|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
7-287 |
0e+00 |
|
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: 566.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 7 APCGLPRIGLGTAVQGPRPDPVRAAVLRAIQLGYRHFDTAAHYATEAPIGEAAAEAVRTGLVASREDLFVTSKVWCADAH 86
Cdd:cd19124 1 SGQTMPVIGMGTASDPPSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKSRDELFVTSKLWCSDAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 87 RDRVLPALRRTLSNLQMEYVDLYMVHWPVTMKAGRFTAPFTPEDFEPFDMRAVWEAMEECHRLGLAKAIGVCNFSCKKLE 166
Cdd:cd19124 81 PDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKPGKFSFPIEEEDFLPFDIKGVWEAMEECQRLGLTKAIGVSNFSCKKLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 167 TLLSFATIPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLGAKGTHWGSDSVMDSGVLHEIAKSKGKTVAQVCLRWV 246
Cdd:cd19124 161 ELLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTKWGSNAVMESDVLKEIAAAKGKTVAQVSLRWV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1279751533 247 YEQGDCLIVKSFDEGRMKENLDIVDWELSEEERQRISKIPQ 287
Cdd:cd19124 241 YEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEIPQ 281
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
11-289 |
3.83e-116 |
|
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: 336.63 E-value: 3.83e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTAVQGPrpDPVRAAVLRAIQLGYRHFDTAAHYATEAPIGEAAAEAVRTGLVaSREDLFVTSKVWCADAHRDRV 90
Cdd:cd19125 11 IPAVGLGTWQADP--GVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVV-KREDLFITSKLWCTDHAPEDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 91 LPALRRTLSNLQMEYVDLYMVHWPVTMKAGrfTAPFTPEDFEPFDMRAVWEAMEECHRLGLAKAIGVCNFSCKKLETLLS 170
Cdd:cd19125 88 PPALEKTLKDLQLDYLDLYLIHWPVRLKKG--AHMPEPEEVLPPDIPSTWKAMEKLVDSGKVRAIGVSNFSVKKLEDLLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 171 FATIPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLGAKGTHWGSDSVMDSGVLHEIAKSKGKTVAQVCLRWVYEQG 250
Cdd:cd19125 166 VARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGTTWVKKNVLKDPIVTKVAEKLGKTPAQVALRWGLQRG 245
|
250 260 270
....*....|....*....|....*....|....*....
gi 1279751533 251 DCLIVKSFDEGRMKENLDIVDWELSEEERQRISKIPQRK 289
Cdd:cd19125 246 TSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSIEQQR 284
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
11-282 |
2.66e-114 |
|
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. The family includes AKR1A/B/C/D/E/G/I, AKR2A/B/C/D/E, AKR3A/B/C/D/E/G, AKR4A/B/C, AKR5A/B/C/D/E/F/G/H, and similar proteins.
Pssm-ID: 381297 [Multi-domain] Cd Length: 251 Bit Score: 330.21 E-value: 2.66e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTAvqGPRPDPVRAAVLRAIQLGYRHFDTAAHYATEAPIGEAaaeaVRTGLVaSREDLFVTSKVWCADAHRDRV 90
Cdd:cd19071 1 MPLIGLGTY--KLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEA----IRESGV-PREELFITTKLWPTDHGYERV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 91 LPALRRTLSNLQMEYVDLYMVHWPVTMKagrftapftpEDFEPFDMRAVWEAMEECHRLGLAKAIGVCNFSCKKLETLLS 170
Cdd:cd19071 74 REALEESLKDLGLDYLDLYLIHWPVPGK----------EGGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 171 FATIPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLGakgthWGSDSVMDSGVLHEIAKSKGKTVAQVCLRWVYEQG 250
Cdd:cd19071 144 AARIKPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLG-----RGRRPLLDDPVLKEIAKKYGKTPAQVLLRWALQRG 218
|
250 260 270
....*....|....*....|....*....|..
gi 1279751533 251 DCLIVKSFDEGRMKENLDIVDWELSEEERQRI 282
Cdd:cd19071 219 VVVIPKSSNPERIKENLDVFDFELSEEDMAAI 250
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
11-296 |
8.49e-107 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 311.60 E-value: 8.49e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTAvqGPRPDPVRAAVLRAIQLGYRHFDTAAHYATEAPIGEAAAEAvrtGLvaSREDLFVTSKVWCADAHRDRV 90
Cdd:COG0656 5 IPALGLGTW--QLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAAS---GV--PREELFVTTKVWNDNHGYDDT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 91 LPALRRTLSNLQMEYVDLYMVHWPVtmkagrftapftpedfePFDMRAVWEAMEECHRLGLAKAIGVCNFSCKKLETLLS 170
Cdd:COG0656 78 LAAFEESLERLGLDYLDLYLIHWPG-----------------PGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 171 FATIPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLGAKGthwgsdsVMDSGVLHEIAKSKGKTVAQVCLRWVYEQG 250
Cdd:COG0656 141 ETGVKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGRGK-------LLDDPVLAEIAEKHGKTPAQVVLRWHLQRG 213
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1279751533 251 DCLIVKSFDEGRMKENLDIVDWELSEEERQRISkipqrKINQGRRY 296
Cdd:COG0656 214 VVVIPKSVTPERIRENLDAFDFELSDEDMAAID-----ALDRGERL 254
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
11-297 |
3.21e-103 |
|
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: 303.95 E-value: 3.21e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTavQGPRPDPVRAAVLRAIQLGYRHFDTAAHYATEAPIGEAAAEAVRTGLVAsREDLFVTSKVWCADAHRDRV 90
Cdd:cd19123 12 IPALGLGT--WKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVK-REDLWITSKLWNNSHAPEDV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 91 LPALRRTLSNLQMEYVDLYMVHWPVTMKAGRFTaPFTPEDFEPFD---MRAVWEAMEECHRLGLAKAIGVCNFSCKKLET 167
Cdd:cd19123 89 LPALEKTLADLQLDYLDLYLMHWPVALKKGVGF-PESGEDLLSLSpipLEDTWRAMEELVDKGLCRHIGVSNFSVKKLED 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 168 LLSFATIPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLGAKGT-----HWGSDSVMDSGVLHEIAKSKGKTVAQVC 242
Cdd:cd19123 168 LLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDRpaamkAEGEPVLLEDPVINKIAEKHGASPAQVL 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1279751533 243 LRWVYEQGDCLIVKSFDEGRMKENLDIVDWELSEEERQRISkipqrKINQGRRYV 297
Cdd:cd19123 248 IAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIA-----ALDRHHRYV 297
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
11-297 |
1.04e-102 |
|
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: 302.66 E-value: 1.04e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTAvQGPRPDPVRAAVLRAIQLGYRHFDTAAHYATEAPIGEAAAEAVRTGLVaSREDLFVTSKVWCADAHRDRV 90
Cdd:cd19116 11 IPAIALGTW-KLKDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVV-KREDLFITTKLWNSYHEREQV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 91 LPALRRTLSNLQMEYVDLYMVHWPVTMKAGRFTAPFTPEDFEPFDMRAVWEAMEECHRLGLAKAIGVCNFSCKKLETLLS 170
Cdd:cd19116 89 EPALRESLKRLGLDYVDLYLIHWPVAFKENNDSESNGDGSLSDIDYLETWRGMEDLVKLGLTRSIGVSNFNSEQINRLLS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 171 FATIPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLG--AKGTHWGSDSVMDSGVLHEIAKSKGKTVAQVCLRWVYE 248
Cdd:cd19116 169 NCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGrlVPRGQTNPPPRLDDPTLVAIAKKYGKTTAQIVLRYLID 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1279751533 249 QGDCLIVKSFDEGRMKENLDIVDWELSEEErqrISKIpqRKINQGRRYV 297
Cdd:cd19116 249 RGVVPIPKSSNKKRIKENIDIFDFQLTPEE---VAAL--NSFNTNQRVY 292
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
11-289 |
1.37e-87 |
|
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: 264.66 E-value: 1.37e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTaVQGpRPDPVRAAVLRAIQLGYRHFDTAAHYATEAPIGEAAAEAVRTGLVaSREDLFVTSKVWCADAHRDRV 90
Cdd:cd19154 12 MPLIGLGT-WQS-KGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVV-KREDLFITTKLWTHEHAPEDV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 91 LPALRRTLSNLQMEYVDLYMVHWPVTMK--AGRFTAPFTPED-FEPFDMRAVWEAMEECHRLGLAKAIGVCNFSCKKLET 167
Cdd:cd19154 89 EEALRESLKKLQLEYVDLYLIHAPAAFKddEGESGTMENGMSiHDAVDVEDVWRGMEKVYDEGLTKAIGVSNFNNDQIQR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 168 LLSFATIPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLGAKG--------THWGSDSVMDSGVLHEIAKSKGKTVA 239
Cdd:cd19154 169 ILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSPGranftkstGVSPAPNLLQDPIVKAIAEKHGKTPA 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1279751533 240 QVCLRWVYEQGDCLIVKSFDEGRMKENLDIVDWELSEEERQRISKIPQRK 289
Cdd:cd19154 249 QVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSL 298
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
11-285 |
4.06e-87 |
|
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: 261.80 E-value: 4.06e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGT-AVQGPrpDPVRAAVLRAIQLGYRHFDTAAHYATEAPIGEAAAEA-VRTGLvaSREDLFVTSKVWCADAHRD 88
Cdd:cd19136 1 MPILGLGTfRLRGE--EEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLlPKYGL--SREDIFITSKLAPKDQGYE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 89 RVLPALRRTLSNLQMEYVDLYMVHWPVTMKagrftapFTPEDFEPFDMRAV-WEAMEECHRLGLAKAIGVCNFSCKKLET 167
Cdd:cd19136 77 KARAACLGSLERLGTDYLDLYLIHWPGVQG-------LKPSDPRNAELRREsWRALEDLYKEGKLRAIGVSNYTVRHLEE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 168 LLSFATIPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLGAkgthwGSDSVMDSGVLHEIAKSKGKTVAQVCLRWVY 247
Cdd:cd19136 150 LLKYCEVPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGS-----GDLRLLEDPTVLAIAKKYGRTPAQVLLRWAL 224
|
250 260 270
....*....|....*....|....*....|....*...
gi 1279751533 248 EQGDCLIVKSFDEGRMKENLDIVDWELSEEERQRISKI 285
Cdd:cd19136 225 QQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
11-297 |
5.51e-85 |
|
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: 258.08 E-value: 5.51e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTavQGPRPDPVRAAVLRAIQLGYRHFDTAAHYATEAPIGEAAAEAVRTGLVASREDLFVTSKVWCADAHRDRV 90
Cdd:cd19106 7 MPLIGLGT--WKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPGKAVPREDLFVTSKLWNTKHHPEDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 91 LPALRRTLSNLQMEYVDLYMVHWPVTMKAGRFTAPFTPED---FEPFDMRAVWEAMEECHRLGLAKAIGVCNFSCKKLET 167
Cdd:cd19106 85 EPALRKTLKDLQLDYLDLYLIHWPYAFERGDNPFPKNPDGtirYDSTHYKETWKAMEKLVDKGLVKAIGLSNFNSRQIDD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 168 LLSFATIPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLGAKGTHW---GSDSVMDSGVLHEIAKSKGKTVAQVCLR 244
Cdd:cd19106 165 ILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPDRPWakpDEPVLLEEPKVKALAKKYNKSPAQILLR 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1279751533 245 WVYEQGDCLIVKSFDEGRMKENLDIVDWELSEEERQRISkipqrKINQGRRYV 297
Cdd:cd19106 245 WQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLD-----ALNRNWRYI 292
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
12-285 |
1.30e-78 |
|
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: 239.78 E-value: 1.30e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 12 PRIGLGTaVQGPRPDPVRAAVLRAIQLGYRHFDTAAHYATEAPIGEAAAeavRTGLvaSREDLFVTSKVWCADAHRDRVL 91
Cdd:cd19133 10 PILGFGV-FQIPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIK---KSGI--PREELFITTKLWIQDAGYEKAK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 92 PALRRTLSNLQMEYVDLYMVHWPVTmkagrftapftpedfepfDMRAVWEAMEECHRLGLAKAIGVCNFSCKKLETLLSF 171
Cdd:cd19133 84 KAFERSLKRLGLDYLDLYLIHQPFG------------------DVYGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLILH 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 172 ATIPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLGAkgthwGSDSVMDSGVLHEIAKSKGKTVAQVCLRWVYEQGD 251
Cdd:cd19133 146 NEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAE-----GRNNLFENPVLTEIAEKYGKSVAQVILRWLIQRGI 220
|
250 260 270
....*....|....*....|....*....|....
gi 1279751533 252 CLIVKSFDEGRMKENLDIVDWELSEEERQRISKI 285
Cdd:cd19133 221 VVIPKSVRPERIAENFDIFDFELSDEDMEAIAAL 254
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
11-296 |
9.87e-78 |
|
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 238.06 E-value: 9.87e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTaVQGPRPDPVRAAVLRAIQLGYRHFDTAAHYATEAPIGEAAAEAVrtglvASREDLFVTSKVWCADAHRDRV 90
Cdd:cd19157 10 MPWLGLGV-FKVEEGSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKESG-----IPREELFITSKVWNADQGYDST 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 91 LPALRRTLSNLQMEYVDLYMVHWPVTMKagrftapftpedfepfdMRAVWEAMEECHRLGLAKAIGVCNFSCKKLETLLS 170
Cdd:cd19157 84 LKAFEASLERLGLDYLDLYLIHWPVKGK-----------------YKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 171 FATIPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLgAKGthwgsdSVMDSGVLHEIAKSKGKTVAQVCLRWVYEQG 250
Cdd:cd19157 147 DAEIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPL-MQG------QLLDNPVLKEIAEKYNKSVAQVILRWDLQNG 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1279751533 251 DCLIVKSFDEGRMKENLDIVDWELSEEERQRISkipqrKINQGRRY 296
Cdd:cd19157 220 VVTIPKSIKEHRIIENADVFDFELSQEDMDKID-----ALNENLRV 260
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
11-285 |
1.10e-77 |
|
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: 237.66 E-value: 1.10e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGtaVQGPRPDPVRAAVLRAIQLGYRHFDTAAHYATEAPIGEAAAEAvrtGLvaSREDLFVTSKVWCADAHRDRV 90
Cdd:cd19131 10 IPQLGLG--VWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRAS---GV--PREELFITTKLWNSDQGYDST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 91 LPALRRTLSNLQMEYVDLYMVHWPVTMKaGRFTApftpedfepfdmraVWEAMEECHRLGLAKAIGVCNFSCKKLETLLS 170
Cdd:cd19131 83 LRAFDESLRKLGLDYVDLYLIHWPVPAQ-DKYVE--------------TWKALIELKKEGRVKSIGVSNFTIEHLQRLID 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 171 FATIPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLGAKGthwgsdsVMDSGVLHEIAKSKGKTVAQVCLRWVYEQG 250
Cdd:cd19131 148 ETGVVPVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGG-------LLSDPVIGEIAEKHGKTPAQVVIRWHLQNG 220
|
250 260 270
....*....|....*....|....*....|....*
gi 1279751533 251 DCLIVKSFDEGRMKENLDIVDWELSEEERQRISKI 285
Cdd:cd19131 221 LVVIPKSVTPSRIAENFDVFDFELDADDMQAIAGL 255
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
11-278 |
2.36e-77 |
|
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: 238.28 E-value: 2.36e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTAV--QGPRPDPVRAAVLrAIQLGYRHFDTAAHYATEAPIGEAAAEAVRTGLVaSREDLFVTSKVWCADAHRD 88
Cdd:cd19108 11 IPVLGFGTYApeEVPKSKALEATKL-AIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTV-KREDIFYTSKLWCTFHRPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 89 RVLPALRRTLSNLQMEYVDLYMVHWPVTMKAGRftaPFTPED------FEPFDMRAVWEAMEECHRLGLAKAIGVCNFSC 162
Cdd:cd19108 89 LVRPALEKSLKKLQLDYVDLYLIHFPVALKPGE---ELFPKDengkliFDTVDLCATWEAMEKCKDAGLAKSIGVSNFNR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 163 KKLETLLSfatIP-----PVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLGA-KGTHW---GSDSVMDSGVLHEIAKS 233
Cdd:cd19108 166 RQLEMILN---KPglkykPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSqRDKEWvdqNSPVLLEDPVLCALAKK 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1279751533 234 KGKTVAQVCLRWVYEQGDCLIVKSFDEGRMKENLDIVDWELSEEE 278
Cdd:cd19108 243 HKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSED 287
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
11-285 |
6.06e-77 |
|
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: 236.54 E-value: 6.06e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTAVQgpRPDPVRAAVLRAIQLGYRHFDTAAHYATEAPIGEAAAEAVRTGLVASREDLFVTSKVWCADAHRDRV 90
Cdd:cd19118 7 IPAIGLGTWQA--EPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEEPGVKREDLFITSKLWNNSHRPEYV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 91 LPALRRTLSNLQMEYVDLYMVHWPVTMKAGRFTAPFTPEDFEPFDMR--------AVWEAMEECHRLGLAKAIGVCNFSC 162
Cdd:cd19118 85 EPALDDTLKELGLDYLDLYLIHWPVAFKPTGDLNPLTAVPTNGGEVDldlsvslvDTWKAMVELKKTGKVKSIGVSNFSI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 163 KKLETLLSFATIPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLGakGTHWGSDSVMDSGVLHEIAKSKGKTVAQVC 242
Cdd:cd19118 165 DHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLG--NNLAGLPLLVQHPEVKAIAAKLGKTPAQVL 242
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1279751533 243 LRWVYEQGDCLIVKSFDEGRMKENLDIVdwELSEEERQRISKI 285
Cdd:cd19118 243 IAWGIQRGHSVIPKSVTPSRIRSNFEQV--ELSDDEFNAVTAL 283
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
11-285 |
1.49e-76 |
|
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: 236.61 E-value: 1.49e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGtaVQGPRPDPVRAAVLRAIQLGYRHFDTAAHYATEAPIGEAAAEAVRTGLVaSREDLFVTSKVWCADahRDRV 90
Cdd:cd19112 11 MPVIGLG--VWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLV-KREDLFITTKLWNSD--HGHV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 91 LPALRRTLSNLQMEYVDLYMVHWPVtmkAGRFTAPFTP----------EDFEPFDMRAVWEAMEECHRLGLAKAIGVCNF 160
Cdd:cd19112 86 IEACKDSLKKLQLDYLDLYLVHFPV---ATKHTGVGTTgsalgedgvlDIDVTISLETTWHAMEKLVSAGLVRSIGISNY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 161 SCKKLETLLSFATIPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLG--AKGTHW-GSDSVMDSGVLHEIAKSKGKT 237
Cdd:cd19112 163 DIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGgaAANAEWfGSVSPLDDPVLKDLAKKYGKS 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1279751533 238 VAQVCLRWVYEQGDCLIVKSFDEGRMKENLDIVDWELSEEERQRISKI 285
Cdd:cd19112 243 AAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSL 290
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
11-282 |
4.76e-76 |
|
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: 232.93 E-value: 4.76e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTAvqGPRPDPVRAAVLRAIQLGYRHFDTAAHYATEAPIGEAAAEA-VRtglvasREDLFVTSKVWCADAHRDR 89
Cdd:cd19073 1 IPALGLGTW--QLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAESgVP------REDLFITTKVWRDHLRPED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 90 VLPALRRTLSNLQMEYVDLYMVHWPVtmkagrftapftPEDfepfDMRAVWEAMEECHRLGLAKAIGVCNFSCKKLETLL 169
Cdd:cd19073 73 LKKSVDRSLEKLGTDYVDLLLIHWPN------------PTV----PLEETLGALKELKEAGKVKSIGVSNFTIELLEEAL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 170 SFATIPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLgAKGThwgsdsVMDSGVLHEIAKSKGKTVAQVCLRWVYEQ 249
Cdd:cd19073 137 DISPLPIAVNQVEFHPFLYQAELLEYCRENDIVITAYSPL-ARGE------VLRDPVIQEIAEKYDKTPAQVALRWLVQK 209
|
250 260 270
....*....|....*....|....*....|...
gi 1279751533 250 GDCLIVKSFDEGRMKENLDIVDWELSEEERQRI 282
Cdd:cd19073 210 GIVVIPKASSEDHLKENLAIFDWELTSEDVAKI 242
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
11-289 |
7.42e-76 |
|
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: 233.28 E-value: 7.42e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTAVQ---GPRPDPVRA---AVLRAIQLGYRHFDTAAHYATEAPIGEAAAEAVrtglvASREDLFVTSKVWCAD 84
Cdd:cd19120 4 IPAIAFGTGTAwykSGDDDIQRDlvdSVKLALKAGFRHIDTAEMYGNEKEVGEALKESG-----VPREDLFITTKVSPGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 85 AHrdrVLPALRRTLSNLQMEYVDLYMVHwpvtmkagrftAPFTpEDFEPFDMRAVWEAMEECHRLGLAKAIGVCNFSCKK 164
Cdd:cd19120 79 KD---PREALRKSLAKLGVDYVDLYLIH-----------SPFF-AKEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIED 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 165 LETLLSFATIPPVVNQVEINP--VWQQRKLREFCRAKGIQLCAYSPLGAkgTHWGSDSVMDSgVLHEIAKSKGKTVAQVC 242
Cdd:cd19120 144 LEELLDTAKIKPAVNQIEFHPylYPQQPALLEYCREHGIVVSAYSPLSP--LTRDAGGPLDP-VLEKIAEKYGVTPAQVL 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1279751533 243 LRWVYEQGDCLIVKSFDEGRMKENLDIVDWELSEEERQRISKIPQRK 289
Cdd:cd19120 221 LRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEIDKAGKQK 267
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
11-285 |
3.14e-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: 231.17 E-value: 3.14e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTaVQGPRPDPVRAAVLRAIQLGYRHFDTAAHYATEAPIGEAAAEavrTGLvaSREDLFVTSKVWCADAHRDRV 90
Cdd:cd19126 9 MPWLGLGV-FQTPDGDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRE---SGV--PREELFVTTKLWNDDQRARRT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 91 LPALRRTLSNLQMEYVDLYMVHWPVTMKAGRftapftpedfepfdmraVWEAMEECHRLGLAKAIGVCNFSCKKLETLLS 170
Cdd:cd19126 83 EDAFQESLDRLGLDYVDLYLIHWPGKDKFID-----------------TWKALEKLYASGKVKAIGVSNFQEHHLEELLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 171 FATIPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLGAKGthwgsdsVMDSGVLHEIAKSKGKTVAQVCLRWVYEQG 250
Cdd:cd19126 146 HADVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQGG-------LLSNPVLAAIGEKYGKSAAQVVLRWDIQHG 218
|
250 260 270
....*....|....*....|....*....|....*
gi 1279751533 251 DCLIVKSFDEGRMKENLDIVDWELSEEERQRISKI 285
Cdd:cd19126 219 VVTIPKSVHASRIKENADIFDFELSEDDMTAIDAL 253
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
11-285 |
4.76e-73 |
|
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: 225.60 E-value: 4.76e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTavQGPRPDPVRAAVLRAIQLGYRHFDTAAHYATEAPIGEAAAeavRTGLvaSREDLFVTSKVWCADAHRDRV 90
Cdd:cd19140 8 IPALGLGT--YPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIA---ASGV--PRDELFLTTKVWPDNYSPDDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 91 LPALRRTLSNLQMEYVDLYMVHWPvtmkagrftapfTPEDfepfDMRAVWEAMEECHRLGLAKAIGVCNFSCKKLETLLS 170
Cdd:cd19140 81 LASVEESLRKLRTDYVDLLLLHWP------------NKDV----PLAETLGALNEAQEAGLARHIGVSNFTVALLREAVE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 171 FATIPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLgAKGthwgsdSVMDSGVLHEIAKSKGKTVAQVCLRWVYEQG 250
Cdd:cd19140 145 LSEAPLFTNQVEYHPYLDQRKLLDAAREHGIALTAYSPL-ARG------EVLKDPVLQEIGRKHGKTPAQVALRWLLQQE 217
|
250 260 270
....*....|....*....|....*....|....*.
gi 1279751533 251 D-CLIVKSFDEGRMKENLDIVDWELSEEERQRISKI 285
Cdd:cd19140 218 GvAAIPKATNPERLEENLDIFDFTLSDEEMARIAAL 253
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
11-288 |
1.85e-71 |
|
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: 223.56 E-value: 1.85e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTAvQGPrPDPVRAAVLRAIQLGYRHFDTAAHYATEAPIGEAAAEAVRTGLVaSREDLFVTSKVWCADAHRDRV 90
Cdd:cd19155 12 MPVVGLGTW-QSS-PEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKV-KREELFIVTKLPPGGNRREKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 91 LPALRRTLSNLQMEYVDLYMVHWPVTMKAGRFTAPFTPEDFE-----PFDMRAVWEAMEECHRLGLAKAIGVCNFSCKKL 165
Cdd:cd19155 89 EKFLLKSLEKLQLDYVDLYLIHFPVGSLSKEDDSGKLDPTGEhkqdyTTDLLDIWKAMEAQVDQGLTRSIGLSNFNREQM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 166 ETLLSFATIPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLGAKGTH----------WGSDSVMDSGVLHEIAKSKG 235
Cdd:cd19155 169 ARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPGAAhfspgtgspsGSSPDLLQDPVVKAIAERHG 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1279751533 236 KTVAQVCLRWVYEQGDCLIVKSFDEGRMKENLDIVDWELSEEERQRISKIPQR 288
Cdd:cd19155 249 KSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKN 301
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
11-286 |
2.51e-71 |
|
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: 221.43 E-value: 2.51e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTAVQGPRPDpvrAAVLRAIQ-LGYRHFDTAAHYATEAPIGEAAAEAvrtGLvaSREDLFVTSKVWCADAHRDR 89
Cdd:cd19135 13 MPILGLGTSHSGGYSH---EAVVYALKeCGYRHIDTAKRYGCEELLGKAIKES---GV--PREDLFLTTKLWPSDYGYES 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 90 VLPALRRTLSNLQMEYVDLYMVHWPVTMKAGRFTAPFTPEdfepfdmraVWEAMEECHRLGLAKAIGVCNFSCKKLETLL 169
Cdd:cd19135 85 TKQAFEASLKRLGVDYLDLYLLHWPDCPSSGKNVKETRAE---------TWRALEELYDEGLCRAIGVSNFLIEHLEQLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 170 SFATIPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLgAKGTHWGSDSVMdsgvlhEIAKSKGKTVAQVCLRWVYEQ 249
Cdd:cd19135 156 EDCSVVPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPL-AKGKALEEPTVT------ELAKKYQKTPAQILIRWSIQN 228
|
250 260 270
....*....|....*....|....*....|....*..
gi 1279751533 250 GDCLIVKSFDEGRMKENLDIVDWELSEEERQRISKIP 286
Cdd:cd19135 229 GVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSLH 265
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
11-287 |
2.53e-71 |
|
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: 221.37 E-value: 2.53e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGT-AVQGprpDPVRAAVLRAIQLGYRHFDTAAHYATEAPIGEAaaeaVRTGLVAsREDLFVTSKVWCADAHRDR 89
Cdd:cd19132 7 IPAIGFGTyPLKG---DEGVEAVVAALQAGYRLLDTAFNYENEGAVGEA----VRRSGVP-REELFVTTKLPGRHHGYEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 90 VLPALRRTLSNLQMEYVDLYMVHWPVTmKAGRFTApftpedfepfdmraVWEAMEECHRLGLAKAIGVCNFSCKKLETLL 169
Cdd:cd19132 79 ALRTIEESLYRLGLDYVDLYLIHWPNP-SRDLYVE--------------AWQALIEAREEGLVRSIGVSNFLPEHLDRLI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 170 SFATIPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLGakgthwGSDSVMDSGVLHEIAKSKGKTVAQVCLRWVYEQ 249
Cdd:cd19132 144 DETGVTPAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLG------RGSGLLDEPVIKAIAEKHGKTPAQVVLRWHVQL 217
|
250 260 270
....*....|....*....|....*....|....*...
gi 1279751533 250 GDCLIVKSFDEGRMKENLDIVDWELSEEERQRISKIPQ 287
Cdd:cd19132 218 GVVPIPKSANPERQRENLAIFDFELSDEDMAAIAALDR 255
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
11-288 |
3.47e-71 |
|
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: 221.99 E-value: 3.47e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTaVQGPrPDPVRAAVLRAIQLGYRHFDTAAHYATEAPIGEAAAEAVRTGLVaSREDLFVTSKVWCADAHRDRV 90
Cdd:cd19111 4 MPVIGLGT-YQSP-PEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKL-KREEVFITTKLPPVYLEFKDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 91 LPALRRTLSNLQMEYVDLYMVHWPV--TMKAGRFTAPFTPEDFEpfdmrAVWEAMEECHRLGLAKAIGVCNFSCKKLETL 168
Cdd:cd19111 81 EKSLEKSLENLKLPYVDLYLIHHPCgfVNKKDKGERELASSDVT-----SVWRAMEALVSEGKVKSIGLSNFNPRQINKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 169 LSFATIPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLGAKG----THWGS--DSVMDSGVLhEIAKSKGKTVAQVC 242
Cdd:cd19111 156 LAYAKVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSPGranqSLWPDqpDLLEDPTVL-AIAKELDKTPAQVL 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1279751533 243 LRWVYEQGDCLIVKSFDEGRMKENLDIVDWELSEEERQRISKIPQR 288
Cdd:cd19111 235 LRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRN 280
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
11-289 |
3.57e-70 |
|
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: 219.29 E-value: 3.57e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTavQGPRPDPVRAAVLRAIQLGYRHFDTAAHYATEAPIGEAaaeaVRTGLVAsREDLFVTSKVWCaDAHRdRV 90
Cdd:cd19117 14 IPAVGLGT--WQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQG----IKDSGVP-REEIFITTKLWC-TWHR-RV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 91 LPALRRTLSNLQMEYVDLYMVHWPVTMKAGRFTAPF-----TPEDFEPFDMRAVWEAMEECHRLGLAKAIGVCNFSCKKL 165
Cdd:cd19117 85 EEALDQSLKKLGLDYVDLYLMHWPVPLDPDGNDFLFkkddgTKDHEPDWDFIKTWELMQKLPATGKVKAIGVSNFSIKNL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 166 ETLLS--FATIPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLGAKGThwgsdSVMDSGVLHEIAKSKGKTVAQVCL 243
Cdd:cd19117 165 EKLLAspSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTNA-----PLLKEPVIIKIAKKHGKTPAQVII 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1279751533 244 RWVYEQGDCLIVKSFDEGRMKENLDIvdWELSEEERQRISKIPQRK 289
Cdd:cd19117 240 SWGLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEIDELHKEY 283
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
11-303 |
8.61e-70 |
|
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: 219.29 E-value: 8.61e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTaVQGPRPDP---VRAAVLRAIQLGYRHFDTAAHYATEAPIGEAAAEAVRTGLVaSREDLFVTSKVWCADAHR 87
Cdd:cd19109 4 IPIIGLGT-YSEPKTTPkgaCAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKV-KREDIFYCGKLWNTCHPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 88 DRVLPALRRTLSNLQMEYVDLYMVHWPVTMKAGrftAPFTPED------FEPFDMRAVWEAMEECHRLGLAKAIGVCNFS 161
Cdd:cd19109 82 ELVRPTLERTLKVLQLDYVDLYIIEMPMAFKPG---DEIYPRDengkwlYHKTNLCATWEALEACKDAGLVKSIGVSNFN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 162 CKKLETLLSFATIP--PVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLGAKGTH-W---GSDSVMDSGVLHEIAKSKG 235
Cdd:cd19109 159 RRQLELILNKPGLKhkPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDPiWvnvSSPPLLEDPLLNSIGKKYN 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1279751533 236 KTVAQVCLRWVYEQGDCLIVKSFDEGRMKENLDIVDWELSEEERQRISkipqrKINQGRRYV-----SEHGPY 303
Cdd:cd19109 239 KTAAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIE-----ALNKNVRYVellmwRDHPEY 306
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
11-296 |
2.58e-69 |
|
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: 216.62 E-value: 2.58e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTAvQGPRPDPVRAAVLRAIQLGYRHFDTAAHYATEAPIGEAAAEavrTGLvaSREDLFVTSKVWCADAHRDRV 90
Cdd:cd19156 9 MPRLGLGVW-RVQDGAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRE---SGV--PREEVFVTTKLWNSDQGYEST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 91 LPALRRTLSNLQMEYVDLYMVHWPVtmkAGRFtapftpedfepfdmRAVWEAMEECHRLGLAKAIGVCNFSCKKLETLLS 170
Cdd:cd19156 83 LAAFEESLEKLGLDYVDLYLIHWPV---KGKF--------------KDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 171 FATIPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLgakgthwGSDSVMDSGVLHEIAKSKGKTVAQVCLRWVYEQG 250
Cdd:cd19156 146 SCKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPL-------GQGKLLSNPVLKAIGKKYGKSAAQVIIRWDIQHG 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1279751533 251 DCLIVKSFDEGRMKENLDIVDWELSEEERQRISkipqrKINQGRRY 296
Cdd:cd19156 219 IITIPKSVHEERIQENFDVFDFELTAEEIRQID-----GLNTDHRY 259
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
11-278 |
2.68e-69 |
|
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: 218.06 E-value: 2.68e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTAvQGPrPDPVRAAVLRAIQLGYRHFDTAAHYATEAPIGEAAAEAVRTGLVaSREDLFVTSKVWCADAHRDRV 90
Cdd:cd19107 4 MPILGLGTW-KSP-PGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVV-KREDLFIVSKLWCTFHEKGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 91 LPALRRTLSNLQMEYVDLYMVHWPVTMKAGRftaPFTPEDFE----PFDMRAV--WEAMEECHRLGLAKAIGVCNFSCKK 164
Cdd:cd19107 81 KGACQKTLSDLKLDYLDLYLIHWPTGFKPGK---ELFPLDESgnviPSDTTFLdtWEAMEELVDEGLVKAIGVSNFNHLQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 165 LETLLSFATI--PPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLGAKGTHW---GSDSVMDSGVLHEIAKSKGKTVA 239
Cdd:cd19107 158 IERILNKPGLkyKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWakpEDPSLLEDPKIKEIAAKHNKTTA 237
|
250 260 270
....*....|....*....|....*....|....*....
gi 1279751533 240 QVCLRWVYEQGDCLIVKSFDEGRMKENLDIVDWELSEEE 278
Cdd:cd19107 238 QVLIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSED 276
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
12-285 |
3.78e-68 |
|
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), also called aldehyde reductase, is the prototype of this family. It catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
Pssm-ID: 381354 [Multi-domain] Cd Length: 277 Bit Score: 213.92 E-value: 3.78e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 12 PRIGLGTAVQGPRPDPvrAAVLRAIQLGYRHFDTAAHYATEAPIGEAAAEAVRTGLVaSREDLFVTSKVWCADAHRDRVL 91
Cdd:cd19128 2 PRLGFGTYKITESESK--EAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGV-KREDLFITSKLWPTMHQPENVK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 92 PALRRTLSNLQMEYVDLYMVHWPVTMKAGRFTAPFTPED---FEPFDMRAVWEAMEECHRLGLAKAIGVCNFSCKKLETL 168
Cdd:cd19128 79 EQLLITLQDLQLEYLDLFLIHWPLAFDMDTDGDPRDDNQiqsLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 169 LSFATIPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLGAKgTHWGSDSVMDSGVLHEIAKSKGKTVAQVCLRW--- 245
Cdd:cd19128 159 LNYCKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGS-YGDGNLTFLNDSELKALATKYNTTPPQVIIAWhlq 237
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1279751533 246 VYEQGDCLIVKSFDEGRMKENLDIVDWELSEEERQRISKI 285
Cdd:cd19128 238 KWPKNYSVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
32-296 |
8.48e-68 |
|
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: 214.21 E-value: 8.48e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 32 VLRAIQLGYRHFDTAAHYATEAPIGEAAAEAVRTGLVaSREDLFVTSKVWCADAHRDRVLPALRRTLSNLQMEYVDLYMV 111
Cdd:cd19115 32 VYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIV-KREDLFIVSKLWNTFHDGERVEPICRKQLADWGIDYFDLFLI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 112 HWPVTMKAGRFTAPFTPEDFEPFDMRA--------VWEAMEECHRLGLAKAIGVCNFSCKKLETLLSFATIPPVVNQVEI 183
Cdd:cd19115 111 HFPIALKYVDPAVRYPPGWFYDGKKVEfsnapiqeTWTAMEKLVDKGLARSIGVSNFSAQLLMDLLRYARIRPATLQIEH 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 184 NPVWQQRKLREFCRAKGIQLCAYSPLG-----------AKGThwgsDSVMDSGVLHEIAKSKGKTVAQVCLRWVYEQGDC 252
Cdd:cd19115 191 HPYLTQPRLVKYAQKEGIAVTAYSSFGpqsfleldlpgAKDT----PPLFEHDVIKSIAEKHGKTPAQVLLRWATQRGIA 266
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1279751533 253 LIVKSFDEGRMKENLDIVDWELSEEERQRISkipqrKINQGRRY 296
Cdd:cd19115 267 VIPKSNNPKRLAQNLDVTGFDLEAEEIKAIS-----ALDIGLRF 305
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
11-282 |
4.55e-67 |
|
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: 210.73 E-value: 4.55e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTaVQGPrPDPVRAAVLRAIQLGYRHFDTAAHYATEAPIGEAAAeavRTGLvaSREDLFVTSKVWCADAHRDRV 90
Cdd:cd19127 9 MPALGLGV-FQTP-PEETADAVATALADGYRLIDTAAAYGNEREVGEGIR---RSGV--DRSDIFVTTKLWISDYGYDKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 91 LPALRRTLSNLQMEYVDLYMVHWPVtmkagrftapftPEDFEpfDMRAVWEAMEECHRLGLAKAIGVCNFSCKKLETLLS 170
Cdd:cd19127 82 LRGFDASLRRLGLDYVDLYLLHWPV------------PNDFD--RTIQAYKALEKLLAEGRVRAIGVSNFTPEHLERLID 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 171 FATIPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLGAKGTHWGSD-----SVMDSGVLHEIAKSKGKTVAQVCLRW 245
Cdd:cd19127 148 ATTVVPAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGGVMRYGASGptgpgDVLQDPTITGLAEKYGKTPAQIVLRW 227
|
250 260 270
....*....|....*....|....*....|....*..
gi 1279751533 246 VYEQGDCLIVKSFDEGRMKENLDIVDWELSEEERQRI 282
Cdd:cd19127 228 HLQNGVSAIPKSVHPERIAENIDIFDFALSAEDMAAI 264
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
11-289 |
1.18e-64 |
|
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: 205.42 E-value: 1.18e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTAVQGPRPDPVRAAVLRAIQLGYRHFDTAAHYATEAPIGEAAAEAVRTGLVaSREDLFVTSKVWcaDAHRDRV 90
Cdd:cd19119 12 IPALGLGTASPHEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSI-KREELFITTKVW--PTFYDEV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 91 LPALRRTLSNLQMEYVDLYMVHWPVTMKA-----GRftaPFTPEDFEPFDMRA-------VWEAMEECHRLGLAKAIGVC 158
Cdd:cd19119 89 ERSLDESLKALGLDYVDLLLVHWPVCFEKdsddsGK---PFTPVNDDGKTRYAasgdhitTYKQLEKIYLDGRAKAIGVS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 159 NFSCKKLETLLSFATIPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLGAKGThwgsdSVMDSGVLHEIAKSKGKTV 238
Cdd:cd19119 166 NYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGA-----PNLKNPLVKKIAEKYNVST 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1279751533 239 AQVCLRWVYEQGDCLIVKSFDEGRMKENLDIVdwELSEEERQRISKIPQRK 289
Cdd:cd19119 241 GDILISYHVRQGVIVLPKSLKPVRIVSNGKIV--SLTKEDLQKLDDIGEKY 289
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
11-285 |
1.49e-64 |
|
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: 204.69 E-value: 1.49e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTAvQGPRPDpVRAAVLRAIQLGYRHFDTAAHYATEAPIGEAAAEAVRTGLvaSREDLFVTSKVWcaDAHRDRV 90
Cdd:cd19121 12 IPAVGLGTW-QAKAGE-VKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAIAGGV--KREDLFVTTKLW--STYHRRV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 91 LPALRRTLSNLQMEYVDLYMVHWPVTMKaGRFTAPFTPE------DFEP-FDMRAVWEAMEECHRLGLAKAIGVCNFSCK 163
Cdd:cd19121 86 ELCLDRSLKSLGLDYVDLYLVHWPVLLN-PNGNHDLFPTlpdgsrDLDWdWNHVDTWKQMEKVLKTGKTKAIGVSNYSIP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 164 KLETLLSFATIPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLGAKgthwGSDSVMDSGVLhEIAKSKGKTVAQVCL 243
Cdd:cd19121 165 YLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGST----GSPLISDEPVV-EIAKKHNVGPGTVLI 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1279751533 244 RWVYEQGDCLIVKSFDEGRMKENLDIVDweLSEEERQRISKI 285
Cdd:cd19121 240 SYQVARGAVVLPKSVTPDRIKSNLEIID--LDDEDMNKLNDI 279
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
32-287 |
5.14e-63 |
|
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: 201.91 E-value: 5.14e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 32 VLRAIQLGYRHFDTAAHYATEAPIGEAAAEAVRTGLVAsREDLFVTSKVWCADAHRDRVLPALRRTLSNLQMEYVDLYMV 111
Cdd:cd19113 30 IYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVK-REELFLTSKLWNNFHDPKNVETALNKTLSDLKLDYVDLFLI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 112 HWPVTMKAGRFTAPFTPE---------DFEPFDMRAVWEAMEECHRLGLAKAIGVCNFSCKKLETLLSFATIPPVVNQVE 182
Cdd:cd19113 109 HFPIAFKFVPIEEKYPPGfycgdgdnfVYEDVPILDTWKALEKLVDAGKIKSIGVSNFPGALILDLLRGATIKPAVLQIE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 183 INPVWQQRKLREFCRAKGIQLCAYSPLGAKG-THWGSDSVMDSGVLHE------IAKSKGKTVAQVCLRWVYEQGDCLIV 255
Cdd:cd19113 189 HHPYLQQPKLIEYAQKAGITITAYSSFGPQSfVELNQGRALNTPTLFEhdtiksIAAKHNKTPAQVLLRWATQRGIAVIP 268
|
250 260 270
....*....|....*....|....*....|..
gi 1279751533 256 KSFDEGRMKENLDIVDWELSEEERQRISKIPQ 287
Cdd:cd19113 269 KSNLPERLLQNLSVNDFDLTKEDFEEIAKLDI 300
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
11-289 |
6.67e-63 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 200.30 E-value: 6.67e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGtaVQGPRPDPVRAAVLRAIQLGYRHFDTAAHYATEAPIGEAAAEavrTGLvaSREDLFVTSKVWCADAHRDRv 90
Cdd:PRK11565 15 MPQLGLG--VWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKE---ASV--AREELFITTKLWNDDHKRPR- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 91 lPALRRTLSNLQMEYVDLYMVHWPVTMKAGRFTApftpedfepfdmravWEAMEECHRLGLAKAIGVCNFSCKKLETLLS 170
Cdd:PRK11565 87 -EALEESLKKLQLDYVDLYLMHWPVPAIDHYVEA---------------WKGMIELQKEGLIKSIGVCNFQIHHLQRLID 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 171 FATIPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLGAkgthwGSDSVMDSGVLHEIAKSKGKTVAQVCLRWVYEQG 250
Cdd:PRK11565 151 ETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQ-----GGKGVFDQKVIRDLADKYGKTPAQIVIRWHLDSG 225
|
250 260 270
....*....|....*....|....*....|....*....
gi 1279751533 251 DCLIVKSFDEGRMKENLDIVDWELSEEERQRISKIPQRK 289
Cdd:PRK11565 226 LVVIPKSVTPSRIAENFDVFDFRLDKDELGEIAKLDQGK 264
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
11-282 |
1.75e-62 |
|
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: 200.19 E-value: 1.75e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTavQGPRPDPVRAAVLRAIQLGYRHFDTAAHYATEAPIGEAAAEAVRTGLVaSREDLFVTSKVWCADAHRDRV 90
Cdd:cd19110 4 IPAVGLGT--WKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVV-RREDLFIVSKLWCTCHKKSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 91 LPALRRTLSNLQMEYVDLYMVHWPVTMKAGRFTAPF------TPEDFEPFDmraVWEAMEECHRLGLAKAIGVCNFSCKK 164
Cdd:cd19110 81 KTACTRSLKALKLNYLDLYLIHWPMGFKPGEPDLPLdrsgmvIPSDTDFLD---TWEAMEDLVIEGLVKNIGVSNFNHEQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 165 LETLLSFAT--IPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLGAKGthwGSDSVMDSGVLHEIAKSKGKTVAQVC 242
Cdd:cd19110 158 LERLLNKPGlrVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSC---EGVDLIDDPVIQRIAKKHGKSPAQIL 234
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1279751533 243 LRWVYEQGDCLIVKSFDEGRMKENLDIVDWELSEEERQRI 282
Cdd:cd19110 235 IRFQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNL 274
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
11-282 |
1.01e-60 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 193.72 E-value: 1.01e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTAvqGPRPDPVRAAVLRAIQLGYRHFDTAAHYATEAPIGEAAAEavrTGLvaSREDLFVTSKVWCADAHRDRV 90
Cdd:cd19139 1 IPAFGLGTF--RLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAE---SGV--PRDELFITTKIWIDNLSKDKL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 91 LPALRRTLSNLQMEYVDLYMVHWPvtmkagrftapfTPEDFEPfdMRAVWEAMEECHRLGLAKAIGVCNFSCKKLETLLS 170
Cdd:cd19139 74 LPSLEESLEKLRTDYVDLTLIHWP------------SPNDEVP--VEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 171 -FATIPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLGakgthWGsdSVMDSGVLHEIAKSKGKTVAQVCLRWVYEQ 249
Cdd:cd19139 140 vVGAGAIATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLA-----YG--KVLDDPVLAAIAERHGATPAQIALAWAMAR 212
|
250 260 270
....*....|....*....|....*....|...
gi 1279751533 250 GDCLIVKSFDEGRMKENLDIVDWELSEEERQRI 282
Cdd:cd19139 213 GYAVIPSSTKREHLRSNLLALDLTLDADDMAAI 245
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
11-283 |
1.25e-60 |
|
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: 193.98 E-value: 1.25e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGT-AVQGPRPDPVR------AAVLRAIQLGYRHFDTAAHYA---TEAPIGEAAAEAVRtglvasrEDLFVTSKV 80
Cdd:cd19072 4 VPVLGLGTwGIGGGMSKDYSddkkaiEALRYAIELGINLIDTAEMYGgghAEELVGKAIKGFDR-------EDLFITTKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 81 WCADAHRDRVLPALRRTLSNLQMEYVDLYMVHWPVtmkagrftaPFTPedfepfdMRAVWEAMEECHRLGLAKAIGVCNF 160
Cdd:cd19072 77 SPDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPN---------PSIP-------IEETLRAMEELVEEGKIRYIGVSNF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 161 SCKKLETLLSFAT-IPPVVNQVEINPV--WQQRKLREFCRAKGIQLCAYSPLGaKGthwGSDSVMDSGVLHEIAKSKGKT 237
Cdd:cd19072 141 SLEELEEAQSYLKkGPIVANQVEYNLFdrEEESGLLPYCQKNGIAIIAYSPLE-KG---KLSNAKGSPLLDEIAKKYGKT 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1279751533 238 VAQVCLRWVYEQGDCL-IVKSFDEGRMKENLDIVDWELSEEERQRIS 283
Cdd:cd19072 217 PAQIALNWLISKPNVIaIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
11-282 |
7.03e-59 |
|
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: 190.85 E-value: 7.03e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTAvqGPRPDPVRAAVLRAIQLGYRHFDTAAHYATEAPIGEAAAEAVRTGLVaSREDLFVTSKVWCADAHRDRV 90
Cdd:cd19114 4 MPLVGFGTA--KIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLV-KREDLFIVTKLWNNFHGKDHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 91 LPALRRTLSNLQMEYVDLYMVHWPVTMK--AGRFTAPFTPED-------FEPFDMRAVWEAMEECHRLGLAKAIGVCNFS 161
Cdd:cd19114 81 REAFDRQLKDYGLDYIDLYLIHFPIPAAyvDPAENYPFLWKDkelkkfpLEQSPMQECWREMEKLVDAGLVRNIGIANFN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 162 CKKLETLLSFATIPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLGA--------KGTHWGsdSVMDSGVLHEIAKS 233
Cdd:cd19114 161 VQLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNavytkvtkHLKHFT--NLLEHPVVKKLADK 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1279751533 234 KGKTVAQVCLRWVYEQGDCLIVKSFDEGRMKENLDIVDWELSEEERQRI 282
Cdd:cd19114 239 HKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEAL 287
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
8-282 |
7.91e-59 |
|
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: 189.35 E-value: 7.91e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 8 PCGLPRIGLGTaVQGPRPDPVRAaVLRAIQLGYRHFDTAAHYATEAPIGEAAAEavrTGLvaSREDLFVTSKVWCADAHR 87
Cdd:cd19130 7 GNSIPQLGYGV-FKVPPADTQRA-VATALEVGYRHIDTAAIYGNEEGVGAAIAA---SGI--PRDELFVTTKLWNDRHDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 88 DRVLPALRRTLSNLQMEYVDLYMVHWPVTMKAgrftapftpedfepfDMRAVWEAMEECHRLGLAKAIGVCNFSCKKLET 167
Cdd:cd19130 80 DEPAAAFAESLAKLGLDQVDLYLVHWPTPAAG---------------NYVHTWEAMIELRAAGRTRSIGVSNFLPPHLER 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 168 LLSFATIPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLgakgthwGSDSVMDSGVLHEIAKSKGKTVAQVCLRWVY 247
Cdd:cd19130 145 IVAATGVVPAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPL-------GQGKLLGDPPVGAIAAAHGKTPAQIVLRWHL 217
|
250 260 270
....*....|....*....|....*....|....*
gi 1279751533 248 EQGDCLIVKSFDEGRMKENLDIVDWELSEEERQRI 282
Cdd:cd19130 218 QKGHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAI 252
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
11-290 |
9.10e-58 |
|
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: 187.66 E-value: 9.10e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTAVqgprPDPV--RAAVLRAIQLGYRHFDTAAHYATEAPIGEAAAEAVRTGLVaSREDLFVTSKVWCADAHRD 88
Cdd:cd19129 6 IPALGFGTLI----PDPSatRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKI-RREDLFVTTKLWNTNHRPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 89 RVLPALRRTLSNLQMEYVDLYMVHWPVTMKAGrftapftpEDFEPFDMRA------------VWEAMEECHRLGLAKAIG 156
Cdd:cd19129 81 RVKPAFEASLKRLQLDYLDLYLIHTPFAFQPG--------DEQDPRDANGnviyddgvtlldTWRAMERLVDEGRCKAIG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 157 VCNFSCKKLETLLSFATIPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLGakgtHWGSDSVMDSGVLHEIAKSKGK 236
Cdd:cd19129 153 LSDVSLEKLREIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLG----HGMEPKLLEDPVITAIARRVNK 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1279751533 237 TVAQVCLRWVYEQGDCLIVKSFDEGRMKENLDIVdwELSEEERQRISKIPQRKI 290
Cdd:cd19129 229 TPAQVLLAWAIQRGTALLTTSKTPSRIRENFDIS--TLPEDAMREINEGIKTRY 280
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
11-278 |
4.09e-56 |
|
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: 182.75 E-value: 4.09e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGtaVQGPRPDPVRAAVLRAIQLGYRHFDTAAHYATEAPIGEAAAeavRTGLvaSREDLFVTSKVWCADAHRDRV 90
Cdd:cd19134 11 MPVIGLG--VGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIA---ASGI--PRGELFVTTKLATPDQGFTAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 91 LPALRRTLSNLQMEYVDLYMVHWPVTmKAGRFTApftpedfepfdmraVWEAMEECHRLGLAKAIGVCNFSCKKLETLLS 170
Cdd:cd19134 84 QAACRASLERLGLDYVDLYLIHWPAG-REGKYVD--------------SWGGLMKLREEGLARSIGVSNFTAEHLENLID 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 171 FATIPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLGAkgthwgsDSVMDSGVLHEIAKSKGKTVAQVCLRWVYEQG 250
Cdd:cd19134 149 LTFFTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGV-------GRLLDNPAVTAIAAAHGRTPAQVLLRWSLQLG 221
|
250 260
....*....|....*....|....*...
gi 1279751533 251 DCLIVKSFDEGRMKENLDIVDWELSEEE 278
Cdd:cd19134 222 NVVISRSSNPERIASNLDVFDFELTADH 249
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
11-285 |
7.43e-55 |
|
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis.
Pssm-ID: 381348 [Multi-domain] Cd Length: 291 Bit Score: 180.13 E-value: 7.43e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGT-AVQGPRPDpVRAAVLRAIQLGYRHFDTAAHYATEAPIGEAAAEAVRTGLVASREDLFVTSKVWCADAHRDR 89
Cdd:cd19122 9 IPAVGFGTfANEGAKGE-TYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENPSVKREDLFICTKVWNHLHEPED 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 90 VLPALRRTLSNLQMEYVDLYMVHWPVTM-KAGRFTAPFTP-----------EDFEPfdmraVWEAMEECHRLGLAKAIGV 157
Cdd:cd19122 88 VKWSIDNSLKNLKLDYIDLFLVHWPIAAeKNDQRSPKLGPdgkyvilkdltENPEP-----TWRAMEEIYESGKAKAIGV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 158 CNFSCKKLETLLSFATIPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLGAKG-THWGSDSVMDSGVLHEIAKSKGK 236
Cdd:cd19122 163 SNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNqVPSTGERVSENPTLNEVAEKGGY 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1279751533 237 TVAQVCLRWVYEQGDCLIVKSFDEGRMKENLDIVdwELSEEERQRISKI 285
Cdd:cd19122 243 SLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSI--ELSDEDFEAINQV 289
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
14-285 |
3.39e-54 |
|
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain regulatory domains - these are reported to have oxidoreductase activity.
Pssm-ID: 425554 [Multi-domain] Cd Length: 290 Bit Score: 178.27 E-value: 3.39e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 14 IGLGTAVQGPRPDP-----VRAAVLRAIQLGYRHFDTAAHYAT---EAPIGEAAAEavrtgLVASREDLFVTSKV----- 80
Cdd:pfam00248 1 IGLGTWQLGGGWGPiskeeALEALRAALEAGINFIDTAEVYGDgksEELLGEALKD-----YPVKRDKVVIATKVpdgdg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 81 -WCADAHRDRVLPALRRTLSNLQMEYVDLYMVHWPvtmkagrftapftpedFEPFDMRAVWEAMEECHRLGLAKAIGVCN 159
Cdd:pfam00248 76 pWPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWP----------------DPDTPIEETWDALEELKKEGKIRAIGVSN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 160 FSCKKLETLLSFATIPPVVNQVEINPVW--QQRKLREFCRAKGIQLCAYSPLGA--------------------KGTHWG 217
Cdd:pfam00248 140 FDAEQIEKALTKGKIPIVAVQVEYNLLRrrQEEELLEYCKKNGIPLIAYSPLGGglltgkytrdpdkgpgerrrLLKKGT 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 218 SDSVMDSGVLHEIAKSKGKTVAQVCLRWVYEQ--GDCLIVKSFDEGRMKENLDIVDWELSEEERQRISKI 285
Cdd:pfam00248 220 PLNLEALEALEEIAKEHGVSPAQVALRWALSKpgVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDEL 289
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
11-301 |
6.07e-54 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 177.14 E-value: 6.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGT-AVQGprpDPVRAAVLRAIQLGYRHFDTAAHYATEAPIGEAAAEavrTGLvaSREDLFVTSKVWCADAHRDR 89
Cdd:PRK11172 3 IPAFGLGTfRLKD---QVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAE---SGV--PRDELFITTKIWIDNLAKDK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 90 VLPALRRTLSNLQMEYVDLYMVHWPvtmkagrftapfTPEDFEPfdMRAVWEAMEECHRLGLAKAIGVCNFSCKKLETLL 169
Cdd:PRK11172 75 LIPSLKESLQKLRTDYVDLTLIHWP------------SPNDEVS--VEEFMQALLEAKKQGLTREIGISNFTIALMKQAI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 170 S------FATippvvNQVEINPVWQQRKLREFCRAKGIQLCAYSPLgAKGthwgsdSVMDSGVLHEIAKSKGKTVAQVCL 243
Cdd:PRK11172 141 AavgaenIAT-----NQIELSPYLQNRKVVAFAKEHGIHVTSYMTL-AYG------KVLKDPVIARIAAKHNATPAQVIL 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1279751533 244 RWVYEQGDCLIVKSFDEGRMKENLDIVDWELSEEERQRISkipqrKINQGRRYVSEHG 301
Cdd:PRK11172 209 AWAMQLGYSVIPSSTKRENLASNLLAQDLQLDAEDMAAIA-----ALDRNGRLVSPEG 261
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
11-285 |
5.26e-48 |
|
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: 162.37 E-value: 5.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTAVQGPR-------PDPVRAAVLRAIQLGYRHFDTAAHYA---TEAPIGEAaaeavrtgLVASREDLFVTSKV 80
Cdd:cd19085 1 VSRLGLGCWQFGGGywwgdqdDEESIATIHAALDAGINFFDTAEAYGdghSEEVLGKA--------LKGRRDDVVIATKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 81 WCADAHRDRVLPALRRTLSNLQMEYVDLYMVHWPVTMkagrftapftpedfepFDMRAVWEAMEECHRLGLAKAIGVCNF 160
Cdd:cd19085 73 SPDNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSD----------------VPLEETMEALEKLKEEGKIRAIGVSNF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 161 SCKKLETLLSFATIppVVNQVEINPVWQQ--RKLREFCRAKGIQLCAYSPLgAKGTHWG---SDSVMDSG---------- 225
Cdd:cd19085 137 GPAQLEEALDAGRI--DSNQLPYNLLWRAieYEILPFCREHGIGVLAYSPL-AQGLLTGkfsSAEDFPPGdartrlfrhf 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1279751533 226 -------------VLHEIAKSKGKTVAQVCLRWVYEQG--DCLIVKSFDEGRMKENLDIVDWELSEEERQRISKI 285
Cdd:cd19085 214 epgaeeetfealeKLKEIADELGVTMAQLALAWVLQQPgvTSVIVGARNPEQLEENAAAVDLELSPSVLERLDEI 288
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
11-282 |
2.53e-46 |
|
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: 157.35 E-value: 2.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTAVQG-------PRPDPVRAAVLRAIQLGYRHFDTAAHYA---TEAPIGEAAaeavrtgLVASREDLFVTSKV 80
Cdd:cd19137 4 IPALGLGTWGIGgfltpdySRDEEMVELLKTAIELGYTHIDTAEMYGgghTEELVGKAI-------KDFPREDLFIVTKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 81 WCADAHRDRVLPALRRTLSNLQMEYVDLYMVHWPvtmkagrftapfTPEDfePFDmrAVWEAMEECHRLGLAKAIGVCNF 160
Cdd:cd19137 77 WPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWP------------NPNI--PLE--ETLSAMAEGVRQGLIRYIGVSNF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 161 SCKKLETLLSFATIPPVVNQVEINPV---WQQRKLREFCRAKGIQLCAYSPLgAKGThwgsdsVMDSGVLHEIAKSKGKT 237
Cdd:cd19137 141 NRRLLEEAISKSQTPIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPL-RRGL------EKTNRTLEEIAKNYGKT 213
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1279751533 238 VAQVCLRWVYEQGDCL-IVKSFDEGRMKENLDIVDWELSEEERQRI 282
Cdd:cd19137 214 IAQIALAWLIQKPNVVaIPKAGRVEHLKENLKATEIKLSEEEMKLL 259
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
11-282 |
5.96e-45 |
|
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: 154.69 E-value: 5.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTAVQGPR---------PDPVRAAVLRAIQLGYRHFDTAAHYAT---EAPIGEAAAEavrtglVASREDLFVTS 78
Cdd:cd19093 2 VSPLGLGTWQWGDRlwwgygeygDEDLQAAFDAALEAGVNLFDTAEVYGTgrsERLLGRFLKE------LGDRDEVVIAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 79 KVWCA--DAHRDRVLPALRRTLSNLQMEYVDLYMVHWPvtmkagrfTAPFTPEDfepfdmrAVWEAMEECHRLGLAKAIG 156
Cdd:cd19093 76 KFAPLpwRLTRRSVVKALKASLERLGLDSIDLYQLHWP--------GPWYSQIE-------ALMDGLADAVEEGLVRAVG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 157 VCNFSCKKLE---TLLSFATIPPVVNQVEINPVWQ---QRKLREFCRAKGIQLCAYSPLgAKGTHWG------------- 217
Cdd:cd19093 141 VSNYSADQLRrahKALKERGVPLASNQVEYSLLYRdpeQNGLLPACDELGITLIAYSPL-AQGLLTGkyspenpppggrr 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1279751533 218 ---SDSVMDS-----GVLHEIAKSKGKTVAQVCLRWVYEQGDCLIVKSFDEGRMKENLDIVDWELSEEERQRI 282
Cdd:cd19093 220 rlfGRKNLEKvqpllDALEEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAEL 292
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
11-285 |
8.00e-45 |
|
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: 154.95 E-value: 8.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTAVQGPRPDPV-----RAAVLRAIQLGYRHFDTAAHY---ATEAPIGEAAAEAvrtglvaSREDLFVTSKV-- 80
Cdd:COG0667 13 VSRLGLGTMTFGGPWGGVdeaeaIAILDAALDAGINFFDTADVYgpgRSEELLGEALKGR-------PRDDVVIATKVgr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 81 ------WCADAHRDRVLPALRRTLSNLQMEYVDLYMVHWPvtmkagrftAPFTPedfepfdMRAVWEAMEECHRLGLAKA 154
Cdd:COG0667 86 rmgpgpNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRP---------DPDTP-------IEETLGALDELVREGKIRY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 155 IGVCNFSCKKLETLLSFA--TIPPVVNQVEINPVWQQ--RKLREFCRAKGIQLCAYSPLGA--------KGTHWGSDSVM 222
Cdd:COG0667 150 IGVSNYSAEQLRRALAIAegLPPIVAVQNEYSLLDRSaeEELLPAARELGVGVLAYSPLAGglltgkyrRGATFPEGDRA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 223 DSG---------------VLHEIAKSKGKTVAQVCLRWVYEQG--DCLIVKSFDEGRMKENLDIVDWELSEEERQRISKI 285
Cdd:COG0667 230 ATNfvqgylternlalvdALRAIAAEHGVTPAQLALAWLLAQPgvTSVIPGARSPEQLEENLAAADLELSAEDLAALDAA 309
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
11-282 |
5.04e-43 |
|
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: 148.94 E-value: 5.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTAVQGPRPDP---VRAAVLRAIQLGYRHFDTAAHYA---TEAPIGEAAAeavrtglvASREDLFVTSKVWCAD 84
Cdd:cd19138 11 VPALGQGTWYMGEDPAKraqEIEALRAGIDLGMTLIDTAEMYGdggSEELVGEAIR--------GRRDKVFLVSKVLPSN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 85 AHRDRVLPALRRTLSNLQMEYVDLYMVHWPvtmkaGRftapftpedfEPFDmrAVWEAMEECHRLGLAKAIGVCNFSCKK 164
Cdd:cd19138 83 ASRQGTVRACERSLRRLGTDYLDLYLLHWR-----GG----------VPLA--ETVAAMEELKKEGKIRAWGVSNFDTDD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 165 LETLLSFAT-IPPVVNQVEINpvWQQR----KLREFCRAKGIQLCAYSPLGAKGTHwgSDSVMDSGVLHEIAKSKGKTVA 239
Cdd:cd19138 146 MEELWAVPGgGNCAANQVLYN--LGSRgieyDLLPWCREHGVPVMAYSPLAQGGLL--RRGLLENPTLKEIAARHGATPA 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1279751533 240 QVCLRWVYEQGDCL-IVKSFDEGRMKENLDIVDWELSEEERQRI 282
Cdd:cd19138 222 QVALAWVLRDGNVIaIPKSGSPEHARENAAAADLELTEEDLAEL 265
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
11-282 |
1.42e-37 |
|
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: 135.35 E-value: 1.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTAVQGPRP------DPVRAAVLRAIQLGYRHFDTAAHYateapiGEAAAEA-VRTGLVASREDLFVTSKV--- 80
Cdd:cd19084 4 VSRIGLGTWAIGGTWwgevddQESIEAIKAAIDLGINFFDTAPVY------GFGHSEEiLGKALKGRRDDVVIATKCglr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 81 W------CADAHRDRVLPALRRTLSNLQMEYVDLYMVHWPvtmkagrftAPFTPedfepfdMRAVWEAMEECHRLGLAKA 154
Cdd:cd19084 78 WdggkgvTKDLSPESIRKEVEQSLRRLQTDYIDLYQIHWP---------DPNTP-------IEETAEALEKLKKEGKIRY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 155 IGVCNFSCKKLETLLSFATIppVVNQVEINPVWQQ--RKLREFCRAKGIQLCAYSPLGA--------KGTHWGSDsvmDS 224
Cdd:cd19084 142 IGVSNFSVEQLEEARKYGPI--VSLQPPYSMLEREieEELLPYCRENGIGVLPYGPLAQglltgkykKEPTFPPD---DR 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1279751533 225 -------------------GVLHEIAKSKGKTVAQVCLRWV--YEQGDCLIVKSFDEGRMKENLDIVDWELSEEERQRI 282
Cdd:cd19084 217 rsrfpffrgenfeknleivDKLKEIAEKYGKSLAQLAIAWTlaQPGVTSAIVGAKNPEQLEENAGALDWELTEEELKEI 295
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
12-268 |
1.10e-36 |
|
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications. Members have very distinct functions and include the prokaryotic 2,5-diketo-D-gluconic acid reductases and beta-keto ester reductases, the eukaryotic aldose reductases, aldehyde reductases, hydroxysteroid dehydrogenases, steroid 5beta-reductases, potassium channel beta-subunits, and aflatoxin aldehyde reductases, among others.
Pssm-ID: 381296 [Multi-domain] Cd Length: 232 Bit Score: 131.10 E-value: 1.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 12 PRIGLGTAVQGPRPDPVRA-AVL-RAIQLGYRHFDTAAHYAT---EAPIGEAAAEavrtglVASREDLFVTSKV------ 80
Cdd:cd06660 1 SRLGLGTMTFGGDGDEEEAfALLdAALEAGGNFFDTADVYGDgrsERLLGRWLKG------RGNRDDVVIATKGghppgg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 81 --WCADAHRDRVLPALRRTLSNLQMEYVDLYMVHWPvtmkagrftAPFTPedfepfdMRAVWEAMEECHRLGLAKAIGVC 158
Cdd:cd06660 75 dpSRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRD---------DPSTP-------VEETLEALNELVREGKIRYIGVS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 159 NFSCKKLETLLSFAT----IPPVVNQVEINPVWQQ---RKLREFCRAKGIQLCAYSPLgAKGthwgsdsvmdsgvlheia 231
Cdd:cd06660 139 NWSAERLAEALAYAKahglPGFAAVQPQYSLLDRSpmeEELLDWAEENGLPLLAYSPL-ARG------------------ 199
|
250 260 270
....*....|....*....|....*....|....*....
gi 1279751533 232 kskgktVAQVCLRWVYEQ--GDCLIVKSFDEGRMKENLD 268
Cdd:cd06660 200 ------PAQLALAWLLSQpfVTVPIVGARSPEQLEENLA 232
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-268 |
7.17e-27 |
|
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: 105.26 E-value: 7.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTAVQGPRPDPVRAAVLR-AIQLGYRHFDTAAHYA-TEAPIGEAaaeavrtgLVASREDLFVTSKVWCADahRD 88
Cdd:cd19100 11 VSRLGFGGGPLGRLSQEEAAAIIRrALDLGINYFDTAPSYGdSEEKIGKA--------LKGRRDKVFLATKTGARD--YE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 89 RVLPALRRTLSNLQMEYVDLYMVHwpvtmkagrftAPFTPEDFE-PFDMRAVWEAMEECHRLGLAKAIGvcnFSCKKLET 167
Cdd:cd19100 81 GAKRDLERSLKRLGTDYIDLYQLH-----------AVDTEEDLDqVFGPGGALEALLEAKEEGKIRFIG---ISGHSPEV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 168 LLSFATIPPV-VNQVEINPVwqQRKLREF-------CRAKGIQLCAYSPLGakGTHWGSDSVMDsgvlheiakskgktvA 239
Cdd:cd19100 147 LLRALETGEFdVVLFPINPA--GDHIDSFreellplAREKGVGVIAMKVLA--GGRLLSGDPLD---------------P 207
|
250 260 270
....*....|....*....|....*....|...
gi 1279751533 240 QVCLRWVYEQG--DCLIV--KSFDEgrMKENLD 268
Cdd:cd19100 208 EQALRYALSLPpvDVVIVgmDSPEE--LDENLA 238
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-285 |
1.47e-24 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 100.83 E-value: 1.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGT-AV--------QGPRPD-PVRAAVLRAIQLGYRHFDTAAHYAT---EAPIGEAAAEAvrtglvasREDLFVT 77
Cdd:cd19102 1 LTTIGLGTwAIggggwgggWGPQDDrDSIAAIRAALDLGINWIDTAAVYGLghsEEVVGRALKGL--------RDRPIVA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 78 SK---VWCADAHRDRVLPA--LRR----TLSNLQMEYVDLYMVHWPVTmkagrftapftPEDFEpfdmrAVWEAMEECHR 148
Cdd:cd19102 73 TKcglLWDEEGRIRRSLKPasIRAeceaSLRRLGVDVIDLYQIHWPDP-----------DEPIE-----EAWGALAELKE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 149 LGLAKAIGVCNFSCKKLETLLSFATI----PP---VVNQVEinpvwqqRKLREFCRAKGIQLCAYSPLGA-----KGT-- 214
Cdd:cd19102 137 EGKVRAIGVSNFSVDQMKRCQAIHPIaslqPPyslLRRGIE-------AEILPFCAEHGIGVIVYSPMQSglltgKMTpe 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 215 --------HWGSDSVMDSG-----------VLHEIAKSKGKTVAQVCLRWVYEQGD--CLIVKSFDEGRMKENLDIVDWE 273
Cdd:cd19102 210 rvaslpadDWRRRSPFFQEpnlarnlalvdALRPIAERHGRTVAQLAIAWVLRRPEvtSAIVGARRPDQIDETVGAADLR 289
|
330
....*....|..
gi 1279751533 274 LSEEERQRISKI 285
Cdd:cd19102 290 LTPEELAEIEAL 301
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
11-255 |
1.89e-24 |
|
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: 99.21 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTA------VQGPRPDPVRA-AVLR-AIQLGYRHFDTAAHYA---TEAPIGEAaaeavrtgLVASREDLFVTSK 79
Cdd:cd19088 1 VSRLGYGAMrltgpgIWGPPADREEAiAVLRrALELGVNFIDTADSYGpdvNERLIAEA--------LHPYPDDVVIATK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 80 V---------WCADAHRDRVLPALRRTLSNLQMEYVDLYMVHWPvtmkagrftAPFTPEDfEPFdmravwEAMEECHRLG 150
Cdd:cd19088 73 GglvrtgpgwWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRI---------DPKVPFE-EQL------GALAELQDEG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 151 LAKAIGVCNFSCKKLETLLSFATIPPVVNQveINPVWQQ-RKLREFCRAKGIQLCAYSPLGAKGTHwgsdsvMDSGVLHE 229
Cdd:cd19088 137 LIRHIGLSNVTVAQIEEARAIVRIVSVQNR--YNLANRDdEGVLDYCEAAGIAFIPWFPLGGGDLA------QPGGLLAE 208
|
250 260
....*....|....*....|....*.
gi 1279751533 230 IAKSKGKTVAQVCLRWVYEQGDCLIV 255
Cdd:cd19088 209 VAARLGATPAQVALAWLLARSPVMLP 234
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-270 |
9.02e-24 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 97.27 E-value: 9.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTavqGPRPDPVRAAVLRAIQLGYRHFDTAAHYA---TEAPIGEAAAEAVRtglvasrEDLFVTSKVWCADAHR 87
Cdd:cd19105 13 VSRLGFGG---GGLPRESPELLRRALDLGINYFDTAEGYGngnSEEIIGEALKGLRR-------DKVFLATKASPRLDKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 88 DR--VLPALRRTLSNLQMEYVDLYMVHwpvtmkagrftAPFTPEDFEPFDmrAVWEAMEECHRLGLAKAIGvcnFSC--K 163
Cdd:cd19105 83 DKaeLLKSVEESLKRLQTDYIDIYQLH-----------GVDTPEERLLNE--ELLEALEKLKKEGKVRFIG---FSThdN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 164 KLETLLSFATIPPV-VNQVEINPVWQQRKLREF---CRAKGIQLCAYSPLGAKGTHWGSDSVMdsgvlheiaKSKGKTVA 239
Cdd:cd19105 147 MAEVLQAAIESGWFdVIMVAYNFLNQPAELEEAlaaAAEKGIGVVAMKTLAGGYLQPALLSVL---------KAKGFSLP 217
|
250 260 270
....*....|....*....|....*....|....*
gi 1279751533 240 QVCLRWVYEQGD---CLI-VKSFDEgrMKENLDIV 270
Cdd:cd19105 218 QAALKWVLSNPRvdtVVPgMRNFAE--LEENLAAA 250
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
13-285 |
2.26e-23 |
|
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: 97.38 E-value: 2.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 13 RIGLGTAV------QGPRPDPVRAAVLRAIQLGYRHFDTAAHY---ATEAPIGEAAAEAvrtglvASREDLFVTSKV--- 80
Cdd:cd19148 6 RIALGTWAiggwmwGGTDEKEAIETIHKALDLGINLIDTAPVYgfgLSEEIVGKALKEY------GKRDRVVIATKVgle 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 81 W------CADAHRDRVLPALRRTLSNLQMEYVDLYMVHWpvtmkagrftapftPEDFEPFDMRAvwEAMEECHRLGLAKA 154
Cdd:cd19148 80 WdeggevVRNSSPARIRKEVEDSLRRLQTDYIDLYQVHW--------------PDPLVPIEETA--EALKELLDEGKIRA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 155 IGVCNFSCKKLETLLSFA---TIPPVVNQVEinpvwqqRKLRE----FCRAKGIQLCAYSPLgAKGTHWG---SDSVMDS 224
Cdd:cd19148 144 IGVSNFSPEQMETFRKVAplhTVQPPYNLFE-------REIEKdvlpYARKHNIVTLAYGAL-CRGLLSGkmtKDTKFEG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 225 G----------------------VLHEIAKSK-GKTVAQVCLRWVYEQGDCLIVksFDEGRMKENLDIVD----WELSEE 277
Cdd:cd19148 216 DdlrrtdpkfqeprfsqylaaveELDKLAQERyGKSVIHLAVRWLLDQPGVSIA--LWGARKPEQLDAVDevfgWSLNDE 293
|
....*...
gi 1279751533 278 ERQRISKI 285
Cdd:cd19148 294 DMKEIDAI 301
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
11-278 |
2.65e-21 |
|
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: 91.46 E-value: 2.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGT---AVQGPRPDPVRAAVLRAIQLGYRHFDTAAHYAT---EAPIGEAAAEavRTGLvasREDLFVTSKvwCA- 83
Cdd:cd19092 6 VSRLVLGCmrlADWGESAEELLSLIEAALELGITTFDHADIYGGgkcEELFGEALAL--NPGL---REKIEIQTK--CGi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 84 --------------DAHRDRVLPALRRTLSNLQMEYVDLYMVHWPVTMkagrftapftpedfepFDMRAVWEAMEECHRL 149
Cdd:cd19092 79 rlgddprpgrikhyDTSKEHILASVEGSLKRLGTDYLDLLLLHRPDPL----------------MDPEEVAEAFDELVKS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 150 GLAKAIGVCNFSCKKLETLLSFATIPPVVNQVEINPV----WQQRKLrEFCRAKGIQLCAYSPLGaKGTHWGSDS----- 220
Cdd:cd19092 143 GKVRYFGVSNFTPSQIELLQSYLDQPLVTNQIELSLLhteaIDDGTL-DYCQLLDITPMAWSPLG-GGRLFGGFDerfqr 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 221 VMDsgVLHEIAKSKGKTVAQVCLRWVYEQGDCL--IVKSFDEGRMKENLDIVDWELSEEE 278
Cdd:cd19092 221 LRA--ALEELAEEYGVTIEAIALAWLLRHPARIqpILGTTNPERIRSAVKALDIELTREE 278
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
12-277 |
3.61e-21 |
|
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: 91.46 E-value: 3.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 12 PRIGLGTA---VQGPRPDP-VRAAVLRAIQ-LGYRHFDTAAHY---ATEAPIGEAAAeAVRTGLVASredlfvtsKV--W 81
Cdd:cd19075 1 PKIILGTMtfgSQGRFTTAeAAAELLDAFLeRGHTEIDTARVYpdgTSEELLGELGL-GERGFKIDT--------KAnpG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 82 CADAH-RDRVLPALRRTLSNLQMEYVDLYMVHWPvtmkagrftAPFTPedFEPfdmraVWEAMEECHRLGLAKAIGVCNF 160
Cdd:cd19075 72 VGGGLsPENVRKQLETSLKRLKVDKVDVFYLHAP---------DRSTP--LEE-----TLAAIDELYKEGKFKEFGLSNY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 161 SCKKLETLLSFAT----IPPVVNQVEINPVWQQ--RKLREFCRAKGIQLCAYSPLG--------------AKGTHWGSDS 220
Cdd:cd19075 136 SAWEVAEIVEICKengwVLPTVYQGMYNAITRQveTELFPCLRKLGIRFYAYSPLAggfltgkykysedkAGGGRFDPNN 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 221 VMDS---------------GVLHEIAKSKGKTVAQVCLRWVY-------EQGDCLIVKSFDEGRMKENLDIVDW-ELSEE 277
Cdd:cd19075 216 ALGKlyrdrywkpsyfealEKVEEAAEKEGISLAEAALRWLYhhsaldgEKGDGVILGASSLEQLEENLAALEKgPLPEE 295
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
12-246 |
1.17e-20 |
|
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: 89.54 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 12 PRIGLGTAVQGPRPDPVR-----AAVLRAIQLGYRHFDTAAHYA-TEAPIGEAAAEavrtglvASREDLFVTSKVWC--- 82
Cdd:cd19090 1 SALGLGTAGLGGVFGGVDddeavATIRAALDLGINYIDTAPAYGdSEERLGLALAE-------LPREPLVLSTKVGRlpe 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 83 --ADAHRDRVLPALRRTLSNLQMEYVDLYMVHWPVTMKAGRFTAPftpedfepfdmRAVWEAMEECHRLGLAKAIGV-CN 159
Cdd:cd19090 74 dtADYSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILAP-----------GGALEALLELKEEGLIKHIGLgGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 160 ---FSCKKLET-----LLSFAtippvvnqvEINPVWQQ--RKLREFCRAKGIQLCAYSPLG----AKGT--------HWG 217
Cdd:cd19090 143 ppdLLRRAIETgdfdvVLTAN---------RYTLLDQSaaDELLPAAARHGVGVINASPLGmgllAGRPpervrytyRWL 213
|
250 260 270
....*....|....*....|....*....|
gi 1279751533 218 SDSVMD-SGVLHEIAKSKGKTVAQVCLRWV 246
Cdd:cd19090 214 SPELLDrAKRLYELCDEHGVPLPALALRFL 243
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
22-282 |
1.12e-19 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 87.26 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 22 GPRPDPVRA--AVLRAIQLGYRHFDTAAHYA-TEAPIGEAAAEAVRTGlvASREDLFVTSKvWCADAHRDRVLPA----- 93
Cdd:cd19101 17 GGIRDEDAAvrAMAAYVDAGLTTFDCADIYGpAEELIGEFRKRLRRER--DAADDVQIHTK-WVPDPGELTMTRAyveaa 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 94 LRRTLSNLQMEYVDLYMVHWpvtmkagrftapftpEDFEPFDMRAVWEAMEECHRLGLAKAIGVCNFSCKKLETLLSfAT 173
Cdd:cd19101 94 IDRSLKRLGVDRLDLVQFHW---------------WDYSDPGYLDAAKHLAELQEEGKIRHLGLTNFDTERLREILD-AG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 174 IPPVVNQVEINpVWQQR---KLREFCRAKGIQLCAY----------------SPLGAKGTHWG----SDSVMDSG----- 225
Cdd:cd19101 158 VPIVSNQVQYS-LLDRRpenGMAALCEDHGIKLLAYgtlaggllsekylgvpEPTGPALETRSlqkyKLMIDEWGgwdlf 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1279751533 226 -----VLHEIAKSKGKTVAQVCLRWVYEQ--GDCLIVKSFDEGRMKENLDIVDWELSEEERQRI 282
Cdd:cd19101 237 qellrTLKAIADKHGVSIANVAVRWVLDQpgVAGVIVGARNSEHIDDNVRAFSFRLDDEDRAAI 300
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
13-282 |
5.07e-19 |
|
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: 85.34 E-value: 5.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 13 RIGLGTAVQGPRPDPVRA-AVLRA-IQLGYRHFDTAAHYATEAP----------IGEAAAEAVRtglvasREDLFVTSKV 80
Cdd:cd19081 11 PLCLGTMVFGWTADEETSfALLDAfVDAGGNFIDTADVYSAWVPgnaggesetiIGRWLKSRGK------RDRVVIATKV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 81 WCADA------HRDRVLPALRRTLSNLQMEYVDLYMVHWPvtmkagrftAPFTPEDfepfdmravwEAMEECHRL---GL 151
Cdd:cd19081 85 GFPMGpngpglSRKHIRRAVEASLRRLQTDYIDLYQAHWD---------DPATPLE----------ETLGALNDLirqGK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 152 AKAIGVCNFSCKKLETLLSFAT----IPPVVNQVEINPVWQQ---RKLREFCRAKGIQLCAYSPLGA------------- 211
Cdd:cd19081 146 VRYIGASNYSAWRLQEALELSRqhglPRYVSLQPEYNLVDREsfeGELLPLCREEGIGVIPYSPLAGgfltgkyrseadl 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 212 KGTHWGSDSVMDS---------GVLHEIAKSKGKTVAQVCLRWVYEQG--DCLIVKSFDEGRMKENLDIVDWELSEEERQ 280
Cdd:cd19081 226 PGSTRRGEAAKRYlnerglrilDALDEVAAEHGATPAQVALAWLLARPgvTAPIAGARTVEQLEDLLAAAGLRLTDEEVA 305
|
..
gi 1279751533 281 RI 282
Cdd:cd19081 306 RL 307
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
32-285 |
8.60e-19 |
|
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: 84.97 E-value: 8.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 32 VLRAIQLGYRHFDTAAHYA---TEAPIGEAaaeavrtgLVASREDLFVTSKV--WCAD------AHRDRVLPALRRTLSN 100
Cdd:cd19091 45 VDIALDAGINFFDTADVYSegeSEEILGKA--------LKGRRDDVLIATKVrgRMGEgpndvgLSRHHIIRAVEASLKR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 101 LQMEYVDLYMVHWPvtmkagrftAPFTPEDfepfdmrAVWEAMEECHRLGLAKAIGVCNFSCKKLETLLSFAT----IPP 176
Cdd:cd19091 117 LGTDYIDLYQLHGF---------DALTPLE-------ETLRALDDLVRQGKVRYIGVSNFSAWQIMKALGISErrglARF 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 177 VVNQVEINPVWQ--QRKLREFCRAKGIQLCAYSPLG--------------AKGTHWGSDS-------------VMDsgVL 227
Cdd:cd19091 181 VALQAYYSLLGRdlEHELMPLALDQGVGLLVWSPLAggllsgkyrrgqpaPEGSRLRRTGfdfppvdrergydVVD--AL 258
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 228 HEIAKSKGKTVAQVCLRWVYEQ--GDCLIVKSFDEGRMKENLDIVDWELSEEERQRISKI 285
Cdd:cd19091 259 REIAKETGATPAQVALAWLLSRptVSSVIIGARNEEQLEDNLGAAGLSLTPEEIARLDKV 318
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
14-277 |
1.43e-18 |
|
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: 84.18 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 14 IGLGTAVQ-GPRPDPVRAA--VLRAIQLGYRHFDTAAHYA---TEAPIGEAAAEAVRTGLVasredlfVTSKV-WCADAH 86
Cdd:cd19074 7 LSLGTWLTfGGQVDDEDAKacVRKAYDLGINFFDTADVYAagqAEEVLGKALKGWPRESYV-------ISTKVfWPTGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 87 -------RDRVLPALRRTLSNLQMEYVDLYMVHwpvtmkagRFTaPFTPedfepfdMRAVWEAMEECHRLGLAKAIGVCN 159
Cdd:cd19074 80 pndrglsRKHIFESIHASLKRLQLDYVDIYYCH--------RYD-PETP-------LEETVRAMDDLIRQGKILYWGTSE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 160 FSCKKLETLLSFAT----IPPVVNQVEINPVWQQR--KLREFCRAKGIQLCAYSPL-----------------GAKGTHW 216
Cdd:cd19074 144 WSAEQIAEAHDLARqfglIPPVVEQPQYNMLWREIeeEVIPLCEKNGIGLVVWSPLaqglltgkyrdgipppsRSRATDE 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1279751533 217 GSDSVMDSGV----------LHEIAKSKGKTVAQVCLRWVYEQ--GDCLIVKSFDEGRMKENLDIVDWELSEE 277
Cdd:cd19074 224 DNRDKKRRLLtdenlekvkkLKPIADELGLTLAQLALAWCLRNpaVSSAIIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
12-268 |
2.34e-18 |
|
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: 82.67 E-value: 2.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 12 PRIGLGTA----VQGPRPDPVRAAVL-RAIQLGYRHFDTAAHYAT-EAPIGEAAAEavrtglvASREDLFVTSKVWCADA 85
Cdd:cd19095 1 SVLGLGTSgigrVWGVPSEAEAARLLnTALDLGINLIDTAPAYGRsEERLGRALAG-------LRRDDLFIATKVGTHGE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 86 H--------RDRVLPALRRTLSNLQMEYVDLYMVHWPvtmkagrftapfTPEDFEPfdmrAVWEAMEECHRLGLAKAIGV 157
Cdd:cd19095 74 GgrdrkdfsPAAIRASIERSLRRLGTDYIDLLQLHGP------------SDDELTG----EVLETLEDLKAAGKVRYIGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 158 CNFSckklETLLSFATIPPV-VNQVEINPVWQ-QRKLREFCRAKGIQLCAYSPLG----AKGTHWGSDSVMDSGVLHEIA 231
Cdd:cd19095 138 SGDG----EELEAAIASGVFdVVQLPYNVLDReEEELLPLAAEAGLGVIVNRPLAngrlRRRVRRRPLYADYARRPEFAA 213
|
250 260 270
....*....|....*....|....*....|....*....
gi 1279751533 232 KSKGKTVAQVCLRWVYEQG--DCLIVKSFDEGRMKENLD 268
Cdd:cd19095 214 EIGGATWAQAALRFVLSHPgvSSAIVGTTNPEHLEENLA 252
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
5-296 |
4.61e-18 |
|
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: 82.88 E-value: 4.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 5 GRAPCGLPRIGLGT----AVQGPR-PDPVRAAVL-RAIQLGYRHFDTAAHYA-TEAPIGEAAAEAVRTglvasREDLFVT 77
Cdd:cd19144 7 GRNGPSVPALGFGAmglsAFYGPPkPDEERFAVLdAAFELGCTFWDTADIYGdSEELIGRWFKQNPGK-----REKIFLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 78 SKV----------WCADAHRDRVLPALRRTLSNLQMEYVDLYMVHwpvtmkagRFTaPFTPedfepfdMRAVWEAMEECH 147
Cdd:cd19144 82 TKFgieknvetgeYSVDGSPEYVKKACETSLKRLGVDYIDLYYQH--------RVD-GKTP-------IEKTVAAMAELV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 148 RLGLAKAIGVCNFSCkklETLLSFATIPPVVN-QVEINPVW-----QQRKLREFCRAKGIQLCAYSPLGaKGTHWGSDSV 221
Cdd:cd19144 146 QEGKIKHIGLSECSA---ETLRRAHAVHPIAAvQIEYSPFSldierPEIGVLDTCRELGVAIVAYSPLG-RGFLTGAIRS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 222 MDS-------------------------GVLHEIAKSKGKTVAQVCLRWVYEQGDCLIV----KSFDegRMKENLDIVDW 272
Cdd:cd19144 222 PDDfeegdfrrmaprfqaenfpknlelvDKIKAIAKKKNVTAGQLTLAWLLAQGDDIIPipgtTKLK--RLEENLGALKV 299
|
330 340
....*....|....*....|....
gi 1279751533 273 ELSEEERQRISKIPQRKINQGRRY 296
Cdd:cd19144 300 KLTEEEEKEIREIAEEAEVVGERY 323
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
34-282 |
2.22e-17 |
|
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: 81.09 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 34 RAIQLGYRHFDTAAHY---ATEAPIGEAAAEavrtglVASREDLFVTSKVWCADAH--------RDRVLPALRRTLSNLQ 102
Cdd:cd19079 43 RALDLGINFFDTANVYsggASEEILGRALKE------FAPRDEVVIATKVYFPMGDgpngrglsRKHIMAEVDASLKRLG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 103 MEYVDLYMVHWPvtmkagrftAPFTPedFEpfdmravwEAMEECHRL---GLAKAIGVCNFSCKKLETLLSFATI----P 175
Cdd:cd19079 117 TDYIDLYQIHRW---------DYETP--IE--------ETLEALHDVvksGKVRYIGASSMYAWQFAKALHLAEKngwtK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 176 PVVNQVEINPVWQ--QRKLREFCRAKGIQLCAYSPLGA----------KGTHWGSDS---------------VMDSgvLH 228
Cdd:cd19079 178 FVSMQNHYNLLYReeEREMIPLCEEEGIGVIPWSPLARgrlarpwgdtTERRRSTTDtaklkydyfteadkeIVDR--VE 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1279751533 229 EIAKSKGKTVAQVCLRWVYEQG--DCLIVKSFDEGRMKENLDIVDWELSEEERQRI 282
Cdd:cd19079 256 EVAKERGVSMAQVALAWLLSKPgvTAPIVGATKLEHLEDAVAALDIKLSEEEIKYL 311
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
12-282 |
3.27e-16 |
|
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: 77.64 E-value: 3.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 12 PRIGLG----TAVQGPRPDPVRAAVL-RAIQLGYRHFDTAAHY---ATEAPIGEAAAEAvrtglvasREDLFVTSK---V 80
Cdd:cd19076 13 SALGLGcmgmSAFYGPADEEESIATLhRALELGVTFLDTADMYgpgTNEELLGKALKDR--------RDEVVIATKfgiV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 81 WCA-------DAHRDRVLPALRRTLSNLQMEYVDLYMVHWPvtmkagrftAPFTP-EDfepfdmraVWEAMEECHRLGLA 152
Cdd:cd19076 85 RDPgsgfrgvDGRPEYVRAACEASLKRLGTDVIDLYYQHRV---------DPNVPiEE--------TVGAMAELVEEGKV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 153 KAIGVCNFSCkklETLLSFATIPPVVN-QVEINPvwQQRKLRE----FCRAKGIQLCAYSPLGaKGTHWG-----SDSVM 222
Cdd:cd19076 148 RYIGLSEASA---DTIRRAHAVHPITAvQSEYSL--WTRDIEDevlpTCRELGIGFVAYSPLG-RGFLTGaikspEDLPE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 223 DSG--------------------VLHEIAKSKGKTVAQVCLRWVYEQGDCLI----VKSfdEGRMKENLDIVDWELSEEE 278
Cdd:cd19076 222 DDFrrnnprfqgenfdknlklveKLEAIAAEKGCTPAQLALAWVLAQGDDIVpipgTKR--IKYLEENVGALDVVLTPEE 299
|
....
gi 1279751533 279 RQRI 282
Cdd:cd19076 300 LAEI 303
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
13-285 |
5.68e-16 |
|
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: 76.69 E-value: 5.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 13 RIGLGT-AVQG----PRPDPV--RAAVLRAIQLGYRHFDTAAHYAT---EAPIGEAAAEAVRTGLVASRED--LFVTSKV 80
Cdd:cd19083 13 PIGLGTnAVGGhnlyPNLDEEegKDLVREALDNGVNLLDTAFIYGLgrsEELVGEVLKEYNRNEVVIATKGahKFGGDGS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 81 wCADAHRDRVLPALRRTLSNLQMEYVDLYMVHWPvtmkagrftAPFTPEDfepfdmRAVwEAMEECHRLGLAKAIGVCNF 160
Cdd:cd19083 93 -VLNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFP---------DGETPKA------EAV-GALQELKDEGKIRAIGVSNF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 161 SckkLETLLSFATIPPV-VNQVEINPVWQ--QRKLREFCRAKGIQLCAYSPL--GAKGTHWGSDSVMDSGV--------- 226
Cdd:cd19083 156 S---LEQLKEANKDGYVdVLQGEYNLLQReaEEDILPYCVENNISFIPYFPLasGLLAGKYTKDTKFPDNDlrndkplfk 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1279751533 227 -------------LHEIAKSKGKTVAQVCLRWVYEQG--DCLIVKSFDEGRMKENLDIVDWELSEEERQRISKI 285
Cdd:cd19083 233 gerfsenldkvdkLKSIADEKGVTVAHLALAWYLTRPaiDVVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
5-246 |
3.15e-15 |
|
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: 74.60 E-value: 3.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 5 GRAPCGLPRIGLGtAVQGP----RPDPVRAAVLRAIQLGYRHFDTAAHYATEAPIGEAA-AEAVRTGLVASREDLFVTSK 79
Cdd:cd19089 5 GRSGLHLPAISLG-LWHNFgdytSPEEARELLRTAFDLGITHFDLANNYGPPPGSAEENfGRILKRDLRPYRDELVISTK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 80 V-----------WcadAHRDRVLPALRRTLSNLQMEYVDLYMVHwpvtmkagRFTaPFTPedfepfdMRAVWEAMEECHR 148
Cdd:cd19089 84 AgygmwpgpygdG---GSRKYLLASLDQSLKRMGLDYVDIFYHH--------RYD-PDTP-------LEETMTALADAVR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 149 LGLAKAIGVCNFSCKKLE---TLLSFATIPPVVNQVEINPV--WQQRKLREFCRAKGIQLCAYSPLG------------- 210
Cdd:cd19089 145 SGKALYVGISNYPGAKARraiALLRELGVPLIIHQPRYSLLdrWAEDGLLEVLEEAGIGFIAFSPLAqglltdkylngip 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1279751533 211 ----AKGTHWGSDSVMDSG-------VLHEIAKSKGKTVAQVCLRWV 246
Cdd:cd19089 225 pdsrRAAESKFLTEEALTPekleqlrKLNKIAAKRGQSLAQLALSWV 271
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
13-285 |
1.03e-14 |
|
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: 73.38 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 13 RIGLGTAVQGPRPDPVRAAVL--RAIQLGYRHFDTAAHYA---TEAPIGEAAAEavrtglvaSREDLFVTSKV------- 80
Cdd:cd19087 15 RLCLGTMNFGGRTDEETSFAImdRALDAGINFFDTADVYGggrSEEIIGRWIAG--------RRDDIVLATKVfgpmgdd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 81 -WCADAHRDRVLPALRRTLSNLQMEYVDLYMVHwpvtmkagRFTaPFTPedfepfdMRAVWEAMEECHRLGLAKAIGVCN 159
Cdd:cd19087 87 pNDRGLSRRHIRRAVEASLRRLQTDYIDLYQMH--------HFD-RDTP-------LEETLRALDDLVRQGKIRYIGVSN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 160 FSCKKLET---------LLSFATIPPVVN------QVEINPVwqqrklrefCRAKGIQLCAYSPLGA--------KGTHW 216
Cdd:cd19087 151 FAAWQIAKaqgiaarrgLLRFVSEQPMYNllkrqaELEILPA---------ARAYGLGVIPYSPLAGglltgkygKGKRP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 217 GSDSVMDSGV----------------LHEIAKSKGKTVAQVCLRWVYEQG--DCLIVKSFDEGRMKENLDIVDWELSEEE 278
Cdd:cd19087 222 ESGRLVERARyqarygleeyrdiaerFEALAAEAGLTPASLALAWVLSHPavTSPIIGPRTLEQLEDSLAALEITLTPEL 301
|
....*..
gi 1279751533 279 RQRISKI 285
Cdd:cd19087 302 LAEIDEL 308
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
12-209 |
1.12e-14 |
|
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381388 [Multi-domain] Cd Length: 290 Bit Score: 72.78 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 12 PRIGLGTAVQGPRP----DPVRAAVLRAIQLGYRHFDTAAHYateapiGEAAAEaVRTGLVAS---REDLFVTSKV---- 80
Cdd:cd19162 1 PRLGLGAASLGNLArageDEAAATLDAAWDAGIRYFDTAPLY------GLGLSE-RRLGAALArhpRAEYVVSTKVgrll 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 81 --------------WcaDAHRDRVLPALRRTLSNLQMEYVDLYMVHwpvtmkagrftapftpeDFEPFDMRAV---WEAM 143
Cdd:cd19162 74 epgaagrpagadrrF--DFSADGIRRSIEASLERLGLDRLDLVFLH-----------------DPDRHLLQALtdaFPAL 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1279751533 144 EECHRLGLAKAIGVcnfSCKKLETLLSFATIPPvVNQVEINPVW---QQRKLREF---CRAKGIQLCAYSPL 209
Cdd:cd19162 135 EELRAEGVVGAIGV---GVTDWAALLRAARRAD-VDVVMVAGRYtllDRRAATELlplCAAKGVAVVAAGVF 202
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
34-285 |
1.24e-14 |
|
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the prototype of this family. It is an NADP(H)-dependent aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NADP(H) as a hydride donor.
Pssm-ID: 381320 [Multi-domain] Cd Length: 328 Bit Score: 73.37 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 34 RAIQLGYRHFDTAAHYA----------TEAPIGEAAAeavRTGlvaSREDLFVTSKV--------WCADA----HRDRVL 91
Cdd:cd19094 26 YAFDEGVNFIDTAEMYPvppspetqgrTEEIIGSWLK---KKG---NRDKVVLATKVagpgegitWPRGGgtrlDRENIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 92 PALRRTLSNLQMEYVDLYMVHWP---VTMKAGR-FTAPFTPEDFEPFDmrAVWEAMEECHRLGLAKAIGVCNFSCKKLET 167
Cdd:cd19094 100 EAVEGSLKRLGTDYIDLYQLHWPdryTPLFGGGyYTEPSEEEDSVSFE--EQLEALGELVKAGKIRHIGLSNETPWGVMK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 168 LLSFAT---IPPVVN-QVEINPVWQQRK--LREFCRAKGIQLCAYSPLGA--------KGTHWGSDSVMDSG-------- 225
Cdd:cd19094 178 FLELAEqlgLPRIVSiQNPYSLLNRNFEegLAEACHRENVGLLAYSPLAGgvltgkylDGAARPEGGRLNLFpgymaryr 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1279751533 226 ---------VLHEIAKSKGKTVAQVCLRWVYEQ---GDCLI-VKSFDEgrMKENLDIVDWELSEEERQRISKI 285
Cdd:cd19094 258 spqaleavaEYVKLARKHGLSPAQLALAWVRSRpfvTSTIIgATTLEQ--LKENIDAFDVPLSDELLAEIDAV 328
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
12-249 |
1.29e-14 |
|
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) and Streptomyces glaucescens aldo-keto reductase (StrT) are founding members of aldo-keto reductase family 10 member A1 (AKR10A1) and A2 (AKR10A2). BlmT is bluensomycin aldo-keto reductase (AKR) and StrT is streptomycin AKR.
Pssm-ID: 381308 [Multi-domain] Cd Length: 291 Bit Score: 72.59 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 12 PRIGLGTAVQGPRPDPVRA-AVLRA-IQLGYRHFDTAAHYAteAPIGEAAAEAV------RTGLvasREDLFVTSK---- 79
Cdd:cd19082 1 SRIVLGTADFGTRIDEEEAfALLDAfVELGGNFIDTARVYG--DWVERGASERVigewlkSRGN---RDKVVIATKgghp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 80 ----VWCADAHRDRVLPALRRTLSNLQMEYVDLYMVHW-----PVtmkagrftapftpedfEPFdMravwEAMEECHRLG 150
Cdd:cd19082 76 dledMSRSRLSPEDIRADLEESLERLGTDYIDLYFLHRddpsvPV----------------GEI-V----DTLNELVRAG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 151 LAKAIGVCNFSCKKLETLLSFATI----PPVVNQV-----EINP--------VWQQRKLREFCRAKGIQLCAYSPL---- 209
Cdd:cd19082 135 KIRAFGASNWSTERIAEANAYAKAhglpGFAASSPqwslaRPNEppwpgptlVAMDEEMRAWHEENQLPVFAYSSQargf 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1279751533 210 --GAKGTHWGSDSVMDSG-----------VLHEIAKSKGKTVAQVCLRWVYEQ 249
Cdd:cd19082 215 fsKRAAGGAEDDSELRRVyyseenferleRAKELAEEKGVSPTQIALAYVLNQ 267
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-246 |
4.68e-14 |
|
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: 71.58 E-value: 4.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 13 RIGLGTAVQGPRPDPV---RAAVLRAIQLGYRHFDTAAHYA---TEAPIGEAAAEAVRTGLVaSREDLFVTSKV------ 80
Cdd:cd19099 5 SLGLGTYRGDSDDETDeeyREALKAALDSGINVIDTAINYRggrSERLIGKALRELIEKGGI-KRDEVVIVTKAgyipgd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 81 ------------WCADAHRDRVL----------PA-----LRRTLSNLQMEYVDLYMVHWPVTMKAGRFTAPFTPEdfep 133
Cdd:cd19099 84 gdeplrplkyleEKLGRGLIDVAdsaglrhcisPAyledqIERSLKRLGLDTIDLYLLHNPEEQLLELGEEEFYDR---- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 134 fdMRAVWEAMEECHRLGLAKAIGV-CNFSCKKLETLLSFATIPPVVN---------------QVEINPV----------W 187
Cdd:cd19099 160 --LEEAFEALEEAVAEGKIRYYGIsTWDGFRAPPALPGHLSLEKLVAaaeevggdnhhfkviQLPLNLLepealtekntV 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1279751533 188 QQRKLR--EFCRAKGIQLCAYSPLGAkgthwGSDSVMDSGVLHEiAKSKGKTVAQVCLRWV 246
Cdd:cd19099 238 KGEALSllEAAKELGLGVIASRPLNQ-----GQLLGELRLADLL-ALPGGATLAQRALQFA 292
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
14-284 |
9.81e-14 |
|
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: 70.34 E-value: 9.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 14 IGLG----TAVQGPRPDPVRA-AVLR-AIQLGYRHFDTAAHYAT---EAPIGEAaaeavrtgLVASREDLFVTSK----- 79
Cdd:cd19078 7 IGLGcmgmSHGYGPPPDKEEMiELIRkAVELGITFFDTAEVYGPytnEELVGEA--------LKPFRDQVVIATKfgfki 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 80 -----VWCA-DAHRDRVLPALRRTLSNLQMEYVDLYMVHwpvtmkagRFTaPFTPedfepfdMRAVWEAMEECHRLGLAK 153
Cdd:cd19078 79 dggkpGPLGlDSRPEHIRKAVEGSLKRLQTDYIDLYYQH--------RVD-PNVP-------IEEVAGTMKELIKEGKIR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 154 AIGVCNFSckkLETLLSFATIPPVVN-QVEINPVWQ--QRKLREFCRAKGIQLCAYSPLGaKGTHWGS---DSVMDSG-- 225
Cdd:cd19078 143 HWGLSEAG---VETIRRAHAVCPVTAvQSEYSMMWRepEKEVLPTLEELGIGFVPFSPLG-KGFLTGKideNTKFDEGdd 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 226 --------------------VLHEIAKSKGKTVAQVCLRWVYEQGDCL--IVKSFDEGRMKENLDIVDWELSEEERQRIS 283
Cdd:cd19078 219 raslprftpealeanqalvdLLKEFAEEKGATPAQIALAWLLAKKPWIvpIPGTTKLSRLEENIGAADIELTPEELREIE 298
|
.
gi 1279751533 284 K 284
Cdd:cd19078 299 D 299
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
5-156 |
1.87e-13 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 69.60 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 5 GRAPCGLPRIGLGTA----VQGP-RPDPVRAAVLRAIQLGYRHFDTAAHY---ATEAPIGEAAAEAvrtglvasREDLFV 76
Cdd:cd19104 6 GRTGLKVSELTFGGGgiggLMGRtTREEQIAAVRRALDLGINFFDTAPSYgdgKSEENLGRALKGL--------PAGPYI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 77 TSKVWCADAHRDRVLPALRR----TLSNLQMEYVDLYMVHWPVTMKAG-RFTAPFTPEDFepFDMRAVWEAMEECHRLGL 151
Cdd:cd19104 78 TTKVRLDPDDLGDIGGQIERsvekSLKRLKRDSVDLLQLHNRIGDERDkPVGGTLSTTDV--LGLGGVADAFERLRSEGK 155
|
....*
gi 1279751533 152 AKAIG 156
Cdd:cd19104 156 IRFIG 160
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
12-284 |
1.95e-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: 69.61 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 12 PRIGLGT------AVQGPRPDPVR-AAVLRAIQLGYRHFDTAAHY---ATEAPIGEAAAE-------AVRTGLVASREDl 74
Cdd:cd19149 12 SVIGLGTwaigggPWWGGSDDNESiRTIHAALDLGINLIDTAPAYgfgHSEEIVGKAIKGrrdkvvlATKCGLRWDREG- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 75 fvTSKVWCADAHR-------DRVLPALRRTLSNLQMEYVDLYMVHWPvtmkagrftAPFTP-EDfepfdmraVWEAMEEC 146
Cdd:cd19149 91 --GSFFFVRDGVTvyknlspESIREEVEQSLKRLGTDYIDLYQTHWQ---------DVETPiEE--------TMEALEEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 147 HRLGLAKAIGVCNFSCKKLETLLSFATIPpvVNQVEINPVWQQ--RKLREFCRAKGIQLCAYSPLG-------------- 210
Cdd:cd19149 152 KRQGKIRAIGASNVSVEQIKEYVKAGQLD--IIQEKYSMLDRGieKELLPYCKKNNIAFQAYSPLEqglltgkitpdref 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 211 AKGTH-----WGS-DSVMDSGVLHE----IAKSKGKTVAQVCLRWVYEQGDC--LIVKSFDEGRMKENLDIVDWELSEEE 278
Cdd:cd19149 230 DAGDArsgipWFSpENREKVLALLEkwkpLCEKYGCTLAQLVIAWTLAQPGItsALCGARKPEQAEENAKAGDIRLSAED 309
|
....*.
gi 1279751533 279 RQRISK 284
Cdd:cd19149 310 IATMRS 315
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-255 |
6.85e-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: 381323 [Multi-domain] Cd Length: 267 Bit Score: 64.47 E-value: 6.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 13 RIGLGTA---------VQGPRPDPVRA-AVLR-AIQLGYRHFDTAAHYAT-EAPIGEAAaeavrtglvASREDLFVTSKV 80
Cdd:cd19097 2 KLALGTAqfgldygiaNKSGKPSEKEAkKILEyALKAGINTLDTAPAYGDsEKVLGKFL---------KRLDKFKIITKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 81 ----WCADAHRDRVLPALRRTLSNLQMEYVDLYMVHWPvtmkagrftapftpeDFEPFDMRAVWEAMEECHRLGLAKAIG 156
Cdd:cd19097 73 pplkEDKKEDEAAIEASVEASLKRLKVDSLDGLLLHNP---------------DDLLKHGGKLVEALLELKKEGLIRKIG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 157 VcnfSC---KKLETLLSfaTIPPVVNQVEINpVWQQRKLRE-FCR---AKGIQLCAYSP-----LGAKGTHWGSDSvmdS 224
Cdd:cd19097 138 V---SVyspEELEKALE--SFKIDIIQLPFN-ILDQRFLKSgLLAklkKKGIEIHARSVflqglLLMEPDKLPAKF---A 208
|
250 260 270
....*....|....*....|....*....|....*....
gi 1279751533 225 GV------LHEIAKSKGKTVAQVCLRWV--YEQGDCLIV 255
Cdd:cd19097 209 PAkpllkkLHELAKKLGLSPLELALGFVlsLPEIDKIVV 247
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
43-282 |
1.31e-11 |
|
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: 64.16 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 43 FDTAAHY---ATEAPIGEAAAEavrtglvaSREDLFVTSK-VWCADA--------HRDRVLPALRRTLSNLQMEYVDLYM 110
Cdd:cd19080 48 IDTANNYtngTSERLLGEFIAG--------NRDRIVLATKyTMNRRPgdpnaggnHRKNLRRSVEASLRRLQTDYIDLLY 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 111 VHWPvtmkagRFTAPftPEDFepfdMRavweAMEECHRLGLAKAIGVCNF------SCKKLETLLSFAtiPPVVNQVEIN 184
Cdd:cd19080 120 VHAW------DFTTP--VEEV----MR----ALDDLVRAGKVLYVGISDTpawvvaRANTLAELRGWS--PFVALQIEYS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 185 PVwqQRKL-REF---CRAKGIQLCAYSPLG------------------AKGTHWGSDSVMD-----SGVLHEIAKSKGKT 237
Cdd:cd19080 182 LL--ERTPeRELlpmARALGLGVTPWSPLGgglltgkyqrgeegrageAKGVTVGFGKLTErnwaiVDVVAAVAEELGRS 259
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1279751533 238 VAQVCLRWVYEQGDCL--IVKSFDEGRMKENLDIVDWELSEEERQRI 282
Cdd:cd19080 260 AAQVALAWVRQKPGVVipIIGARTLEQLKDNLGALDLTLSPEQLARL 306
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
10-172 |
1.78e-11 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 63.84 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 10 GLPRIGLGTAV------QGPRPDPVRAAVLRAIQLGYRHFDTAAHYA-TEAPIGEAAAeAVRTGLvaSREDLFVTSKV-- 80
Cdd:cd19164 12 GLPPLIFGAATfsyqytTDPESIPPVDIVRRALELGIRAFDTSPYYGpSEIILGRALK-ALRDEF--PRDTYFIITKVgr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 81 ---WCADAHRDRVLPALRRTLSNLQMEYVDLYMVHwpvtmkagrfTAPFTPEDfepfdmrAVWEAMEECHRL---GLAKA 154
Cdd:cd19164 89 ygpDDFDYSPEWIRASVERSLRRLHTDYLDLVYLH----------DVEFVADE-------EVLEALKELFKLkdeGKIRN 151
|
170
....*....|....*...
gi 1279751533 155 IGVcnfSCKKLETLLSFA 172
Cdd:cd19164 152 VGI---SGYPLPVLLRLA 166
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
3-278 |
3.91e-10 |
|
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
Pssm-ID: 381376 [Multi-domain] Cd Length: 309 Bit Score: 59.78 E-value: 3.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 3 ATGRAPCGLPRIGLGTAVQGPRPDPV---RAAVLRAIQLGYRHFDTAAHYAteAPIGEAA---AEAVRTGLVASREDLFV 76
Cdd:cd19150 4 RCGKSGLKLPALSLGLWHNFGDDTPLetqRAILRTAFDLGITHFDLANNYG--PPPGSAEenfGRILREDFAGYRDELII 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 77 TSK----VWCAD----AHRDRVLPALRRTLSNLQMEYVDLYMVHwpvtmkagRFTaPFTPedfepfdMRAVWEAMEECHR 148
Cdd:cd19150 82 STKagydMWPGPygewGSRKYLLASLDQSLKRMGLDYVDIFYSH--------RFD-PDTP-------LEETMGALDHAVR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 149 LGLAKAIGVCNFSCKKLE---TLLSFATIPPVVNQVEINPV--WQQRK-LREFCRAKGIQLCAYSPLG------------ 210
Cdd:cd19150 146 SGKALYVGISSYSPERTReaaAILRELGTPLLIHQPSYNMLnrWVEESgLLDTLQELGVGCIAFTPLAqglltdkylngi 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 211 ------AKGTHWGSDSVMDSGV-----LHEIAKSKGKTVAQVCLRWVYEQG---DCLIVKSFDEgRMKENLDIVD-WELS 275
Cdd:cd19150 226 pegsraSKERSLSPKMLTEANLnsiraLNEIAQKRGQSLAQMALAWVLRDGrvtSALIGASRPE-QLEENVGALDnLTFS 304
|
...
gi 1279751533 276 EEE 278
Cdd:cd19150 305 ADE 307
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
12-246 |
6.88e-10 |
|
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: 58.34 E-value: 6.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 12 PRIGLGT----AVQGPRPDPVRAA--VLRAIQLGYRHFDTAAHYAT---EapigEAAAEAVRTGlvaSREDLFVTSK--V 80
Cdd:cd19096 1 SVLGFGTmrlpESDDDSIDEEKAIemIRYAIDAGINYFDTAYGYGGgksE----EILGEALKEG---PREKFYLATKlpP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 81 WCADAHRDrVLPALRRTLSNLQMEYVDLYMVHWPVTmkagrftaPFTPEDFEPFDMravWEAMEECHRLGLAKAIGvcnF 160
Cdd:cd19096 74 WSVKSAED-FRRILEESLKRLGVDYIDFYLLHGLNS--------PEWLEKARKGGL---LEFLEKAKKEGLIRHIG---F 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 161 SckkleTLLSFATIPPVVN-------QVEIN----PVWQQRKLREFCRAKGIQLCAYSPLGaKGTHwgsdsVMDSGVLHE 229
Cdd:cd19096 139 S-----FHDSPELLKEILDsydfdfvQLQYNyldqENQAGRPGIEYAAKKGMGVIIMEPLK-GGGL-----ANNPPEALA 207
|
250
....*....|....*..
gi 1279751533 230 IAKSKGKTVAQVCLRWV 246
Cdd:cd19096 208 ILCGAPLSPAEWALRFL 224
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-245 |
8.34e-10 |
|
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: 58.88 E-value: 8.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGT-----------AVQGPR--PDPVRAAVLRAIQLGYRHFDTAAHYateapiGEAAAEAVRTGLVA--SREDLF 75
Cdd:cd19103 4 LPKIALGTwswgsggaggdQVFGNHldEDTLKAVFDKAMAAGLNLWDTAAVY------GMGASEKILGEFLKryPREDYI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 76 VTSKV--WCADAHRDRVLPALRRTLSNLQMEYVDLYMVHWPVTMKAgrftapFTPedfEPFDMRAVweameechrlGLAK 153
Cdd:cd19103 78 ISTKFtpQIAGQSADPVADMLEGSLARLGTDYIDIYWIHNPADVER------WTP---ELIPLLKS----------GKVK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 154 AIGVCNFS---CKKLETLLSFATIP--PVVNQVE-INPVWQQRKLREFCRAKGIQLCAYSPL------GAKGTH----WG 217
Cdd:cd19103 139 HVGVSNHNlaeIKRANEILAKAGVSlsAVQNHYSlLYRSSEEAGILDYCKENGITFFAYMVLeqgalsGKYDTKhplpEG 218
|
250 260 270
....*....|....*....|....*....|....*....
gi 1279751533 218 SDSVMD-----------SGVLHEIAKSKGKTVAQVCLRW 245
Cdd:cd19103 219 SGRAETynpllpqleelTAVMAEIGAKHGASIAQVAIAW 257
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
26-284 |
1.37e-09 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 58.46 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 26 DPVRAAVLRAIQLGYRHFDTAAHYAteAPIGEAA---AEAVRTGLVASREDLFVTSK----VW----CADAHRDRVLPAL 94
Cdd:PRK09912 43 ESQRAILRKAFDLGITHFDLANNYG--PPPGSAEenfGRLLREDFAAYRDELIISTKagydMWpgpyGSGGSRKYLLASL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 95 RRTLSNLQMEYVDLYMVHwpvtmkagRFTAPfTPedfepfdMRAVWEAMEECHRLGLAKAIGVCNFS---CKKLETLLSF 171
Cdd:PRK09912 121 DQSLKRMGLEYVDIFYSH--------RVDEN-TP-------MEETASALAHAVQSGKALYVGISSYSperTQKMVELLRE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 172 ATIPPVVNQVEINPV--W-QQRKLREFCRAKGIQLCAYSPLgAKGTHWG-------SDSVMDS----------------- 224
Cdd:PRK09912 185 WKIPLLIHQPSYNLLnrWvDKSGLLDTLQNNGVGCIAFTPL-AQGLLTGkylngipQDSRMHRegnkvrgltpkmltean 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1279751533 225 ----GVLHEIAKSKGKTVAQVCLRWVYEQG---DCLIVKSFDEgRMKENLDIV-DWELSEEERQRISK 284
Cdd:PRK09912 264 lnslRLLNEMAQQRGQSMAQMALSWLLKDErvtSVLIGASRAE-QLEENVQALnNLTFSTEELAQIDQ 330
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
26-209 |
2.49e-09 |
|
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: 57.22 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 26 DPVRAAVLRAIQLGYRHFDTAAHYA---TEAPIGEAAAEavrtgLVASREDLFVTSKV---WCADAHRDR------VLPA 93
Cdd:cd19143 31 DEAKECMKAAYDAGVNFFDNAEVYAngqSEEIMGQAIKE-----LGWPRSDYVVSTKIfwgGGGPPPNDRglsrkhIVEG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 94 LRRTLSNLQMEYVDLYMVHWPvtmkagrftAPFTPedfepfdMRAVWEAMEECHRLGLAKAIGVCNFSCKKLETLLSFAT 173
Cdd:cd19143 106 TKASLKRLQLDYVDLVFCHRP---------DPATP-------IEETVRAMNDLIDQGKAFYWGTSEWSAQQIEEAHEIAD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1279751533 174 ----IPPVVNQVEINPVWQQRKLREF---CRAKGIQLCAYSPL 209
Cdd:cd19143 170 rlglIPPVMEQPQYNLFHRERVEVEYaplYEKYGLGTTTWSPL 212
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
14-288 |
4.79e-09 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 56.79 E-value: 4.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 14 IGLGTAVQGPRPDPVRA------AVLRAIQLgyrhFDTAAHYA----------TEAPIGEAAAEAvrtglvASREDLFVT 77
Cdd:PRK10625 16 LGLGTMTFGEQNSEADAhaqldyAVAQGINL----IDVAEMYPvpprpetqglTETYIGNWLAKR------GSREKLIIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 78 SKV----WCADA--------HRDRVLPALRRTLSNLQMEYVDLYMVHWPV--TMKAGRFTAPFTpEDFEPFDMRAVWEAM 143
Cdd:PRK10625 86 SKVsgpsRNNDKgirpnqalDRKNIREALHDSLKRLQTDYLDLYQVHWPQrpTNCFGKLGYSWT-DSAPAVSLLETLDAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 144 EECHRLGLAKAIGVCNFSCKKLETLLSFATIPPVVNQVEI-NPVWQQRK-----LREFCRAKGIQLCAYS---------- 207
Cdd:PRK10625 165 AEQQRAGKIRYIGVSNETAFGVMRYLHLAEKHDLPRIVTIqNPYSLLNRsfevgLAEVSQYEGVELLAYSclafgtltgk 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 208 ------PLGAKGT-------HWGSDSVMDSGVLHEIAKSKGKTVAQVCLRWVYEQGdclIVKSFDEG-----RMKENLDI 269
Cdd:PRK10625 245 ylngakPAGARNTlfsrftrYSGEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQP---FVASTLLGattmeQLKTNIES 321
|
330
....*....|....*....
gi 1279751533 270 VDWELSEEERQRISKIPQR 288
Cdd:PRK10625 322 LHLTLSEEVLAEIEAVHQV 340
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
4-210 |
6.41e-09 |
|
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381379 [Multi-domain] Cd Length: 294 Bit Score: 56.00 E-value: 6.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 4 TGRAPCGLPRIGLGTAVQ-GPRPDPVRAAVLRAIQLGYRHFDTAAHYA---TEAPIGEAAAeavrtGLVASREDLFVTSK 79
Cdd:cd19153 10 GNVSPVGLGTAALGGVYGdGLEQDEAVAIVAEAFAAGINHFDTSPYYGaesSEAVLGKALA-----ALQVPRSSYTVATK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 80 V-----WCADAHRDRVLPALRRTLSNLQMEYVDLYMVHwpvtmkagrftapftpeDFEPFDM-RAVWEAMEECHRL---G 150
Cdd:cd19153 85 VgryrdSEFDYSAERVRASVATSLERLHTTYLDVVYLH-----------------DIEFVDYdTLVDEALPALRTLkdeG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1279751533 151 LAKAIGVCNFSCKKLETLLSFATI-PPVVNQVEINPVWQQRKL----REFCRAKGIQLCAYSPLG 210
Cdd:cd19153 148 VIKRIGIAGYPLDTLTRATRRCSPgSLDAVLSYCHLTLQDARLesdaPGLVRGAGPHVINASPLS 212
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
11-282 |
8.22e-09 |
|
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: 55.71 E-value: 8.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 11 LPRIGLGTAVQGPRPDPVR-----AAVLRAIQLGYRHFDTAAHYATEAP------IGEAAAEAVRtglvaSREDLFVTSK 79
Cdd:cd19077 5 VGPIGLGLMGLTWRPNPTPdeeafETMKAALDAGSNLWNGGEFYGPPDPhanlklLARFFRKYPE-----YADKVVLSVK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 80 VWC------ADAHRDRVLPALRRTLSNLQM-EYVDLYmvhwpvtmKAGRFTAPFTPEDFepfdMRAVWEAMEEchrlGLA 152
Cdd:cd19077 80 GGLdpdtlrPDGSPEAVRKSIENILRALGGtKKIDIF--------EPARVDPNVPIEET----IKALKELVKE----GKI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 153 KAIGVCNFSckkLETLL-SFATIPPVVNQVEINPvWQQRKLR----EFCRAKGIQLCAYSPLGaKGT---HWGSDSVMDS 224
Cdd:cd19077 144 RGIGLSEVS---AETIRrAHAVHPIAAVEVEYSL-FSREIEEngvlETCAELGIPIIAYSPLG-RGLltgRIKSLADIPE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 225 G----------------------VLHEIAKSKGKTVAQVCLRWVYEQGDCLIVK---SFDEGRMKENLDIVDWELSEEER 279
Cdd:cd19077 219 GdfrrhldrfngenfeknlklvdALQELAEKKGCTPAQLALAWILAQSGPKIIPipgSTTLERVEENLKAANVELTDEEL 298
|
...
gi 1279751533 280 QRI 282
Cdd:cd19077 299 KEI 301
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
12-245 |
9.06e-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: 381391 [Multi-domain] Cd Length: 291 Bit Score: 55.42 E-value: 9.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 12 PRIGLGTAVQGPRPDPVRA-AVL-RAIQLGYRHFDTAAHYAT----------EAPIGEAAAEAVRtglvasREDLFVTSK 79
Cdd:cd19752 1 SELCLGTMYFGTRTDEETSfAILdRYVAAGGNFLDTANNYAFwteggvggesERLIGRWLKDRGN------RDDVVIATK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 80 V---------WCADAH---RDRVLPALRRTLSNLQMEYVDLYMVHwpvtmkAGRFTAPFTpedfepfdmravwEAMEECH 147
Cdd:cd19752 75 VgagprdpdgGPESPEglsAETIEQEIDKSLRRLGTDYIDLYYAH------VDDRDTPLE-------------ETLEAFN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 148 RL---GLAKAIGVCNFSCKKLET---------LLSFATIPPVVNQVEINP---VWQQRKLR----EFCRAKG-IQLCAYS 207
Cdd:cd19752 136 ELvkaGKVRAIGASNFAAWRLERarqiarqqgWAEFSAIQQRHSYLRPRPgadFGVQRIVTdellDYASSRPdLTLLAYS 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1279751533 208 PL--GAKGTHW--------GSDSVMDSGVLHEIAKSKGKTVAQVCLRW 245
Cdd:cd19752 216 PLlsGAYTRPDrplpeqydGPDSDARLAVLEEVAGELGATPNQVVLAW 263
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
4-246 |
2.06e-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: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 4 TGRAPCGLPRIGLG-----TAVQgpRPDPVRAAVLRAIQLGYRHFDTAAHYAteAPIGEAAA---EAVRTGLVASREDLF 75
Cdd:cd19151 5 CGRSGLKLPAISLGlwhnfGDVD--RYENSRAMLRRAFDLGITHFDLANNYG--PPPGSAEEnfgRILKEDLKPYRDELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 76 VTSKV-----------WcadAHRDRVLPALRRTLSNLQMEYVDLYMVHWPvtmkagrftAPFTPedfepfdMRAVWEAME 144
Cdd:cd19151 81 ISTKAgytmwpgpygdW---GSKKYLIASLDQSLKRMGLDYVDIFYHHRP---------DPETP-------LEETMGALD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 145 ECHRLGLAKAIGVCNFS---CKKLETLLSFATIPPVVNQVEINPV--WQQRKLREFCRAKGIQLCAYSPL---------- 209
Cdd:cd19151 142 QIVRQGKALYVGISNYPpeeAREAAAILKDLGTPCLIHQPKYSMFnrWVEEGLLDVLEEEGIGCIAFSPLaqglltdryl 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1279751533 210 ---------GAKGTHWGSDSVMDSGV-----LHEIAKSKGKTVAQVCLRWV 246
Cdd:cd19151 222 ngipedsraAKGSSFLKPEQITEEKLakvrrLNEIAQARGQKLAQMALAWV 272
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
6-245 |
4.50e-08 |
|
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo sapiens, Rattus norvegicus, and Mus musculus, are founding members of aldo-keto reductase family 6 member A9 (AKR6A9), A12 (AKR6A12), A14 (AKR6A14), respectively. KCAB3B, also called Shaker channel b-subunit 3 (Kvb3), K(+) channel subunit beta-3, or Kv-beta-3, is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. It alters the functional properties of Kv1.5.
Pssm-ID: 381386 [Multi-domain] Cd Length: 325 Bit Score: 53.84 E-value: 4.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 6 RAPCglprIGLGTAVQ-GPR-PDPVRAAVLR-AIQLGYRHFDTAAHYATeapigeAAAEAVRTGLVAS----REDLFVTS 78
Cdd:cd19160 14 RVSC----LGLGTWVTfGSQiSDETAEDLLTvAYEHGVNLFDTAEVYAA------GKAERTLGNILKSkgwrRSSYVVTT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 79 KV-WCADAHRDR------VLPALRRTLSNLQMEYVDLYMvhwpvtmkAGRfTAPFTPedfepfdMRAVWEAMEECHRLGL 151
Cdd:cd19160 84 KIyWGGQAETERglsrkhIIEGLRGSLDRLQLEYVDIVF--------ANR-SDPNSP-------MEEIVRAMTYVINQGM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 152 AKAIGVCNFSCKKLETLLS----FATIPPVVNQVEINpVWQQRK----LREFCRAKGIQLCAYSPLGA------------ 211
Cdd:cd19160 148 AMYWGTSRWSAMEIMEAYSvarqFNLIPPVCEQAEYH-LFQREKvemqLPELYHKIGVGSVTWSPLACglitgkydgrvp 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1279751533 212 -------KGTHWGSDSVMDSG---------VLHEIAKSKGKTVAQVCLRW 245
Cdd:cd19160 227 dtcraavKGYQWLKEKVQSEEgkkqqakvkELHPIADRLGCTVAQLAIAW 276
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
10-282 |
2.55e-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: 51.28 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 10 GLPRIGLGTAVQGPRPDPVRAAVLR-AIQLGYRHFDTAAHY---ATEAPIGEAAAEAVRtglvasrEDLFVTSKVWCADA 85
Cdd:cd19145 16 GLGCMGLSGDYGAPKPEEEGIALIHhAFNSGVTFLDTSDIYgpnTNEVLLGKALKDGPR-------EKVQLATKFGIHEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 86 HRDRVL----PALRR-----TLSNLQMEYVDLYMVHwpvtmkagRFTAPFTPEDfepfDMRAVWEAMEEchrlGLAKAIG 156
Cdd:cd19145 89 GGSGVEvrgdPAYVRaaceaSLKRLDVDYIDLYYQH--------RIDTTVPIEI----TMGELKKLVEE----GKIKYIG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 157 VCNFSCkklETLLSFATIPPVVN-QVEINpVWQqRKLRE----FCRAKGIQLCAYSPLGaKGTHWGSDSVMDSG------ 225
Cdd:cd19145 153 LSEASA---DTIRRAHAVHPITAvQLEWS-LWT-RDIEEeiipTCRELGIGIVPYSPLG-RGFFAGKAKLEELLensdvr 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1279751533 226 ---------------VLHE----IAKSKGKTVAQVCLRWVYEQGD--CLIVKSFDEGRMKENLDIVDWELSEEERQRI 282
Cdd:cd19145 227 kshprfqgenleknkVLYErveaLAKKKGCTPAQLALAWVLHQGEdvVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
14-210 |
1.84e-06 |
|
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: 48.88 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 14 IGLGTAVQ--GPRPDPVRAAVLR-AIQLGYRHFDTAAHYATeapigeAAAEAVRTGLVAS----REDLFVTSKV-WCADA 85
Cdd:cd19159 16 LGLGTWVTfgGQISDEVAERLMTiAYESGVNLFDTAEVYAA------GKAEVILGSIIKKkgwrRSSLVITTKLyWGGKA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 86 HRDR------VLPALRRTLSNLQMEYVDLYMVHWPVTMkagrftapfTPedfepfdMRAVWEAMEECHRLGLAKAIGVCN 159
Cdd:cd19159 90 ETERglsrkhIIEGLKGSLQRLQLEYVDVVFANRPDSN---------TP-------MEEIVRAMTHVINQGMAMYWGTSR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1279751533 160 FSCKKLETLLS----FATIPPVVNQVEINpVWQQRK----LREFCRAKGIQLCAYSPLG 210
Cdd:cd19159 154 WSAMEIMEAYSvarqFNMIPPVCEQAEYH-LFQREKvevqLPELYHKIGVGAMTWSPLA 211
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
14-267 |
7.90e-06 |
|
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381367 [Multi-domain] Cd Length: 310 Bit Score: 46.67 E-value: 7.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 14 IGLGTAVQ--GPRPDPVRAAVLR-AIQLGYRHFDTAAHYATEApigeaaAEAVRTGLVAS----REDLFVTSKV-WCADA 85
Cdd:cd19141 15 LGLGTWVTfgSQISDEVAEELVTlAYENGINLFDTAEVYAAGK------AEIVLGKILKKkgwrRSSYVITTKIfWGGKA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 86 HRDR------VLPALRRTLSNLQMEYVDLYMVHWPvtmkagrftAPFTPedfepfdMRAVWEAMEECHRLGLAKAIGVCN 159
Cdd:cd19141 89 ETERglsrkhIIEGLKASLERLQLEYVDIVFANRP---------DPNTP-------MEEIVRAFTHVINQGMAMYWGTSR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 160 FSCKKLETLLS----FATIPPVVNQVEINpVWQQRK----LREFCRAKGIQLCAYSPLGA-------------------K 212
Cdd:cd19141 153 WSAMEIMEAYSvarqFNLIPPIVEQAEYH-LFQREKvemqLPELFHKIGVGAMTWSPLACgilsgkyddgvpeysraslK 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1279751533 213 GTHWGSDSVMD-SGVLHE--------IAKSKGKTVAQVCLRWV--YEQGDCLIVKSFDEGRMKENL 267
Cdd:cd19141 232 GYQWLKEKILSeEGRRQQaklkelqiIADRLGCTLPQLAIAWClkNEGVSSVLLGASSTEQLYENL 297
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
14-267 |
1.51e-05 |
|
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.
Pssm-ID: 381384 [Multi-domain] Cd Length: 324 Bit Score: 45.85 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 14 IGLGTAVQ--GPRPDPVRAAVLR-AIQLGYRHFDTAAHYATeapigeAAAEAVRTGLVAS----REDLFVTSKV-WCADA 85
Cdd:cd19158 16 LGLGTWVTfgGQITDEMAEHLMTlAYDNGINLFDTAEVYAA------GKAEVVLGNIIKKkgwrRSSLVITTKIfWGGKA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 86 HRDR------VLPALRRTLSNLQMEYVDLYMVHWPvtmkagrftAPFTPedfepfdMRAVWEAMEECHRLGLAKAIGVCN 159
Cdd:cd19158 90 ETERglsrkhIIEGLKASLERLQLEYVDVVFANRP---------DPNTP-------MEETVRAMTHVINQGMAMYWGTSR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 160 FSCKKLETLLS----FATIPPVVNQVEINPVWQQR---KLREFCRAKGIQLCAYSPLGA-------------------KG 213
Cdd:cd19158 154 WSSMEIMEAYSvarqFNLIPPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPLACgivsgkydsgippysraslKG 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1279751533 214 THWGSDSVMDS---------GVLHEIAKSKGKTVAQVCLRWVY--EQGDCLIVKSFDEGRMKENL 267
Cdd:cd19158 234 YQWLKDKILSEegrrqqaklKELQAIAERLGCTLPQLAIAWCLrnEGVSSVLLGASNAEQLMENI 298
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
14-112 |
1.46e-04 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 42.84 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279751533 14 IGLGTA----VQGPRP-DPVRAAVLRAIQLGYRHFDTAAHYateapiGEAAAEAVR-TGLVAS---REDLFVTSKvwCA- 83
Cdd:PLN02587 14 VGFGASplgsVFGPVSeEDAIASVREAFRLGINFFDTSPYY------GGTLSEKVLgKALKALgipREKYVVSTK--CGr 85
|
90 100 110
....*....|....*....|....*....|....
gi 1279751533 84 -----DAHRDRVLPALRRTLSNLQMEYVDLYMVH 112
Cdd:PLN02587 86 ygegfDFSAERVTKSVDESLARLQLDYVDILHCH 119
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
12-80 |
1.63e-03 |
|
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381378 [Multi-domain] Cd Length: 308 Bit Score: 39.51 E-value: 1.63e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1279751533 12 PRIGLGTAVQG----PRPDP-VRAAVLRAIQLGYRHFDTAAHY---ATEAPIGEAAAEavrtglvASREDLFVTSKV 80
Cdd:cd19152 1 PKLGFGTAPLGnlyeAVSDEeAKATLVAAWDLGIRYFDTAPWYgagLSEERLGAALRE-------LGREDYVISTKV 70
|
|
| |
