 151
Cdd:cd19086 78 DGgperpqdfspeYIREAVEASLKRLGTDYIDLYQLHNP----------PDEVLDNDELFEA------------LEKLKQ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 152 LGLVRSIGLS--NYELFltRDCLSYAKIkpQVSQFETHPYFQR--ESLVRFCKKHGVVPMAHTPLggatanvkAFGsisp 227
Cdd:cd19086 136 EGKIRAYGVSvgDPEEA--LAALRRGGI--DVVQVIYNLLDQRpeEELFPLAEEHGVGVIARVPL--------ASG---- 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
7S5I_A 228 ledpvliGLAKKyqksVAQIALRW---NIERGTpVIPKSSKVERLKENLEV 275
Cdd:cd19086 200 -------LLTGK----LAQAALRFilsHPAVST-VIPGARSPEQVEENAAA 238
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
9-290 |
5.74e-08 |
|
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: 53.01 E-value: 5.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 9 GFEMPVIGLGLWRL--------EKEELRSAILNAIKLGYRHFDAAAHYKT---EIDVGNAIAEaiqsglvKREELFITSK 77
Cdd:cd19078 1 GLEVSAIGLGCMGMshgygpppDKEEMIELIRKAVELGITFFDTAEVYGPytnEELVGEALKP-------FRDQVVIATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 78 -------------VWNSDHGHVVEACKNSLKKlqldyldlylvhypLATKHSGvgttasLLDENKVldiDVTVSLETTWH 144
Cdd:cd19078 74 fgfkidggkpgplGLDSRPEHIRKAVEGSLKR--------------LQTDYID------LYYQHRV---DPNVPIEEVAG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 145 DMEKTVSLGLVRSIGLSNyelfLTRDCLSYA-KIKPQVS-QFETHPYFQR--ESLVRFCKKHGVVPMAHTPLG-----GA 215
Cdd:cd19078 131 TMKELIKEGKIRHWGLSE----AGVETIRRAhAVCPVTAvQSEYSMMWREpeKEVLPTLEELGIGFVPFSPLGkgfltGK 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 216 -TANVK----------------AFGSISPLEDpVLIGLAKKYQKSVAQIALRWNIERGTPV--IPKSSKVERLKENLEVL 276
Cdd:cd19078 207 iDENTKfdegddraslprftpeALEANQALVD-LLKEFAEEKGATPAQIALAWLLAKKPWIvpIPGTTKLSRLEENIGAA 285
|
330
....*....|....
7S5I_A 277 NFKLEKEDIELINT 290
Cdd:cd19078 286 DIELTPEELREIED 299
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
8-277 |
1.62e-07 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 51.91 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 8 NGFEMPVIGLGLWR-------LEKEelRSAILNAIKLGYRHFDAAAHY-----KTEIDVGNAIAEAIQSglvKREELFIT 75
Cdd:PRK09912 21 SGLRLPALSLGLWHnfghvnaLESQ--RAILRKAFDLGITHFDLANNYgpppgSAEENFGRLLREDFAA---YRDELIIS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 76 SK----VWNSDHG------HVVEACKNSLKKLQLDYLDLYLVHYplatkhsgvgttaslLDENkvldidvtVSLETTWHD 145
Cdd:PRK09912 96 TKagydMWPGPYGsggsrkYLLASLDQSLKRMGLEYVDIFYSHR---------------VDEN--------TPMEETASA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 146 MEKTVSLGLVRSIGLSNYELFLTR---DCLSYAKIK---PQVSQFETHPYFQRESLVRFCKKHGVVPMAHTPLG------ 213
Cdd:PRK09912 153 LAHAVQSGKALYVGISSYSPERTQkmvELLREWKIPlliHQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAqglltg 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 214 --------------------GATANVKAFGSISPLEdpVLIGLAKKYQKSVAQIALRWNI--ERGTPVIPKSSKVERLKE 271
Cdd:PRK09912 233 kylngipqdsrmhregnkvrGLTPKMLTEANLNSLR--LLNEMAQQRGQSMAQMALSWLLkdERVTSVLIGASRAEQLEE 310
|
....*.
7S5I_A 272 NLEVLN 277
Cdd:PRK09912 311 NVQALN 316
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
25-291 |
3.20e-07 |
|
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: 51.03 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 25 EELRSAILN-AIKLGYRHFDAAAHY----------KTEIDVGNAIAeaiQSGlvKREELFITSKV--------WNS---- 81
Cdd:cd19094 17 EAEAHEQLDyAFDEGVNFIDTAEMYpvppspetqgRTEEIIGSWLK---KKG--NRDKVVLATKVagpgegitWPRgggt 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 82 --DHGHVVEACKNSLKKLQLDYLDLYLVHYP-LATKHSGVGTtasLLDENKVLDidvTVSLETTWHDMEKTVSLGLVRSI 158
Cdd:cd19094 92 rlDRENIREAVEGSLKRLGTDYIDLYQLHWPdRYTPLFGGGY---YTEPSEEED---SVSFEEQLEALGELVKAGKIRHI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 159 GLSNYELFLTRDCLSYAKI----KPQVSQfetHPY--FQR---ESLVRFCKKHGVVPMAHTPLGG--------------A 215
Cdd:cd19094 166 GLSNETPWGVMKFLELAEQlglpRIVSIQ---NPYslLNRnfeEGLAEACHRENVGLLAYSPLAGgvltgkyldgaarpE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 216 TANVKAFGS-----ISPL-EDPV--LIGLAKKYQKSVAQIALRWNIERG--TPVIPKSSKVERLKENLEVLNFKLEKEDI 285
Cdd:cd19094 243 GGRLNLFPGymaryRSPQaLEAVaeYVKLARKHGLSPAQLALAWVRSRPfvTSTIIGATTLEQLKENIDAFDVPLSDELL 322
|
....*.
7S5I_A 286 ELINTI 291
Cdd:cd19094 323 AEIDAV 328
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
34-163 |
3.58e-07 |
|
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: 50.65 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 34 AIKLGYRHFDAAAHY---KTEIDVGNAIAEaiqsglvKREELFITSKV------WNSDHG----HVVEACKNSLKKLQLD 100
Cdd:cd19087 39 ALDAGINFFDTADVYgggRSEEIIGRWIAG-------RRDDIVLATKVfgpmgdDPNDRGlsrrHIRRAVEASLRRLQTD 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
7S5I_A 101 YLDLYLVHYplatkhsgvgttaslldenkvldIDVTVSLETTWHDMEKTVSLGLVRSIGLSNY 163
Cdd:cd19087 112 YIDLYQMHH-----------------------FDRDTPLEETLRALDDLVRQGKIRYIGVSNF 151
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
9-288 |
4.02e-07 |
|
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: 50.51 E-value: 4.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 9 GFEMPVIGLGLWRL--------EKEELRSAILNAIKLGYRHFDAAAHY---KTEIDVGNAIAEAIqsglvkREELFITSK 77
Cdd:cd19145 9 GLEVSAQGLGCMGLsgdygapkPEEEGIALIHHAFNSGVTFLDTSDIYgpnTNEVLLGKALKDGP------REKVQLATK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 78 V-----------WNSDHGHVVEACKNSLKKLQldyldlylVHY-PLATKHSgvgttaslldenkvldIDVTVSLETTWHD 145
Cdd:cd19145 83 FgiheiggsgveVRGDPAYVRAACEASLKRLD--------VDYiDLYYQHR----------------IDTTVPIEITMGE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 146 MEKTVSLGLVRSIGLSNYELFLTRDclSYAkIKPQVS-QFETHPYFQ--RESLVRFCKKHGVVPMAHTPLGGATANVKAF 222
Cdd:cd19145 139 LKKLVEEGKIKYIGLSEASADTIRR--AHA-VHPITAvQLEWSLWTRdiEEEIIPTCRELGIGIVPYSPLGRGFFAGKAK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 223 GSISPLEDPVLIG---------------------LAKKYQKSVAQIALRWNIERGTPV--IPKSSKVERLKENLEVLNFK 279
Cdd:cd19145 216 LEELLENSDVRKShprfqgenleknkvlyerveaLAKKKGCTPAQLALAWVLHQGEDVvpIPGTTKIKNLNQNIGALSVK 295
|
....*....
7S5I_A 280 LEKEDIELI 288
Cdd:cd19145 296 LTKEDLKEI 304
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
13-275 |
5.38e-07 |
|
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: 49.93 E-value: 5.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 13 PVIGLGLWRL-------EKEELRSAILNAIKLGYRHFDAAAHYKT-EIDVGNAIAEaiqsglVKREELFITSKVWNSDHG 84
Cdd:cd19095 1 SVLGLGTSGIgrvwgvpSEAEAARLLNTALDLGINLIDTAPAYGRsEERLGRALAG------LRRDDLFIATKVGTHGEG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 85 ----------HVVEACKNSLKKLQLDYLDLYLVHYPlatkhsgvgttaSLLDENKVLdidvtvsLETtwhdMEKTVSLGL 154
Cdd:cd19095 75 grdrkdfspaAIRASIERSLRRLGTDYIDLLQLHGP------------SDDELTGEV-------LET----LEDLKAAGK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 155 VRSIGLSNYELFLTRDCLSyakikPQVSQFEThPY----FQRESLVRFCKKHGVVPMAHTPLGGATANVKAFGSISPLED 230
Cdd:cd19095 132 VRYIGVSGDGEELEAAIAS-----GVFDVVQL-PYnvldREEEELLPLAAEAGLGVIVNRPLANGRLRRRVRRRPLYADY 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
7S5I_A 231 PVLIGLAKKY-QKSVAQIALRWNIERG--TPVIPKSSKVERLKENLEV 275
Cdd:cd19095 206 ARRPEFAAEIgGATWAQAALRFVLSHPgvSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
9-287 |
2.63e-06 |
|
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: 48.22 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 9 GFEMPVIGLGLWR-----LEKEELRSAILNAIKLGYRHFDAAAHY-----KTEIDVGNAIAEAIQSglvKREELFITSK- 77
Cdd:cd19150 9 GLKLPALSLGLWHnfgddTPLETQRAILRTAFDLGITHFDLANNYgpppgSAEENFGRILREDFAG---YRDELIISTKa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 78 ---VWNSDHG------HVVEACKNSLKKLQldyldlylvhyplatkhsgvgttaslLDenkVLDI------DVTVSLETT 142
Cdd:cd19150 86 gydMWPGPYGewgsrkYLLASLDQSLKRMG--------------------------LD---YVDIfyshrfDPDTPLEET 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 143 WHDMEKTVSLGLVRSIGLSNYELFLTR---DCLSYAKI-----KPQVSQFEThpYFQRESLVRFCKKHGVVPMAHTP--- 211
Cdd:cd19150 137 MGALDHAVRSGKALYVGISSYSPERTReaaAILRELGTpllihQPSYNMLNR--WVEESGLLDTLQELGVGCIAFTPlaq 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 212 -------LGGATANVKAF--GSISP---LEDPV-----LIGLAKKYQKSVAQIALRWNIERG--TPVIPKSSKVERLKEN 272
Cdd:cd19150 215 glltdkyLNGIPEGSRASkeRSLSPkmlTEANLnsiraLNEIAQKRGQSLAQMALAWVLRDGrvTSALIGASRPEQLEEN 294
|
330
....*....|....*
7S5I_A 273 LEVLNfKLEKEDIEL 287
Cdd:cd19150 295 VGALD-NLTFSADEL 308
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
18-293 |
3.80e-06 |
|
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: 47.65 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 18 GLW-RLEKEELRSAILNAIKLGYRHFDAAAHY---KTEIDVGNAIAEaiqsglvKREELFITSKV------WNSDHGHVV 87
Cdd:cd19104 24 GLMgRTTREEQIAAVRRALDLGINFFDTAPSYgdgKSEENLGRALKG-------LPAGPYITTKVrldpddLGDIGGQIE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 88 EACKNSLKKLQLDyldlylvHYPLATKHSGVGTTASLLDENK--VLDIDVtvsLETTWHDMEKTVSLGLVRSIGLS---N 162
Cdd:cd19104 97 RSVEKSLKRLKRD-------SVDLLQLHNRIGDERDKPVGGTlsTTDVLG---LGGVADAFERLRSEGKIRFIGITglgN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 163 YELF---LTRDCLS-----YAKIKPqvSQFETHP----YFQRESLVRFCKKHGVVPMAHTPL--GGATANVKAFGSISPL 228
Cdd:cd19104 167 PPAIrelLDSGKFDavqvyYNLLNP--SAAEARPrgwsAQDYGGIIDAAAEHGVGVMGIRVLaaGALTTSLDRGREAPPT 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
7S5I_A 229 ED-PV---------LIGLAKKYQKSVAQIALRWNI-ERGTP-VIPKSSKVERLKENLEVLNF-KLEKediELINTIDK 293
Cdd:cd19104 245 SDsDVaidfrraaaFRALAREWGETLAQLAHRFALsNPGVStVLVGVKNREELEEAVAAEAAgPLPA---ENLARLEA 319
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
20-289 |
1.23e-05 |
|
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: 46.06 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 20 WRLEKEELRsAILNA-IKLGYRHFDAAAHY---KTEIDVGNAIAEaiqsglvKREELFITSKVWNSDHGHVVEACKN--- 92
Cdd:cd19080 26 WGADREEAR-AMFDAyVEAGGNFIDTANNYtngTSERLLGEFIAG-------NRDRIVLATKYTMNRRPGDPNAGGNhrk 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 93 --------SLKKLQLDYLDLYLVHYPlatkhsgvgttaslldenkvldiDVTVSLETTWHDMEKTVSLGLVRSIGLSNYE 164
Cdd:cd19080 98 nlrrsveaSLRRLQTDYIDLLYVHAW-----------------------DFTTPVEEVMRALDDLVRAGKVLYVGISDTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 165 LFLTRDCLSYAKI--KPQVSQFETHpY------FQREsLVRFCKKHGVVPMAHTPLGG--------------ATANVKAF 222
Cdd:cd19080 155 AWVVARANTLAELrgWSPFVALQIE-YsllertPERE-LLPMARALGLGVTPWSPLGGglltgkyqrgeegrAGEAKGVT 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
7S5I_A 223 GSISPLED------PVLIGLAKKYQKSVAQIALRWNIERGTPVIP--KSSKVERLKENLEVLNFKLEKEDIELIN 289
Cdd:cd19080 233 VGFGKLTErnwaivDVVAAVAEELGRSAAQVALAWVRQKPGVVIPiiGARTLEQLKDNLGALDLTLSPEQLARLD 307
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
9-274 |
2.50e-05 |
|
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: 44.78 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 9 GFEMPVIGLG---LWRLEKEELRSAILNAIKLGYRHFDAAAHY-KTEIDVGNAIAEaiqsglvKREELFITSKVWNSDHG 84
Cdd:cd19100 8 GLKVSRLGFGggpLGRLSQEEAAAIIRRALDLGINYFDTAPSYgDSEEKIGKALKG-------RRDKVFLATKTGARDYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 85 HVVEACKNSLKKLQLDYLDLYLVHYpLATKHsgvgTTASLLDENKVLDIdvtvslettwhdMEKTVSLGLVRSIGLS--N 162
Cdd:cd19100 81 GAKRDLERSLKRLGTDYIDLYQLHA-VDTEE----DLDQVFGPGGALEA------------LLEAKEEGKIRFIGISghS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 163 YELFLTR------DCLSYAkikpqVSQFETHPYFQRESLVRFCKKHGVvpmahtplgGATANvKAFGSISpledpvligL 236
Cdd:cd19100 144 PEVLLRAletgefDVVLFP-----INPAGDHIDSFREELLPLAREKGV---------GVIAM-KVLAGGR---------L 199
|
250 260 270 280
....*....|....*....|....*....|....*....|
7S5I_A 237 AKKYQKSVAQiALRWNIERGTP--VIPKSSKVERLKENLE 274
Cdd:cd19100 200 LSGDPLDPEQ-ALRYALSLPPVdvVIVGMDSPEELDENLA 238
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
8-292 |
2.98e-05 |
|
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: 45.03 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 8 NGFEMPVIGLGLW-----RLEKEELRSAILNAIKLGYRHFDAAAHY---KTEIDVGNAIAEAIQsglvKREELFITSKVW 79
Cdd:cd19159 9 SGLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGW----RRSSLVITTKLY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 80 -----NSDHG----HVVEACKNSLKKLQLDYLDLYLVHYPlatkhsgvgttaslldenkvldiDVTVSLETTWHDMEKTV 150
Cdd:cd19159 85 wggkaETERGlsrkHIIEGLKGSLQRLQLEYVDVVFANRP-----------------------DSNTPMEEIVRAMTHVI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 151 SLGLVRSIGLSNYELFLTRDCLSYAK----IKPQVSQFETHpYFQRE----SLVRFCKKHGVVPMAHTPLG--------- 213
Cdd:cd19159 142 NQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYH-LFQREkvevQLPELYHKIGVGAMTWSPLAcgiisgkyg 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 214 -GATANVKA-FGSISPLEDPV--------------LIGLAKKYQKSVAQIALRWNI--ERGTPVIPKSSKVERLKENLEV 275
Cdd:cd19159 221 nGVPESSRAsLKCYQWLKERIvseegrkqqnklkdLSPIAERLGCTLPQLAVAWCLrnEGVSSVLLGSSTPEQLIENLGA 300
|
330
....*....|....*..
7S5I_A 276 LNFkLEKEDIELINTID 292
Cdd:cd19159 301 IQV-LPKMTSHVVNEID 316
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
14-274 |
5.73e-05 |
|
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: 44.08 E-value: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 14 VIGLGLW----RLEKEELRSAILNAIK-LGYRHFDAAAHY---KTEIDVGNAiaeaiqsgLVKREELFITSKV---WNSD 82
Cdd:cd19075 4 ILGTMTFgsqgRFTTAEAAAELLDAFLeRGHTEIDTARVYpdgTSEELLGEL--------GLGERGFKIDTKAnpgVGGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 83 HGH--VVEACKNSLKKLQLDYLDLYLVHYPlatkhsgvgttaslldenkvldiDVTVSLETTWHDMEKTVSLGLVRSIGL 160
Cdd:cd19075 76 LSPenVRKQLETSLKRLKVDKVDVFYLHAP-----------------------DRSTPLEETLAAIDELYKEGKFKEFGL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 161 SNYELFLTRDCLSYAK----IKPQVSQ---------FEThpyfqreSLVRFCKKHGVVPMAHTPL-GGATANVKAFGSIS 226
Cdd:cd19075 133 SNYSAWEVAEIVEICKengwVLPTVYQgmynaitrqVET-------ELFPCLRKLGIRFYAYSPLaGGFLTGKYKYSEDK 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 227 PLE---DP----------------------VLIGLAKKYQKSVAQIALRW-------NIERGTPVIPKSSKVERLKENLE 274
Cdd:cd19075 206 AGGgrfDPnnalgklyrdrywkpsyfealeKVEEAAEKEGISLAEAALRWlyhhsalDGEKGDGVILGASSLEQLEENLA 285
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
7-293 |
1.26e-04 |
|
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: 42.97 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 7 NNGFEMPVIGLGLW-----RLEKEELRSAILNAIKLGYRHFDAAAHY---KTEIDVGNAIAEaiqsGLVKREELFITSKV 78
Cdd:cd19143 8 RSGLKVSALSFGSWvtfgnQVDVDEAKECMKAAYDAGVNFFDNAEVYangQSEEIMGQAIKE----LGWPRSDYVVSTKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 79 -W------NSDHG----HVVEACKNSLKKLQLDYLDLYLVHYPlatkhsgvgttaslldenkvldiDVTVSLETTWHDME 147
Cdd:cd19143 84 fWggggppPNDRGlsrkHIVEGTKASLKRLQLDYVDLVFCHRP-----------------------DPATPIEETVRAMN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 148 KTVSLGLVRSIGLSNYELFLTRDCLSYAK----IKPQVSQFETHpYFQRESL----VRFCKKHGV-----VPMAHTPLGG 214
Cdd:cd19143 141 DLIDQGKAFYWGTSEWSAQQIEEAHEIADrlglIPPVMEQPQYN-LFHRERVeveyAPLYEKYGLgtttwSPLASGLLTG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 215 ------------ATANVKAFGSISPLEDPVLIGLAKKYQK-------SVAQIALRWNI--ERGTPVIPKSSKVERLKENL 273
Cdd:cd19143 220 kynngipegsrlALPGYEWLKDRKEELGQEKIEKVRKLKPiaeelgcSLAQLAIAWCLknPNVSTVITGATKVEQLEENL 299
|
330 340
....*....|....*....|
7S5I_A 274 EVLNFkLEKEDIELINTIDK 293
Cdd:cd19143 300 KALEV-LPKLTPEVMEKIEA 318
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
153-291 |
1.28e-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: 381327 [Multi-domain] Cd Length: 304 Bit Score: 42.97 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 153 GLVRSIGLSNYELFLTRDCLSyAKIKP-----QVSQFETHPyfqRESLVRFCKKHGVVPMAHTPLGGA------------ 215
Cdd:cd19101 135 GKIRHLGLTNFDTERLREILD-AGVPIvsnqvQYSLLDRRP---ENGMAALCEDHGIKLLAYGTLAGGllsekylgvpep 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 216 ------TAN-------VKAFGSISPLED--PVLIGLAKKYQKSVAQIALRWNIERgtP----VIPKSSKVERLKENLEVL 276
Cdd:cd19101 211 tgpaleTRSlqkyklmIDEWGGWDLFQEllRTLKAIADKHGVSIANVAVRWVLDQ--PgvagVIVGARNSEHIDDNVRAF 288
|
170
....*....|....*
7S5I_A 277 NFKLEKEDIELINTI 291
Cdd:cd19101 289 SFRLDDEDRAAIDAV 303
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
13-277 |
1.65e-04 |
|
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: 42.16 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 13 PVIGLGLWRLEKEELRSA--------ILNAIKLGYRHFDAAAHY---KTEIDVGNAIAEaiqsglVKREELFITSK--VW 79
Cdd:cd19096 1 SVLGFGTMRLPESDDDSIdeekaiemIRYAIDAGINYFDTAYGYgggKSEEILGEALKE------GPREKFYLATKlpPW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 80 N-SDHGHVVEACKNSLKKLQLDYLDLYLVHyplatkhsGVGTTASL--LDENKVLDIdvtvslettwhdMEKTVSLGLVR 156
Cdd:cd19096 75 SvKSAEDFRRILEESLKRLGVDYIDFYLLH--------GLNSPEWLekARKGGLLEF------------LEKAKKEGLIR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 157 SIGLS---NYELFLtrdclsyaKIkpqvsqFETHP--------------YFQRESLVRFCKKHGVVPMAHTPLGGatanv 219
Cdd:cd19096 135 HIGFSfhdSPELLK--------EI------LDSYDfdfvqlqynyldqeNQAGRPGIEYAAKKGMGVIIMEPLKG----- 195
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 220 kafGSISPLEDPVLIgLAKKYQKSVAQIALRW--NIERGTPVIPKSSKVERLKENLEVLN 277
Cdd:cd19096 196 ---GGLANNPPEALA-ILCGAPLSPAEWALRFllSHPEVTTVLSGMSTPEQLDENIAAAD 251
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
153-288 |
1.96e-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: 381329 [Multi-domain] Cd Length: 299 Bit Score: 42.32 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 153 GLVRSIGLSNY---ELFLTRDCLSYAKIKpqVSQFETHpY--FQRES----LVRFCKKHGVVPMA--------------- 208
Cdd:cd19103 135 GKVKHVGVSNHnlaEIKRANEILAKAGVS--LSAVQNH-YslLYRSSeeagILDYCKENGITFFAymvleqgalsgkydt 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 209 HTPLGGATANVKAFGSISP-LED--PVLIGLAKKYQKSVAQIALRWNIERGTPVIPKSSKVERLKENLEVLNFKLEKEDI 285
Cdd:cd19103 212 KHPLPEGSGRAETYNPLLPqLEEltAVMAEIGAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDDEI 291
|
...
7S5I_A 286 ELI 288
Cdd:cd19103 292 KEL 294
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
25-78 |
5.93e-04 |
|
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: 40.77 E-value: 5.93e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
7S5I_A 25 EELRSAILNAIKLGYRHFDAAAHY---KTEIDVGNAIAEaiqsglVKREELFITSKV 78
Cdd:cd19161 20 ADADATLDAAWDSGIRYFDTAPMYghgLAEHRLGDFLRE------KPRDEFVLSTKV 70
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
8-292 |
1.13e-03 |
|
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: 40.07 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 8 NGFEMPVIGLGLW-----RLEKEELRSAILNAIKLGYRHFDAAAHY---KTEIDVGNAIAeaiQSGLvKREELFITSKVW 79
Cdd:cd19158 9 SGLRVSCLGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIK---KKGW-RRSSLVITTKIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 80 -----NSDHG----HVVEACKNSLKKLQLDYLDLYLVHYPlatkhsgvgttaslldenkvldiDVTVSLETTWHDMEKTV 150
Cdd:cd19158 85 wggkaETERGlsrkHIIEGLKASLERLQLEYVDVVFANRP-----------------------DPNTPMEETVRAMTHVI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 151 SLGLVRSIGLSNYELFLTRDCLSYAK----IKPQVSQFETHpYFQRE----SLVRFCKKHGVVPMAHTPLGGATANVKAF 222
Cdd:cd19158 142 NQGMAMYWGTSRWSSMEIMEAYSVARqfnlIPPICEQAEYH-MFQREkvevQLPELFHKIGVGAMTWSPLACGIVSGKYD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 223 GSISP-----------LEDPVLI--------------GLAKKYQKSVAQIALRWNI--ERGTPVIPKSSKVERLKENLEV 275
Cdd:cd19158 221 SGIPPysraslkgyqwLKDKILSeegrrqqaklkelqAIAERLGCTLPQLAIAWCLrnEGVSSVLLGASNAEQLMENIGA 300
|
330
....*....|....*..
7S5I_A 276 LNFkLEKEDIELINTID 292
Cdd:cd19158 301 IQV-LPKLSSSIVHEID 316
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
13-78 |
1.88e-03 |
|
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: 39.26 E-value: 1.88e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
7S5I_A 13 PVIGLG------LWRLEKEELRSAILNAIKLGYRHFDAAAHY---KTEIDVGNAIAEAiqsglvKREELFITSKV 78
Cdd:cd19162 1 PRLGLGaaslgnLARAGEDEAAATLDAAWDAGIRYFDTAPLYglgLSERRLGAALARH------PRAEYVVSTKV 69
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
153-291 |
2.12e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 39.18 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7S5I_A 153 GLVRSIGLSNyelfLTRDCLSYA-KIKPQVSQFETHPYFQR--ESLVRFCKKHGVVPMAHTPLGGatanvkafgsISPLE 229
Cdd:PRK10376 157 GLVRHIGLSN----VTPTQVAEArKIAEIVCVQNHYNLAHRadDALIDALARDGIAYVPFFPLGG----------FTPLQ 222
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
7S5I_A 230 DPVLIGLAKKYQKSVAQIALRWNIERgTP---VIPKSSKVERLKENLEVLNFKLEKEDIELINTI 291
Cdd:PRK10376 223 SSTLSDVAASLGATPMQVALAWLLQR-SPnilLIPGTSSVAHLRENLAAAELVLSEEVLAELDGI 286
|
|
| |
