|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
6-287 |
0e+00 |
|
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: 534.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 6 RFFELNTGAKLPCVGLGTY----AMVATAIEQAIKIGYRHIDCASIYGNEKEIGGVLKKLIGDGFVKREELFITSKLWSN 81
Cdd:cd19125 1 RFFKLNTGAKIPAVGLGTWqadpGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLWCT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 82 DHLPEDVPKALEKTLQDLQIDYVDLYLIHWPASLKKESLMPTPEMLTKPDITSTWKAMEALYDSGKARAIGVSNFSSKKL 161
Cdd:cd19125 81 DHAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKGAHMPEPEEVLPPDIPSTWKAMEKLVDSGKVRAIGVSNFSVKKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 162 TDLLNVARVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGSQSKGEVRLKVLQNPIVTEVAEKLGKTTAQVALRW 241
Cdd:cd19125 161 EDLLAVARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGTTWVKKNVLKDPIVTKVAEKLGKTPAQVALRW 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 145330687 242 GLQTGHSVLPKSSSGARLKENLDVFDWSIPEDLFTKFSNIPQAKVL 287
Cdd:cd19125 241 GLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSIEQQRRV 286
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
16-273 |
2.03e-126 |
|
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: 360.26 E-value: 2.03e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 16 LPCVGLGTYAM----VATAIEQAIKIGYRHIDCASIYGNEKEIGGVLKKLigdgFVKREELFITSKLWSNDHLPEDVPKA 91
Cdd:cd19071 1 MPLIGLGTYKLkpeeTAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRES----GVPREELFITTKLWPTDHGYERVREA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 92 LEKTLQDLQIDYVDLYLIHWPaslkkeslMPTPEMLTKPDITSTWKAMEALYDSGKARAIGVSNFSSKKLTDLLNVARVT 171
Cdd:cd19071 77 LEESLKDLGLDYLDLYLIHWP--------VPGKEGGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAARIK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 172 PAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGSQskgevRLKVLQNPIVTEVAEKLGKTTAQVALRWGLQTGHSVLP 251
Cdd:cd19071 149 PAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRG-----RRPLLDDPVLKEIAKKYGKTPAQVLLRWALQRGVVVIP 223
|
250 260
....*....|....*....|..
gi 145330687 252 KSSSGARLKENLDVFDWSIPED 273
Cdd:cd19071 224 KSSNPERIKENLDVFDFELSEE 245
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
13-273 |
1.86e-119 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 342.81 E-value: 1.86e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 13 GAKLPCVGLGTYAM----VATAIEQAIKIGYRHIDCASIYGNEKEIGGVLKKLigdGfVKREELFITSKLWSNDHLPEDV 88
Cdd:COG0656 2 GVEIPALGLGTWQLpgeeAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAAS---G-VPREELFVTTKVWNDNHGYDDT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 89 PKALEKTLQDLQIDYVDLYLIHWPAslkkeslmptPEmltkpDITSTWKAMEALYDSGKARAIGVSNFSSKKLTDLLNVA 168
Cdd:COG0656 78 LAAFEESLERLGLDYLDLYLIHWPG----------PG-----PYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAET 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 169 RVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGsqskgevRLKVLQNPIVTEVAEKLGKTTAQVALRWGLQTGHS 248
Cdd:COG0656 143 GVKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLG-------RGKLLDDPVLAEIAEKHGKTPAQVVLRWHLQRGVV 215
|
250 260
....*....|....*....|....*
gi 145330687 249 VLPKSSSGARLKENLDVFDWSIPED 273
Cdd:COG0656 216 VIPKSVTPERIRENLDAFDFELSDE 240
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
5-273 |
3.13e-118 |
|
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: 341.31 E-value: 3.13e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 5 IRFFELNTGAKLPCVGLGTY----AMVATAIEQAIKIGYRHIDCASIYGNEKEIGGVLKKLIGDGFVKREELFITSKLWS 80
Cdd:cd19123 1 MKTLPLSNGDLIPALGLGTWkskpGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 81 NDHLPEDVPKALEKTLQDLQIDYVDLYLIHWPASLKKESLMPTP--EMLTKPDI--TSTWKAMEALYDSGKARAIGVSNF 156
Cdd:cd19123 81 NSHAPEDVLPALEKTLADLQLDYLDLYLMHWPVALKKGVGFPESgeDLLSLSPIplEDTWRAMEELVDKGLCRHIGVSNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 157 SSKKLTDLLNVARVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGS-----QSKGEVRLKVLQNPIVTEVAEKLG 231
Cdd:cd19123 161 SVKKLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSgdrpaAMKAEGEPVLLEDPVINKIAEKHG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 145330687 232 KTTAQVALRWGLQTGHSVLPKSSSGARLKENLDVFDWSIPED 273
Cdd:cd19123 241 ASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDAS 282
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
12-283 |
9.54e-118 |
|
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: 339.24 E-value: 9.54e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 12 TGAKLPCVGLGTYA------MVATAIEQAIKIGYRHIDCASIYGNEKEIGGVLKKLIGDGFVK-REELFITSKLWSNDHL 84
Cdd:cd19124 1 SGQTMPVIGMGTASdppspeDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKLWCSDAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 85 PEDVPKALEKTLQDLQIDYVDLYLIHWPASLKKESLM--PTPEMLTKPDITSTWKAMEALYDSGKARAIGVSNFSSKKLT 162
Cdd:cd19124 81 PDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKPGKFSfpIEEEDFLPFDIKGVWEAMEECQRLGLTKAIGVSNFSCKKLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 163 DLLNVARVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGSQSKGEVRLKVLQNPIVTEVAEKLGKTTAQVALRWG 242
Cdd:cd19124 161 ELLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTKWGSNAVMESDVLKEIAAAKGKTVAQVSLRWV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 145330687 243 LQTGHSVLPKSSSGARLKENLDVFDWSIPEDLFTKFSNIPQ 283
Cdd:cd19124 241 YEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEIPQ 281
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
10-273 |
1.01e-109 |
|
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: 319.72 E-value: 1.01e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 10 LNTGAKLPCVGLGTY----AMVATAIEQAIKIGYRHIDCASIYGNEKEIGGVLKKLIGDGF-VKREELFITSKLWSNDHL 84
Cdd:cd19106 1 LHTGQKMPLIGLGTWkskpGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPGKaVPREDLFVTSKLWNTKHH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 85 PEDVPKALEKTLQDLQIDYVDLYLIHWPASLKK-ESLMP-TPEMLTKPDITS---TWKAMEALYDSGKARAIGVSNFSSK 159
Cdd:cd19106 81 PEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERgDNPFPkNPDGTIRYDSTHykeTWKAMEKLVDKGLVKAIGLSNFNSR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 160 KLTDLLNVARVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGSQSK-----GEVRLkvLQNPIVTEVAEKLGKTT 234
Cdd:cd19106 161 QIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPDRpwakpDEPVL--LEEPKVKALAKKYNKSP 238
|
250 260 270
....*....|....*....|....*....|....*....
gi 145330687 235 AQVALRWGLQTGHSVLPKSSSGARLKENLDVFDWSIPED 273
Cdd:cd19106 239 AQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPE 277
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
10-281 |
4.00e-109 |
|
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: 317.43 E-value: 4.00e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 10 LNTGAKLPCVGLGTY----AMVATAIEQAIKIGYRHIDCASIYGNEKEIGGVLKKLIGD-GFVKREELFITSKLWSNDHL 84
Cdd:cd19118 1 LNTGNKIPAIGLGTWqaepGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEePGVKREDLFITSKLWNNSHR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 85 PEDVPKALEKTLQDLQIDYVDLYLIHWPASLKKE-SLMPTPEMLTKPD---------ITSTWKAMEALYDSGKARAIGVS 154
Cdd:cd19118 81 PEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTgDLNPLTAVPTNGGevdldlsvsLVDTWKAMVELKKTGKVKSIGVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 155 NFSSKKLTDLLNVARVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGSQSKGEVRLkvLQNPIVTEVAEKLGKTT 234
Cdd:cd19118 161 NFSIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGNNLAGLPLL--VQHPEVKAIAAKLGKTP 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 145330687 235 AQVALRWGLQTGHSVLPKSSSGARLKENLDVFDwsIPEDLFTKFSNI 281
Cdd:cd19118 239 AQVLIAWGIQRGHSVIPKSVTPSRIRSNFEQVE--LSDDEFNAVTAL 283
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
8-272 |
5.72e-107 |
|
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: 312.81 E-value: 5.72e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 8 FELNTGAKLPCVGLGTYAM----VATAIEQAIKIGYRHIDCASIYGNEKEIGGVLKKLIGDGFVKREELFITSKLWSNDH 83
Cdd:cd19154 4 ITLSNGVKMPLIGLGTWQSkgaeGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLWTHEH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 84 LPEDVPKALEKTLQDLQIDYVDLYLIHWPASLKKE----SLMPTPEMLTKP-DITSTWKAMEALYDSGKARAIGVSNFSS 158
Cdd:cd19154 84 APEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDegesGTMENGMSIHDAvDVEDVWRGMEKVYDEGLTKAIGVSNFNN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 159 KKLTDLLNVARVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGS-------QSKGEVRLKV-LQNPIVTEVAEKL 230
Cdd:cd19154 164 DQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSpgranftKSTGVSPAPNlLQDPIVKAIAEKH 243
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 145330687 231 GKTTAQVALRWGLQTGHSVLPKSSSGARLKENLDVFDWSIPE 272
Cdd:cd19154 244 GKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSE 285
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
8-274 |
1.50e-106 |
|
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: 311.52 E-value: 1.50e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 8 FELNTGAKLPCVGLGTYAM-----VATAIEQAIKIGYRHIDCASIYGNEKEIGGVLKKLIGDGFVKREELFITSKLWSND 82
Cdd:cd19116 3 IKLNDGNEIPAIALGTWKLkddegVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLWNSY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 83 HLPEDVPKALEKTLQDLQIDYVDLYLIHWPASLKKE--SLMPTPEMLTKPDITSTWKAMEALYDSGKARAIGVSNFSSKK 160
Cdd:cd19116 83 HEREQVEPALRESLKRLGLDYVDLYLIHWPVAFKENndSESNGDGSLSDIDYLETWRGMEDLVKLGLTRSIGVSNFNSEQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 161 LTDLLNVARVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGSQ--SKGEVRLKVLQNPIVTEVAEKLGKTTAQVA 238
Cdd:cd19116 163 INRLLSNCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLvpRGQTNPPPRLDDPTLVAIAKKYGKTTAQIV 242
|
250 260 270
....*....|....*....|....*....|....*..
gi 145330687 239 LRWGLQTGHSVLPKSSSGARLKENLDVFDWSI-PEDL 274
Cdd:cd19116 243 LRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLtPEEV 279
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
16-273 |
2.49e-106 |
|
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: 309.56 E-value: 2.49e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 16 LPCVGLGTY-----AMVATAIEQAIKIGYRHIDCASIYGNEKEIGGVLKKLIGDGFVKREELFITSKLWSNDHLPEDVPK 90
Cdd:cd19136 1 MPILGLGTFrlrgeEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 91 ALEKTLQDLQIDYVDLYLIHWPASLKKESLMPTPEMLTKpditSTWKAMEALYDSGKARAIGVSNFSSKKLTDLLNVARV 170
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWPGVQGLKPSDPRNAELRR----ESWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYCEV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 171 TPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGSQskgevRLKVLQNPIVTEVAEKLGKTTAQVALRWGLQTGHSVL 250
Cdd:cd19136 157 PPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSG-----DLRLLEDPTVLAIAKKYGRTPAQVLLRWALQQGIGVI 231
|
250 260
....*....|....*....|...
gi 145330687 251 PKSSSGARLKENLDVFDWSIPED 273
Cdd:cd19136 232 PKSTNPERIAENIKVFDFELSEE 254
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
9-274 |
2.20e-97 |
|
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: 288.36 E-value: 2.20e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 9 ELNTGAKLPCVGLGTYA-------MVATAIEQAIKIGYRHIDCASIYGNEKEIGGVLKKLIGDGFVKREELFITSKLWSN 81
Cdd:cd19108 4 KLNDGHFIPVLGFGTYApeevpksKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKLWCT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 82 DHLPEDVPKALEKTLQDLQIDYVDLYLIHWPASLKK-ESLMPTPE----MLTKPDITSTWKAMEALYDSGKARAIGVSNF 156
Cdd:cd19108 84 FHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPgEELFPKDEngklIFDTVDLCATWEAMEKCKDAGLAKSIGVSNF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 157 SSKKLTDLLNVA--RVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGSQskgevRLK---------VLQNPIVTE 225
Cdd:cd19108 164 NRRQLEMILNKPglKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQ-----RDKewvdqnspvLLEDPVLCA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 145330687 226 VAEKLGKTTAQVALRWGLQTGHSVLPKSSSGARLKENLDVFDWSI-PEDL 274
Cdd:cd19108 239 LAKKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLtSEDM 288
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
10-273 |
2.33e-95 |
|
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid reductase (2,5-DKG reductase) is a founding member of aldo-keto reductase family 5 member F1 (AKR5F1). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381359 [Multi-domain] Cd Length: 255 Bit Score: 281.39 E-value: 2.33e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 10 LNTGAKLPCVGLGTYAMVAT-----AIEQAIKIGYRHIDCASIYGNEKEIGGVLKKLIgdgfVKREELFITSKLWSNDHL 84
Cdd:cd19133 3 LNNGVEMPILGFGVFQIPDPeecerAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKSG----IPREELFITTKLWIQDAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 85 PEDVPKALEKTLQDLQIDYVDLYLIHWPASlkkeslmptpemltkpDITSTWKAMEALYDSGKARAIGVSNFSSKKLTDL 164
Cdd:cd19133 79 YEKAKKAFERSLKRLGLDYLDLYLIHQPFG----------------DVYGAWRAMEELYKEGKIRAIGVSNFYPDRLVDL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 165 LNVARVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLgsqskGEVRLKVLQNPIVTEVAEKLGKTTAQVALRWGLQ 244
Cdd:cd19133 143 ILHNEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPF-----AEGRNNLFENPVLTEIAEKYGKSVAQVILRWLIQ 217
|
250 260
....*....|....*....|....*....
gi 145330687 245 TGHSVLPKSSSGARLKENLDVFDWSIPED 273
Cdd:cd19133 218 RGIVVIPKSVRPERIAENFDIFDFELSDE 246
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
10-273 |
1.45e-92 |
|
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: 274.63 E-value: 1.45e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 10 LNTGAKLPCVGLGTYAM----VATAIEQAIKIGYRHIDCASIYGNEKEIGgvlkKLIGDGFVKREELFITSKLWSNDHLP 85
Cdd:cd19131 4 LNDGNTIPQLGLGVWQVsndeAASAVREALEVGYRSIDTAAIYGNEEGVG----KAIRASGVPREELFITTKLWNSDQGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 86 EDVPKALEKTLQDLQIDYVDLYLIHWPaslkkeslMPTpemltKPDITSTWKAMEALYDSGKARAIGVSNFSSKKLTDLL 165
Cdd:cd19131 80 DSTLRAFDESLRKLGLDYVDLYLIHWP--------VPA-----QDKYVETWKALIELKKEGRVKSIGVSNFTIEHLQRLI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 166 NVARVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGSQskgevrlKVLQNPIVTEVAEKLGKTTAQVALRWGLQT 245
Cdd:cd19131 147 DETGVVPVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQG-------GLLSDPVIGEIAEKHGKTPAQVVIRWHLQN 219
|
250 260
....*....|....*....|....*...
gi 145330687 246 GHSVLPKSSSGARLKENLDVFDWSIPED 273
Cdd:cd19131 220 GLVVIPKSVTPSRIAENFDVFDFELDAD 247
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
7-283 |
1.46e-92 |
|
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: 276.33 E-value: 1.46e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 7 FFELNTGAKLPCVGLGTY----AMVATAIEQAIKIGYRHIDCASIYGNEKEIGGVLKKLIGDGFVKREELFITSKLWSND 82
Cdd:cd19155 3 CVTFNNGEKMPVVGLGTWqsspEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLPPGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 83 HLPEDVPKALEKTLQDLQIDYVDLYLIHWPASLKKES-----LMPTPEML--TKPDITSTWKAMEALYDSGKARAIGVSN 155
Cdd:cd19155 83 NRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLSKEddsgkLDPTGEHKqdYTTDLLDIWKAMEAQVDQGLTRSIGLSN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 156 FSSKKLTDLLNVARVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGSQSKGEV----------RLKVLQNPIVTE 225
Cdd:cd19155 163 FNREQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPGAAHFspgtgspsgsSPDLLQDPVVKA 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 145330687 226 VAEKLGKTTAQVALRWGLQTGHSVLPKSSSGARLKENLDVFDWSIPEDLFTKFSNIPQ 283
Cdd:cd19155 243 IAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDK 300
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
13-277 |
2.26e-92 |
|
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: 275.15 E-value: 2.26e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 13 GAKLPCVGLGTYAM----VATAIEQAIKIGYRHIDCASIYGNEKEIGGVLKKLIGDGFVKREELFITSKLWSNDHLPEDV 88
Cdd:cd19111 1 GFPMPVIGLGTYQSppeeVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLEFKDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 89 PKALEKTLQDLQIDYVDLYLIHWPASL--KKESLMptpEMLTKPDITSTWKAMEALYDSGKARAIGVSNFSSKKLTDLLN 166
Cdd:cd19111 81 EKSLEKSLENLKLPYVDLYLIHHPCGFvnKKDKGE---RELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINKILA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 167 VARVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGSQSKGEVRLK-----VLQNPIVTEVAEKLGKTTAQVALRW 241
Cdd:cd19111 158 YAKVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSPGRANQSLWpdqpdLLEDPTVLAIAKELDKTPAQVLLRF 237
|
250 260 270
....*....|....*....|....*....|....*.
gi 145330687 242 GLQTGHSVLPKSSSGARLKENLDVFDWSIPEDLFTK 277
Cdd:cd19111 238 VLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKK 273
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
7-274 |
4.46e-92 |
|
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: 273.50 E-value: 4.46e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 7 FFELNTGAKLPCVGLGTYAM-----VATAIEQAIKIGYRHIDCASIYGNEKEIGgvlkKLIGDGFVKREELFITSKLWSN 81
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVeegseVVNAVKTALKNGYRSIDTAAIYGNEEGVG----KGIKESGIPREELFITSKVWNA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 82 DHLPEDVPKALEKTLQDLQIDYVDLYLIHWPASLK-KEslmptpemltkpditsTWKAMEALYDSGKARAIGVSNFSSKK 160
Cdd:cd19157 77 DQGYDSTLKAFEASLERLGLDYLDLYLIHWPVKGKyKE----------------TWKALEKLYKDGRVRAIGVSNFQVHH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 161 LTDLLNVARVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLgsqSKGevrlKVLQNPIVTEVAEKLGKTTAQVALR 240
Cdd:cd19157 141 LEDLLADAEIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPL---MQG----QLLDNPVLKEIAEKYNKSVAQVILR 213
|
250 260 270
....*....|....*....|....*....|....*
gi 145330687 241 WGLQTGHSVLPKSSSGARLKENLDVFDWSI-PEDL 274
Cdd:cd19157 214 WDLQNGVVTIPKSIKEHRIIENADVFDFELsQEDM 248
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
8-283 |
3.33e-91 |
|
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: 272.06 E-value: 3.33e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 8 FELNTGAKLPCVGLGTYAM----VATAIEQAIKIGYRHIDCASIYGNEKEIGGVLKkligDGFVKREELFITSKLWSNDH 83
Cdd:cd19117 6 FKLNTGAEIPAVGLGTWQSkpneVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIK----DSGVPREEIFITTKLWCTWH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 84 lpEDVPKALEKTLQDLQIDYVDLYLIHWPASLKKE--SLMPTPEMLTKPDITS-----TWKAMEALYDSGKARAIGVSNF 156
Cdd:cd19117 82 --RRVEEALDQSLKKLGLDYVDLYLMHWPVPLDPDgnDFLFKKDDGTKDHEPDwdfikTWELMQKLPATGKVKAIGVSNF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 157 SSKKLTDLLN--VARVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGSQSKgevrlKVLQNPIVTEVAEKLGKTT 234
Cdd:cd19117 160 SIKNLEKLLAspSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTNA-----PLLKEPVIIKIAKKHGKTP 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 145330687 235 AQVALRWGLQTGHSVLPKSSSGARLKENLDVfdWSIPEDLFTKFSNIPQ 283
Cdd:cd19117 235 AQVIISWGLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEIDELHK 281
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
16-273 |
1.59e-90 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti isatin reductase and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381299 [Multi-domain] Cd Length: 243 Bit Score: 268.76 E-value: 1.59e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 16 LPCVGLGTY----AMVATAIEQAIKIGYRHIDCASIYGNEKEIGGVlkklIGDGFVKREELFITSKLWSNDHLPEDVPKA 91
Cdd:cd19073 1 IPALGLGTWqlrgDDCANAVKEALELGYRHIDTAEIYNNEAEVGEA----IAESGVPREDLFITTKVWRDHLRPEDLKKS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 92 LEKTLQDLQIDYVDLYLIHWPASLKkeslmptpemltkpDITSTWKAMEALYDSGKARAIGVSNFSSKKLTDLLNVARVT 171
Cdd:cd19073 77 VDRSLEKLGTDYVDLLLIHWPNPTV--------------PLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPLP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 172 PAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGsqskgevRLKVLQNPIVTEVAEKLGKTTAQVALRWGLQTGHSVLP 251
Cdd:cd19073 143 IAVNQVEFHPFLYQAELLEYCRENDIVITAYSPLA-------RGEVLRDPVIQEIAEKYDKTPAQVALRWLVQKGIVVIP 215
|
250 260
....*....|....*....|..
gi 145330687 252 KSSSGARLKENLDVFDWSIPED 273
Cdd:cd19073 216 KASSEDHLKENLAIFDWELTSE 237
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
8-274 |
6.10e-90 |
|
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, EC 1.1.1.365), also called D-galacturonic acid reductase, or GalUR, is a founding member of aldo-keto reductase family 3 member D1 (AKR3D1). It mediates the reduction of D-galacturonate to L-galactonate, the first step in D-galacturonate catabolic process. It also has activity with D-glucuronate and DL-glyceraldehyde. Its activity is seen only with NADPH and not with NADH.
Pssm-ID: 381347 [Multi-domain] Cd Length: 279 Bit Score: 268.63 E-value: 6.10e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 8 FELNTGAKLPCVGLGTY----AMVATAIEQAIKIGYRHIDCASIYGNEKEIGGVLKKLIgDGFVKREELFITSKLWSNDH 83
Cdd:cd19121 4 FKLNTGASIPAVGLGTWqakaGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAI-AGGVKREDLFVTTKLWSTYH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 84 lpEDVPKALEKTLQDLQIDYVDLYLIHWPASLKKESlmPTPEMLTKPD----------ITSTWKAMEALYDSGKARAIGV 153
Cdd:cd19121 83 --RRVELCLDRSLKSLGLDYVDLYLVHWPVLLNPNG--NHDLFPTLPDgsrdldwdwnHVDTWKQMEKVLKTGKTKAIGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 154 SNFSSKKLTDLLNVARVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGSQSKgevrlKVLQNPIVTEVAEKLGKT 233
Cdd:cd19121 159 SNYSIPYLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTGS-----PLISDEPVVEIAKKHNVG 233
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 145330687 234 TAQVALRWGLQTGHSVLPKSSSGARLKENLDVFDWSiPEDL 274
Cdd:cd19121 234 PGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDLD-DEDM 273
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
8-279 |
2.36e-89 |
|
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: 268.16 E-value: 2.36e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 8 FELNTGAKLPCVGLGTYAM-VATAIEQ---AIKIGYRHIDCASIYGNEKEIGGVLKKLIGDGFVKREELFITSKLWSNDH 83
Cdd:cd19113 3 IKLNSGYKMPSVGFGCWKLdNATAADQiyqAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWNNFH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 84 LPEDVPKALEKTLQDLQIDYVDLYLIHWPASLKK---ESLMPTPEMLTKPD--------ITSTWKAMEALYDSGKARAIG 152
Cdd:cd19113 83 DPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKFvpiEEKYPPGFYCGDGDnfvyedvpILDTWKALEKLVDAGKIKSIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 153 VSNFSSKKLTDLLNVARVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGSQSKGEVRLK-------VLQNPIVTE 225
Cdd:cd19113 163 VSNFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGPQSFVELNQGralntptLFEHDTIKS 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 145330687 226 VAEKLGKTTAQVALRWGLQTGHSVLPKSSSGARLKENLDVFDWSIPEDLFTKFS 279
Cdd:cd19113 243 IAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIA 296
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
9-281 |
3.29e-89 |
|
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes prostaglandin F2-alpha synthase (PGFS) from Leishmania major (AKR5A1) and Trypanosoma brucei (AKR5A2). PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity for synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde. The AKR5G family of AKR includes Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase, which corresponds to aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381352 [Multi-domain] Cd Length: 254 Bit Score: 265.84 E-value: 3.29e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 9 ELNTGAKLPCVGLGTYAM-----VATAIEQAIKIGYRHIDCASIYGNEKEIGgvlkKLIGDGFVKREELFITSKLWSNDH 83
Cdd:cd19126 2 TLNNGTRMPWLGLGVFQTpdgdeTERAVQTALENGYRSIDTAAIYKNEEGVG----EAIRESGVPREELFVTTKLWNDDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 84 LPEDVPKALEKTLQDLQIDYVDLYLIHWPASLKkeslmptpemltkpdITSTWKAMEALYDSGKARAIGVSNFSSKKLTD 163
Cdd:cd19126 78 RARRTEDAFQESLDRLGLDYVDLYLIHWPGKDK---------------FIDTWKALEKLYASGKVKAIGVSNFQEHHLEE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 164 LLNVARVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGsqskgevRLKVLQNPIVTEVAEKLGKTTAQVALRWGL 243
Cdd:cd19126 143 LLAHADVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLG-------QGGLLSNPVLAAIGEKYGKSAAQVVLRWDI 215
|
250 260 270
....*....|....*....|....*....|....*...
gi 145330687 244 QTGHSVLPKSSSGARLKENLDVFDWSIPEDLFTKFSNI 281
Cdd:cd19126 216 QHGVVTIPKSVHASRIKENADIFDFELSEDDMTAIDAL 253
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
8-273 |
7.73e-88 |
|
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: 264.35 E-value: 7.73e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 8 FELNTGAKLPCVGLGTYAM----VATAIEQAIKIGYRHIDCASIYGNEKEIGGVLKKLIGDGFVKREELFITSKLWSNDH 83
Cdd:cd19112 3 ITLNSGHKMPVIGLGVWRMepgeIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLWNSDH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 84 lpEDVPKALEKTLQDLQIDYVDLYLIHWPASLKKESLMPTPEMLTKP-----DIT----STWKAMEALYDSGKARAIGVS 154
Cdd:cd19112 83 --GHVIEACKDSLKKLQLDYLDLYLVHFPVATKHTGVGTTGSALGEDgvldiDVTisleTTWHAMEKLVSAGLVRSIGIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 155 NFSSKKLTDLLNVARVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGSQSKGEVR---LKVLQNPIVTEVAEKLG 231
Cdd:cd19112 161 NYDIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGGAAANAEWfgsVSPLDDPVLKDLAKKYG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 145330687 232 KTTAQVALRWGLQTGHSVLPKSSSGARLKENLDVFDWSIPED 273
Cdd:cd19112 241 KSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKE 282
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
9-283 |
1.15e-87 |
|
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: 263.90 E-value: 1.15e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 9 ELNTGAKLPCVGLGTY----AMVATAIEQAIKIGYRHIDCASIYGNEKEIGGVLKKLIGDGFVKREELFITSKLWSNDHL 84
Cdd:cd19115 6 KLNSGYDMPLVGFGLWkvnnDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLWNTFHD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 85 PEDVPKALEKTLQDLQIDYVDLYLIHWPASLK--KESLMPTPE--------MLTKPDITSTWKAMEALYDSGKARAIGVS 154
Cdd:cd19115 86 GERVEPICRKQLADWGIDYFDLFLIHFPIALKyvDPAVRYPPGwfydgkkvEFSNAPIQETWTAMEKLVDKGLARSIGVS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 155 NFSSKKLTDLLNVARVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGSQSKGEVRLK-------VLQNPIVTEVA 227
Cdd:cd19115 166 NFSAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGPQSFLELDLPgakdtppLFEHDVIKSIA 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 145330687 228 EKLGKTTAQVALRWGLQTGHSVLPKSSSGARLKENLDVFDWSIPEDLFTKFSNIPQ 283
Cdd:cd19115 246 EKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDI 301
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
17-281 |
6.68e-87 |
|
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: 260.92 E-value: 6.68e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 17 PCVGLGTY----AMVATAIEQAIKIGYRHIDCASIYGNEKEIGGVLKKLIGDGFVKREELFITSKLWSNDHLPEDVPKAL 92
Cdd:cd19128 2 PRLGFGTYkiteSESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVKEQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 93 EKTLQDLQIDYVDLYLIHWP-ASLKKESLMPTP----EMLTKPDITSTWKAMEALYDSGKARAIGVSNFSSKKLTDLLNV 167
Cdd:cd19128 82 LITLQDLQLEYLDLFLIHWPlAFDMDTDGDPRDdnqiQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLNY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 168 ARVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGSqSKGEVRLKVLQNPIVTEVAEKLGKTTAQVALRWGLQ--- 244
Cdd:cd19128 162 CKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGG-SYGDGNLTFLNDSELKALATKYNTTPPQVIIAWHLQkwp 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 145330687 245 TGHSVLPKSSSGARLKENLDVFDWSIPEDLFTKFSNI 281
Cdd:cd19128 241 KNYSVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
13-279 |
3.65e-86 |
|
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase (AR, EC 1.1.1.21) from Homo sapiens (AKR1B1), Oryctolagus cuniculus (kidney, AKR1B2), Mus musculus (AKR1B3), Rattus norvegicus (lens, AKR1B4), Bos taurus (lens/testis, AKR1B5), and Sus scrofa (lens, AKR1B6), aldose reductase-related protein 1 (ALD1, EC1.1.1.21) from Mus musculus (AKR1B7), Rattus norvegicus (AKR1B14), and Homo sapiens (AKR1B15), Mus musculus fibroblast growth factor induced protein (FR-1 or AKR1B8, EC 1.1.1.21), Cricetulus griseus aldose reductase-related protein 2 (ALD2 or AKR1B9, EC 1.1.1.21), aldose reductase-like from Homo sapiens (ARL-1 or AKR1B10) and Rattus norvegicus (AKR1B13), aldo-keto reductase from Gallus domesticus (eye, tongue, esophagus, AKR1B12), and Oryctolagus cuniculus AR-like protein (3beta-HSD, AKR1B19). AR, also called aldehyde reductase, catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. ALD1 reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. It may play a role in the metabolism of xenobiotic aromatic aldehydes. FR-1, also called aldose reductase-related protein 2, or fibroblast growth factor-regulated protein (FGFRP), is induced by fibroblast growth factor-1. It may play a role in the regulation of the cell cycle. FR-1 belongs to the NADPH-dependent aldo-keto reductase family. ALD2 is an inducible aldo-keto reductase with a preference for aliphatic substrates. It can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. ARL-1, also called aldose reductase-like, or aldose reductase-related protein (ARP), or small intestine reductase, or SI reductase, acts as all-trans-retinaldehyde reductase that can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). It may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. AKR1B15, also called estradiol 17-beta-dehydrogenase AKR1B15, is a mitochondrial aldo-keto reductase that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. It has a strong selectivity towards NADP(H). AKR1B19 is aldose reductase-like that may show 3-beta-hydroxysteroid dehydrogenase (3beta-HSD) activity.
Pssm-ID: 381333 [Multi-domain] Cd Length: 307 Bit Score: 260.04 E-value: 3.65e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 13 GAKLPCVGLGTY----AMVATAIEQAIKIGYRHIDCASIYGNEKEIGGVLKKLIGDGFVKREELFITSKLWSNDHLPEDV 88
Cdd:cd19107 1 GAKMPILGLGTWksppGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEKGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 89 PKALEKTLQDLQIDYVDLYLIHWPASLKK-ESLMPTPE----MLTKPDITSTWKAMEALYDSGKARAIGVSNFSSKKLTD 163
Cdd:cd19107 81 KGACQKTLSDLKLDYLDLYLIHWPTGFKPgKELFPLDEsgnvIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 164 LLNVA--RVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGSQSKGEVRLK---VLQNPIVTEVAEKLGKTTAQVA 238
Cdd:cd19107 161 ILNKPglKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEdpsLLEDPKIKEIAAKHNKTTAQVL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 145330687 239 LRWGLQTGHSVLPKSSSGARLKENLDVFDWSI-PEDLFTKFS 279
Cdd:cd19107 241 IRFPIQRNLVVIPKSVTPERIAENFKVFDFELsSEDMATILS 282
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
5-274 |
6.82e-83 |
|
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381361 [Multi-domain] Cd Length: 265 Bit Score: 250.32 E-value: 6.82e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 5 IRFFELNTGAKLPCVGLGT-----YAMvaTAIEQAIKI-GYRHIDCASIYGNEKEIGgvlkKLIGDGFVKREELFITSKL 78
Cdd:cd19135 2 TPTVRLSNGVEMPILGLGTshsggYSH--EAVVYALKEcGYRHIDTAKRYGCEELLG----KAIKESGVPREDLFLTTKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 79 WSNDHLPEDVPKALEKTLQDLQIDYVDLYLIHWPASlkkeslmPTPEMLTKPDITSTWKAMEALYDSGKARAIGVSNFSS 158
Cdd:cd19135 76 WPSDYGYESTKQAFEASLKRLGVDYLDLYLLHWPDC-------PSSGKNVKETRAETWRALEELYDEGLCRAIGVSNFLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 159 KKLTDLLNVARVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLgsqSKGevrlKVLQNPIVTEVAEKLGKTTAQVA 238
Cdd:cd19135 149 EHLEQLLEDCSVVPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPL---AKG----KALEEPTVTELAKKYQKTPAQIL 221
|
250 260 270
....*....|....*....|....*....|....*..
gi 145330687 239 LRWGLQTGHSVLPKSSSGARLKENLDVFDWSI-PEDL 274
Cdd:cd19135 222 IRWSIQNGVVTIPKSTKEERIKENCQVFDFSLsEEDM 258
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
13-274 |
1.44e-82 |
|
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: 249.46 E-value: 1.44e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 13 GAKLPCVGLGT----YAM--------VATAIEQAIKIGYRHIDCASIYGNEKEIGGVLKKLIgdgfVKREELFITSKLWS 80
Cdd:cd19120 1 GSKIPAIAFGTgtawYKSgdddiqrdLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALKESG----VPREDLFITTKVSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 81 NDhlpEDVPKALEKTLQDLQIDYVDLYLIHWPASLKKEslmptpemltKPDITSTWKAMEALYDSGKARAIGVSNFSSKK 160
Cdd:cd19120 77 GI---KDPREALRKSLAKLGVDYVDLYLIHSPFFAKEG----------GPTLAEAWAELEALKDAGLVRSIGVSNFRIED 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 161 LTDLLNVARVTPAVNQVECHP--VWQQQGLHELCKSKGVHLSGYSPLGSQSKGEVRLKvlqNPIVTEVAEKLGKTTAQVA 238
Cdd:cd19120 144 LEELLDTAKIKPAVNQIEFHPylYPQQPALLEYCREHGIVVSAYSPLSPLTRDAGGPL---DPVLEKIAEKYGVTPAQVL 220
|
250 260 270
....*....|....*....|....*....|....*..
gi 145330687 239 LRWGLQTGHSVLPKSSSGARLKENLDVFDWSI-PEDL 274
Cdd:cd19120 221 LRWALQKGIVVVTTSSKEERMKEYLEAFDFELtEEEV 257
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
13-273 |
2.01e-82 |
|
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes 3-oxo-5-beta-steroid 4-dehydrogenase (EC 1.3.1.3) from Homo sapiens (AKR1D1), Rattus norvegicus (liver, AKR1D2), and Oryctolagus cuniculus (AKR1D3). 3-oxo-5-beta-steroid 4-dehydrogenase, also called delta(4)-3-ketosteroid 5-beta-reductase (EC 1.3.99.6), or delta(4)-3-oxosteroid 5-beta-reductase, or 5-beta-reductase, efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites.
Pssm-ID: 381335 [Multi-domain] Cd Length: 308 Bit Score: 250.49 E-value: 2.01e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 13 GAKLPCVGLGTYA--------MVATAIEQAIKIGYRHIDCASIYGNEKEIGGVLKKLIGDGFVKREELFITSKLWSNDHL 84
Cdd:cd19109 1 GNSIPIIGLGTYSepkttpkgACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 85 PEDVPKALEKTLQDLQIDYVDLYLIHWPASLKK-ESLMPTPE----MLTKPDITSTWKAMEALYDSGKARAIGVSNFSSK 159
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAFKPgDEIYPRDEngkwLYHKTNLCATWEALEACKDAGLVKSIGVSNFNRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 160 KLTDLLNVA--RVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGSQSKGE-VRLK---VLQNPIVTEVAEKLGKT 233
Cdd:cd19109 161 QLELILNKPglKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDPIwVNVSsppLLEDPLLNSIGKKYNKT 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 145330687 234 TAQVALRWGLQTGHSVLPKSSSGARLKENLDVFDWSIPED 273
Cdd:cd19109 241 AAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEE 280
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
13-273 |
4.53e-81 |
|
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: 245.25 E-value: 4.53e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 13 GAKLPCVGLGTYAMV----ATAIEQAIKIGYRHIDCASIYGNEKEIGGVLKKlIGdgfVKREELFITSKLWSNDHLPEDV 88
Cdd:cd19140 5 GVRIPALGLGTYPLTgeecTRAVEHALELGYRHIDTAQMYGNEAQVGEAIAA-SG---VPRDELFLTTKVWPDNYSPDDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 89 PKALEKTLQDLQIDYVDLYLIHWpaslkkeslmPTPEMltkpDITSTWKAMEALYDSGKARAIGVSNFSSKKLTDLLNVA 168
Cdd:cd19140 81 LASVEESLRKLRTDYVDLLLLHW----------PNKDV----PLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 169 RVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGsqskgevRLKVLQNPIVTEVAEKLGKTTAQVALRWGL-QTGH 247
Cdd:cd19140 147 EAPLFTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLA-------RGEVLKDPVLQEIGRKHGKTPAQVALRWLLqQEGV 219
|
250 260
....*....|....*....|....*.
gi 145330687 248 SVLPKSSSGARLKENLDVFDWSIPED 273
Cdd:cd19140 220 AAIPKATNPERLEENLDIFDFTLSDE 245
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
8-269 |
1.37e-80 |
|
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: 245.22 E-value: 1.37e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 8 FELNTGAKLPCVGLGTYAM------VATAIEQAIKIGYRHIDCASIYGNEKEIGGVLKKLIGDG-FVKREELFITSKLWS 80
Cdd:cd19122 1 FTLNNGVKIPAVGFGTFANegakgeTYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKVWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 81 NDHLPEDVPKALEKTLQDLQIDYVDLYLIHWPASLKKES-----LMPTPEMLTKPDITS----TWKAMEALYDSGKARAI 151
Cdd:cd19122 81 HLHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAEKNDqrspkLGPDGKYVILKDLTEnpepTWRAMEEIYESGKAKAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 152 GVSNFSSKKLTDLLNVARVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGSQ----SKGEvrlKVLQNPIVTEVA 227
Cdd:cd19122 161 GVSNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQnqvpSTGE---RVSENPTLNEVA 237
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 145330687 228 EKLGKTTAQVALRWGLQTGHSVLPKSSSGARLKENLDVFDWS 269
Cdd:cd19122 238 EKGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIELS 279
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
10-273 |
4.51e-80 |
|
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: 242.56 E-value: 4.51e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 10 LNTGAKLPCVGLGTYAMV----ATAIEQAIKIGYRHIDCASIYGNEKEIGGVLKkligDGFVKREELFITSKLWSNDHLP 85
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKgdegVEAVVAALQAGYRLLDTAFNYENEGAVGEAVR----RSGVPREELFVTTKLPGRHHGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 86 EDVPKALEKTLQDLQIDYVDLYLIHWPasLKKESLMptpemltkpdiTSTWKAMEALYDSGKARAIGVSNFSSKKLTDLL 165
Cdd:cd19132 77 EEALRTIEESLYRLGLDYVDLYLIHWP--NPSRDLY-----------VEAWQALIEAREEGLVRSIGVSNFLPEHLDRLI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 166 NVARVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGsqsKGEvrlKVLQNPIVTEVAEKLGKTTAQVALRWGLQT 245
Cdd:cd19132 144 DETGVTPAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLG---RGS---GLLDEPVIKAIAEKHGKTPAQVVLRWHVQL 217
|
250 260
....*....|....*....|....*...
gi 145330687 246 GHSVLPKSSSGARLKENLDVFDWSIPED 273
Cdd:cd19132 218 GVVPIPKSANPERQRENLAIFDFELSDE 245
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
9-274 |
1.07e-79 |
|
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: 242.04 E-value: 1.07e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 9 ELNTGAKLPCVGLGTY-----AMVATAIEQAIKIGYRHIDCASIYGNEKEIGGVLKKligdGFVKREELFITSKLWSNDH 83
Cdd:cd19156 2 KLANGVEMPRLGLGVWrvqdgAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRE----SGVPREEVFVTTKLWNSDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 84 LPEDVPKALEKTLQDLQIDYVDLYLIHWPASLKkeslmptpemltkpdITSTWKAMEALYDSGKARAIGVSNFSSKKLTD 163
Cdd:cd19156 78 GYESTLAAFEESLEKLGLDYVDLYLIHWPVKGK---------------FKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 164 LLNVARVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGSQskgevrlKVLQNPIVTEVAEKLGKTTAQVALRWGL 243
Cdd:cd19156 143 LLKSCKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQG-------KLLSNPVLKAIGKKYGKSAAQVIIRWDI 215
|
250 260 270
....*....|....*....|....*....|..
gi 145330687 244 QTGHSVLPKSSSGARLKENLDVFDWSI-PEDL 274
Cdd:cd19156 216 QHGIITIPKSVHEERIQENFDVFDFELtAEEI 247
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
11-286 |
2.07e-79 |
|
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: 242.36 E-value: 2.07e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 11 NTGAKLPCVGLGTYAMVATAIEQAIK----IGYRHIDCASIYGNEKEIGGVLKKLIGDGFVKREELFITSKLWSNDHLPE 86
Cdd:cd19129 1 NGSGAIPALGFGTLIPDPSATRNAVKaaleAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNHRPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 87 DVPKALEKTLQDLQIDYVDLYLIHWPASLKkeslmPTPEMLTKPD-----------ITSTWKAMEALYDSGKARAIGVSN 155
Cdd:cd19129 81 RVKPAFEASLKRLQLDYLDLYLIHTPFAFQ-----PGDEQDPRDAngnviyddgvtLLDTWRAMERLVDEGRCKAIGLSD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 156 FSSKKLTDLLNVARVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGSQSkgevRLKVLQNPIVTEVAEKLGKTTA 235
Cdd:cd19129 156 VSLEKLREIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGM----EPKLLEDPVITAIARRVNKTPA 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 145330687 236 QVALRWGLQTGHSVLPKSSSGARLKENLDVFdwSIPEDLFTKFSNIPQAKV 286
Cdd:cd19129 232 QVLLAWAIQRGTALLTTSKTPSRIRENFDIS--TLPEDAMREINEGIKTRY 280
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
10-274 |
1.28e-78 |
|
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) is a founding member of the aldo-keto reductase family 5 member B1 (AKR5B1). M6DH (EC 1.1.1.218), also called naloxone reductase, oxidizes the C-6 hydroxy group of morphine and codeine.
Pssm-ID: 381353 [Multi-domain] Cd Length: 268 Bit Score: 239.62 E-value: 1.28e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 10 LNTGAKLPCVGLGTYAM----VATAIEQAIKIGYRHIDCASIYGNEKEIGGVLKKligDGfVKREELFITSKLWSNDHLP 85
Cdd:cd19127 3 LNNGVEMPALGLGVFQTppeeTADAVATALADGYRLIDTAAAYGNEREVGEGIRR---SG-VDRSDIFVTTKLWISDYGY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 86 EDVPKALEKTLQDLQIDYVDLYLIHWPASLKKEslmptpemltkpDITSTWKAMEALYDSGKARAIGVSNFSSKKLTDLL 165
Cdd:cd19127 79 DKALRGFDASLRRLGLDYVDLYLLHWPVPNDFD------------RTIQAYKALEKLLAEGRVRAIGVSNFTPEHLERLI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 166 NVARVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLG-----SQSKGEVRLKVLQNPIVTEVAEKLGKTTAQVALR 240
Cdd:cd19127 147 DATTVVPAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGgvmryGASGPTGPGDVLQDPTITGLAEKYGKTPAQIVLR 226
|
250 260 270
....*....|....*....|....*....|....*
gi 145330687 241 WGLQTGHSVLPKSSSGARLKENLDVFDWSI-PEDL 274
Cdd:cd19127 227 WHLQNGVSAIPKSVHPERIAENIDIFDFALsAEDM 261
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
5-263 |
1.52e-78 |
|
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: 240.09 E-value: 1.52e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 5 IRFFELNTGAKLPCVGLGTY------AMVATAIEQAIKIGYRHIDCASIYGNEKEIGGVLKKLIGDGFVKREELFITSKL 78
Cdd:cd19119 1 EISFKLNTGASIPALGLGTAsphedrAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 79 WSNDHlpEDVPKALEKTLQDLQIDYVDLYLIHWPASLKKES-LMPTPEMLTKP----------DITSTWKAMEALYDSGK 147
Cdd:cd19119 81 WPTFY--DEVERSLDESLKALGLDYVDLLLVHWPVCFEKDSdDSGKPFTPVNDdgktryaasgDHITTYKQLEKIYLDGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 148 ARAIGVSNFSSKKLTDLLNVARVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGSQSKGevrlkVLQNPIVTEVA 227
Cdd:cd19119 159 AKAIGVSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAP-----NLKNPLVKKIA 233
|
250 260 270
....*....|....*....|....*....|....*.
gi 145330687 228 EKLGKTTAQVALRWGLQTGHSVLPKSSSGARLKENL 263
Cdd:cd19119 234 EKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNG 269
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
10-273 |
6.37e-77 |
|
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: 234.80 E-value: 6.37e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 10 LNTGAKLPCVGLGTY----AMVATAIEQAIKIGYRHIDCASIYGNEKEIGgvlkKLIGDGFVKREELFITSKLWSNDHLP 85
Cdd:cd19130 4 LNDGNSIPQLGYGVFkvppADTQRAVATALEVGYRHIDTAAIYGNEEGVG----AAIAASGIPRDELFVTTKLWNDRHDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 86 EDVPKALEKTLQDLQIDYVDLYLIHWPASlkkeslmptpemlTKPDITSTWKAMEALYDSGKARAIGVSNFSSKKLTDLL 165
Cdd:cd19130 80 DEPAAAFAESLAKLGLDQVDLYLVHWPTP-------------AAGNYVHTWEAMIELRAAGRTRSIGVSNFLPPHLERIV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 166 NVARVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGSQskgevrlKVLQNPIVTEVAEKLGKTTAQVALRWGLQT 245
Cdd:cd19130 147 AATGVVPAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQG-------KLLGDPPVGAIAAAHGKTPAQIVLRWHLQK 219
|
250 260
....*....|....*....|....*...
gi 145330687 246 GHSVLPKSSSGARLKENLDVFDWSIPED 273
Cdd:cd19130 220 GHVVFPKSVRRERMEDNLDVFDFDLTDT 247
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
13-273 |
1.10e-76 |
|
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: 235.91 E-value: 1.10e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 13 GAKLPCVGLGTYAMVAT----AIEQAIKIGYRHIDCASIYGNEKEIGGVLKKLIGDGFVKREELFITSKLWSNDHLPEDV 88
Cdd:cd19114 1 GDKMPLVGFGTAKIKANeteeVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGKDHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 89 PKALEKTLQDLQIDYVDLYLIHWPASLK----KESLMP---TPEMLTKP----DITSTWKAMEALYDSGKARAIGVSNFS 157
Cdd:cd19114 81 REAFDRQLKDYGLDYIDLYLIHFPIPAAyvdpAENYPFlwkDKELKKFPleqsPMQECWREMEKLVDAGLVRNIGIANFN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 158 SKKLTDLLNVARVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGSQS------KGEVRLKVLQNPIVTEVAEKLG 231
Cdd:cd19114 161 VQLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAVytkvtkHLKHFTNLLEHPVVKKLADKHK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 145330687 232 KTTAQVALRWGLQTGHSVLPKSSSGARLKENLDVFDWSIPED 273
Cdd:cd19114 241 RDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEE 282
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
1-287 |
7.40e-75 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 229.96 E-value: 7.40e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 1 MAAPiRFFELNTGAKLPCVGLGTYAM----VATAIEQAIKIGYRHIDCASIYGNEKEIGGVLKkligDGFVKREELFITS 76
Cdd:PRK11565 1 MANP-TVIKLQDGNVMPQLGLGVWQAsneeVITAIHKALEVGYRSIDTAAIYKNEEGVGKALK----EASVAREELFITT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 77 KLWSNDHLpeDVPKALEKTLQDLQIDYVDLYLIHWPASLKKESLmptpemltkpditSTWKAMEALYDSGKARAIGVSNF 156
Cdd:PRK11565 76 KLWNDDHK--RPREALEESLKKLQLDYVDLYLMHWPVPAIDHYV-------------EAWKGMIELQKEGLIKSIGVCNF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 157 SSKKLTDLLNVARVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGSQSKGevrlkVLQNPIVTEVAEKLGKTTAQ 236
Cdd:PRK11565 141 QIHHLQRLIDETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGKG-----VFDQKVIRDLADKYGKTPAQ 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 145330687 237 VALRWGLQTGHSVLPKSSSGARLKENLDVFDWSIPEDLFTKFSNIPQAKVL 287
Cdd:PRK11565 216 IVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRLDKDELGEIAKLDQGKRL 266
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
15-272 |
7.89e-75 |
|
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: 231.00 E-value: 7.89e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 15 KLPCVGLGTY----AMVATAIEQAIKIGYRHIDCASIYGNEKEIGGVLKKLIGDGFVKREELFITSKLWSNDHLPEDVPK 90
Cdd:cd19110 3 DIPAVGLGTWkaspGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKSLVKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 91 ALEKTLQDLQIDYVDLYLIHWPASLKK-ESLMPTPE----MLTKPDITSTWKAMEALYDSGKARAIGVSNFSSKKLTDLL 165
Cdd:cd19110 83 ACTRSLKALKLNYLDLYLIHWPMGFKPgEPDLPLDRsgmvIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLERLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 166 NVA--RVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGSQSKGevrLKVLQNPIVTEVAEKLGKTTAQVALRWGL 243
Cdd:cd19110 163 NKPglRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSCEG---VDLIDDPVIQRIAKKHGKSPAQILIRFQI 239
|
250 260
....*....|....*....|....*....
gi 145330687 244 QTGHSVLPKSSSGARLKENLDVFDWSIPE 272
Cdd:cd19110 240 QRNVIVIPKSVTPSRIKENIQVFDFELTE 268
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
10-273 |
2.11e-67 |
|
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: 210.87 E-value: 2.11e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 10 LNTGAKLPCVGLGTYAMVATAIEQ----AIKIGYRHIDCASIYGNEKEIGgvlkKLIGDGFVKREELFITSKLWSNDHLP 85
Cdd:cd19134 5 LNDDNTMPVIGLGVGELSDDEAERsvsaALEAGYRLIDTAAAYGNEAAVG----RAIAASGIPRGELFVTTKLATPDQGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 86 EDVPKALEKTLQDLQIDYVDLYLIHWPAslkkeslmptPEMLTKPDitsTWKAMEALYDSGKARAIGVSNFSSKKLTDLL 165
Cdd:cd19134 81 TASQAACRASLERLGLDYVDLYLIHWPA----------GREGKYVD---SWGGLMKLREEGLARSIGVSNFTAEHLENLI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 166 NVARVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGSQSkgevrlkVLQNPIVTEVAEKLGKTTAQVALRWGLQT 245
Cdd:cd19134 148 DLTFFTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGR-------LLDNPAVTAIAAAHGRTPAQVLLRWSLQL 220
|
250 260
....*....|....*....|....*...
gi 145330687 246 GHSVLPKSSSGARLKENLDVFDWSIPED 273
Cdd:cd19134 221 GNVVISRSSNPERIASNLDVFDFELTAD 248
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
16-267 |
1.65e-62 |
|
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: 197.58 E-value: 1.65e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 16 LPCVGLGTYAM----VATAIEQAIKIGYRHIDCASIYGNEKEIGgvlkKLIGDGFVKREELFITSKLWSNDHLPEDVPKA 91
Cdd:cd19139 1 IPAFGLGTFRLkddvVIDSVRTALELGYRHIDTAQIYDNEAAVG----QAIAESGVPRDELFITTKIWIDNLSKDKLLPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 92 LEKTLQDLQIDYVDLYLIHWPASLKKESLMPTPEMLtkpditstwkaMEAlYDSGKARAIGVSNFSSKkltdLLNVARVT 171
Cdd:cd19139 77 LEESLEKLRTDYVDLTLIHWPSPNDEVPVEEYIGAL-----------AEA-KEQGLTRHIGVSNFTIA----LLDEAIAV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 172 P-----AVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGsqskgevRLKVLQNPIVTEVAEKLGKTTAQVALRWGLQTG 246
Cdd:cd19139 141 VgagaiATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLA-------YGKVLDDPVLAAIAERHGATPAQIALAWAMARG 213
|
250 260
....*....|....*....|.
gi 145330687 247 HSVLPKSSSGARLKENLDVFD 267
Cdd:cd19139 214 YAVIPSSTKREHLRSNLLALD 234
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
13-274 |
6.89e-62 |
|
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: 196.68 E-value: 6.89e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 13 GAKLPCVGLGTYAMVA-------------TAIEQAIKIGYRHIDCASIYGN---EKEIGGVLKKligdgfVKREELFITS 76
Cdd:cd19072 1 GEEVPVLGLGTWGIGGgmskdysddkkaiEALRYAIELGINLIDTAEMYGGghaEELVGKAIKG------FDREDLFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 77 KLWSnDHL-PEDVPKALEKTLQDLQIDYVDLYLIHWPASlkkeslmptpemltKPDITSTWKAMEALYDSGKARAIGVSN 155
Cdd:cd19072 75 KVSP-DHLkYDDVIKAAKESLKRLGTDYIDLYLIHWPNP--------------SIPIEETLRAMEELVEEGKIRYIGVSN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 156 FSSKKLTDLLNVARVTP-AVNQVECHPV--WQQQGLHELCKSKGVHLSGYSPLGsqsKGEVRLKVLQnPIVTEVAEKLGK 232
Cdd:cd19072 140 FSLEELEEAQSYLKKGPiVANQVEYNLFdrEEESGLLPYCQKNGIAIIAYSPLE---KGKLSNAKGS-PLLDEIAKKYGK 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 145330687 233 TTAQVALRWGLQTGHSV-LPKSSSGARLKENLDVFDWSI-PEDL 274
Cdd:cd19072 216 TPAQIALNWLISKPNVIaIPKASNIEHLEENAGALGWELsEEDL 259
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
15-263 |
9.14e-58 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 186.00 E-value: 9.14e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 15 KLPCVGLGTYAM----VATAIEQAIKIGYRHIDCASIYGNEKEIGgvlkKLIGDGFVKREELFITSKLWSNDHLPEDVPK 90
Cdd:PRK11172 2 SIPAFGLGTFRLkdqvVIDSVKTALELGYRAIDTAQIYDNEAAVG----QAIAESGVPRDELFITTKIWIDNLAKDKLIP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 91 ALEKTLQDLQIDYVDLYLIHWPASlkkESLMPTPEMltkpditstwkaMEALYDS---GKARAIGVSNFS---SKKLTDL 164
Cdd:PRK11172 78 SLKESLQKLRTDYVDLTLIHWPSP---NDEVSVEEF------------MQALLEAkkqGLTREIGISNFTialMKQAIAA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 165 LNVARVtpAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGSQskgevrlKVLQNPIVTEVAEKLGKTTAQVALRWGLQ 244
Cdd:PRK11172 143 VGAENI--ATNQIELSPYLQNRKVVAFAKEHGIHVTSYMTLAYG-------KVLKDPVIARIAAKHNATPAQVILAWAMQ 213
|
250
....*....|....*....
gi 145330687 245 TGHSVLPKSSSGARLKENL 263
Cdd:PRK11172 214 LGYSVIPSSTKRENLASNL 232
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
19-273 |
1.35e-53 |
|
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: 175.96 E-value: 1.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 19 VGLGTYAM-----------VATAIEQAIKIGYRHIDCASIYG---NEKEIGGVLKKLIgdgfVKREELFITSKL------ 78
Cdd:pfam00248 1 IGLGTWQLgggwgpiskeeALEALRAALEAGINFIDTAEVYGdgkSEELLGEALKDYP----VKRDKVVIATKVpdgdgp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 79 WSNDHLPEDVPKALEKTLQDLQIDYVDLYLIHWPaslkkeslmpTPEMltkpDITSTWKAMEALYDSGKARAIGVSNFSS 158
Cdd:pfam00248 77 WPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWP----------DPDT----PIEETWDALEELKKEGKIRAIGVSNFDA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 159 KKLTDLLNVARVTPAVNQVECHPVW--QQQGLHELCKSKGVHLSGYSPLGS--------------------QSKGEVRLK 216
Cdd:pfam00248 143 EQIEKALTKGKIPIVAVQVEYNLLRrrQEEELLEYCKKNGIPLIAYSPLGGglltgkytrdpdkgpgerrrLLKKGTPLN 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 145330687 217 VLQNPIVTEVAEKLGKTTAQVALRWGLQ--TGHSVLPKSSSGARLKENLDVFDWSIPED 273
Cdd:pfam00248 223 LEALEALEEIAKEHGVSPAQVALRWALSkpGVTIPIPGASNPEQLEDNLGALEFPLSDE 281
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
10-263 |
7.36e-49 |
|
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: 163.19 E-value: 7.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 10 LNTGAKLPCVGLGTYAM---------VATAIEQAIKIGYRHIDCASIYGN---EKEIGGVLKkliGDgfvkREELFITSK 77
Cdd:cd19138 5 LPDGTKVPALGQGTWYMgedpakraqEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIR---GR----RDKVFLVSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 78 LWSNDHLPEDVPKALEKTLQDLQIDYVDLYLIHWPASlkkeslMPTPEmltkpditsTWKAMEALYDSGKARAIGVSNFS 157
Cdd:cd19138 78 VLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWRGG------VPLAE---------TVAAMEELKKEGKIRAWGVSNFD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 158 SKKLTDLLNVARVTP-AVNQVECHpvWQQQGL-HEL---CKSKGVHLSGYSPLGsqSKGEVRLKVLQNPIVTEVAEKLGK 232
Cdd:cd19138 143 TDDMEELWAVPGGGNcAANQVLYN--LGSRGIeYDLlpwCREHGVPVMAYSPLA--QGGLLRRGLLENPTLKEIAARHGA 218
|
250 260 270
....*....|....*....|....*....|...
gi 145330687 233 TTAQVALRWGLQTGhSVL--PKSSSGARLKENL 263
Cdd:cd19138 219 TPAQVALAWVLRDG-NVIaiPKSGSPEHARENA 250
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
16-281 |
4.93e-47 |
|
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: 159.29 E-value: 4.93e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 16 LPCVGLGTYAM-------------VATAIEQAIKIGYRHIDCASIYGN---EKEIGGVLKKligdgfvKREELFITSKLW 79
Cdd:cd19085 1 VSRLGLGCWQFgggywwgdqddeeSIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKG-------RRDDVVIATKVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 80 SNDHLPEDVPKALEKTLQDLQIDYVDLYLIHWPASlkkeslmptpemltKPDITSTWKAMEALYDSGKARAIGVSNFSSK 159
Cdd:cd19085 74 PDNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSS--------------DVPLEETMEALEKLKEEGKIRAIGVSNFGPA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 160 KLTDLLNVARVTpaVNQVECHPVWQQ--QGLHELCKSKGVHLSGYSPL------GSQSKGEV--------RLKVLQNPI- 222
Cdd:cd19085 140 QLEEALDAGRID--SNQLPYNLLWRAieYEILPFCREHGIGVLAYSPLaqglltGKFSSAEDfppgdartRLFRHFEPGa 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145330687 223 ----------VTEVAEKLGKTTAQVALRWGLQTGH--SVLPKSSSGARLKENLDVFDWSIPEDLFTKFSNI 281
Cdd:cd19085 218 eeetfealekLKEIADELGVTMAQLALAWVLQQPGvtSVIVGARNPEQLEENAAAVDLELSPSVLERLDEI 288
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
13-274 |
1.17e-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: 1.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 13 GAKLPCVGLGTYAM-------------VATAIEQAIKIGYRHIDCASIYGnekeiGGVLKKLIGDG--FVKREELFITSK 77
Cdd:cd19137 1 GEKIPALGLGTWGIggfltpdysrdeeMVELLKTAIELGYTHIDTAEMYG-----GGHTEELVGKAikDFPREDLFIVTK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 78 LWSNDHLPEDVPKALEKTLQDLQIDYVDLYLIHWPaslkkeslmptpemltKPDIT--STWKAMEALYDSGKARAIGVSN 155
Cdd:cd19137 76 VWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWP----------------NPNIPleETLSAMAEGVRQGLIRYIGVSN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 156 FSSKKLTDLLNVARVTPAVNQVECHPV---WQQQGLHELCKSKGVHLSGYSPLGsqskgevRLKVLQNPIVTEVAEKLGK 232
Cdd:cd19137 140 FNRRLLEEAISKSQTPIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPLR-------RGLEKTNRTLEEIAKNYGK 212
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 145330687 233 TTAQVALRWGLQTGHSV-LPKSSSGARLKENLDVFDWSI-PEDL 274
Cdd:cd19137 213 TIAQIALAWLIQKPNVVaIPKAGRVEHLKENLKATEIKLsEEEM 256
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
15-273 |
3.14e-41 |
|
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: 143.91 E-value: 3.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 15 KLPCVGLGT---------------YAMVATAIEQAIKIGYRHIDCASIYGN---EKEIGGVLKKLigdgfVKREELFITS 76
Cdd:cd19093 1 EVSPLGLGTwqwgdrlwwgygeygDEDLQAAFDAALEAGVNLFDTAEVYGTgrsERLLGRFLKEL-----GDRDEVVIAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 77 KLWS--NDHLPEDVPKALEKTLQDLQIDYVDLYLIHWPASlkkeslmptpemlTKPDITSTWKAMEALYDSGKARAIGVS 154
Cdd:cd19093 76 KFAPlpWRLTRRSVVKALKASLERLGLDSIDLYQLHWPGP-------------WYSQIEALMDGLADAVEEGLVRAVGVS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 155 NFSSKKL---TDLLNVARVTPAVNQVE---CHPVWQQQGLHELCKSKGVHLSGYSPLGS------------QSKGEVRLK 216
Cdd:cd19093 143 NYSADQLrraHKALKERGVPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAQglltgkyspenpPPGGRRRLF 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145330687 217 VLQN-----PIVT---EVAEKLGKTTAQVALRWGLQTGHSVLPKSSSGARLKENLDVFDWSIPED 273
Cdd:cd19093 223 GRKNlekvqPLLDaleEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEE 287
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
11-277 |
7.13e-41 |
|
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: 143.78 E-value: 7.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 11 NTGAKLPCVGLGTYAM--------VATAIEQ---AIKIGYRHIDCASIYG---NEKEIGGVLKKLigdgfvKREELFITS 76
Cdd:COG0667 8 RSGLKVSRLGLGTMTFggpwggvdEAEAIAIldaALDAGINFFDTADVYGpgrSEELLGEALKGR------PRDDVVIAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 77 KL--------WSNDHLPEDVPKALEKTLQDLQIDYVDLYLIHWpaslkkeslmPTPEMltkpDITSTWKAMEALYDSGKA 148
Cdd:COG0667 82 KVgrrmgpgpNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHR----------PDPDT----PIEETLGALDELVREGKI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 149 RAIGVSNFSSKKLTDLLNVARVTP--AVNQVECHPVWQQ--QGLHELCKSKGVHLSGYSPLGS-----------QSKGEV 213
Cdd:COG0667 148 RYIGVSNYSAEQLRRALAIAEGLPpiVAVQNEYSLLDRSaeEELLPAARELGVGVLAYSPLAGglltgkyrrgaTFPEGD 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145330687 214 RLKVLQNPI------------VTEVAEKLGKTTAQVALRWGLQTG--HSVLPKSSSGARLKENLDVFDWSIPEDLFTK 277
Cdd:COG0667 228 RAATNFVQGylternlalvdaLRAIAAEHGVTPAQLALAWLLAQPgvTSVIPGARSPEQLEENLAAADLELSAEDLAA 305
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
13-273 |
9.71e-39 |
|
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: 137.66 E-value: 9.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 13 GAKLPCVGLGTYAMVAT------------AIEQAIKIGYRHIDCASIYGN---EKEIGGVLKKligdgfvKREELFITSK 77
Cdd:cd19084 1 DLKVSRIGLGTWAIGGTwwgevddqesieAIKAAIDLGINFFDTAPVYGFghsEEILGKALKG-------RRDDVVIATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 78 ---LWSNDHL------PEDVPKALEKTLQDLQIDYVDLYLIHWPASLkkeslmpTPemltkpdITSTWKAMEALYDSGKA 148
Cdd:cd19084 74 cglRWDGGKGvtkdlsPESIRKEVEQSLRRLQTDYIDLYQIHWPDPN-------TP-------IEETAEALEKLKKEGKI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 149 RAIGVSNFSSKKLTDLLNVARVtpAVNQVECHPVWQQQG--LHELCKSKGVHLSGYSPLGS------------------- 207
Cdd:cd19084 140 RYIGVSNFSVEQLEEARKYGPI--VSLQPPYSMLEREIEeeLLPYCRENGIGVLPYGPLAQglltgkykkeptfppddrr 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145330687 208 ----QSKGEVRLKVLQnpIV---TEVAEKLGKTTAQVALRWGLQT--GHSVLpkssSGAR----LKENLDVFDWSIPED 273
Cdd:cd19084 218 srfpFFRGENFEKNLE--IVdklKEIAEKYGKSLAQLAIAWTLAQpgVTSAI----VGAKnpeqLEENAGALDWELTEE 290
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
17-264 |
3.45e-33 |
|
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: 121.47 E-value: 3.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 17 PCVGLGTYAM-----VATAIE---QAIKIGYRHIDCASIYGN---EKEIGGVLKkligdGFVKREELFITSKL------- 78
Cdd:cd06660 1 SRLGLGTMTFggdgdEEEAFAlldAALEAGGNFFDTADVYGDgrsERLLGRWLK-----GRGNRDDVVIATKGghppggd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 79 -WSNDHLPEDVPKALEKTLQDLQIDYVDLYLIHWPASlkkeslmptpemltKPDITSTWKAMEALYDSGKARAIGVSNFS 157
Cdd:cd06660 76 pSRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDP--------------STPVEETLEALNELVREGKIRYIGVSNWS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 158 SKKLTDLLNVAR----VTPAVNQVECHPVWQQ---QGLHELCKSKGVHLSGYSPLGSqskgevrlkvlqnpivtevaekl 230
Cdd:cd06660 142 AERLAEALAYAKahglPGFAAVQPQYSLLDRSpmeEELLDWAEENGLPLLAYSPLAR----------------------- 198
|
250 260 270
....*....|....*....|....*....|....*.
gi 145330687 231 GKttAQVALRWGLQ--TGHSVLPKSSSGARLKENLD 264
Cdd:cd06660 199 GP--AQLALAWLLSqpFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
22-241 |
2.13e-29 |
|
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: 112.65 E-value: 2.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 22 GTYAMVATAIEQAIKIGYRHIDCASIYGN---EKEIGGVLKKLIGdgfvKREELFITSK----LWSN---------DHLP 85
Cdd:cd19092 21 ESAEELLSLIEAALELGITTFDHADIYGGgkcEELFGEALALNPG----LREKIEIQTKcgirLGDDprpgrikhyDTSK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 86 EDVPKALEKTLQDLQIDYVDLYLIHwpaslkkeslmpTPEMLTKPDITStwKAMEALYDSGKARAIGVSNFSSKKLtDLL 165
Cdd:cd19092 97 EHILASVEGSLKRLGTDYLDLLLLH------------RPDPLMDPEEVA--EAFDELVKSGKVRYFGVSNFTPSQI-ELL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 166 NVARVTP-AVNQVEC---HPVWQQQGLHELCKSKGVHLSGYSPL------GSQSKGEVRLKVLqnpiVTEVAEKLGKTTA 235
Cdd:cd19092 162 QSYLDQPlVTNQIELsllHTEAIDDGTLDYCQLLDITPMAWSPLgggrlfGGFDERFQRLRAA----LEELAEEYGVTIE 237
|
....*.
gi 145330687 236 QVALRW 241
Cdd:cd19092 238 AIALAW 243
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-265 |
1.21e-28 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 109.98 E-value: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 11 NTGAKLPCVGLGTYA---MVATAIEQAIKIGYRHIDCASIYGN---EKEIGGVLKKligdgfVKREELFITSKLWSNDHL 84
Cdd:cd19105 8 KTGLKVSRLGFGGGGlprESPELLRRALDLGINYFDTAEGYGNgnsEEIIGEALKG------LRRDKVFLATKASPRLDK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 85 --PEDVPKALEKTLQDLQIDYVDLYLIHwpaslkkeSLMPTPEMLTKPDITstwKAMEALYDSGKARAIGVSnfSSKKLT 162
Cdd:cd19105 82 kdKAELLKSVEESLKRLQTDYIDIYQLH--------GVDTPEERLLNEELL---EALEKLKKEGKVRFIGFS--THDNMA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 163 DLLNVArvtpavnqVECHPV-------------WQQQGLHELCKSKGVHLSGYSPLGSqskgevrlkVLQNPIVTEVAEK 229
Cdd:cd19105 149 EVLQAA--------IESGWFdvimvaynflnqpAELEEALAAAAEKGIGVVAMKTLAG---------GYLQPALLSVLKA 211
|
250 260 270
....*....|....*....|....*....|....*...
gi 145330687 230 LGKTTAQVALRWGLQTG--HSVLPKSSSGARLKENLDV 265
Cdd:cd19105 212 KGFSLPQAALKWVLSNPrvDTVVPGMRNFAELEENLAA 249
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
13-274 |
3.10e-27 |
|
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: 107.29 E-value: 3.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 13 GAKLPCVGLGTY-------------AMVATAIEQAIkigyRHIDCASIYGN---EKEIGGVLKKLigdgfvKREELFITS 76
Cdd:cd19074 1 GLKVSELSLGTWltfggqvddedakACVRKAYDLGI----NFFDTADVYAAgqaEEVLGKALKGW------PRESYVIST 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 77 KL------WSND------HLPEdvpkALEKTLQDLQIDYVDLYLIHWPaslkKESlmpTPemltkpdITSTWKAMEALYD 144
Cdd:cd19074 71 KVfwptgpGPNDrglsrkHIFE----SIHASLKRLQLDYVDIYYCHRY----DPE---TP-------LEETVRAMDDLIR 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 145 SGKARAIGVSNFSSKKLTDLLNVAR----VTPAVNQVECHPVWQQ--QGLHELCKSKGVHLSGYSPL------------- 205
Cdd:cd19074 133 QGKILYWGTSEWSAEQIAEAHDLARqfglIPPVVEQPQYNMLWREieEEVIPLCEKNGIGLVVWSPLaqglltgkyrdgi 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 206 ----GSQSKGE-------------VRLKVLQnpiVTEVAEKLGKTTAQVALRWGLQTGH--SVLPKSSSGARLKENLDVF 266
Cdd:cd19074 213 pppsRSRATDEdnrdkkrrlltdeNLEKVKK---LKPIADELGLTLAQLALAWCLRNPAvsSAIIGASRPEQLEENVKAS 289
|
....*...
gi 145330687 267 DWSIPEDL 274
Cdd:cd19074 290 GVKLSPEV 297
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
11-274 |
1.61e-24 |
|
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: 99.98 E-value: 1.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 11 NTGAKLPCVGLGTYAM------------VATaIEQAIKIGYRHIDCASIYG---NEKEIGGVLKKligdgfvKREELFIT 75
Cdd:cd19076 7 TQGLEVSALGLGCMGMsafygpadeeesIAT-LHRALELGVTFLDTADMYGpgtNEELLGKALKD-------RRDEVVIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 76 SK---LWS-------NDHLPEDVPKALEKTLQDLQIDYVDLYLIHWPASlkkeslmPTPemltkpdITSTWKAMEALYDS 145
Cdd:cd19076 79 TKfgiVRDpgsgfrgVDGRPEYVRAACEASLKRLGTDVIDLYYQHRVDP-------NVP-------IEETVGAMAELVEE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 146 GKARAIGVSNFSSKkltDLLNVARVTP--AVnQVEcHPVWQ---QQGLHELCKSKGVHLSGYSPLG---------SQSK- 210
Cdd:cd19076 145 GKVRYIGLSEASAD---TIRRAHAVHPitAV-QSE-YSLWTrdiEDEVLPTCRELGIGFVAYSPLGrgfltgaikSPEDl 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 211 -------------GEVR---LKVLQNpiVTEVAEKLGKTTAQVALRWGLQTGHSVL--PKSSSGARLKENLDVFDWSI-P 271
Cdd:cd19076 220 peddfrrnnprfqGENFdknLKLVEK--LEAIAAEKGCTPAQLALAWVLAQGDDIVpiPGTKRIKYLEENVGALDVVLtP 297
|
...
gi 145330687 272 EDL 274
Cdd:cd19076 298 EEL 300
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-273 |
1.91e-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: 99.67 E-value: 1.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 19 VGLGTYAM----------------VATAIEQAIKIGYRHIDCASIYG---NEKEIGGVLKKLigdgfvkREELFITSK-- 77
Cdd:cd19102 4 IGLGTWAIggggwgggwgpqddrdSIAAIRAALDLGINWIDTAAVYGlghSEEVVGRALKGL-------RDRPIVATKcg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 78 -LW------SNDHLPEDVPKALEKTLQDLQIDYVDLYLIHWPAslkkeslmptPEmltkPDITSTWKAMEALYDSGKARA 150
Cdd:cd19102 77 lLWdeegriRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPD----------PD----EPIEEAWGALAELKEEGKVRA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 151 IGVSNFSSKKLTDLLNVARVT---PAVNQVEcHPVwqQQGLHELCKSKGVHLSGYSPLGS----------------QSKG 211
Cdd:cd19102 143 IGVSNFSVDQMKRCQAIHPIAslqPPYSLLR-RGI--EAEILPFCAEHGIGVIVYSPMQSglltgkmtpervaslpADDW 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145330687 212 EVRLKVLQNP----------IVTEVAEKLGKTTAQVALRWGLQtghsvLPKSSS---GAR----LKENLDVFDWSIPED 273
Cdd:cd19102 220 RRRSPFFQEPnlarnlalvdALRPIAERHGRTVAQLAIAWVLR-----RPEVTSaivGARrpdqIDETVGAADLRLTPE 293
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
19-273 |
2.89e-24 |
|
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: 99.30 E-value: 2.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 19 VGLGTYAM-------------VATaIEQAIKIGYRHIDCASIYG---NEKEIGGVLKkligdGFVKREELFITSKL---W 79
Cdd:cd19148 7 IALGTWAIggwmwggtdekeaIET-IHKALDLGINLIDTAPVYGfglSEEIVGKALK-----EYGKRDRVVIATKVgleW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 80 SNDHL------PEDVPKALEKTLQDLQIDYVDLYLIHWPASLkkeslmpTPemltkpdITSTWKAMEALYDSGKARAIGV 153
Cdd:cd19148 81 DEGGEvvrnssPARIRKEVEDSLRRLQTDYIDLYQVHWPDPL-------VP-------IEETAEALKELLDEGKIRAIGV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 154 SNFSSKKLTDLLNVAR---VTPAVNQVECH------PVWQQQGLHELCKS---KGVhLSGYSPLGSQSKGEVRLKV---L 218
Cdd:cd19148 147 SNFSPEQMETFRKVAPlhtVQPPYNLFEREiekdvlPYARKHNIVTLAYGalcRGL-LSGKMTKDTKFEGDDLRRTdpkF 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145330687 219 QNPIVTE---VAEKL--------GKTTAQVALRWGL-QTGHSVlpkSSSGARLKENLD----VFDWSIPED 273
Cdd:cd19148 226 QEPRFSQylaAVEELdklaqeryGKSVIHLAVRWLLdQPGVSI---ALWGARKPEQLDavdeVFGWSLNDE 293
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-264 |
3.71e-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: 381326 [Multi-domain] Cd Length: 238 Bit Score: 97.55 E-value: 3.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 11 NTGAKLPCVGLGTYAMVATAIEQAIKI-------GYRHIDCASIYGN-EKEIGGVLKKligdgfvKREELFITSKLWSND 82
Cdd:cd19100 6 RTGLKVSRLGFGGGPLGRLSQEEAAAIirraldlGINYFDTAPSYGDsEEKIGKALKG-------RRDKVFLATKTGARD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 83 hlPEDVPKALEKTLQDLQIDYVDLYLIHwpaSLKKeslMPTPEMLTKPDitSTWKAMEALYDSGKARAIGVSNFSSKKLT 162
Cdd:cd19100 79 --YEGAKRDLERSLKRLGTDYIDLYQLH---AVDT---EEDLDQVFGPG--GALEALLEAKEEGKIRFIGISGHSPEVLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 163 DLLNVAR---VTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPLGsqsKGevRLKvlqnpivtevaeKLGKTTAQVAL 239
Cdd:cd19100 149 RALETGEfdvVLFPINPAGDHIDSFREELLPLAREKGVGVIAMKVLA---GG--RLL------------SGDPLDPEQAL 211
|
250 260
....*....|....*....|....*..
gi 145330687 240 RWGLQTG--HSVLPKSSSGARLKENLD 264
Cdd:cd19100 212 RYALSLPpvDVVIVGMDSPEELDENLA 238
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-264 |
2.39e-23 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 97.00 E-value: 2.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 19 VGLGTY---------AMVATAIEQAIKIGYRHIDCASIYGN---EKEIGGVLKKLIGDGFVKREELFITSK--LWSNDHL 84
Cdd:cd19099 6 LGLGTYrgdsddetdEEYREALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGIKRDEVVIVTKagYIPGDGD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 85 PEDVPK-------------------------------ALEKTLQDLQIDYVDLYLIHWPAslkkESLMPTPEMLTKPDIT 133
Cdd:cd19099 86 EPLRPLkyleeklgrglidvadsaglrhcispayledQIERSLKRLGLDTIDLYLLHNPE----EQLLELGEEEFYDRLE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 134 STWKAMEALYDSGKARAIGVSNFS-------SKKLTDLLNVARVTPAVNQVECH--------PVWQQQGLH--------- 189
Cdd:cd19099 162 EAFEALEEAVAEGKIRYYGISTWDgfrappaLPGHLSLEKLVAAAEEVGGDNHHfkviqlplNLLEPEALTekntvkgea 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 190 ----ELCKSKGVHLSGYSPLGSQSKGEVrlkvlqNPIVTEVAEKLGKTTAQVALRWGLQT--GHSVLPKSSSGARLKENL 263
Cdd:cd19099 242 lsllEAAKELGLGVIASRPLNQGQLLGE------LRLADLLALPGGATLAQRALQFARSTpgVDSALVGMRRPEHVDENL 315
|
.
gi 145330687 264 D 264
Cdd:cd19099 316 A 316
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
11-267 |
1.26e-22 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 96.04 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 11 NTGAKLPCVGLGT-----------YAMVATAIEQAIkigyRHIDCASIYGN-EKEIGGVLKKLigdgfvkREELFITSKL 78
Cdd:COG1453 8 KTGLEVSVLGFGGmrlprkdeeeaEALIRRAIDNGI----NYIDTARGYGDsEEFLGKALKGP-------RDKVILATKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 79 --WSNDhlPEDVPKALEKTLQDLQIDYVDLYLIHwpaSLKKESLMptpEMLTKPDitSTWKAMEALYDSGKARAIGvsnF 156
Cdd:COG1453 77 ppWVRD--PEDMRKDLEESLKRLQTDYIDLYLIH---GLNTEEDL---EKVLKPG--GALEALEKAKAEGKIRHIG---F 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 157 SSKKLTDLLNVArvtpavnqVECHPV-----------WQQQG---LHELCKSKGVHLSGYSPLGSQSkgevrlkvLQNPi 222
Cdd:COG1453 144 STHGSLEVIKEA--------IDTGDFdfvqlqynyldQDNQAgeeALEAAAEKGIGVIIMKPLKGGR--------LANP- 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 145330687 223 vTEVAEKL---GKTTAQVALRWGL-QTGHSVLpksSSGAR----LKENLDVFD 267
Cdd:COG1453 207 -PEKLVELlcpPLSPAEWALRFLLsHPEVTTV---LSGMStpeqLDENLKTAD 255
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
11-258 |
1.33e-21 |
|
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381375 [Multi-domain] Cd Length: 315 Bit Score: 92.34 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 11 NTGAKLPCVGLGTYAM--------------VATaIEQAIKIGYRHIDCASIYGN---EKEIGGVLKKligdgfvKREELF 73
Cdd:cd19149 6 KSGIEASVIGLGTWAIgggpwwggsddnesIRT-IHAALDLGINLIDTAPAYGFghsEEIVGKAIKG-------RRDKVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 74 ITSK---LWSNDHL----------------PEDVPKALEKTLQDLQIDYVDLYLIHWPAslkkeslMPTPemltkpdITS 134
Cdd:cd19149 78 LATKcglRWDREGGsfffvrdgvtvyknlsPESIREEVEQSLKRLGTDYIDLYQTHWQD-------VETP-------IEE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 135 TWKAMEALYDSGKARAIGVSNFSSKKLTDLLNVARVtpAVNQVECHPVWQQQG--LHELCKSKGVHLSGYSPL------- 205
Cdd:cd19149 144 TMEALEELKRQGKIRAIGASNVSVEQIKEYVKAGQL--DIIQEKYSMLDRGIEkeLLPYCKKNNIAFQAYSPLeqglltg 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145330687 206 ----------GSQSKG------EVRLKVLQ-----NPIvtevAEKLGKTTAQVALRWGLQTGH--SVLpkssSGAR 258
Cdd:cd19149 222 kitpdrefdaGDARSGipwfspENREKVLAllekwKPL----CEKYGCTLAQLVIAWTLAQPGitSAL----CGAR 289
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
31-263 |
1.91e-21 |
|
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: 90.74 E-value: 1.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 31 IEQAIKIGYRHIDCASIYG---NEKEIGGVLKKligdgfvKREELFITSKL---------WSNDHLPEDVPKALEKTLQD 98
Cdd:cd19088 30 LRRALELGVNFIDTADSYGpdvNERLIAEALHP-------YPDDVVIATKGglvrtgpgwWGPDGSPEYLRQAVEASLRR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 99 LQIDYVDLYLIHWPAslkkeslmptpemlTKPDITSTWKAMEALYDSGKARAIGVSNFSSKKLTDLLNVARVTpAVnQVE 178
Cdd:cd19088 103 LGLDRIDLYQLHRID--------------PKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAIVRIV-SV-QNR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 179 CHPVWQQ-QGLHELCKSKGVHLSGYSPLGS----QSKGEVRlkvlqnpivtEVAEKLGKTTAQVALRWGLQTGHSVL--P 251
Cdd:cd19088 167 YNLANRDdEGVLDYCEAAGIAFIPWFPLGGgdlaQPGGLLA----------EVAARLGATPAQVALAWLLARSPVMLpiP 236
|
250
....*....|..
gi 145330687 252 KSSSGARLKENL 263
Cdd:cd19088 237 GTSSVEHLEENL 248
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
26-273 |
2.29e-21 |
|
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: 91.52 E-value: 2.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 26 MVATAIEQAIKigyrHIDCASIYGN-EKEIggVLKKLIGDgfvKREELFITSKLWS------ND------HLPEdvpkAL 92
Cdd:cd19091 44 LVDIALDAGIN----FFDTADVYSEgESEE--ILGKALKG---RRDDVLIATKVRGrmgegpNDvglsrhHIIR----AV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 93 EKTLQDLQIDYVDLYLIHWPASLkkeslmpTPemltkpdITSTWKAMEALYDSGKARAIGVSNFS------SKKLTDLLN 166
Cdd:cd19091 111 EASLKRLGTDYIDLYQLHGFDAL-------TP-------LEETLRALDDLVRQGKVRYIGVSNFSawqimkALGISERRG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 167 VARV-------TPAVNQVEchpvwqqqglHE---LCKSKGVHLSGYSPL------GSQSKGE-------VRLKVLQNPIV 223
Cdd:cd19091 177 LARFvalqayySLLGRDLE----------HElmpLALDQGVGLLVWSPLaggllsGKYRRGQpapegsrLRRTGFDFPPV 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145330687 224 T------------EVAEKLGKTTAQVALRWGLQ--TGHSVLPKSSSGARLKENLDVFDWSIPED 273
Cdd:cd19091 247 DrergydvvdalrEIAKETGATPAQVALAWLLSrpTVSSVIIGARNEEQLEDNLGAAGLSLTPE 310
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
11-263 |
3.05e-21 |
|
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor.
Pssm-ID: 381370 [Multi-domain] Cd Length: 323 Bit Score: 91.35 E-value: 3.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 11 NTGAKLPCVGLGTYAMVA------------TAIEQAIKIGYRHIDCASIYG-NEKEIGGVLKKLIGdgfvKREELFITSK 77
Cdd:cd19144 8 RNGPSVPALGFGAMGLSAfygppkpdeerfAVLDAAFELGCTFWDTADIYGdSEELIGRWFKQNPG----KREKIFLATK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 78 L----------WSNDHLPEDVPKALEKTLQDLQIDYVDLYLIHwpaslkkeslmptpEMLTKPDITSTWKAMEALYDSGK 147
Cdd:cd19144 84 FgieknvetgeYSVDGSPEYVKKACETSLKRLGVDYIDLYYQH--------------RVDGKTPIEKTVAAMAELVQEGK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 148 ARAIGVSNFSSKKLTDLLNVARVTpAVnQVECHPVW-----QQQGLHELCKSKGVHLSGYSPLG---------SQS---K 210
Cdd:cd19144 150 IKHIGLSECSAETLRRAHAVHPIA-AV-QIEYSPFSldierPEIGVLDTCRELGVAIVAYSPLGrgfltgairSPDdfeE 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145330687 211 GEVRLKV-------------LQNPIvTEVAEKLGKTTAQVALRWGLQTGHSVL--PKSSSGARLKENL 263
Cdd:cd19144 228 GDFRRMAprfqaenfpknleLVDKI-KAIAKKKNVTAGQLTLAWLLAQGDDIIpiPGTTKLKRLEENL 294
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
11-267 |
1.28e-20 |
|
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: 89.62 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 11 NTGAKLPCVGLG---------TYAMVATAIEQAIKIGYRHIDCASIYGN-----EKEIGGVLKKligDGFVKREELFITS 76
Cdd:cd19089 6 RSGLHLPAISLGlwhnfgdytSPEEARELLRTAFDLGITHFDLANNYGPppgsaEENFGRILKR---DLRPYRDELVIST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 77 K----LW--------SNDHLPEdvpkALEKTLQDLQIDYVDLYLIHwpaslkkeslMPTPEmltkpdiTSTWKAMEALYD 144
Cdd:cd19089 83 KagygMWpgpygdggSRKYLLA----SLDQSLKRMGLDYVDIFYHH----------RYDPD-------TPLEETMTALAD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 145 ---SGKARAIGVSNFSSKKLT---DLLNVARVTPAVNQVECHPV--WQQQGLHELCKSKGVHLSGYSPL----------- 205
Cdd:cd19089 142 avrSGKALYVGISNYPGAKARraiALLRELGVPLIIHQPRYSLLdrWAEDGLLEVLEEAGIGFIAFSPLaqglltdkyln 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 206 ----------------GSQSKGEVRLKVLQnpiVTEVAEKLGKTTAQVALRWGLQTGH--SVLPKSSSGARLKENLDVFD 267
Cdd:cd19089 222 gippdsrraaeskfltEEALTPEKLEQLRK---LNKIAAKRGQSLAQLALSWVLRDPRvtSVLIGASSPSQLEDNVAALK 298
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
11-273 |
2.38e-20 |
|
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a founding member of aldo-keto reductase family 9 member C1 (AKR9C1).
Pssm-ID: 381307 [Multi-domain] Cd Length: 308 Bit Score: 88.81 E-value: 2.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 11 NTGAKLPCVGLGTyaMV--ATAIEQA--------IKIGYRHIDCASIYGN----------EKEIGGVLKKLigdgfVKRE 70
Cdd:cd19081 4 RTGLSVSPLCLGT--MVfgWTADEETsfalldafVDAGGNFIDTADVYSAwvpgnaggesETIIGRWLKSR-----GKRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 71 ELFITSKLWSNDHL------PEDVPKALEKTLQDLQIDYVDLYLIHWPaslkkESLMPTPEMLTkpditstwkAMEALYD 144
Cdd:cd19081 77 RVVIATKVGFPMGPngpglsRKHIRRAVEASLRRLQTDYIDLYQAHWD-----DPATPLEETLG---------ALNDLIR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 145 SGKARAIGVSNFSSKKLTDLLNVAR---------VTPAVNQVECHPVwqQQGLHELCKSKGVHLSGYSPLGS-------- 207
Cdd:cd19081 143 QGKVRYIGASNYSAWRLQEALELSRqhglpryvsLQPEYNLVDRESF--EGELLPLCREEGIGVIPYSPLAGgfltgkyr 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 208 -------QSKGEVRLKVLQNP----IVT---EVAEKLGKTTAQVALRWGLQTG--HSVLPKSSSGARLKENLDVFDWSIP 271
Cdd:cd19081 221 seadlpgSTRRGEAAKRYLNErglrILDaldEVAAEHGATPAQVALAWLLARPgvTAPIAGARTVEQLEDLLAAAGLRLT 300
|
..
gi 145330687 272 ED 273
Cdd:cd19081 301 DE 302
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
17-265 |
5.98e-20 |
|
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381321 [Multi-domain] Cd Length: 253 Bit Score: 86.52 E-value: 5.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 17 PCVGLGT-----------YAMVATAIEQAIKIGYRHIDCASIYGN-EKEIGGVLKKLIgdgfvkREELFITSKLWSN--- 81
Cdd:cd19095 1 SVLGLGTsgigrvwgvpsEAEAARLLNTALDLGINLIDTAPAYGRsEERLGRALAGLR------RDDLFIATKVGTHgeg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 82 -----DHLPEDVPKALEKTLQDLQIDYVDLYLIHWPASLKKeslmpTPEMLTkpditstwkAMEALYDSGKARAIGVSNF 156
Cdd:cd19095 75 grdrkDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDEL-----TGEVLE---------TLEDLKAAGKVRYIGVSGD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 157 sskklTDLLNVARVTPAVN--QVECHPVWQ-QQGLHELCKSKGVHLSGYSPLGSqskGEVRLKVLQNPIVTEVAEKL--- 230
Cdd:cd19095 141 -----GEELEAAIASGVFDvvQLPYNVLDReEEELLPLAAEAGLGVIVNRPLAN---GRLRRRVRRRPLYADYARRPefa 212
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 145330687 231 ----GKTTAQVALRWGLQTG--HSVLPKSSSGARLKENLDV 265
Cdd:cd19095 213 aeigGATWAQAALRFVLSHPgvSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
31-273 |
9.55e-20 |
|
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: 87.25 E-value: 9.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 31 IEQAIKIGYRHIDCASIYGN---EKeiggVLKKLIGDgFVKREELFITSKLWSN-DHLPED-------VPKALEKTLQDL 99
Cdd:cd19079 41 IKRALDLGINFFDTANVYSGgasEE----ILGRALKE-FAPRDEVVIATKVYFPmGDGPNGrglsrkhIMAEVDASLKRL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 100 QIDYVDLYLIH-WPASlkkeslmpTPemltkpdITSTWKAMEALYDSGKARAIGVSNFSSKKLTDLLNVARvtpavnQVE 178
Cdd:cd19079 116 GTDYIDLYQIHrWDYE--------TP-------IEETLEALHDVVKSGKVRYIGASSMYAWQFAKALHLAE------KNG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 179 CHPVWQQQGLHEL------------CKSKGVHLSGYSPL------------GSQSKGEVRLKVLQN--------PI---V 223
Cdd:cd19079 175 WTKFVSMQNHYNLlyreeeremiplCEEEGIGVIPWSPLargrlarpwgdtTERRRSTTDTAKLKYdyfteadkEIvdrV 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 145330687 224 TEVAEKLGKTTAQVALRWGLQTGHSVLP--KSSSGARLKENLDVFDWSIPED 273
Cdd:cd19079 255 EEVAKERGVSMAQVALAWLLSKPGVTAPivGATKLEHLEDAVAALDIKLSEE 306
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
12-273 |
1.94e-19 |
|
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: 86.32 E-value: 1.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 12 TGAKLPCVGLGTYAM----------VATAIE---QAIKIGYRHIDCASIYG---NEKEIGGVLKKLigdgfvKREELFIT 75
Cdd:cd19083 7 SDIDVNPIGLGTNAVgghnlypnldEEEGKDlvrEALDNGVNLLDTAFIYGlgrSEELVGEVLKEY------NRNEVVIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 76 SK----------LWSNDhlPEDVPKALEKTLQDLQIDYVDLYLIHWPaslkkESLMPTPEMLTkpditstwkAMEALYDS 145
Cdd:cd19083 81 TKgahkfggdgsVLNNS--PEFLRSAVEKSLKRLNTDYIDLYYIHFP-----DGETPKAEAVG---------ALQELKDE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 146 GKARAIGVSNFSSKKLTDllnvARVTPAVNQVE-CHPVWQQQGLHEL---CKSKGVHLSGYSPLGS-------------- 207
Cdd:cd19083 145 GKIRAIGVSNFSLEQLKE----ANKDGYVDVLQgEYNLLQREAEEDIlpyCVENNISFIPYFPLASgllagkytkdtkfp 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145330687 208 -----QSKGEVRLKVLQNPI-----VTEVAEKLGKTTAQVALRWGLQTG--HSVLPKSSSGARLKENLDVFDWSIPED 273
Cdd:cd19083 221 dndlrNDKPLFKGERFSENLdkvdkLKSIADEKGVTVAHLALAWYLTRPaiDVVIPGAKRAEQVIDNLKALDVTLTEE 298
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
20-264 |
9.50e-19 |
|
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: 84.14 E-value: 9.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 20 GLGTYAMVATAIEQAIKIGYRHIDCASIYGnekeiGGVLKKLIGDGFVKREELFITSK---LWSNDHLPEDVPKALEKTL 96
Cdd:cd19075 15 RFTTAEAAAELLDAFLERGHTEIDTARVYP-----DGTSEELLGELGLGERGFKIDTKanpGVGGGLSPENVRKQLETSL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 97 QDLQIDYVDLYLIHwpaslkkeslmpTPEMLTkpDITSTWKAMEALYDSGKARAIGVSNFSSKKLTDLLNVAR----VTP 172
Cdd:cd19075 90 KRLKVDKVDVFYLH------------APDRST--PLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKengwVLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 173 AVNQVECHPVWQQQG--LHELCKSKGVHLSGYSPL------GSQSKGEVRL------------KVLQ----NP------- 221
Cdd:cd19075 156 TVYQGMYNAITRQVEteLFPCLRKLGIRFYAYSPLaggfltGKYKYSEDKAgggrfdpnnalgKLYRdrywKPsyfeale 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 145330687 222 IVTEVAEKLGKTTAQVALRWGLQtgHSVLPKS---------SSGARLKENLD 264
Cdd:cd19075 236 KVEEAAEKEGISLAEAALRWLYH--HSALDGEkgdgvilgaSSLEQLEENLA 285
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
23-267 |
1.17e-18 |
|
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: 82.99 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 23 TYAMVATAIEQaikiGYRHIDCASIYGN---EKEIGGVLKKLigdgfvKREELFITSKL-WSNDHLPEDVPKALEKTLQD 98
Cdd:cd19096 23 AIEMIRYAIDA----GINYFDTAYGYGGgksEEILGEALKEG------PREKFYLATKLpPWSVKSAEDFRRILEESLKR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 99 LQIDYVDLYLIHWPaslkkeSLMPTPEMLTKPDItstWKAMEALYDSGKARAIGvsnFSSKKLTDLLNVArvtpavnqVE 178
Cdd:cd19096 93 LGVDYIDFYLLHGL------NSPEWLEKARKGGL---LEFLEKAKKEGLIRHIG---FSFHDSPELLKEI--------LD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 179 CHPV--------------WQQQGLHELCKSKGVHLSGYSPLGsqsKGevrLKVLQNPIVTEVAEKLGKTTAQVALRWGLQ 244
Cdd:cd19096 153 SYDFdfvqlqynyldqenQAGRPGIEYAAKKGMGVIIMEPLK---GG---GLANNPPEALAILCGAPLSPAEWALRFLLS 226
|
250 260
....*....|....*....|....*....
gi 145330687 245 TG--HSVLpkssSGAR----LKENLDVFD 267
Cdd:cd19096 227 HPevTTVL----SGMStpeqLDENIAAAD 251
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
19-154 |
5.29e-18 |
|
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase YqkF is a founding member of aldo-keto reductase family 11 member C1 (AKR11C1). It may function as oxidoreductase. This family also includes Bacillus halodurans AKR11C1, an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase.
Pssm-ID: 381312 [Multi-domain] Cd Length: 238 Bit Score: 80.98 E-value: 5.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 19 VGLGTYAM------------VATAIEQAIKIGYRHIDCASIYGN---EKEIGGVLKKligdgfvKREELFITSKL----- 78
Cdd:cd19086 6 IGFGTWGLggdwwgdvddaeAIRALRAALDLGINFFDTADVYGDghsERLLGKALKG-------RRDKVVIATKFgnrfd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 79 ----WSNDHLPEDVPKALEKTLQDLQIDYVDLYLIHwpaslkkeslMPTPEMLTKPDItstWKAMEALYDSGKARAIGVS 154
Cdd:cd19086 79 ggpeRPQDFSPEYIREAVEASLKRLGTDYIDLYQLH----------NPPDEVLDNDEL---FEALEKLKQEGKIRAYGVS 145
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
19-275 |
3.02e-17 |
|
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH) and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. The family also includes L-galactose dehydrogenase (L-galDH) and D-arabinose 1-dehydrogenase (ARA2). L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381316 [Multi-domain] Cd Length: 278 Bit Score: 79.52 E-value: 3.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 19 VGLGTYAM------------VATaIEQAIKIGYRHIDCASIYGN-EKEIGGVLKKligdgfVKREELFITSKL-----WS 80
Cdd:cd19090 3 LGLGTAGLggvfggvdddeaVAT-IRAALDLGINYIDTAPAYGDsEERLGLALAE------LPREPLVLSTKVgrlpeDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 81 NDHLPEDVPKALEKTLQDLQIDYVDLYLIHWPAslkkeslMPTPEMLTKPDitSTWKAMEALYDSGKARAIGVSNFSSKK 160
Cdd:cd19090 76 ADYSADRVRRSVEESLERLGRDRIDLLMIHDPE-------RVPWVDILAPG--GALEALLELKEEGLIKHIGLGGGPPDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 161 LTDLLNVARVTPAVnqveCH----PVWQQ--QGLHELCKSKGVHLSGYSPLGSQSKGEVRLKVLQNPIVT---------- 224
Cdd:cd19090 147 LRRAIETGDFDVVL----TAnrytLLDQSaaDELLPAAARHGVGVINASPLGMGLLAGRPPERVRYTYRWlspelldrak 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 145330687 225 ---EVAEKLGKTTAQVALRWGLQ--TGHSVLPKSSSGARLKENLDVFDWSIPEDLF 275
Cdd:cd19090 223 rlyELCDEHGVPLPALALRFLLRdpRISTVLVGASSPEELEQNVAAAEGPLPEELW 278
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
19-274 |
7.29e-17 |
|
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: 79.15 E-value: 7.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 19 VGLGTYAMV-----ATAIEQ---AIKIGYRHIDCASIYG--NEKEIGGVLKKLIGD---GFVKREELFITSKL------- 78
Cdd:cd19094 4 ICLGTMTWGeqnteAEAHEQldyAFDEGVNFIDTAEMYPvpPSPETQGRTEEIIGSwlkKKGNRDKVVLATKVagpgegi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 79 -WSN----DHLPEDVPKALEKTLQDLQIDYVDLYLIHWPASlkkeslmPTP-----------EMLTKPDITSTWKAMEAL 142
Cdd:cd19094 84 tWPRgggtRLDRENIREAVEGSLKRLGTDYIDLYQLHWPDR-------YTPlfgggyytepsEEEDSVSFEEQLEALGEL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 143 YDSGKARAIGVSNFSSKKLTDLLNVARvtpavnQVEC-HPVWQQQ-----------GLHELCKSKGVHLSGYSPL----- 205
Cdd:cd19094 157 VKAGKIRHIGLSNETPWGVMKFLELAE------QLGLpRIVSIQNpysllnrnfeeGLAEACHRENVGLLAYSPLaggvl 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 206 ------GSQSKGEVRL-------KVLQNPIVTE-------VAEKLGKTTAQVALRWGLQTGH--SVLPKSSSGARLKENL 263
Cdd:cd19094 231 tgkyldGAARPEGGRLnlfpgymARYRSPQALEavaeyvkLARKHGLSPAQLALAWVRSRPFvtSTIIGATTLEQLKENI 310
|
330
....*....|.
gi 145330687 264 DVFDWSIPEDL 274
Cdd:cd19094 311 DAFDVPLSDEL 321
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
24-281 |
1.13e-16 |
|
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, Saccharopolyspora erythraea EryBII, and Streptomyces avermitilis aveBVIII are founding members of aldo-keto reductase family 12 member A1 (AKR12A1), B1 (AKR12B1), and C1(AKR12C1), respectively. TylCII acts as a NDP-hexose 2,3-enoyl reductase. EryBII is a mycarose/desosamine reductase involved in L-mycarose and D-desosamine production. aveBVIII functions as a dTDP-4-keto-6-deoxy-L-hexose-2,3-reductase.
Pssm-ID: 381313 [Multi-domain] Cd Length: 310 Bit Score: 78.38 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 24 YAMVATAIEQAIKIgyrhIDCASIYGNEK--EIGGvlkKLIGDgfvKREELFITSKL------WSND------HlpedVP 89
Cdd:cd19087 33 FAIMDRALDAGINF----FDTADVYGGGRseEIIG---RWIAG---RRDDIVLATKVfgpmgdDPNDrglsrrH----IR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 90 KALEKTLQDLQIDYVDLYLIHWPaslkkesLMPTPemltkpdITSTWKAMEALYDSGKARAIGVSNFSSKKLTDLLNVAR 169
Cdd:cd19087 99 RAVEASLRRLQTDYIDLYQMHHF-------DRDTP-------LEETLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGIAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 170 ---------VTPAVNQVECHPvwqQQGLHELCKSKGVHLSGYSPLG---------SQSKGEVRLKVLQNPIV-------- 223
Cdd:cd19087 165 rrgllrfvsEQPMYNLLKRQA---ELEILPAARAYGLGVIPYSPLAgglltgkygKGKRPESGRLVERARYQarygleey 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145330687 224 -------TEVAEKLGKTTAQVALRWGLqtGHSVLPKSSSGAR----LKENLDVFDWSIPEDLFTKFSNI 281
Cdd:cd19087 242 rdiaerfEALAAEAGLTPASLALAWVL--SHPAVTSPIIGPRtleqLEDSLAALEITLTPELLAEIDEL 308
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
12-263 |
2.60e-15 |
|
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: 74.69 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 12 TGAKLPCVGLGTYAMVATAI-----EQAIKIGYRH----IDCASIYGNEKE---IGGVLKKligDGFvKREELFITSKLW 79
Cdd:cd19159 9 SGLRVSCLGLGTWVTFGGQIsdevaERLMTIAYESgvnlFDTAEVYAAGKAeviLGSIIKK---KGW-RRSSLVITTKLY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 80 -----------SNDHLPEdvpkALEKTLQDLQIDYVDLYLIHWPaslkkESLMPTPEMLtkpditstwKAMEALYDSGKA 148
Cdd:cd19159 85 wggkaeterglSRKHIIE----GLKGSLQRLQLEYVDVVFANRP-----DSNTPMEEIV---------RAMTHVINQGMA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 149 RAIGVSNFSSKKLTDLLNVAR----VTPAVNQVECHpVWQQQG----LHELCKSKGVHLSGYSPL-----------GSQS 209
Cdd:cd19159 147 MYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYH-LFQREKvevqLPELYHKIGVGAMTWSPLacgiisgkygnGVPE 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145330687 210 KGEVRLKV---LQNPIVTE--------------VAEKLGKTTAQVALRWGLQTG--HSVLPKSSSGARLKENL 263
Cdd:cd19159 226 SSRASLKCyqwLKERIVSEegrkqqnklkdlspIAERLGCTLPQLAVAWCLRNEgvSSVLLGSSTPEQLIENL 298
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
31-263 |
1.07e-14 |
|
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: 73.01 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 31 IEQAIKIGYRHIDCASIYGN---EKEIGGVLKKLIgdgfVKREELFITSKL-W------------SNDHLPEdvpkALEK 94
Cdd:cd19143 37 MKAAYDAGVNFFDNAEVYANgqsEEIMGQAIKELG----WPRSDYVVSTKIfWggggpppndrglSRKHIVE----GTKA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 95 TLQDLQIDYVDLYLIHWPASLkkeslmpTPemltkpdITSTWKAMEALYDSGKARAIGVSNFSSKKLTDLLNVAR----V 170
Cdd:cd19143 109 SLKRLQLDYVDLVFCHRPDPA-------TP-------IEETVRAMNDLIDQGKAFYWGTSEWSAQQIEEAHEIADrlglI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 171 TPAVNQVECHPVWQQQGLHE---LCKSKGVHLSGYSPLGS-----------------------------QSKGEVRLKVL 218
Cdd:cd19143 175 PPVMEQPQYNLFHRERVEVEyapLYEKYGLGTTTWSPLASglltgkynngipegsrlalpgyewlkdrkEELGQEKIEKV 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 145330687 219 QNpiVTEVAEKLGKTTAQVALRWGLQTGH--SVLPKSSSGARLKENL 263
Cdd:cd19143 255 RK--LKPIAEELGCSLAQLAIAWCLKNPNvsTVITGATKVEQLEENL 299
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-264 |
1.80e-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: 381391 [Multi-domain] Cd Length: 291 Bit Score: 71.98 E-value: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 17 PCVGLGT-YAMVATAIEQAIKI-------GYRHIDCASIYG--NEKEIGGVLKKLIGD-----GfvKREELFITSKLW-- 79
Cdd:cd19752 1 SELCLGTmYFGTRTDEETSFAIldryvaaGGNFLDTANNYAfwTEGGVGGESERLIGRwlkdrG--NRDDVVIATKVGag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 80 --SNDHLPED--------VPKALEKTLQDLQIDYVDLYLIHwpaslkkeslmptpEMLTKPDITSTWKAMEALYDSGKAR 149
Cdd:cd19752 79 prDPDGGPESpeglsaetIEQEIDKSLRRLGTDYIDLYYAH--------------VDDRDTPLEETLEAFNELVKAGKVR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 150 AIGVSNFSSKKLTDLLNVARvtpaVNQVECHPVWQQQ--------------------GLHELCKSKG-VHLSGYSPL--G 206
Cdd:cd19752 145 AIGASNFAAWRLERARQIAR----QQGWAEFSAIQQRhsylrprpgadfgvqrivtdELLDYASSRPdLTLLAYSPLlsG 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145330687 207 SQSK-------------GEVRLKVLQnpivtEVAEKLGKTTAQVALRWGLQTGHSVLP--KSSSGARLKENLD 264
Cdd:cd19752 221 AYTRpdrplpeqydgpdSDARLAVLE-----EVAGELGATPNQVVLAWLLHRTPAIIPllGASTVEQLEENLA 288
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
31-166 |
3.15e-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: 381323 [Multi-domain] Cd Length: 267 Bit Score: 71.02 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 31 IEQAIKIGYRHIDCASIYGN-EKeiggvlkkLIGDGFVKREELFITSKLWSNDHLPEDVPKA----LEKTLQDLQIDYVD 105
Cdd:cd19097 32 LEYALKAGINTLDTAPAYGDsEK--------VLGKFLKRLDKFKIITKLPPLKEDKKEDEAAieasVEASLKRLKVDSLD 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145330687 106 LYLIHWPASLKKEslmptpemltKPDItstWKAMEALYDSGKARAIGVSNFSSKKLTDLLN 166
Cdd:cd19097 104 GLLLHNPDDLLKH----------GGKL---VEALLELKKEGLIRKIGVSVYSPEELEKALE 151
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
12-263 |
3.29e-14 |
|
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: 71.32 E-value: 3.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 12 TGAKLPCVGLGTYAMVATAI-----EQAIKIGYRH----IDCASIYGNEK-EIggVLKKLIGDGFVKREELFITSKL-W- 79
Cdd:cd19141 8 SGLRVSCLGLGTWVTFGSQIsdevaEELVTLAYENginlFDTAEVYAAGKaEI--VLGKILKKKGWRRSSYVITTKIfWg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 80 ---------SNDHLPEdvpkALEKTLQDLQIDYVDLYLIHwpaslKKESLMPTPEMLtkpditstwKAMEALYDSGKARA 150
Cdd:cd19141 86 gkaeterglSRKHIIE----GLKASLERLQLEYVDIVFAN-----RPDPNTPMEEIV---------RAFTHVINQGMAMY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 151 IGVSNFSSKKLTDLLNVAR----VTPAVNQVECHPVWQQQ---GLHELCKSKGVHLSGYSPLG----------------- 206
Cdd:cd19141 148 WGTSRWSAMEIMEAYSVARqfnlIPPIVEQAEYHLFQREKvemQLPELFHKIGVGAMTWSPLAcgilsgkyddgvpeysr 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145330687 207 SQSKGEVRLKvlqNPIVTE--------------VAEKLGKTTAQVALRWGL--QTGHSVLPKSSSGARLKENL 263
Cdd:cd19141 228 ASLKGYQWLK---EKILSEegrrqqaklkelqiIADRLGCTLPQLAIAWCLknEGVSSVLLGASSTEQLYENL 297
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
26-263 |
6.05e-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: 70.72 E-value: 6.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 26 MVATaIEQAIKIGYRHIDCASIYG---NEKEIGGVLKkligdGFvkREELFITSKL-WSNDHL----------PEDVPKA 91
Cdd:cd19078 27 MIEL-IRKAVELGITFFDTAEVYGpytNEELVGEALK-----PF--RDQVVIATKFgFKIDGGkpgplgldsrPEHIRKA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 92 LEKTLQDLQIDYVDLYLIHwpaslkkeslmptpEMLTKPDITSTWKAMEALYDSGKARAIGVSNFSSKKLTDLLNVARVT 171
Cdd:cd19078 99 VEGSLKRLQTDYIDLYYQH--------------RVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETIRRAHAVCPVT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 172 pAVnQVECHPVWQ--QQGLHELCKSKGVHLSGYSPLGSQ------------SKGEVRLKVLQN---------PIVT---E 225
Cdd:cd19078 165 -AV-QSEYSMMWRepEKEVLPTLEELGIGFVPFSPLGKGfltgkidentkfDEGDDRASLPRFtpealeanqALVDllkE 242
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 145330687 226 VAEKLGKTTAQVALRWGL-QTGHSV-LPKSSSGARLKENL 263
Cdd:cd19078 243 FAEEKGATPAQIALAWLLaKKPWIVpIPGTTKLSRLEENI 282
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
12-263 |
7.10e-14 |
|
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo sapiens, Rattus norvegicus, and Mus musculus, are founding members of aldo-keto reductase family 6 member A9 (AKR6A9), A12 (AKR6A12), A14 (AKR6A14), respectively. KCAB3B, also called Shaker channel b-subunit 3 (Kvb3), K(+) channel subunit beta-3, or Kv-beta-3, is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. It alters the functional properties of Kv1.5.
Pssm-ID: 381386 [Multi-domain] Cd Length: 325 Bit Score: 70.78 E-value: 7.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 12 TGAKLPCVGLGTYAMVATAI-----EQAIKIGYRH----IDCASIYGN---EKEIGGVLKKligDGFvKREELFITSKLW 79
Cdd:cd19160 11 SGLRVSCLGLGTWVTFGSQIsdetaEDLLTVAYEHgvnlFDTAEVYAAgkaERTLGNILKS---KGW-RRSSYVVTTKIY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 80 -----------SNDHLPEdvpkALEKTLQDLQIDYVDLYLIHwpaslKKESLMPTPEMLtkpditstwKAMEALYDSGKA 148
Cdd:cd19160 87 wggqaeterglSRKHIIE----GLRGSLDRLQLEYVDIVFAN-----RSDPNSPMEEIV---------RAMTYVINQGMA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 149 RAIGVSNFSSKKLTDLLNVAR----VTPAVNQVECHpVWQQQG----LHELCKSKGVHLSGYSPLG-------------- 206
Cdd:cd19160 149 MYWGTSRWSAMEIMEAYSVARqfnlIPPVCEQAEYH-LFQREKvemqLPELYHKIGVGSVTWSPLAcglitgkydgrvpd 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145330687 207 ---SQSKGEVRLK--------VLQNPIVTE---VAEKLGKTTAQVALRWGLQTG--HSVLPKSSSGARLKENL 263
Cdd:cd19160 228 tcrAAVKGYQWLKekvqseegKKQQAKVKElhpIADRLGCTVAQLAIAWCLRSEgvSSVLLGVSSAEQLIENL 300
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
42-267 |
1.07e-13 |
|
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: 69.89 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 42 IDCASIYGNEKEIGgVLKKLIGDGF---VKREELFITSK--------LWSNDHLPEDVPKALEKTLQDLQIDYVDLYLIH 110
Cdd:cd19082 34 IDTARVYGDWVERG-ASERVIGEWLksrGNRDKVVIATKgghpdledMSRSRLSPEDIRADLEESLERLGTDYIDLYFLH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 111 W-----PAslkkESLMPTpemltkpditstwkaMEALYDSGKARAIGVSNFSSKKLTDLLNVAR----VTPAVNQV---- 177
Cdd:cd19082 113 RddpsvPV----GEIVDT---------------LNELVRAGKIRAFGASNWSTERIAEANAYAKahglPGFAASSPqwsl 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 178 -----ECHP----VWQQQGLHELCKSKGVHLSGYSplgSQSKG-------------EVRLKVLQNPI-------VTEVAE 228
Cdd:cd19082 174 arpnePPWPgptlVAMDEEMRAWHEENQLPVFAYS---SQARGffskraaggaeddSELRRVYYSEEnferlerAKELAE 250
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 145330687 229 KLGKTTAQVALRWGLQTGHSVLP--KSSSGARLKENLDVFD 267
Cdd:cd19082 251 EKGVSPTQIALAYVLNQPFPTVPiiGPRTPEQLRDSLAAAD 291
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
20-243 |
1.81e-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: 69.22 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 20 GLGTYAMVATAIEQAIKIGYRHIDCASIYGN---EKEIGGVLKKLigdgfvkREELFITSKLWSNDHLPEDVP----KAL 92
Cdd:cd19104 27 GRTTREEQIAAVRRALDLGINFFDTAPSYGDgksEENLGRALKGL-------PAGPYITTKVRLDPDDLGDIGgqieRSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 93 EKTLQDLQIDYVDLYLIHwpASLKKESLMPTPEMLTKPDI---TSTWKAMEALYDSGKARAIGVSNFSSKKLT------- 162
Cdd:cd19104 100 EKSLKRLKRDSVDLLQLH--NRIGDERDKPVGGTLSTTDVlglGGVADAFERLRSEGKIRFIGITGLGNPPAIrelldsg 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 163 ---------DLLNvarvTPAVNQVecHPVWQQQ---GLHELCKSKGVHLSGYSPLG---------------SQSKGEVRL 215
Cdd:cd19104 178 kfdavqvyyNLLN----PSAAEAR--PRGWSAQdygGIIDAAAEHGVGVMGIRVLAagalttsldrgreapPTSDSDVAI 251
|
250 260
....*....|....*....|....*...
gi 145330687 216 KVLQNPIVTEVAEKLGKTTAQVALRWGL 243
Cdd:cd19104 252 DFRRAAAFRALAREWGETLAQLAHRFAL 279
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
42-274 |
2.28e-13 |
|
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: 68.79 E-value: 2.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 42 IDCASIYGN---EKEIGGVLKKligdgfvKREELFITSKLWSNDHlPEDVP----------KALEKTLQDLQIDYVDLYL 108
Cdd:cd19080 48 IDTANNYTNgtsERLLGEFIAG-------NRDRIVLATKYTMNRR-PGDPNaggnhrknlrRSVEASLRRLQTDYIDLLY 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 109 IHWPaslkkESLMPTPEMLtkpditstwKAMEALYDSGKARAIGVSNF------SSKKLTDLLNVARvtPAVNQVECHPV 182
Cdd:cd19080 120 VHAW-----DFTTPVEEVM---------RALDDLVRAGKVLYVGISDTpawvvaRANTLAELRGWSP--FVALQIEYSLL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 183 wQQQGLHEL---CKSKGVHLSGYSPLGS-----------QSKGEVRLKVLQNP------------IVTEVAEKLGKTTAQ 236
Cdd:cd19080 184 -ERTPERELlpmARALGLGVTPWSPLGGglltgkyqrgeEGRAGEAKGVTVGFgklternwaivdVVAAVAEELGRSAAQ 262
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 145330687 237 VALRWGLQTGHSVLPksSSGAR----LKENLDVFDWSIPEDL 274
Cdd:cd19080 263 VALAWVRQKPGVVIP--IIGARtleqLKDNLGALDLTLSPEQ 302
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
12-264 |
2.38e-13 |
|
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: 68.80 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 12 TGAKLPCVGLGTYAMVATAI----EQAIKI-------GYRHIDCASIYGNEKEIGGVlkKLIGDGFVK----REELFITS 76
Cdd:cd19077 1 NGKLVGPIGLGLMGLTWRPNptpdEEAFETmkaaldaGSNLWNGGEFYGPPDPHANL--KLLARFFRKypeyADKVVLSV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 77 KLWSNDHL------PEDVPKALEKTLQDL-QIDYVDLYLihwPASLKkeslmptpemlTKPDITSTWKAMEALYDSGKAR 149
Cdd:cd19077 79 KGGLDPDTlrpdgsPEAVRKSIENILRALgGTKKIDIFE---PARVD-----------PNVPIEETIKALKELVKEGKIR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 150 AIGVSNFSSKKLTDLLNVARVtpAVNQVECHPvW----QQQGLHELCKSKGVHLSGYSPLGS-----QSK-------GEV 213
Cdd:cd19077 145 GIGLSEVSAETIRRAHAVHPI--AAVEVEYSL-FsreiEENGVLETCAELGIPIIAYSPLGRglltgRIKsladipeGDF 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145330687 214 R--------------LKVLQNpiVTEVAEKLGKTTAQVALRWGLQTGHSV---LPKSSSGARLKENLD 264
Cdd:cd19077 222 RrhldrfngenfeknLKLVDA--LQELAEKKGCTPAQLALAWILAQSGPKiipIPGSTTLERVEENLK 287
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
12-263 |
2.46e-13 |
|
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.
Pssm-ID: 381368 [Multi-domain] Cd Length: 325 Bit Score: 69.03 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 12 TGAKLPCVGLGTYAMVATAIEQ---------AIKIGYRHIDCASIYGN---EKEIGGVLKKligdGFVKREELFITSKL- 78
Cdd:cd19142 9 SGLRVSNVGLGTWSTFSTAISEeqaeeivtlAYENGINYFDTSDAFTSgqaETELGRILKK----KGWKRSSYIVSTKIy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 79 WSNDhlPED-------VPKALEKTLQDLQIDYVDLYLIHwpaslKKESLMPTPEMLtkpditstwKAMEALYDSGKARAI 151
Cdd:cd19142 85 WSYG--SEErglsrkhIIESVRASLRRLQLDYIDIVIIH-----KADPMCPMEEVV---------RAMSYLIDNGLIMYW 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 152 GVSNFSSKKLTDLLNVAR----VTPAVNQVECHPVWQQQ---GLHELCKSKGVHLSGYSPL------------------- 205
Cdd:cd19142 149 GTSRWSPVEIMEAFSIARqfncPTPICEQSEYHMFCREKmelYMPELYNKVGVGLITWSPLslgldpgiseetrrlvtkl 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145330687 206 ---------GSQSKGEVRLKVLQNPIVTE---VAEKLGKTTAQVALRWGLQ--TGHSVLPKSSSGARLKENL 263
Cdd:cd19142 229 sfksskykvGSDGNGIHEETRRASHKLRElslIAERLGCDLTQLLIAWSLKneNVQCVLIGASSLEQLYSQL 300
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-251 |
2.71e-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: 381329 [Multi-domain] Cd Length: 299 Bit Score: 68.51 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 15 KLPCVGLGTYAM-------------------VATAIEQAIKIGYRHIDCASIYG---NEKEIGGVLKKligdgfVKREEL 72
Cdd:cd19103 3 KLPKIALGTWSWgsggaggdqvfgnhldedtLKAVFDKAMAAGLNLWDTAAVYGmgaSEKILGEFLKR------YPREDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 73 FITSKLWSN--DHLPEDVPKALEKTLQDLQIDYVDLYLIHWPASLKKEslmpTPEMLtkpditstwkameALYDSGKARA 150
Cdd:cd19103 77 IISTKFTPQiaGQSADPVADMLEGSLARLGTDYIDIYWIHNPADVERW----TPELI-------------PLLKSGKVKH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 151 IGVSNFS---SKKLTDLLNVARVTpaVNQVECH-----PVWQQQGLHELCKSKGVH-----------LSG-YS-----PL 205
Cdd:cd19103 140 VGVSNHNlaeIKRANEILAKAGVS--LSAVQNHysllyRSSEEAGILDYCKENGITffaymvleqgaLSGkYDtkhplPE 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 145330687 206 GSQSKG-----EVRLKVLqNPIVTEVAEKLGKTTAQVALRWGLQTGhsVLP 251
Cdd:cd19103 218 GSGRAEtynplLPQLEEL-TAVMAEIGAKHGASIAQVAIAWAIAKG--TTP 265
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
27-274 |
1.01e-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: 381327 [Multi-domain] Cd Length: 304 Bit Score: 66.85 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 27 VATAIEQAIKIGYRHIDCASIYGNEKEIGGVLKKLIGDGFVKREELFITSKLWSNDHL----PEDVPKALEKTLQDLQID 102
Cdd:cd19101 25 AVRAMAAYVDAGLTTFDCADIYGPAEELIGEFRKRLRRERDAADDVQIHTKWVPDPGEltmtRAYVEAAIDRSLKRLGVD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 103 YVDLYLIHW-----PASLkkeslmptpemltkpditSTWKAMEALYDSGKARAIGVSNFSSKKLTDLLNvARVTPAVNQV 177
Cdd:cd19101 105 RLDLVQFHWwdysdPGYL------------------DAAKHLAELQEEGKIRHLGLTNFDTERLREILD-AGVPIVSNQV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 178 ECHPVWQ--QQGLHELCKSKGVHLSGYSP----------LGSQSKGEVR-------------------------LKVLQn 220
Cdd:cd19101 166 QYSLLDRrpENGMAALCEDHGIKLLAYGTlaggllsekyLGVPEPTGPAletrslqkyklmidewggwdlfqelLRTLK- 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145330687 221 pivtEVAEKLGKTTAQVALRWGLQT---GHSVLpksssGARL----KENLDVFDWSI-PEDL 274
Cdd:cd19101 245 ----AIADKHGVSIANVAVRWVLDQpgvAGVIV-----GARNsehiDDNVRAFSFRLdDEDR 297
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
16-251 |
1.21e-12 |
|
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: 66.69 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 16 LPCVGL-GTY-------AMVATaIEQAIKIGYRHIDCASIYG---NEKEIGGVLKKLIgdgfvkREELFITSK----LWS 80
Cdd:cd19145 17 LGCMGLsGDYgapkpeeEGIAL-IHHAFNSGVTFLDTSDIYGpntNEVLLGKALKDGP------REKVQLATKfgihEIG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 81 NDHL-----PEDVPKALEKTLQDLQIDYVDLYLIHwpaslkkeslmptpEMLTKPDITSTWKAMEALYDSGKARAIGVSN 155
Cdd:cd19145 90 GSGVevrgdPAYVRAACEASLKRLDVDYIDLYYQH--------------RIDTTVPIEITMGELKKLVEEGKIKYIGLSE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 156 FSSKKLTDLLNVARVTpAVnQVEcHPVWQQQGLHE---LCKSKGVHLSGYSPLG------------SQSKGEVRLK---- 216
Cdd:cd19145 156 ASADTIRRAHAVHPIT-AV-QLE-WSLWTRDIEEEiipTCRELGIGIVPYSPLGrgffagkakleeLLENSDVRKShprf 232
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 145330687 217 ----VLQNPIVTE----VAEKLGKTTAQVALRWGLQTGHSVLP 251
Cdd:cd19145 233 qgenLEKNKVLYErveaLAKKKGCTPAQLALAWVLHQGEDVVP 275
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
11-267 |
2.11e-12 |
|
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: 66.02 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 11 NTGAKLPCVGLGTYAM-------------VATaIEQAIKIGYRHIDCASIYGN---EKEIGGVLKKLIgdgfVKREELFI 74
Cdd:cd19153 7 IALGNVSPVGLGTAALggvygdgleqdeaVAI-VAEAFAAGINHFDTSPYYGAessEAVLGKALAALQ----VPRSSYTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 75 TSKL-----WSNDHLPEDVPKALEKTLQDLQIDYVDLYLIHWPASLKKEslmptpemltkPDITSTWKAMEALYDSGKAR 149
Cdd:cd19153 82 ATKVgryrdSEFDYSAERVRASVATSLERLHTTYLDVVYLHDIEFVDYD-----------TLVDEALPALRTLKDEGVIK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 150 AIGVSNFSSKKLTDLLN-VARVTPAVNQVECHPVWQQQGLHE----LCKSKGVHLSGYSPLG-----SQ-------SKGE 212
Cdd:cd19153 151 RIGIAGYPLDTLTRATRrCSPGSLDAVLSYCHLTLQDARLESdapgLVRGAGPHVINASPLSmglltSQgpppwhpASGE 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 145330687 213 VRLKVLQNpiVTEVAEKlGKTTAQVALRWGL--QTG-HSVLPKSSSGARLKENLDVFD 267
Cdd:cd19153 231 LRHYAAAA--DAVCASV-EASLPDLALQYSLaaHAGvGTVLLGPSSLAQLRSMLAAVD 285
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
17-274 |
3.11e-12 |
|
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: 65.46 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 17 PCVGLGTYAM----------VATAIEQAIKIGYRHIDCASIYG---NEKEIGGVLKKLigdgfvKREELFITSKLWSNDH 83
Cdd:cd19162 1 PRLGLGAASLgnlaragedeAAATLDAAWDAGIRYFDTAPLYGlglSERRLGAALARH------PRAEYVVSTKVGRLLE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 84 LPEDVPKA----------------LEKTLQDLQIDYVDLYLIHwpaslkkeslmpTPEMLTKPDITSTWKAMEALYDSGK 147
Cdd:cd19162 75 PGAAGRPAgadrrfdfsadgirrsIEASLERLGLDRLDLVFLH------------DPDRHLLQALTDAFPALEELRAEGV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 148 ARAIGVSNFSSKKLTDLLNVARVTpAVNQVECHPVWQQQGLHEL---CKSKGVHLSGYSPLGS----------------Q 208
Cdd:cd19162 143 VGAIGVGVTDWAALLRAARRADVD-VVMVAGRYTLLDRRAATELlplCAAKGVAVVAAGVFNSgilatddpagdrydyrP 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 209 SKGEVRLKVLQnpiVTEVAEKLGKTTAQVALRWGLQtgH----SVLPKSSSGARLKENLDVFDWSIPEDL 274
Cdd:cd19162 222 ATPEVLARARR---LAAVCRRYGVPLPAAALQFPLR--HpavaSVVVGAASPAELRDNLALLRTPIPAEF 286
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
12-263 |
9.86e-12 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 64.63 E-value: 9.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 12 TGAKLPCVGLGTYAMVA---------TAIEQAIKIGYRHIDCASIYG-----NEKEIGGVLKKligDGFVKREELFITSK 77
Cdd:PRK09912 21 SGLRLPALSLGLWHNFGhvnalesqrAILRKAFDLGITHFDLANNYGpppgsAEENFGRLLRE---DFAAYRDELIISTK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 78 ----LWSNDHLPEDVPK----ALEKTLQDLQIDYVDLYLIHwpaslKKESLMPTPEmltkpditsTWKAMEALYDSGKAR 149
Cdd:PRK09912 98 agydMWPGPYGSGGSRKyllaSLDQSLKRMGLEYVDIFYSH-----RVDENTPMEE---------TASALAHAVQSGKAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 150 AIGVSNFSS---KKLTDLLNVARVTPAVNQVECHPV--W-QQQGLHELCKSKGVHLSGYSPL------------------ 205
Cdd:PRK09912 164 YVGISSYSPertQKMVELLREWKIPLLIHQPSYNLLnrWvDKSGLLDTLQNNGVGCIAFTPLaqglltgkylngipqdsr 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145330687 206 ----GSQSKG-------EVRLKVLQnpIVTEVAEKLGKTTAQVALRWGLQTGH--SVLPKSSSGARLKENL 263
Cdd:PRK09912 244 mhreGNKVRGltpkmltEANLNSLR--LLNEMAQQRGQSMAQMALSWLLKDERvtSVLIGASRAEQLEENV 312
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
19-289 |
1.59e-11 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 63.72 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 19 VGLGTYAM-----VATAIEQ---AIKIGYRHIDCASIYG--NEKEIGGVLKKLIGDGFVK---REELFITSKL----WSN 81
Cdd:PRK10625 16 LGLGTMTFgeqnsEADAHAQldyAVAQGINLIDVAEMYPvpPRPETQGLTETYIGNWLAKrgsREKLIIASKVsgpsRNN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 82 DHL--P------EDVPKALEKTLQDLQIDYVDLYLIHWPA----SLKKESLMPTPEmltKPDIT--STWKAMEALYDSGK 147
Cdd:PRK10625 96 DKGirPnqaldrKNIREALHDSLKRLQTDYLDLYQVHWPQrptnCFGKLGYSWTDS---APAVSllETLDALAEQQRAGK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 148 ARAIGVSNFSSKKLTDLLNVA------RVTPAVNQVECHPVWQQQGLHELCKSKGVHLSGYSPL-----------GSQSK 210
Cdd:PRK10625 173 IRYIGVSNETAFGVMRYLHLAekhdlpRIVTIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLafgtltgkylnGAKPA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 211 GE--------VRLKVLQNPIVT----EVAEKLGKTTAQVALRWGLQTGH--SVLPKSSSGARLKENLDVFDWSIPEDLFT 276
Cdd:PRK10625 253 GArntlfsrfTRYSGEQTQKAVaayvDIAKRHGLDPAQMALAFVRRQPFvaSTLLGATTMEQLKTNIESLHLTLSEEVLA 332
|
330
....*....|...
gi 145330687 277 KFSNIPQAKVLPS 289
Cdd:PRK10625 333 EIEAVHQVYTYPA 345
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
11-262 |
4.90e-11 |
|
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: 62.04 E-value: 4.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 11 NTGAKLPCVGLGTY-------------AMVATAIEqaikIGYRHIDCASIYG-----NEKEIGGVLKKligDGFVKREEL 72
Cdd:cd19151 7 RSGLKLPAISLGLWhnfgdvdryensrAMLRRAFD----LGITHFDLANNYGpppgsAEENFGRILKE---DLKPYRDEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 73 FITSK----LW--------SNDHLPedvpKALEKTLQDLQIDYVDLYLIHWPaslKKEslmpTPemltkpdITSTWKAME 140
Cdd:cd19151 80 IISTKagytMWpgpygdwgSKKYLI----ASLDQSLKRMGLDYVDIFYHHRP---DPE----TP-------LEETMGALD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 141 ALYDSGKARAIGVSNFSSKKLTDLLNVARV--TPAVNQVECHPV---WQQQGLHELCKSKGVHLSGYSPLGS-------- 207
Cdd:cd19151 142 QIVRQGKALYVGISNYPPEEAREAAAILKDlgTPCLIHQPKYSMfnrWVEEGLLDVLEEEGIGCIAFSPLAQglltdryl 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145330687 208 --------QSKGEVRLKVLQnpiVTE-----------VAEKLGKTTAQVALRWGLQTGH--SVLPKSSSGARLKEN 262
Cdd:cd19151 222 ngipedsrAAKGSSFLKPEQ---ITEeklakvrrlneIAQARGQKLAQMALAWVLRNKRvtSVLIGASKPSQIEDA 294
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
11-274 |
8.35e-11 |
|
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+).
Pssm-ID: 381389 [Multi-domain] Cd Length: 293 Bit Score: 61.41 E-value: 8.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 11 NTGAKLPCVGLGTYAM-----------VATAIEQAIKIGYRHIDCASIYGN---EKEIGGVLKKligdgfVKREELFITS 76
Cdd:cd19163 8 KTGLKVSKLGFGASPLggvfgpvdeeeAIRTVHEALDSGINYIDTAPWYGQgrsETVLGKALKG------IPRDSYYLAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 77 K------LWSN--DHLPEDVPKALEKTLQDLQIDYVDLYLIHwpaslkkeslmpTPEMLTKPD--ITSTWKAMEALYDSG 146
Cdd:cd19163 82 KvgryglDPDKmfDFSAERITKSVEESLKRLGLDYIDIIQVH------------DIEFAPSLDqiLNETLPALQKLKEEG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 147 KARAIGVSNFSSKKLTDLLnvARVTPAVNQV--ECHPVWQQQGLHEL---CKSKGVHLSGYSPLGS---QSKG------- 211
Cdd:cd19163 150 KVRFIGITGYPLDVLKEVL--ERSPVKIDTVlsYCHYTLNDTSLLELlpfFKEKGVGVINASPLSMgllTERGppdwhpa 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145330687 212 --EVRLKVLQnpiVTEVAEKLGKTTAQVALRWGLQT--GHSVLPKSSSGARLKENLDVFDWSIPEDL 274
Cdd:cd19163 228 spEIKEACAK---AAAYCKSRGVDISKLALQFALSNpdIATTLVGTASPENLRKNLEAAEEPLDAHL 291
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
33-285 |
2.09e-10 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 59.98 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 33 QAIKIGYRHIDCASIYGNekeigGVLKKLIGDG-FVKREELFITSKL---------WSNDHLPEDVPKALEKTLQDLQ-- 100
Cdd:PRK10376 48 EAVALGVNHIDTSDFYGP-----HVTNQLIREAlHPYPDDLTIVTKVgarrgedgsWLPAFSPAELRRAVHDNLRNLGld 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 101 -IDYVDLYLIHWPASlkkeslmPTPEMLTKPditstWKAMEALYDSGKARAIGVSNFSSKKLTDLLNVARVTPAVNQVE- 178
Cdd:PRK10376 123 vLDVVNLRLMGDGHG-------PAEGSIEEP-----LTVLAELQRQGLVRHIGLSNVTPTQVAEARKIAEIVCVQNHYNl 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 179 CHPvwQQQGLHELCKSKGVHLSGYSPLGSQSKgevrlkvLQNPIVTEVAEKLGKTTAQVALRWGLQTGHSVL--PKSSSG 256
Cdd:PRK10376 191 AHR--ADDALIDALARDGIAYVPFFPLGGFTP-------LQSSTLSDVAASLGATPMQVALAWLLQRSPNILliPGTSSV 261
|
250 260
....*....|....*....|....*....
gi 145330687 257 ARLKENLDVFDWSIPEDLFTKFSNIPQAK 285
Cdd:PRK10376 262 AHLRENLAAAELVLSEEVLAELDGIAREA 290
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
12-263 |
6.15e-10 |
|
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.
Pssm-ID: 381384 [Multi-domain] Cd Length: 324 Bit Score: 58.94 E-value: 6.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 12 TGAKLPCVGLGTYAMVATAI-----EQAIKIGYRH----IDCASIYGNEKE---IGGVLKKligDGFvKREELFITSKL- 78
Cdd:cd19158 9 SGLRVSCLGLGTWVTFGGQItdemaEHLMTLAYDNginlFDTAEVYAAGKAevvLGNIIKK---KGW-RRSSLVITTKIf 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 79 WSNDHLPE------DVPKALEKTLQDLQIDYVDLYLIHWPAslkkeslmPTPEMltkpdiTSTWKAMEALYDSGKARAIG 152
Cdd:cd19158 85 WGGKAETErglsrkHIIEGLKASLERLQLEYVDVVFANRPD--------PNTPM------EETVRAMTHVINQGMAMYWG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 153 VSNFSSKKLTDLLNVAR----VTPAVNQVECHPVWQQQ---GLHELCKSKGVHLSGYSPLG-------------SQSKGE 212
Cdd:cd19158 151 TSRWSSMEIMEAYSVARqfnlIPPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPLAcgivsgkydsgipPYSRAS 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145330687 213 VR-LKVLQNPIVTE--------------VAEKLGKTTAQVALRWGLQTG--HSVLPKSSSGARLKENL 263
Cdd:cd19158 231 LKgYQWLKDKILSEegrrqqaklkelqaIAERLGCTLPQLAIAWCLRNEgvSSVLLGASNAEQLMENI 298
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
11-205 |
2.23e-09 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 57.10 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 11 NTGAKLPCVGLG------TYAMVA--TAIE---QAIKIGYRHIDCASIYGN---EKEIGGVLKKLIgdgfVKREELFITS 76
Cdd:PLN02587 6 STGLKVSSVGFGasplgsVFGPVSeeDAIAsvrEAFRLGINFFDTSPYYGGtlsEKVLGKALKALG----IPREKYVVST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 77 KLWSN----DHLPEDVPKALEKTLQDLQIDYVDLYLIHwpaSLKKESLMPTpemltkpdITSTWKAMEALYDSGKARAIG 152
Cdd:PLN02587 82 KCGRYgegfDFSAERVTKSVDESLARLQLDYVDILHCH---DIEFGSLDQI--------VNETIPALQKLKESGKVRFIG 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 145330687 153 VSNFSSKKLTDLLNvaRVTPAVNQV---ECHPVWQQQGLHELC---KSKGVHLSGYSPL 205
Cdd:PLN02587 151 ITGLPLAIFTYVLD--RVPPGTVDVilsYCHYSLNDSSLEDLLpylKSKGVGVISASPL 207
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
12-267 |
2.75e-09 |
|
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: 57.08 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 12 TGAKLPCVGLG--------TYAMVATAI-EQAIKIGYRHIDCASIYG-----NEKEIGGVLKKligDGFVKREELFITSK 77
Cdd:cd19150 8 SGLKLPALSLGlwhnfgddTPLETQRAIlRTAFDLGITHFDLANNYGpppgsAEENFGRILRE---DFAGYRDELIISTK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 78 ----LWSNDHLPEDVPK----ALEKTLQDLQIDYVDLYLIHwpaslKKESLMPTPEmltkpditsTWKAMEALYDSGKAR 149
Cdd:cd19150 85 agydMWPGPYGEWGSRKyllaSLDQSLKRMGLDYVDIFYSH-----RFDPDTPLEE---------TMGALDHAVRSGKAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 150 AIGVSNFSSKKLTDLLNVARV--TPAVNQVECHPV---W-QQQGLHELCKSKGVHLSGYSPL---------------GSQ 208
Cdd:cd19150 151 YVGISSYSPERTREAAAILRElgTPLLIHQPSYNMlnrWvEESGLLDTLQELGVGCIAFTPLaqglltdkylngipeGSR 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145330687 209 -SKGEVRLKVLQNP-------IVTEVAEKLGKTTAQVALRWGLQTGH--SVLPKSSSGARLKENLDVFD 267
Cdd:cd19150 231 aSKERSLSPKMLTEanlnsirALNEIAQKRGQSLAQMALAWVLRDGRvtSALIGASRPEQLEENVGALD 299
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
16-278 |
3.73e-04 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 41.54 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 16 LPCVGLG------TYAMVATAIEQAIKIGYRHIDCASIYGN---EKEIGGVLKKLIGDGFV----------KREELFITS 76
Cdd:cd19161 5 LGTAGLGnlytavSNADADATLDAAWDSGIRYFDTAPMYGHglaEHRLGDFLREKPRDEFVlstkvgrllkPAREGSVPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 77 KLWSNDHLP---------EDVPKALEKTLQDLQIDYVDLYLIH--WPASLKKESLMPTPEMLTKpditSTWKAMEALYDS 145
Cdd:cd19161 85 PNGFVDPLPfeivydysyDGIMRSFEDSLQRLGLNRIDILYVHdiGVYTHGDRKERHHFAQLMS----GGFKALEELKKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 146 GKARAIGvsnfsskkltdlLNVARVTPAVN-----QVEC------HPVWQQQGLHEL---CKSKGVHL-------SGYsp 204
Cdd:cd19161 161 GVIKAFG------------LGVNEVQICLEaldeaDLDCfllagrYSLLDQSAEEEFlprCEQRGTSLviggvfnSGI-- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 205 LGSQSKGEVRLKVLQNP--IVTEVAE------KLGKTTAQVALRWGLQtgH----SVLPKSSSGARLKENLDVFDWSIPE 272
Cdd:cd19161 227 LATGTKSGAKFNYGDAPaeIISRVMEiekicdAYNVPLAAAALQFPLR--HpavaSVLTGARNPAQLRQNVEAFQTDIPE 304
|
....*.
gi 145330687 273 DLFTKF 278
Cdd:cd19161 305 ELWQAL 310
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
30-153 |
3.04e-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: 38.36 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145330687 30 AIEQAIKIGYRHIDCASIYGN---EKEIGGVLKKLigdgfvKREELFITSKL-WSNDHLPEDVP---------------- 89
Cdd:cd19152 25 TLVAAWDLGIRYFDTAPWYGAglsEERLGAALREL------GREDYVISTKVgRLLVPLQEVEPtfepgfwnplpfdavf 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145330687 90 --------KALEKTLQDLQIDYVDLYLIHWPA--SLKKESLMPTPEmltkpDITSTWKAMEALYDSGKARAIGV 153
Cdd:cd19152 99 dysydgilRSIEDSLQRLGLSRIDLLSIHDPDedLAGAESDEHFAQ-----AIKGAFRALEELREEGVIKAIGL 167
|
|
| |
