|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
4-279 |
0e+00 |
|
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: 523.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 4 PTSFKLNTGATIPAVGLGTWQAKAGEVRQAVAHALKAGYRHIDGALCYQNEEEVGLGIKDS---GIPRSEIFLTSKVWSS 80
Cdd:cd19121 1 MTSFKLNTGASIPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAiagGVKREDLFVTTKLWST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 81 YHDRVEECLDTTLKSLQTDYLDLYLIHWPVRLVPNGTHPLFPTKPDGSRNLDWDWDQAKTWAQMEDVLKKGKVKAIGLSN 160
Cdd:cd19121 81 YHRRVELCLDRSLKSLGLDYVDLYLVHWPVLLNPNGNHDLFPTLPDGSRDLDWDWNHVDTWKQMEKVLKTGKTKAIGVSN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 161 AGIPIIEHIIKTGKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGSTSSPLHEDPDLVAVAKKHNVPTATVLIS 240
Cdd:cd19121 161 YSIPYLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTGSPLISDEPVVEIAKKHNVGPGTVLIS 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 2781183762 241 YQVNRGVVVLPKSVTPARIESNLKTIKLDEEDMNRLDKL 279
Cdd:cd19121 241 YQVARGAVVLPKSVTPDRIKSNLEIIDLDDEDMNKLNDI 279
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
7-279 |
2.08e-133 |
|
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: 380.31 E-value: 2.08e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 7 FKLNTGATIPAVGLGTWQAKAGEVRQAVAHALKAGYRHIDGALCYQNEEEVGLGIKDSGIPRSEIFLTSKVWSSYHDRVE 86
Cdd:cd19117 6 FKLNTGAEIPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIKDSGVPREEIFITTKLWCTWHRRVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 87 ECLDTTLKSLQTDYLDLYLIHWPVRLVPNGTHPLfPTKPDGSRNLDWDWDQAKTWAQMEDVLKKGKVKAIGLSNAGIPII 166
Cdd:cd19117 86 EALDQSLKKLGLDYVDLYLMHWPVPLDPDGNDFL-FKKDDGTKDHEPDWDFIKTWELMQKLPATGKVKAIGVSNFSIKNL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 167 EHIIKT--GKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGSTSSPLHEDPDLVAVAKKHNVPTATVLISYQVN 244
Cdd:cd19117 165 EKLLASpsAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTNAPLLKEPVIIKIAKKHGKTPAQVIISWGLQ 244
|
250 260 270
....*....|....*....|....*....|....*
gi 2781183762 245 RGVVVLPKSVTPARIESNLKTIKLDEEDMNRLDKL 279
Cdd:cd19117 245 RGYSVLPKSVTPSRIESNFKLFTLSDEEFKEIDEL 279
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
15-277 |
2.33e-122 |
|
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: 351.01 E-value: 2.33e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 15 IPAVGLGTWQAKAGEVRQAVAHALKAGYRHIDGALCYQNEEEVGLGIKDSGIPRSEIFLTSKVWSSYH--DRVEECLDTT 92
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESGVPREELFITTKLWPTDHgyERVREALEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 93 LKSLQTDYLDLYLIHWPVrlvpngthplfptkPDGSRNLDWDWdqAKTWAQMEDVLKKGKVKAIGLSNAGIPIIEHIIKT 172
Cdd:cd19071 81 LKDLGLDYLDLYLIHWPV--------------PGKEGGSKEAR--LETWRALEELVDEGLVRSIGVSNFNVEHLEELLAA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 173 GKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGSTSSPLHEDPDLVAVAKKHNVPTATVLISYQVNRGVVVLPK 252
Cdd:cd19071 145 ARIKPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRRPLLDDPVLKEIAKKYGKTPAQVLLRWALQRGVVVIPK 224
|
250 260
....*....|....*....|....*..
gi 2781183762 253 SVTPARIESNLK--TIKLDEEDMNRLD 277
Cdd:cd19071 225 SSNPERIKENLDvfDFELSEEDMAAID 251
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
12-292 |
3.30e-113 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 328.17 E-value: 3.30e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 12 GATIPAVGLGTWQAKAGEVRQAVAHALKAGYRHIDGALCYQNEEEVGLGIKDSGIPRSEIFLTSKVWSSYH--DRVEECL 89
Cdd:COG0656 2 GVEIPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAASGVPREELFVTTKVWNDNHgyDDTLAAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 90 DTTLKSLQTDYLDLYLIHWPVRlvpngtHPLfptkpdgsrnldwdwdqAKTWAQMEDVLKKGKVKAIGLSNAGIPIIEHI 169
Cdd:COG0656 82 EESLERLGLDYLDLYLIHWPGP------GPY-----------------VETWRALEELYEEGLIRAIGVSNFDPEHLEEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 170 IKTGKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGSTSspLHEDPDLVAVAKKHNVPTATVLISYQVNRGVVV 249
Cdd:COG0656 139 LAETGVKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGRGK--LLDDPVLAEIAEKHGKTPAQVVLRWHLQRGVVV 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2781183762 250 LPKSVTPARIESNLK--TIKLDEEDMNRLDKLAesgKQTRFTTPP 292
Cdd:COG0656 217 IPKSVTPERIRENLDafDFELSDEDMAAIDALD---RGERLGPDP 258
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
9-279 |
1.85e-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: 319.74 E-value: 1.85e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 9 LNTGATIPAVGLGTWQAKAGEVRQAVAHALKAGYRHIDGALCYQNEEEVGLGIKDS-----GIPRSEIFLTSKVWSSYH- 82
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELlkeepGVKREDLFITSKLWNNSHr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 83 -DRVEECLDTTLKSLQTDYLDLYLIHWPVRLVP-NGTHPLFPTKPDGS-RNLDWDWDQAKTWAQMEDVLKKGKVKAIGLS 159
Cdd:cd19118 81 pEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPtGDLNPLTAVPTNGGeVDLDLSVSLVDTWKAMVELKKTGKVKSIGVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 160 NAGIPIIEHIIKTGKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGSTSS---PLHEDPDLVAVAKKHNVPTAT 236
Cdd:cd19118 161 NFSIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGNNLAglpLLVQHPEVKAIAAKLGKTPAQ 240
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2781183762 237 VLISYQVNRGVVVLPKSVTPARIESNLKTIKLDEEDMNRLDKL 279
Cdd:cd19118 241 VLIAWGIQRGHSVIPKSVTPSRIRSNFEQVELSDDEFNAVTAL 283
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
6-288 |
3.74e-107 |
|
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: 314.44 E-value: 3.74e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 6 SFKLNTGATIPAVGLGTW--QAKAGEVRQAVAHALKAGYRHIDGALCYQNEEEVGLGIK----DSGIPRSEIFLTSKVWS 79
Cdd:cd19119 3 SFKLNTGASIPALGLGTAspHEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKraidDGSIKREELFITTKVWP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 80 SYHDRVEECLDTTLKSLQTDYLDLYLIHWPVRLV----PNGThPLFPTKPDGSRNLDWDWDQAKTWAQMEDVLKKGKVKA 155
Cdd:cd19119 83 TFYDEVERSLDESLKALGLDYVDLLLVHWPVCFEkdsdDSGK-PFTPVNDDGKTRYAASGDHITTYKQLEKIYLDGRAKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 156 IGLSNAGIPIIEHIIKTGKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGSTSSPLHEDPDLVAVAKKHNVPTA 235
Cdd:cd19119 162 IGVSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAPNLKNPLVKKIAEKYNVSTG 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2781183762 236 TVLISYQVNRGVVVLPKSVTPARIESNLKTIKLDEEDMNRLDKLAESgKQTRF 288
Cdd:cd19119 242 DILISYHVRQGVIVLPKSLKPVRIVSNGKIVSLTKEDLQKLDDIGEK-YPVRF 293
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
9-291 |
4.73e-105 |
|
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: 309.32 E-value: 4.73e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 9 LNTGATIPAVGLGTWQAKAGEVRQAVAHALKAGYRHIDGALCYQNEEEVGLGIK-----DSGIPRSEIFLTSKVWSSYH- 82
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKekvgpGKAVPREDLFVTSKLWNTKHh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 83 -DRVEECLDTTLKSLQTDYLDLYLIHWPVRLVPNGThpLFPTKPDGSRNLDwDWDQAKTWAQMEDVLKKGKVKAIGLSNA 161
Cdd:cd19106 81 pEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGDN--PFPKNPDGTIRYD-STHYKETWKAMEKLVDKGLVKAIGLSNF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 162 GIPIIEHIIKTGKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGSTSSP--------LHEDPDLVAVAKKHNVP 233
Cdd:cd19106 158 NSRQIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPDRPwakpdepvLLEEPKVKALAKKYNKS 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 234 TATVLISYQVNRGVVVLPKSVTPARIESNLKT--IKLDEEDMNRLDKLaesGKQTRFTTP 291
Cdd:cd19106 238 PAQILLRWQVQRGVVVIPKSVTPSRIKQNIQVfdFTLSPEEMKQLDAL---NRNWRYIVP 294
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
5-279 |
1.93e-102 |
|
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: 301.96 E-value: 1.93e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 5 TSFKLNTGATIPAVGLGTWQAKAGEVRQAVAHALKAGYRHIDGALCYQNEEEVGLGIK---DSGIP-RSEIFLTSKVWSS 80
Cdd:cd19125 1 RFFKLNTGAKIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKklfEDGVVkREDLFITSKLWCT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 81 YHD--RVEECLDTTLKSLQTDYLDLYLIHWPVRLvPNGTHplfptKPDGSRNLDWDWdqAKTWAQMEDVLKKGKVKAIGL 158
Cdd:cd19125 81 DHApeDVPPALEKTLKDLQLDYLDLYLIHWPVRL-KKGAH-----MPEPEEVLPPDI--PSTWKAMEKLVDSGKVRAIGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 159 SNAGIPIIEHIIKTGKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGSTSSP-----LHEDPDLVAVAKKHNVP 233
Cdd:cd19125 153 SNFSVKKLEDLLAVARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGTTwvkknVLKDPIVTKVAEKLGKT 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2781183762 234 TATVLISYQVNRGVVVLPKSVTPARIESNLKT--IKLDEEDMNRLDKL 279
Cdd:cd19125 233 PAQVALRWGLQRGTSVLPKSTNEERIKENIDVfdWSIPEEDFAKFSSI 280
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
6-279 |
1.59e-101 |
|
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: 300.10 E-value: 1.59e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 6 SFKLNTGATIPAVGLGTWQAKAGEVRQAVAHALKAGYRHIDGALCYQNEEEVGLGI----KDSGIPRSEIFLTSKVWSSY 81
Cdd:cd19123 3 TLPLSNGDLIPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALaevfKEGKVKREDLWITSKLWNNS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 82 H--DRVEECLDTTLKSLQTDYLDLYLIHWPVRLVPNgthPLFPTKPDGSRNLDwDWDQAKTWAQMEDVLKKGKVKAIGLS 159
Cdd:cd19123 83 HapEDVLPALEKTLADLQLDYLDLYLMHWPVALKKG---VGFPESGEDLLSLS-PIPLEDTWRAMEELVDKGLCRHIGVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 160 NAGIPIIEHIIKTGKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGSTSSP----------LHEDPDLVAVAKK 229
Cdd:cd19123 159 NFSVKKLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDRPaamkaegepvLLEDPVINKIAEK 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2781183762 230 HNVPTATVLISYQVNRGVVVLPKSVTPARIESNL--KTIKLDEEDMNRLDKL 279
Cdd:cd19123 239 HGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLeaAEVELDASDMATIAAL 290
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
5-279 |
2.42e-93 |
|
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: 279.17 E-value: 2.42e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 5 TSFKLNTGATIPAVGLGTWQAK-AGEVRQAVAHALKAGYRHIDGALCYQNEEEVGLG----IKDSGIPRSEIFLTSKVWS 79
Cdd:cd19116 1 PTIKLNDGNEIPAIALGTWKLKdDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAirekIAEGVVKREDLFITTKLWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 80 SYHDR--VEECLDTTLKSLQTDYLDLYLIHWPVRLVPNGthplfptKPDGSRNLDW-DWDQAKTWAQMEDVLKKGKVKAI 156
Cdd:cd19116 81 SYHEReqVEPALRESLKRLGLDYVDLYLIHWPVAFKENN-------DSESNGDGSLsDIDYLETWRGMEDLVKLGLTRSI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 157 GLSNAGIPIIEHIIKTGKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGSTSSPLHE-------DPDLVAVAKK 229
Cdd:cd19116 154 GVSNFNSEQINRLLSNCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLVPRGQTnppprldDPTLVAIAKK 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2781183762 230 HNVPTATVLISYQVNRGVVVLPKSVTPARIESNLKTI--KLDEEDMNRLDKL 279
Cdd:cd19116 234 YGKTTAQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFdfQLTPEEVAALNSF 285
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
15-279 |
7.40e-93 |
|
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: 276.82 E-value: 7.40e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 15 IPAVGLGTWQAKAGE-VRQAVAHALKAGYRHIDGALCYQNEEEVGLGIKDS----GIPRSEIFLTSKVWSSYH--DRVEE 87
Cdd:cd19136 1 MPILGLGTFRLRGEEeVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLlpkyGLSREDIFITSKLAPKDQgyEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 88 CLDTTLKSLQTDYLDLYLIHWPvrlvpnGTHPLFPTKPDGSRNldwdwdQAKTWAQMEDVLKKGKVKAIGLSNAGIPIIE 167
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWP------GVQGLKPSDPRNAEL------RRESWRALEDLYKEGKLRAIGVSNYTVRHLE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 168 HIIKTGKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGSTSSPLHEDPDLVAVAKKHNVPTATVLISYQVNRGV 247
Cdd:cd19136 149 ELLKYCEVPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGDLRLLEDPTVLAIAKKYGRTPAQVLLRWALQQGI 228
|
250 260 270
....*....|....*....|....*....|....
gi 2781183762 248 VVLPKSVTPARIESNLKTIK--LDEEDMNRLDKL 279
Cdd:cd19136 229 GVIPKSTNPERIAENIKVFDfeLSEEDMAELNAL 262
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
5-287 |
1.04e-91 |
|
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: 275.44 E-value: 1.04e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 5 TSFKLNTGATIPAVGLGTWQAKAGEVRQAVAHALKAGYRHIDGALCYQNEEEVGLGIKD---SGI-PRSEIFLTSKVWSS 80
Cdd:cd19154 2 ASITLSNGVKMPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAElleEGVvKREDLFITTKLWTH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 81 YH--DRVEECLDTTLKSLQTDYLDLYLIHWPvrlvpngthplFPTKPD-GSRNLDW-------DWDQAKTWAQMEDVLKK 150
Cdd:cd19154 82 EHapEDVEEALRESLKKLQLEYVDLYLIHAP-----------AAFKDDeGESGTMEngmsihdAVDVEDVWRGMEKVYDE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 151 GKVKAIGLSNAGIPIIEHIIKTGKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGSTSSPLH------------ 218
Cdd:cd19154 151 GLTKAIGVSNFNNDQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSPGRANFtkstgvspapnl 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2781183762 219 -EDPDLVAVAKKHNVPTATVLISYQVNRGVVVLPKSVTPARIESNLKT--IKLDEEDMNRLDKLaESGKQTR 287
Cdd:cd19154 231 lQDPIVKAIAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIfdFSLSEEDMATLEEI-EKSLRLF 301
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
12-276 |
1.85e-89 |
|
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: 269.67 E-value: 1.85e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 12 GATIPAVGLGTWQAKAGEVRQAVAHALKAGYRHIDGALCYQNEEEVGLGI----KDSGIPRSEIFLTSKVWSSYHDR--V 85
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIqekiKEQVVKREDLFIVSKLWCTFHEKglV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 86 EECLDTTLKSLQTDYLDLYLIHWPVRLVPNgtHPLFPTKPDGsRNLDWDWDQAKTWAQMEDVLKKGKVKAIGLSNAGIPI 165
Cdd:cd19107 81 KGACQKTLSDLKLDYLDLYLIHWPTGFKPG--KELFPLDESG-NVIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 166 IEHII-KTG-KVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGSTSSP--------LHEDPDLVAVAKKHNVPTA 235
Cdd:cd19107 158 IERILnKPGlKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPwakpedpsLLEDPKIKEIAAKHNKTTA 237
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2781183762 236 TVLISYQVNRGVVVLPKSVTPARIESNLKT--IKLDEEDMNRL 276
Cdd:cd19107 238 QVLIRFPIQRNLVVIPKSVTPERIAENFKVfdFELSSEDMATI 280
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
15-277 |
6.78e-87 |
|
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: 260.67 E-value: 6.78e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 15 IPAVGLGTWQAKAGEVRQAVAHALKAGYRHIDGALCYQNEEEVGLGIKDSGIPRSEIFLTSKVWSSY--HDRVEECLDTT 92
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAESGVPREDLFITTKVWRDHlrPEDLKKSVDRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 93 LKSLQTDYLDLYLIHWPVRLVPngthplfptkpdgsrnldwdwdQAKTWAQMEDVLKKGKVKAIGLSNAGIPIIEHIIKT 172
Cdd:cd19073 81 LEKLGTDYVDLLLIHWPNPTVP----------------------LEETLGALKELKEAGKVKSIGVSNFTIELLEEALDI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 173 GKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGSTSspLHEDPDLVAVAKKHNVPTATVLISYQVNRGVVVLPK 252
Cdd:cd19073 139 SPLPIAVNQVEFHPFLYQAELLEYCRENDIVITAYSPLARGE--VLRDPVIQEIAEKYDKTPAQVALRWLVQKGIVVIPK 216
|
250 260
....*....|....*....|....*..
gi 2781183762 253 SVTPARIESNLKT--IKLDEEDMNRLD 277
Cdd:cd19073 217 ASSEDHLKENLAIfdWELTSEDVAKID 243
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
8-279 |
1.86e-86 |
|
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: 260.20 E-value: 1.86e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 8 KLNTGATIPAVGLGTWQAK-AGEVRQAVAHALKAGYRHIDGALCYQNEEEVGLGIKDSGIPRSEIFLTSKVW--SSYHDR 84
Cdd:cd19133 2 TLNNGVEMPILGFGVFQIPdPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKSGIPREELFITTKLWiqDAGYEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 85 VEECLDTTLKSLQTDYLDLYLIHWPVRlvpngthplfptkpdgsrnldwdwDQAKTWAQMEDVLKKGKVKAIGLSNAGIP 164
Cdd:cd19133 82 AKKAFERSLKRLGLDYLDLYLIHQPFG------------------------DVYGAWRAMEELYKEGKIRAIGVSNFYPD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 165 IIEHIIKTGKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGSTSSPLHEDPDLVAVAKKHNVPTATVLISYQVN 244
Cdd:cd19133 138 RLVDLILHNEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAEGRNNLFENPVLTEIAEKYGKSVAQVILRWLIQ 217
|
250 260 270
....*....|....*....|....*....|....*..
gi 2781183762 245 RGVVVLPKSVTPARIESNLKT--IKLDEEDMNRLDKL 279
Cdd:cd19133 218 RGIVVIPKSVRPERIAENFDIfdFELSDEDMEAIAAL 254
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
6-282 |
6.65e-86 |
|
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 259.25 E-value: 6.65e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 6 SFKLNTGATIPAVGLGTWQAKAG-EVRQAVAHALKAGYRHIDGALCYQNEEEVGLGIKDSGIPRSEIFLTSKVWSSYH-- 82
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEEGsEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKESGIPREELFITSKVWNADQgy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 83 DRVEECLDTTLKSLQTDYLDLYLIHWPVrlvpngthplfptkpdGSRNLDwdwdqakTWAQMEDVLKKGKVKAIGLSNAG 162
Cdd:cd19157 81 DSTLKAFEASLERLGLDYLDLYLIHWPV----------------KGKYKE-------TWKALEKLYKDGRVRAIGVSNFQ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 163 IPIIEHIIKTGKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLgsTSSPLHEDPDLVAVAKKHNVPTATVLISYQ 242
Cdd:cd19157 138 VHHLEDLLADAEIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPL--MQGQLLDNPVLKEIAEKYNKSVAQVILRWD 215
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2781183762 243 VNRGVVVLPKSVTPARIESNLKT--IKLDEEDMNRLDKLAES 282
Cdd:cd19157 216 LQNGVVTIPKSIKEHRIIENADVfdFELSQEDMDKIDALNEN 257
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
8-279 |
8.50e-85 |
|
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: 255.76 E-value: 8.50e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 8 KLNTGATIPAVGLGTWQAKAGEVRQAVAHALKAGYRHIDGALCYQNEEEVGLGIKDSGIPRSEIFLTSKVWSSYH--DRV 85
Cdd:cd19131 3 TLNDGNTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRASGVPREELFITTKLWNSDQgyDST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 86 EECLDTTLKSLQTDYLDLYLIHWPVrlvpngthplfptkPDGSRNLDwdwdqakTWAQMEDVLKKGKVKAIGLSNAGIPI 165
Cdd:cd19131 83 LRAFDESLRKLGLDYVDLYLIHWPV--------------PAQDKYVE-------TWKALIELKKEGRVKSIGVSNFTIEH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 166 IEHIIKTGKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGSTSspLHEDPDLVAVAKKHNVPTATVLISYQVNR 245
Cdd:cd19131 142 LQRLIDETGVVPVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGG--LLSDPVIGEIAEKHGKTPAQVVIRWHLQN 219
|
250 260 270
....*....|....*....|....*....|....*.
gi 2781183762 246 GVVVLPKSVTPARIESNLKT--IKLDEEDMNRLDKL 279
Cdd:cd19131 220 GLVVIPKSVTPSRIAENFDVfdFELDADDMQAIAGL 255
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
8-279 |
2.63e-84 |
|
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: 254.67 E-value: 2.63e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 8 KLNTGATIPAVGLGTWQAKAG-EVRQAVAHALKAGYRHIDGALCYQNEEEVGLGIKDSGIPRSEIFLTSKVWSS--YHDR 84
Cdd:cd19126 2 TLNNGTRMPWLGLGVFQTPDGdETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRESGVPREELFVTTKLWNDdqRARR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 85 VEECLDTTLKSLQTDYLDLYLIHWPVrlvpngthplfptkPDGSrnldwdwdqAKTWAQMEDVLKKGKVKAIGLSNAGIP 164
Cdd:cd19126 82 TEDAFQESLDRLGLDYVDLYLIHWPG--------------KDKF---------IDTWKALEKLYASGKVKAIGVSNFQEH 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 165 IIEHIIKTGKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGSTSspLHEDPDLVAVAKKHNVPTATVLISYQVN 244
Cdd:cd19126 139 HLEELLAHADVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQGG--LLSNPVLAAIGEKYGKSAAQVVLRWDIQ 216
|
250 260 270
....*....|....*....|....*....|....*..
gi 2781183762 245 RGVVVLPKSVTPARIESNLKT--IKLDEEDMNRLDKL 279
Cdd:cd19126 217 HGVVTIPKSVHASRIKENADIfdFELSEDDMTAIDAL 253
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
12-288 |
1.31e-83 |
|
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: 253.96 E-value: 1.31e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 12 GATIPAVGLGTWQAKAGEVRQAVAHALKAGYRHIDGALCYQNEEEVGLGIK---DSG-IPRSEIFLTSKVWSSYH--DRV 85
Cdd:cd19111 1 GFPMPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKwwlKNGkLKREEVFITTKLPPVYLefKDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 86 EECLDTTLKSLQTDYLDLYLIHWPVRlvpngthplFPTKPDGSRNLDWDWDQAKTWAQMEDVLKKGKVKAIGLSNAGIPI 165
Cdd:cd19111 81 EKSLEKSLENLKLPYVDLYLIHHPCG---------FVNKKDKGERELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 166 IEHIIKTGKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGSTSSP----------LHEDPDLVAVAKKHNVPTA 235
Cdd:cd19111 152 INKILAYAKVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSPGRAnqslwpdqpdLLEDPTVLAIAKELDKTPA 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2781183762 236 TVLISYQVNRGVVVLPKSVTPARIESNLKTI--KLDEEDMNRLDKLAESGKQTRF 288
Cdd:cd19111 232 QVLLRFVLQRGTGVLPKSTNKERIEENFEVFdfELTEEHFKKLKTLDRNMKYFDF 286
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
8-279 |
2.39e-81 |
|
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: 248.68 E-value: 2.39e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 8 KLNTGATIPAVGLGTWQAKA---GEVRQAVAHALKAGYRHIDGALCYQNEEEVGLGI----KDSGIPRSEIFLTSKVWSS 80
Cdd:cd19108 4 KLNDGHFIPVLGFGTYAPEEvpkSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIrskiADGTVKREDIFYTSKLWCT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 81 YH--DRVEECLDTTLKSLQTDYLDLYLIHWPVRLVPNGThpLFPTKPDGSRNLDwDWDQAKTWAQMEDVLKKGKVKAIGL 158
Cdd:cd19108 84 FHrpELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEE--LFPKDENGKLIFD-TVDLCATWEAMEKCKDAGLAKSIGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 159 SNAGIPIIEHII-KTG-KVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGST--------SSP-LHEDPDLVAVA 227
Cdd:cd19108 161 SNFNRRQLEMILnKPGlKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQrdkewvdqNSPvLLEDPVLCALA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2781183762 228 KKHNVPTATVLISYQVNRGVVVLPKSVTPARIESNLKTI--KLDEEDMNRLDKL 279
Cdd:cd19108 241 KKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFefQLTSEDMKALDGL 294
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
12-288 |
1.21e-80 |
|
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: 245.60 E-value: 1.21e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 12 GATIPAVGLGT---WQAKAGEVRQ-----AVAHALKAGYRHIDGALCYQNEEEVGLGIKDSGIPRSEIFLTSKVWSSyHD 83
Cdd:cd19120 1 GSKIPAIAFGTgtaWYKSGDDDIQrdlvdSVKLALKAGFRHIDTAEMYGNEKEVGEALKESGVPREDLFITTKVSPG-IK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 84 RVEECLDTTLKSLQTDYLDLYLIHWPvRLVPNGTHPLfptkpdgsrnldwdwdqAKTWAQMEDVLKKGKVKAIGLSNAGI 163
Cdd:cd19120 80 DPREALRKSLAKLGVDYVDLYLIHSP-FFAKEGGPTL-----------------AEAWAELEALKDAGLVRSIGVSNFRI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 164 PIIEHIIKTGKVTPAALQVELHPYC--PQHALLKYCKEKGIILEAYSPLGST--SSPLHEDPDLVAVAKKHNVPTATVLI 239
Cdd:cd19120 142 EDLEELLDTAKIKPAVNQIEFHPYLypQQPALLEYCREHGIVVSAYSPLSPLtrDAGGPLDPVLEKIAEKYGVTPAQVLL 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2781183762 240 SYQVNRGVVVLPKSVTPARIESNLKT--IKLDEEDMNRLDKLaesGKQTRF 288
Cdd:cd19120 222 RWALQKGIVVVTTSSKEERMKEYLEAfdFELTEEEVEEIDKA---GKQKHF 269
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
9-280 |
2.95e-79 |
|
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: 241.79 E-value: 2.95e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 9 LNTGATIPAVGLGTWQAKAGEVRQAVAHALKAGYRHIDGALCYQNEEEVGLGIKDSGIPRSEIFLTSKVWSSYHDRVE-- 86
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRRSGVPREELFVTTKLPGRHHGYEEal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 87 ECLDTTLKSLQTDYLDLYLIHWPVrlvpngthplfptkPdgSRNLdwdwdQAKTWAQMEDVLKKGKVKAIGLSNAGIPII 166
Cdd:cd19132 81 RTIEESLYRLGLDYVDLYLIHWPN--------------P--SRDL-----YVEAWQALIEAREEGLVRSIGVSNFLPEHL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 167 EHIIKTGKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGSTSSPLhEDPDLVAVAKKHNVPTATVLISYQVNRG 246
Cdd:cd19132 140 DRLIDETGVTPAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLGRGSGLL-DEPVIKAIAEKHGKTPAQVVLRWHVQLG 218
|
250 260 270
....*....|....*....|....*....|....*.
gi 2781183762 247 VVVLPKSVTPARIESNLKT--IKLDEEDMNRLDKLA 280
Cdd:cd19132 219 VVPIPKSANPERQRENLAIfdFELSDEDMAAIAALD 254
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
7-281 |
6.04e-78 |
|
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: 239.83 E-value: 6.04e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 7 FKLNTGATIPAVGLGTW--QAKAGEVRQAVAHALKAGYRHIDGALCYQNEEEVGLGIKD-----SGIPRSEIFLTSKVWS 79
Cdd:cd19122 1 FTLNNGVKIPAVGFGTFanEGAKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDflkenPSVKREDLFICTKVWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 80 SYHdRVEECL---DTTLKSLQTDYLDLYLIHWPVRLVPNGTHPLfPTKPDGSR--NLDWDWDQAKTWAQMEDVLKKGKVK 154
Cdd:cd19122 81 HLH-EPEDVKwsiDNSLKNLKLDYIDLFLVHWPIAAEKNDQRSP-KLGPDGKYviLKDLTENPEPTWRAMEEIYESGKAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 155 AIGLSNAGIPIIEHIIKTGKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGS------TSSPLHEDPDLVAVAK 228
Cdd:cd19122 159 AIGVSNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSqnqvpsTGERVSENPTLNEVAE 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2781183762 229 KHNVPTATVLISYQVNRGVVVLPKSVTPARIESNLKTIKLDEEDMNRLDKLAE 281
Cdd:cd19122 239 KGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIELSDEDFEAINQVAK 291
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
9-279 |
5.91e-76 |
|
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381361 [Multi-domain] Cd Length: 265 Bit Score: 233.76 E-value: 5.91e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 9 LNTGATIPAVGLGTWQAkAGEVRQAVAHALK-AGYRHIDGALCYQNEEEVGLGIKDSGIPRSEIFLTSKVWSS--YHDRV 85
Cdd:cd19135 7 LSNGVEMPILGLGTSHS-GGYSHEAVVYALKeCGYRHIDTAKRYGCEELLGKAIKESGVPREDLFLTTKLWPSdyGYEST 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 86 EECLDTTLKSLQTDYLDLYLIHWPvrLVPNGTHPLFPTKpdgsrnldwdwdqAKTWAQMEDVLKKGKVKAIGLSNAGIPI 165
Cdd:cd19135 86 KQAFEASLKRLGVDYLDLYLLHWP--DCPSSGKNVKETR-------------AETWRALEELYDEGLCRAIGVSNFLIEH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 166 IEHIIKTGKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGstSSPLHEDPDLVAVAKKHNVPTATVLISYQVNR 245
Cdd:cd19135 151 LEQLLEDCSVVPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLA--KGKALEEPTVTELAKKYQKTPAQILIRWSIQN 228
|
250 260 270
....*....|....*....|....*....|....*.
gi 2781183762 246 GVVVLPKSVTPARIESNLKT--IKLDEEDMNRLDKL 279
Cdd:cd19135 229 GVVTIPKSTKEERIKENCQVfdFSLSEEDMATLDSL 264
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
12-279 |
1.42e-74 |
|
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: 229.84 E-value: 1.42e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 12 GATIPAVGLGTWQAKAGEVRQAVAHALKAGYRHIDGALCYQNEEEVGLGIKDSGIPRSEIFLTSKVWSS--YHDRVEECL 89
Cdd:cd19140 5 GVRIPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIAASGVPRDELFLTTKVWPDnySPDDFLASV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 90 DTTLKSLQTDYLDLYLIHWPVRLVPNgthplfptkpdgsrnldwdwdqAKTWAQMEDVLKKGKVKAIGLSNAGIPIIEHI 169
Cdd:cd19140 85 EESLRKLRTDYVDLLLLHWPNKDVPL----------------------AETLGALNEAQEAGLARHIGVSNFTVALLREA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 170 IKTGKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGSTSSPlhEDPDLVAVAKKHNVPTATVLISYQVNR-GVV 248
Cdd:cd19140 143 VELSEAPLFTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLARGEVL--KDPVLQEIGRKHGKTPAQVALRWLLQQeGVA 220
|
250 260 270
....*....|....*....|....*....|...
gi 2781183762 249 VLPKSVTPARIESNLKTI--KLDEEDMNRLDKL 279
Cdd:cd19140 221 AIPKATNPERLEENLDIFdfTLSDEEMARIAAL 253
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
8-279 |
2.25e-74 |
|
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: 229.71 E-value: 2.25e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 8 KLNTGATIPAVGLGTWQAKAG-EVRQAVAHALKAGYRHIDGALCYQNEEEVGLGIKDSGIPRSEIFLTSKVWSSY--HDR 84
Cdd:cd19156 2 KLANGVEMPRLGLGVWRVQDGaEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRESGVPREEVFVTTKLWNSDqgYES 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 85 VEECLDTTLKSLQTDYLDLYLIHWPVrlvpngthplfptkpdGSRNLDwdwdqakTWAQMEDVLKKGKVKAIGLSNAGIP 164
Cdd:cd19156 82 TLAAFEESLEKLGLDYVDLYLIHWPV----------------KGKFKD-------TWKAFEKLYKEKKVRAIGVSNFHEH 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 165 IIEHIIKTGKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGstSSPLHEDPDLVAVAKKHNVPTATVLISYQVN 244
Cdd:cd19156 139 HLEELLKSCKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLG--QGKLLSNPVLKAIGKKYGKSAAQVIIRWDIQ 216
|
250 260 270
....*....|....*....|....*....|....*..
gi 2781183762 245 RGVVVLPKSVTPARIESNLKT--IKLDEEDMNRLDKL 279
Cdd:cd19156 217 HGIITIPKSVHEERIQENFDVfdFELTAEEIRQIDGL 253
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
15-299 |
1.51e-73 |
|
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: 228.69 E-value: 1.51e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 15 IPAVGLGTWQAKAGEVRQAVAHALKAGYRHIDGALCYQNEEEVGLG----IKDSGIPRSEIFLTSKVWSSYHDR--VEEC 88
Cdd:cd19110 4 IPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGirekIKEGVVRREDLFIVSKLWCTCHKKslVKTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 89 LDTTLKSLQTDYLDLYLIHWPVRLVPNgtHPLFPTKPDGsRNLDWDWDQAKTWAQMEDVLKKGKVKAIGLSNAGIPIIEH 168
Cdd:cd19110 84 CTRSLKALKLNYLDLYLIHWPMGFKPG--EPDLPLDRSG-MVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 169 II-KTG-KVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGSTSS--PLHEDPDLVAVAKKHNVPTATVLISYQVN 244
Cdd:cd19110 161 LLnKPGlRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSCEgvDLIDDPVIQRIAKKHGKSPAQILIRFQIQ 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2781183762 245 RGVVVLPKSVTPARIESNLKT--IKLDEEDMNRLDKLAESGKQTRFTTPPWGSDFGF 299
Cdd:cd19110 241 RNVIVIPKSVTPSRIKENIQVfdFELTEHDMDNLLSLDRNLRLATFPITENHKDYPF 297
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
9-288 |
1.56e-73 |
|
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: 228.95 E-value: 1.56e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 9 LNTGATIPAVGLGTWQAKAGEVRQAVAHALKAGYRHIDGALCYQNEEEVGLGIK---DSG-IPRSEIFLTSKV--WSSYH 82
Cdd:cd19155 6 FNNGEKMPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKkwiDSGkVKREELFIVTKLppGGNRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 83 DRVEECLDTTLKSLQTDYLDLYLIHWPVRLVPNGTHPLFpTKPDGSRNLDWDWDQAKTWAQMEDVLKKGKVKAIGLSNAG 162
Cdd:cd19155 86 EKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLSKEDDSGK-LDPTGEHKQDYTTDLLDIWKAMEAQVDQGLTRSIGLSNFN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 163 IPIIEHIIKTGKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGS---------TSSP------LHEDPDLVAVA 227
Cdd:cd19155 165 REQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSpgaahfspgTGSPsgsspdLLQDPVVKAIA 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2781183762 228 KKHNVPTATVLISYQVNRGVVVLPKSVTPARIESNLKT--IKLDEEDMNRLDKLAESGKQTRF 288
Cdd:cd19155 245 ERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVfdFELTEADMAKLSSLDKNIRGRTF 307
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
6-296 |
3.10e-73 |
|
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: 228.14 E-value: 3.10e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 6 SFKLNTGATIPAVGLGTWQAKAGEVRQAVAHALKAGYRHIDGALCYQNEEEVGLGIK---DSG-IPRSEIFLTSKVWSSY 81
Cdd:cd19112 2 TITLNSGHKMPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAeafKTGlVKREDLFITTKLWNSD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 82 HDRVEECLDTTLKSLQTDYLDLYLIHWPVRLVPNGT-HPLFPTKPDGSRNLDWDWDQAKTWAQMEDVLKKGKVKAIGLSN 160
Cdd:cd19112 82 HGHVIEACKDSLKKLQLDYLDLYLVHFPVATKHTGVgTTGSALGEDGVLDIDVTISLETTWHAMEKLVSAGLVRSIGISN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 161 AGIPIIEHIIKTGKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLG---------STSSPLhEDPDLVAVAKKHN 231
Cdd:cd19112 162 YDIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGgaaanaewfGSVSPL-DDPVLKDLAKKYG 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2781183762 232 VPTATVLISYQVNRGVVVLPKSVTPARIESNLKTI--KLDEEDMNRLDKLaesGKQTRFTTPP--WGSD 296
Cdd:cd19112 241 KSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFdfQLSKEDMKLIKSL---DRKYRTNQPAkfWGID 306
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
8-279 |
8.68e-73 |
|
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: 225.75 E-value: 8.68e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 8 KLNTGATIPAVGLGTWQAKAGEVRQAVAHALKAGYRHIDGALCYQNEEEVGLGIKDSGIPRSEIFLTSKVW-SSY-HDRV 85
Cdd:cd19127 2 TLNNGVEMPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRSGVDRSDIFVTTKLWiSDYgYDKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 86 EECLDTTLKSLQTDYLDLYLIHWPvrlVPNgthplfptkpdgsrnlDWDwDQAKTWAQMEDVLKKGKVKAIGLSNAGIPI 165
Cdd:cd19127 82 LRGFDASLRRLGLDYVDLYLLHWP---VPN----------------DFD-RTIQAYKALEKLLAEGRVRAIGVSNFTPEH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 166 IEHIIKTGKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGST-----------SSPLhEDPDLVAVAKKHNVPT 234
Cdd:cd19127 142 LERLIDATTVVPAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGGVmrygasgptgpGDVL-QDPTITGLAEKYGKTP 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2781183762 235 ATVLISYQVNRGVVVLPKSVTPARIESNLKTI--KLDEEDMNRLDKL 279
Cdd:cd19127 221 AQIVLRWHLQNGVSAIPKSVHPERIAENIDIFdfALSAEDMAAIDAL 267
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
12-291 |
2.14e-71 |
|
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: 223.20 E-value: 2.14e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 12 GATIPAVGLGTWQAKAGEVRQAVAHALKAGYRHIDGALCYQNEEEVGLGIK---DSGI-PRSEIFLTSKVWSSYH--DRV 85
Cdd:cd19114 1 GDKMPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRkaiQEGLvKREDLFIVTKLWNNFHgkDHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 86 EECLDTTLKSLQTDYLDLYLIHWPVRLVPNGTHPLFPTKPDGSRNLDWDWDQA---KTWAQMEDVLKKGKVKAIGLSNAG 162
Cdd:cd19114 81 REAFDRQLKDYGLDYIDLYLIHFPIPAAYVDPAENYPFLWKDKELKKFPLEQSpmqECWREMEKLVDAGLVRNIGIANFN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 163 IPIIEHIIKTGKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGSTS-----------SPLHEDPDLVAVAKKHN 231
Cdd:cd19114 161 VQLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAVytkvtkhlkhfTNLLEHPVVKKLADKHK 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2781183762 232 VPTATVLISYQVNRGVVVLPKSVTPARIESNLK--TIKLDEEDMNRLDKLAESgkqTRFTTP 291
Cdd:cd19114 241 RDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDitSYKLDEEDMEALYELEAN---ARFNDP 299
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
1-304 |
2.49e-71 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 222.26 E-value: 2.49e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 1 MSAPTSFKLNTGATIPAVGLGTWQAKAGEVRQAVAHALKAGYRHIDGALCYQNEEEVGLGIKDSGIPRSEIFLTSKVWSS 80
Cdd:PRK11565 1 MANPTVIKLQDGNVMPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKEASVAREELFITTKLWND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 81 YHDRVEECLDTTLKSLQTDYLDLYLIHWPVrlvpngthplfptkPDGSRNLDwdwdqakTWAQMEDVLKKGKVKAIGLSN 160
Cdd:PRK11565 81 DHKRPREALEESLKKLQLDYVDLYLMHWPV--------------PAIDHYVE-------AWKGMIELQKEGLIKSIGVCN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 161 AGIPIIEHIIKTGKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGSTSSPLHEDPDLVAVAKKHNVPTATVLIS 240
Cdd:PRK11565 140 FQIHHLQRLIDETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGKGVFDQKVIRDLADKYGKTPAQIVIR 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2781183762 241 YQVNRGVVVLPKSVTPARIESNLKT--IKLDEEDMNRLDKLaESGKQTrfttppwGSDfgfPDWFG 304
Cdd:PRK11565 220 WHLDSGLVVIPKSVTPSRIAENFDVfdFRLDKDELGEIAKL-DQGKRL-------GPD---PDQFG 274
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
2-292 |
3.67e-71 |
|
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: 223.07 E-value: 3.67e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 2 SAPTSfKLNTGATIPAVGLGTWQAKAGEVRQAVAHALKAGYRHIDGALCYQNEEEVGLG----IKDSGIPRSEIFLTSKV 77
Cdd:cd19115 1 ASPTV-KLNSGYDMPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGvaraIKEGIVKREDLFIVSKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 78 WSSYHD--RVEECLDTTLKSLQTDYLDLYLIHWPVRLV---PNGTHPlfPTKPDGSRNLDWDWDQ-AKTWAQMEDVLKKG 151
Cdd:cd19115 80 WNTFHDgeRVEPICRKQLADWGIDYFDLFLIHFPIALKyvdPAVRYP--PGWFYDGKKVEFSNAPiQETWTAMEKLVDKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 152 KVKAIGLSNAGIPIIEHIIKTGKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGSTS------------SPLHE 219
Cdd:cd19115 158 LARSIGVSNFSAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGPQSfleldlpgakdtPPLFE 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2781183762 220 DPDLVAVAKKHNVPTATVLISYQVNRGVVVLPKSVTPARIESNLKTI--KLDEEDMNRLDKLaesGKQTRFTTPP 292
Cdd:cd19115 238 HDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTgfDLEAEEIKAISAL---DIGLRFNNPL 309
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
16-279 |
7.90e-71 |
|
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: 221.24 E-value: 7.90e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 16 PAVGLGTWQAKAGEVRQAVAHALKAGYRHIDGALCYQNEEEVGLGI----KDSGIPRSEIFLTSKVWSSYH--DRVEECL 89
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFseifKDGGVKREDLFITSKLWPTMHqpENVKEQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 90 DTTLKSLQTDYLDLYLIHWPVRLVPNGTHPLFPtkpDGSRNLDWDWDQAKTWAQMEDVLKKGKVKAIGLSNAGIPIIEHI 169
Cdd:cd19128 82 LITLQDLQLEYLDLFLIHWPLAFDMDTDGDPRD---DNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 170 IKTGKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGST----SSPLHEDPDLVAVAKKHNVPTATVLISYQVNR 245
Cdd:cd19128 159 LNYCKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGSygdgNLTFLNDSELKALATKYNTTPPQVIIAWHLQK 238
|
250 260 270
....*....|....*....|....*....|....*....
gi 2781183762 246 ---GVVVLPKSVTPARIESNLK--TIKLDEEDMNRLDKL 279
Cdd:cd19128 239 wpkNYSVIPKSANKSRCQQNFDinDLALTKEDMDAINTL 277
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
10-290 |
8.44e-71 |
|
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: 221.56 E-value: 8.44e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 10 NTGATIPAVGLGTWQAKAGEVRQAVAHALKAGYRHIDGALCYQNEEEVGLGIKD----SGIPRSEIFLTSKVWSSYH--D 83
Cdd:cd19129 1 NGSGAIPALGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEvfkaGKIRREDLFVTTKLWNTNHrpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 84 RVEECLDTTLKSLQTDYLDLYLIHWPVRLVPNGTHPlfPTKPDGSRNLDWDWDQAKTWAQMEDVLKKGKVKAIGLSNAGI 163
Cdd:cd19129 81 RVKPAFEASLKRLQLDYLDLYLIHTPFAFQPGDEQD--PRDANGNVIYDDGVTLLDTWRAMERLVDEGRCKAIGLSDVSL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 164 PIIEHIIKTGKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGSTSSP-LHEDPDLVAVAKKHNVPTATVLISYQ 242
Cdd:cd19129 159 EKLREIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGMEPkLLEDPVITAIARRVNKTPAQVLLAWA 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2781183762 243 VNRGVVVLPKSVTPARIESNLKTIKLDEEDMNRLDKLAESgkQTRFTT 290
Cdd:cd19129 239 IQRGTALLTTSKTPSRIRENFDISTLPEDAMREINEGIKT--RYRFNS 284
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
6-291 |
4.53e-70 |
|
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: 220.40 E-value: 4.53e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 6 SFKLNTGATIPAVGLGTWQAKAGEVRQAVAHALKAGYRHIDGALCYQNEEEVGLGIK---DSGI-PRSEIFLTSKVWSSY 81
Cdd:cd19113 2 DIKLNSGYKMPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNraiDEGLvKREELFLTSKLWNNF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 82 HD--RVEECLDTTLKSLQTDYLDLYLIHWPV--RLVP--NGTHPLFPTKpDGSRNLDWDWDQAKTWAQMEDVLKKGKVKA 155
Cdd:cd19113 82 HDpkNVETALNKTLSDLKLDYVDLFLIHFPIafKFVPieEKYPPGFYCG-DGDNFVYEDVPILDTWKALEKLVDAGKIKS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 156 IGLSNAGIPIIEHIIKTGKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGSTS------------SPLHEDPDL 223
Cdd:cd19113 161 IGVSNFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGPQSfvelnqgralntPTLFEHDTI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 224 VAVAKKHNVPTATVLISYQVNRGVVVLPKSVTPARIESNLKTIKLD--EEDmnrLDKLAESGKQTRFTTP 291
Cdd:cd19113 241 KSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDltKED---FEEIAKLDIGLRFNDP 307
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
12-288 |
3.92e-69 |
|
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: 217.74 E-value: 3.92e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 12 GATIPAVGLGTW----QAKAGEVRQAVAHALKAGYRHIDGALCYQNEEEVGLGIK----DSGIPRSEIFLTSKVWSSYHD 83
Cdd:cd19109 1 GNSIPIIGLGTYsepkTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIRekiaEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 84 --RVEECLDTTLKSLQTDYLDLYLIHWPVRLVPNGThpLFPTKPDGSrnldWDWDQA---KTWAQMEDVLKKGKVKAIGL 158
Cdd:cd19109 81 peLVRPTLERTLKVLQLDYVDLYIIEMPMAFKPGDE--IYPRDENGK----WLYHKTnlcATWEALEACKDAGLVKSIGV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 159 SNAGIPIIEHII-KTG-KVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGS---------TSSPLHEDPDLVAVA 227
Cdd:cd19109 155 SNFNRRQLELILnKPGlKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTcrdpiwvnvSSPPLLEDPLLNSIG 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2781183762 228 KKHNVPTATVLISYQVNRGVVVLPKSVTPARIESNLKT--IKLDEEDMNRLDKLaesGKQTRF 288
Cdd:cd19109 235 KKYNKTAAQVVLRFNIQRGVVVIPKSFNPERIKENFQIfdFSLTEEEMKDIEAL---NKNVRY 294
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
15-279 |
4.21e-68 |
|
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: 212.98 E-value: 4.21e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 15 IPAVGLGTWQAKAGEVRQAVAHALKAGYRHIDGALCYQNEEEVGLGIKDSGIPRSEIFLTSKVW-SSY-HDRVEECLDTT 92
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWiDNLsKDKLLPSLEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 93 LKSLQTDYLDLYLIHWPvrlVPNGTHPLfptkpdgsrnldwdwdqAKTWAQMEDVLKKGKVKAIGLSNAGIPIIEHIIKT 172
Cdd:cd19139 81 LEKLRTDYVDLTLIHWP---SPNDEVPV-----------------EEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 173 -GKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGstSSPLHEDPDLVAVAKKHNVPTATVLISYQVNRGVVVLP 251
Cdd:cd19139 141 vGAGAIATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLA--YGKVLDDPVLAAIAERHGATPAQIALAWAMARGYAVIP 218
|
250 260 270
....*....|....*....|....*....|
gi 2781183762 252 KSVTPARIESNLK--TIKLDEEDMNRLDKL 279
Cdd:cd19139 219 SSTKREHLRSNLLalDLTLDADDMAAIAAL 248
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
11-279 |
8.82e-66 |
|
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: 208.28 E-value: 8.82e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 11 TGATIPAVGLGT--WQAKAGEVRQAVAHALKAGYRHIDGALCYQNEEEVGLGIK---DSG--IPRSEIFLTSKVWSS--Y 81
Cdd:cd19124 1 SGQTMPVIGMGTasDPPSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAealRLGlvKSRDELFVTSKLWCSdaH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 82 HDRVEECLDTTLKSLQTDYLDLYLIHWPVRLVPnGTHPLFPTKPDgsrnlDWDWDQAKTWAQMEDVLKKGKVKAIGLSNA 161
Cdd:cd19124 81 PDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKP-GKFSFPIEEED-----FLPFDIKGVWEAMEECQRLGLTKAIGVSNF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 162 GIPIIEHIIKTGKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGSTSSP-----LHEDPDLVAVAKKHNVPTAT 236
Cdd:cd19124 155 SCKKLQELLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTKwgsnaVMESDVLKEIAAAKGKTVAQ 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2781183762 237 VLISYQVNRGVVVLPKSVTPARIESNLKT--IKLDEEDMNRLDKL 279
Cdd:cd19124 235 VSLRWVYEQGVSLVVKSFNKERMKQNLDIfdWELTEEDLEKISEI 279
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
9-279 |
3.06e-62 |
|
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: 198.21 E-value: 3.06e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 9 LNTGATIPAVGLGTWQAKAGEVRQAVAHALKAGYRHIDGALCYQNEEEVGLGIKDSGIPRSEIFLTSKVWSSYH--DRVE 86
Cdd:cd19130 4 LNDGNSIPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIAASGIPRDELFVTTKLWNDRHdgDEPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 87 ECLDTTLKSLQTDYLDLYLIHWPVrlvpngthplfPTKPdgsrnldwdwDQAKTWAQMEDVLKKGKVKAIGLSNAGIPII 166
Cdd:cd19130 84 AAFAESLAKLGLDQVDLYLVHWPT-----------PAAG----------NYVHTWEAMIELRAAGRTRSIGVSNFLPPHL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 167 EHIIKTGKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGSTSspLHEDPDLVAVAKKHNVPTATVLISYQVNRG 246
Cdd:cd19130 143 ERIVAATGVVPAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQGK--LLGDPPVGAIAAAHGKTPAQIVLRWHLQKG 220
|
250 260 270
....*....|....*....|....*....|....*
gi 2781183762 247 VVVLPKSVTPARIESNLKT--IKLDEEDMNRLDKL 279
Cdd:cd19130 221 HVVFPKSVRRERMEDNLDVfdFDLTDTEIAAIDAL 255
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
6-288 |
4.60e-61 |
|
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: 195.46 E-value: 4.60e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 6 SFKLNTGATIPAVGLGTWQAKAGEVRQAVAHALKAGYRHIDGALCYQNEEEVGLGIKDSGIPRSEIFLTSKVWSSYH--D 83
Cdd:cd19134 2 TVTLNDDNTMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAASGIPRGELFVTTKLATPDQgfT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 84 RVEECLDTTLKSLQTDYLDLYLIHWPVrlvpngthplfptkPDGSRNLDwdwdqakTWAQMEDVLKKGKVKAIGLSNAGI 163
Cdd:cd19134 82 ASQAACRASLERLGLDYVDLYLIHWPA--------------GREGKYVD-------SWGGLMKLREEGLARSIGVSNFTA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 164 PIIEHIIKTGKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGSTSspLHEDPDLVAVAKKHNVPTATVLISYQV 243
Cdd:cd19134 141 EHLENLIDLTFFTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGR--LLDNPAVTAIAAAHGRTPAQVLLRWSL 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2781183762 244 NRGVVVLPKSVTPARIESNLKT--IKLDEEDMNRLDKLAESgkqTRF 288
Cdd:cd19134 219 QLGNVVISRSSNPERIASNLDVfdFELTADHMDALDGLDDG---TRF 262
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
18-280 |
6.44e-61 |
|
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: 195.99 E-value: 6.44e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 18 VGLGTWQAKAG-------EVRQAVAHALKAGYRHIDGALCY---QNEEEVGLGIKDSGIPRSEIFLTSKV------WSSY 81
Cdd:pfam00248 1 IGLGTWQLGGGwgpiskeEALEALRAALEAGINFIDTAEVYgdgKSEELLGEALKDYPVKRDKVVIATKVpdgdgpWPSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 82 H--DRVEECLDTTLKSLQTDYLDLYLIHWPvrlvpngthplfptkpdgsrnlDWDWDQAKTWAQMEDVLKKGKVKAIGLS 159
Cdd:pfam00248 81 GskENIRKSLEESLKRLGTDYIDLYYLHWP----------------------DPDTPIEETWDALEELKKEGKIRAIGVS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 160 NAGIPIIEHIIKTGKVTPAALQVELHPYCPQHA--LLKYCKEKGIILEAYSPLGS------------------------- 212
Cdd:pfam00248 139 NFDAEQIEKALTKGKIPIVAVQVEYNLLRRRQEeeLLEYCKKNGIPLIAYSPLGGglltgkytrdpdkgpgerrrllkkg 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2781183762 213 TSSPLHEDPDLVAVAKKHNVPTATVLISY--QVNRGVVVLPKSVTPARIESNLK--TIKLDEEDMNRLDKLA 280
Cdd:pfam00248 219 TPLNLEALEALEEIAKEHGVSPAQVALRWalSKPGVTIPIPGASNPEQLEDNLGalEFPLSDEEVARIDELL 290
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
14-302 |
8.78e-59 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 189.85 E-value: 8.78e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 14 TIPAVGLGTWQAKAGEVRQAVAHALKAGYRHIDGALCYQNEEEVGLGIKDSGIPRSEIFLTSKVWSSYH--DRVEECLDT 91
Cdd:PRK11172 2 SIPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLakDKLIPSLKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 92 TLKSLQTDYLDLYLIHWPvrlVPNGTHPLfptkpdgsrnldwdwdqAKTWAQMEDVLKKGKVKAIGLSNAGIPIIEHIIK 171
Cdd:PRK11172 82 SLQKLRTDYVDLTLIHWP---SPNDEVSV-----------------EEFMQALLEAKKQGLTREIGISNFTIALMKQAIA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 172 T-GKVTPAALQVELHPYCPQHALLKYCKEKGIILEAYSPLGstSSPLHEDPDLVAVAKKHNVPTATVLISYQVNRGVVVL 250
Cdd:PRK11172 142 AvGAENIATNQIELSPYLQNRKVVAFAKEHGIHVTSYMTLA--YGKVLKDPVIARIAAKHNATPAQVILAWAMQLGYSVI 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2781183762 251 PKSVTPARIESNLK--TIKLDEEDMNRLDKLAESGkqtRFTTPPwgsdfGF-PDW 302
Cdd:PRK11172 220 PSSTKRENLASNLLaqDLQLDAEDMAAIAALDRNG---RLVSPE-----GLaPEW 266
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
12-277 |
1.62e-55 |
|
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: 181.27 E-value: 1.62e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 12 GATIPAVGLGTWQAKAGEVR---------QAVAHALKAGYRHIDGALCYQN---EEEVGLGIKdsGIPRSEIFLTSKVW- 78
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGMSKdysddkkaiEALRYAIELGINLIDTAEMYGGghaEELVGKAIK--GFDREDLFITTKVSp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 79 --SSYHDrVEECLDTTLKSLQTDYLDLYLIHWPVRLVPngthplfptkpdgsrnldwdwdQAKTWAQMEDVLKKGKVKAI 156
Cdd:cd19072 79 dhLKYDD-VIKAAKESLKRLGTDYIDLYLIHWPNPSIP----------------------IEETLRAMEELVEEGKIRYI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 157 GLSNAGIPIIEHIIK-TGKVTPAALQVE---LHPYcPQHALLKYCKEKGIILEAYSPLGSTS-SPLHEDPDLVAVAKKHN 231
Cdd:cd19072 136 GVSNFSLEELEEAQSyLKKGPIVANQVEynlFDRE-EESGLLPYCQKNGIAIIAYSPLEKGKlSNAKGSPLLDEIAKKYG 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2781183762 232 VPTATVLISYQVNR-GVVVLPKSVTPARIESNLKT--IKLDEEDMNRLD 277
Cdd:cd19072 215 KTPAQIALNWLISKpNVIAIPKASNIEHLEENAGAlgWELSEEDLQRLD 263
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
8-277 |
2.99e-54 |
|
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: 178.21 E-value: 2.99e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 8 KLNTGATIPAVGLGTWQ-----AKAGEVRQAVAHALKAGYRHIDGALCYQN---EEEVGLGIKDSgipRSEIFLTSKVWS 79
Cdd:cd19138 4 TLPDGTKVPALGQGTWYmgedpAKRAQEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR---RDKVFLVSKVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 80 S--YHDRVEECLDTTLKSLQTDYLDLYLIHWPvrlvpnGTHPLfptkpdgsrnldwdwdqAKTWAQMEDVLKKGKVKAIG 157
Cdd:cd19138 81 SnaSRQGTVRACERSLRRLGTDYLDLYLLHWR------GGVPL-----------------AETVAAMEELKKEGKIRAWG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 158 LSNAGIPIIEHIIKT-GKVTPAALQVELH--PYCPQHALLKYCKEKGIILEAYSPL---GSTSSPLHEDPDLVAVAKKHN 231
Cdd:cd19138 138 VSNFDTDDMEELWAVpGGGNCAANQVLYNlgSRGIEYDLLPWCREHGVPVMAYSPLaqgGLLRRGLLENPTLKEIAARHG 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2781183762 232 VPTATVLISYQVNRG-VVVLPKSVTPARIESNLKT--IKLDEEDMNRLD 277
Cdd:cd19138 218 ATPAQVALAWVLRDGnVIAIPKSGSPEHARENAAAadLELTEEDLAELD 266
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
10-283 |
1.06e-39 |
|
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: 141.47 E-value: 1.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 10 NTGATIPAVGLGTWQ-------AKAGEVRQAVAHALKAGYRHIDGALCY---QNEEEVGLGIKDSgiPRSEIFLTSKVWS 79
Cdd:COG0667 8 RSGLKVSRLGLGTMTfggpwggVDEAEAIAILDAALDAGINFFDTADVYgpgRSEELLGEALKGR--PRDDVVIATKVGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 80 SYH----------DRVEECLDTTLKSLQTDYLDLYLIHWPvrlvpngthplfptkpdgsrnlDWDWDQAKTWAQMEDVLK 149
Cdd:COG0667 86 RMGpgpngrglsrEHIRRAVEASLRRLGTDYIDLYQLHRP----------------------DPDTPIEETLGALDELVR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 150 KGKVKAIGLSNAGIPIIEHIIKT--GKVTPAALQVELHPYC--PQHALLKYCKEKGIILEAYSPLGS---TSSPLHEDPD 222
Cdd:COG0667 144 EGKIRYIGVSNYSAEQLRRALAIaeGLPPIVAVQNEYSLLDrsAEEELLPAARELGVGVLAYSPLAGgllTGKYRRGATF 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 223 -------------------------LVAVAKKHNVPTATVLISYQVNRGVV--VLPKSVTPARIESNLK--TIKLDEEDM 273
Cdd:COG0667 224 pegdraatnfvqgylternlalvdaLRAIAAEHGVTPAQLALAWLLAQPGVtsVIPGARSPEQLEENLAaaDLELSAEDL 303
|
330
....*....|
gi 2781183762 274 NRLDKLAESG 283
Cdd:COG0667 304 AALDAALAAV 313
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
12-277 |
2.06e-39 |
|
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: 139.24 E-value: 2.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 12 GATIPAVGLGTWQ---------AKAGEVRQAVAHALKAGYRHIDGALCY---QNEEEVGLGIKDsgIPRSEIFLTSKVWS 79
Cdd:cd19137 1 GEKIPALGLGTWGiggfltpdySRDEEMVELLKTAIELGYTHIDTAEMYgggHTEELVGKAIKD--FPREDLFIVTKVWP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 80 SY--HDRVEECLDTTLKSLQTDYLDLYLIHWPvrlvpngtHPLFPTKpdgsrnldwdwdqaKTWAQMEDVLKKGKVKAIG 157
Cdd:cd19137 79 TNlrYDDLLRSLQNSLRRLDTDYIDLYLIHWP--------NPNIPLE--------------ETLSAMAEGVRQGLIRYIG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 158 LSNAGIPIIEHIIKTGKVTPAALQVELHPY---CPQHALLKYCKEKGIILEAYSPLGSTSSPLHEdpDLVAVAKKHNVPT 234
Cdd:cd19137 137 VSNFNRRLLEEAISKSQTPIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPLRRGLEKTNR--TLEEIAKNYGKTI 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2781183762 235 ATVLISYQVNR-GVVVLPKSVTPARIESNLKT--IKLDEEDMNRLD 277
Cdd:cd19137 215 AQIALAWLIQKpNVVAIPKAGRVEHLKENLKAteIKLSEEEMKLLD 260
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
15-282 |
4.64e-38 |
|
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: 136.56 E-value: 4.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 15 IPAVGLGTWQAKAG---------EVRQAVAHALKAGYRHIDGALCYQN---EEEVGLGIKDsgiPRSEIFLTSKVWS--S 80
Cdd:cd19085 1 VSRLGLGCWQFGGGywwgdqddeESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKG---RRDDVVIATKVSPdnL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 81 YHDRVEECLDTTLKSLQTDYLDLYLIHWPVRLVPngthplfptkpdgsrnldwdwdQAKTWAQMEDVLKKGKVKAIGLSN 160
Cdd:cd19085 78 TPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVP----------------------LEETMEALEKLKEEGKIRAIGVSN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 161 AGIPIIEHIIKTGKVTpaALQVelhPY-----CPQHALLKYCKEKGIILEAYSPL------GSTSSPLHEDPD------- 222
Cdd:cd19085 136 FGPAQLEEALDAGRID--SNQL---PYnllwrAIEYEILPFCREHGIGVLAYSPLaqglltGKFSSAEDFPPGdartrlf 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 223 -----------------LVAVAKKHNVPTATVLISYQVNRGVV--VLPKSVTPARIESNLK--TIKLDEEDMNRLDKLAE 281
Cdd:cd19085 211 rhfepgaeeetfealekLKEIADELGVTMAQLALAWVLQQPGVtsVIVGARNPEQLEENAAavDLELSPSVLERLDEISD 290
|
.
gi 2781183762 282 S 282
Cdd:cd19085 291 P 291
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
15-277 |
4.04e-36 |
|
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: 131.58 E-value: 4.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 15 IPAVGLGTWQA-----------KAGEVRQAVAHALKAGYRHIDGALCY---QNEEEVGLGIKDSGiPRSEIFLTSKV--- 77
Cdd:cd19093 2 VSPLGLGTWQWgdrlwwgygeyGDEDLQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFLKELG-DRDEVVIATKFapl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 78 -WSSYHDRVEECLDTTLKSLQTDYLDLYLIHWPvrlvpngTHPLFPTKPdgsrnldwdwdqakTWAQMEDVLKKGKVKAI 156
Cdd:cd19093 81 pWRLTRRSVVKALKASLERLGLDSIDLYQLHWP-------GPWYSQIEA--------------LMDGLADAVEEGLVRAV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 157 GLSNAGIPIIEHIIKTGK---VTPAALQVE---LHPYCPQHALLKYCKEKGIILEAYSPLG--------STSSP------ 216
Cdd:cd19093 140 GVSNYSADQLRRAHKALKergVPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAqglltgkySPENPppggrr 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2781183762 217 -------LHEDPDLV----AVAKKHNVPTATVLISYQVNRGVVVLPKSVTPARIESNLK--TIKLDEEDMNRLD 277
Cdd:cd19093 220 rlfgrknLEKVQPLLdaleEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGalGWRLSEEEVAELD 293
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
16-264 |
1.29e-31 |
|
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: 118.00 E-value: 1.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 16 PAVGLGTWQ----AKAGEVRQAVAHALKAGYRHIDGALCY---QNEEEVGLGIKDSGIpRSEIFLTSKVWSSY------- 81
Cdd:cd06660 1 SRLGLGTMTfggdGDEEEAFALLDAALEAGGNFFDTADVYgdgRSERLLGRWLKGRGN-RDDVVIATKGGHPPggdpsrs 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 82 ---HDRVEECLDTTLKSLQTDYLDLYLIHWPVRLVPNGthplfptkpdgsrnldwdwdqaKTWAQMEDVLKKGKVKAIGL 158
Cdd:cd06660 80 rlsPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVE----------------------ETLEALNELVREGKIRYIGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 159 SNAGIPIIEHIIKT----GKVTPAALQVELHPYCPQHA---LLKYCKEKGIILEAYSPLGSTSsplhedpdlvavakkhn 231
Cdd:cd06660 138 SNWSAERLAEALAYakahGLPGFAAVQPQYSLLDRSPMeeeLLDWAEENGLPLLAYSPLARGP----------------- 200
|
250 260 270
....*....|....*....|....*....|....*
gi 2781183762 232 vptATVLISYQVNR--GVVVLPKSVTPARIESNLK 264
Cdd:cd06660 201 ---AQLALAWLLSQpfVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
15-277 |
1.60e-30 |
|
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: 116.86 E-value: 1.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 15 IPAVGLGTWQ---AKAGEV-----RQAVAHALKAGYRHIDGALCYQN---EEEVGLGIKDSgipRSEIFLTSKV------ 77
Cdd:cd19084 4 VSRIGLGTWAiggTWWGEVddqesIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKGR---RDDVVIATKCglrwdg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 78 -WSSYHD----RVEECLDTTLKSLQTDYLDLYLIHWPvrlvpngthplfptkpdgsrnlDWDWDQAKTWAQMEDVLKKGK 152
Cdd:cd19084 81 gKGVTKDlspeSIRKEVEQSLRRLQTDYIDLYQIHWP----------------------DPNTPIEETAEALEKLKKEGK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 153 VKAIGLSNAGIPIIEHIIKTGKVtpAALQVELHPYCPQHA--LLKYCKEKGIILEAYSPLGS-------TSSPL------ 217
Cdd:cd19084 139 IRYIGVSNFSVEQLEEARKYGPI--VSLQPPYSMLEREIEeeLLPYCRENGIGVLPYGPLAQglltgkyKKEPTfppddr 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 218 -HEDPD---------------LVAVAKKHNVPTATVLISYQVNR-GV-VVLPKSVTPARIESNLKT--IKLDEEDMNRLD 277
Cdd:cd19084 217 rSRFPFfrgenfeknleivdkLKEIAEKYGKSLAQLAIAWTLAQpGVtSAIVGAKNPEQLEENAGAldWELTEEELKEID 296
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
4-281 |
2.15e-28 |
|
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: 111.77 E-value: 2.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 4 PTSFKLNTGATIPAVGLGTWQAKAG-------EVRQAV-AHALKAGYRHIDGALCYQ-NEEEVGLGIKDSGIPRSEIFLT 74
Cdd:cd19144 2 PTRTLGRNGPSVPALGFGAMGLSAFygppkpdEERFAVlDAAFELGCTFWDTADIYGdSEELIGRWFKQNPGKREKIFLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 75 SKV-----------W-SSYHDRVEECLDTTLKSLQTDYLDLYLIHwpvRLvpNGTHPLfptkpdgsrnldwdwdqAKTWA 142
Cdd:cd19144 82 TKFgieknvetgeySvDGSPEYVKKACETSLKRLGVDYIDLYYQH---RV--DGKTPI-----------------EKTVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 143 QMEDVLKKGKVKAIGLSNagiPIIEHIIKTGKVTP-AALQVELHPYC-----PQHALLKYCKEKGIILEAYSPL------ 210
Cdd:cd19144 140 AMAELVQEGKIKHIGLSE---CSAETLRRAHAVHPiAAVQIEYSPFSldierPEIGVLDTCRELGVAIVAYSPLgrgflt 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 211 GSTSSPLHEDPD-------------------LV----AVAKKHNVPTATVLISYQVNRG--VVVLPKSVTPARIESNLKT 265
Cdd:cd19144 217 GAIRSPDDFEEGdfrrmaprfqaenfpknleLVdkikAIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLEENLGA 296
|
330
....*....|....*...
gi 2781183762 266 --IKLDEEDMNRLDKLAE 281
Cdd:cd19144 297 lkVKLTEEEEKEIREIAE 314
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
10-276 |
4.68e-28 |
|
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: 110.38 E-value: 4.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 10 NTGATIPAVGLG----TW---QAKAGEVRQAVAHALKAGYRHIDGALCYQ---NEEEVGLGIKDsgiPRSEIFLTSK--- 76
Cdd:cd19076 7 TQGLEVSALGLGcmgmSAfygPADEEESIATLHRALELGVTFLDTADMYGpgtNEELLGKALKD---RRDEVVIATKfgi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 77 VWSS-----YHD----RVEECLDTTLKSLQTDYLDLYLIHwpvRLVPNGthPLfptkpdgsrnldwdwdqAKTWAQMEDV 147
Cdd:cd19076 84 VRDPgsgfrGVDgrpeYVRAACEASLKRLGTDVIDLYYQH---RVDPNV--PI-----------------EETVGAMAEL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 148 LKKGKVKAIGLSNAGipiIEHIIKTGKVTP-AALQVELHPYC--PQHALLKYCKEKGIILEAYSPL------GSTSSP-- 216
Cdd:cd19076 142 VEEGKVRYIGLSEAS---ADTIRRAHAVHPiTAVQSEYSLWTrdIEDEVLPTCRELGIGFVAYSPLgrgfltGAIKSPed 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 217 LHEDPD---------------------LVAVAKKHNVPTATVLISYQVNRG--VVVLPKSVTPARIESNLKT--IKLDEE 271
Cdd:cd19076 219 LPEDDFrrnnprfqgenfdknlklvekLEAIAAEKGCTPAQLALAWVLAQGddIVPIPGTKRIKYLEENVGAldVVLTPE 298
|
....*
gi 2781183762 272 DMNRL 276
Cdd:cd19076 299 ELAEI 303
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-202 |
9.77e-26 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 102.56 E-value: 9.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 10 NTGATIPAVGLGT---WQAKAGEVRQAVAHALKAGYRHIDGALCYQN-EEEVGLGIKDsgiPRSEIFLTSKVWSSYHDRV 85
Cdd:cd19100 6 RTGLKVSRLGFGGgplGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKG---RRDKVFLATKTGARDYEGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 86 EECLDTTLKSLQTDYLDLYLIHwpvrlvpngthplFPTKPDgsrnldwDWDQAKTWAQMEDVL----KKGKVKAIGLSNA 161
Cdd:cd19100 83 KRDLERSLKRLGTDYIDLYQLH-------------AVDTEE-------DLDQVFGPGGALEALleakEEGKIRFIGISGH 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2781183762 162 GIPIIEHIIKTGKVtpAALQVELHPYCPQH-----ALLKYCKEKGI 202
Cdd:cd19100 143 SPEVLLRALETGEF--DVVLFPINPAGDHIdsfreELLPLAREKGV 186
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
10-281 |
2.19e-24 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 101.43 E-value: 2.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 10 NTGATIPAVGLGTW------QAKAGEVrqaVAHALKAGYRHIDGALCYQNEEE-VGLGIKDsgiPRSEIFLTSK--VWSS 80
Cdd:COG1453 8 KTGLEVSVLGFGGMrlprkdEEEAEAL---IRRAIDNGINYIDTARGYGDSEEfLGKALKG---PRDKVILATKlpPWVR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 81 YHDRVEECLDTTLKSLQTDYLDLYLIH-------WPVRLVPNGThplfptkpdgsrnldWDW-DQAKtwaqmedvlKKGK 152
Cdd:COG1453 82 DPEDMRKDLEESLKRLQTDYIDLYLIHglnteedLEKVLKPGGA---------------LEAlEKAK---------AEGK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 153 VKAIGLSNAGIP-IIEHIIKTGKVTpaALQVELHP----YCPQHALLKYCKEKGIILEAYSPL--GStsspLHEDPDLVA 225
Cdd:COG1453 138 IRHIGFSTHGSLeVIKEAIDTGDFD--FVQLQYNYldqdNQAGEEALEAAAEKGIGVIIMKPLkgGR----LANPPEKLV 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2781183762 226 VAKKHNVPTATVLISY-----QVnrgVVVLPKSVTPARIESNLKT----IKLDEEDMNRLDKLAE 281
Cdd:COG1453 212 ELLCPPLSPAEWALRFllshpEV---TTVLSGMSTPEQLDENLKTadnlEPLTEEELAILERLAE 273
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-264 |
6.80e-24 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 98.04 E-value: 6.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 10 NTGATIPAVGLGT--WQAKAGEVrqaVAHALKAGYRHIDGALCYQN---EEEVGLGIKdsGIPRSEIFLTSKVWSSY--- 81
Cdd:cd19105 8 KTGLKVSRLGFGGggLPRESPEL---LRRALDLGINYFDTAEGYGNgnsEEIIGEALK--GLRRDKVFLATKASPRLdkk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 82 -HDRVEECLDTTLKSLQTDYLDLYLIHwpvrlvpngthplfptkpdGSRNLDWDWDQAKTWAQMEDVLKKGKVKAIGLS- 159
Cdd:cd19105 83 dKAELLKSVEESLKRLQTDYIDIYQLH-------------------GVDTPEERLLNEELLEALEKLKKEGKVRFIGFSt 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 160 -NAGIPIIEHIIKTGkvtpaALQVELHPYCP--QHA----LLKYCKEKGIILEAYSPLGstSSPLHEDPDLVAVAKKHNV 232
Cdd:cd19105 144 hDNMAEVLQAAIESG-----WFDVIMVAYNFlnQPAeleeALAAAAEKGIGVVAMKTLA--GGYLQPALLSVLKAKGFSL 216
|
250 260 270
....*....|....*....|....*....|....*.
gi 2781183762 233 PTA---TVLisyqVNRGV-VVLPKSVTPARIESNLK 264
Cdd:cd19105 217 PQAalkWVL----SNPRVdTVVPGMRNFAELEENLA 248
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
14-212 |
1.22e-23 |
|
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: 96.78 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 14 TIPAVGLGTWQ--------AKAGEVRQAVAHALKAGYRHIDGALCYQN---EEEVGLGIKDsgiPRSEIFLTSKV----- 77
Cdd:cd19086 2 EVSEIGFGTWGlggdwwgdVDDAEAIRALRAALDLGINFFDTADVYGDghsERLLGKALKG---RRDKVVIATKFgnrfd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 78 --------WSSyhDRVEECLDTTLKSLQTDYLDLYLIH-WPVRLVPNGthplfptkpdgsrnldwdwdqaKTWAQMEDVL 148
Cdd:cd19086 79 ggperpqdFSP--EYIREAVEASLKRLGTDYIDLYQLHnPPDEVLDND----------------------ELFEALEKLK 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2781183762 149 KKGKVKAIGLSNAGIPIIEHIIKTGKVtpAALQVELHPYC--PQHALLKYCKEKGIILEAYSPLGS 212
Cdd:cd19086 135 QEGKIRAYGVSVGDPEEALAALRRGGI--DVVQVIYNLLDqrPEEELFPLAEEHGVGVIARVPLAS 198
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-280 |
9.44e-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: 381328 [Multi-domain] Cd Length: 302 Bit Score: 95.82 E-value: 9.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 15 IPAVGLGTWQAKAG------------EVRQAVAHALKAGYRHIDGALCY---QNEEEVGLGIKDSgipRSEIFLTSK--- 76
Cdd:cd19102 1 LTTIGLGTWAIGGGgwgggwgpqddrDSIAAIRAALDLGINWIDTAAVYglgHSEEVVGRALKGL---RDRPIVATKcgl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 77 VW------SSYHDR--VEECLDTTLKSLQTDYLDLYLIHWPvrlvpngthplfptkpDGSRNLDwdwdqaKTWAQMEDVL 148
Cdd:cd19102 78 LWdeegriRRSLKPasIRAECEASLRRLGVDVIDLYQIHWP----------------DPDEPIE------EAWGALAELK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 149 KKGKVKAIGLSNAGIPIIEHIIKTGKVtpAALQvelhpycPQHALLK---------YCKEKGIILEAYSPLGS------- 212
Cdd:cd19102 136 EEGKVRAIGVSNFSVDQMKRCQAIHPI--ASLQ-------PPYSLLRrgieaeilpFCAEHGIGVIVYSPMQSglltgkm 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 213 TSSPLHEDPD------------------------LVAVAKKHNVPTATVLISYQVNRGVV--VLPKSVTPARIESNLKT- 265
Cdd:cd19102 207 TPERVASLPAddwrrrspffqepnlarnlalvdaLRPIAERHGRTVAQLAIAWVLRRPEVtsAIVGARRPDQIDETVGAa 286
|
330
....*....|....*.
gi 2781183762 266 -IKLDEEDMNRLDKLA 280
Cdd:cd19102 287 dLRLTPEELAEIEALL 302
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
19-272 |
1.98e-21 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 92.14 E-value: 1.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 19 GLGTWQAKAGEVRQAVAHALKAGYRHIDGALCY---QNEEEVGLGIKDSGIPRSEIFLTSK-----VWSSYHDRVE---- 86
Cdd:COG4989 22 RLGEWDLSPAEAAALIEAALELGITTFDHADIYggyTCEALFGEALKLSPSLREKIELQTKcgirlPSEARDNRVKhydt 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 87 ------ECLDTTLKSLQTDYLDLYLIHWPvrlvpngtHPLFptkpdgsrnldwDWDQ-AKTwaqMEDVLKKGKVKAIGLS 159
Cdd:COG4989 102 skehiiASVEGSLRRLGTDYLDLLLLHRP--------DPLM------------DPEEvAEA---FDELKASGKVRHFGVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 160 NAGIPIIEHIIKTGKVTPAALQVELHPYCPQH---ALLKYCKEKGIILEAYSPL--GSTSSPLHEDPD-----LVAVAKK 229
Cdd:COG4989 159 NFTPSQFELLQSALDQPLVTNQIELSLLHTDAfddGTLDYCQLNGITPMAWSPLagGRLFGGFDEQFPrlraaLDELAEK 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2781183762 230 HNVPTATVLISYqVNR---GVVVLPKSVTPARIESNLK--TIKLDEED 272
Cdd:COG4989 239 YGVSPEAIALAW-LLRhpaGIQPVIGTTNPERIKAAAAalDIELTREE 285
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
10-277 |
2.43e-21 |
|
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: 92.26 E-value: 2.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 10 NTGATIPAVGLGT----------WQAKAGEVRQAVAHALKAGYRHIDGALCYQN---EEEVGLGIKDSgIPRSEIFLTSK 76
Cdd:cd19079 7 NSGLKVSRLCLGCmsfgdpkwrpWVLDEEESRPIIKRALDLGINFFDTANVYSGgasEEILGRALKEF-APRDEVVIATK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 77 VWSSYHDRVEEC----------LDTTLKSLQTDYLDLYLIHWpvrlvpngthplfptkpdgsrnldWDWDQAK--TWAQM 144
Cdd:cd19079 86 VYFPMGDGPNGRglsrkhimaeVDASLKRLGTDYIDLYQIHR------------------------WDYETPIeeTLEAL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 145 EDVLKKGKVKAIGLSN---------AGIPIIEHIIKtgkvtPAALQvelhpycPQHALL---------KYCKEKGIILEA 206
Cdd:cd19079 142 HDVVKSGKVRYIGASSmyawqfakaLHLAEKNGWTK-----FVSMQ-------NHYNLLyreeeremiPLCEEEGIGVIP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 207 YSPLGS--------TSSPLHEDPD--------------------LVAVAKKHNVPTATVLISYQVNRGVVVLP--KSVTP 256
Cdd:cd19079 210 WSPLARgrlarpwgDTTERRRSTTdtaklkydyfteadkeivdrVEEVAKERGVSMAQVALAWLLSKPGVTAPivGATKL 289
|
330 340
....*....|....*....|...
gi 2781183762 257 ARIESNLK--TIKLDEEDMNRLD 277
Cdd:cd19079 290 EHLEDAVAalDIKLSEEEIKYLE 312
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
10-278 |
4.51e-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: 91.57 E-value: 4.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 10 NTGATIPAVGLGTWQAKAG---------EVRQAVAHALKAGYRHIDGALCYQN---EEEVGLGIKDSgipRSEIFLTSK- 76
Cdd:cd19149 6 KSGIEASVIGLGTWAIGGGpwwggsddnESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKGR---RDKVVLATKc 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 77 --VW-----SSYHDRV--------------EEClDTTLKSLQTDYLDLYLIHWpvrlvPNGTHPLfptkpdgsrnldwdw 135
Cdd:cd19149 83 glRWdreggSFFFVRDgvtvyknlspesirEEV-EQSLKRLGTDYIDLYQTHW-----QDVETPI--------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 136 dqAKTWAQMEDVLKKGKVKAIGLSNAGIPIIEHIIKTGKVtpAALQVelhPYC---PQH--ALLKYCKEKGIILEAYSPL 210
Cdd:cd19149 142 --EETMEALEELKRQGKIRAIGASNVSVEQIKEYVKAGQL--DIIQE---KYSmldRGIekELLPYCKKNNIAFQAYSPL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 211 ------GSTSSPLHEDPDL---------------VA--------VAKKHNVPTATVLISYQVNRG--VVVLPKSVTPARI 259
Cdd:cd19149 215 eqglltGKITPDREFDAGDarsgipwfspenrekVLallekwkpLCEKYGCTLAQLVIAWTLAQPgiTSALCGARKPEQA 294
|
330 340
....*....|....*....|.
gi 2781183762 260 ESNLK--TIKLDEEDMNRLDK 278
Cdd:cd19149 295 EENAKagDIRLSAEDIATMRS 315
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
16-212 |
6.83e-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: 86.91 E-value: 6.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 16 PAVGLGTWQAKA-------GEVRQAVAHALKAGYRHIDGALCYQNEEEVgLGIKDSGIPRSEIFLTSKVWSSYHDR---- 84
Cdd:cd19095 1 SVLGLGTSGIGRvwgvpseAEAARLLNTALDLGINLIDTAPAYGRSEER-LGRALAGLRRDDLFIATKVGTHGEGGrdrk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 85 ------VEECLDTTLKSLQTDYLDLYLIHWPVRLVPNGTHplfptkpdgsrnLDWdwdqaktwaqMEDVLKKGKVKAIGL 158
Cdd:cd19095 80 dfspaaIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEV------------LET----------LEDLKAAGKVRYIGV 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2781183762 159 SNAGiPIIEHIIKTGKVTpaALQVELHPYCPQHA-LLKYCKEKGIILEAYSPLGS 212
Cdd:cd19095 138 SGDG-EELEAAIASGVFD--VVQLPYNVLDREEEeLLPLAAEAGLGVIVNRPLAN 189
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
10-272 |
5.54e-18 |
|
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and Escherichia coli YdhF are prototypes of this family. They are uncharacterized aldo/keto reductase family oxidoreductases.
Pssm-ID: 381318 [Multi-domain] Cd Length: 287 Bit Score: 82.22 E-value: 5.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 10 NTGATIPAVGLGTW-----QAKAGEVRQAVAHALKAGYRHIDGALCYQN---EEEVGLGIKDSGIPRSEIFLTSKV---- 77
Cdd:cd19092 1 PEGLEVSRLVLGCMrladwGESAEELLSLIEAALELGITTFDHADIYGGgkcEELFGEALALNPGLREKIEIQTKCgirl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 78 ------WSSYH-----DRVEECLDTTLKSLQTDYLDLYLIHWPvrlvpngtHPLF-PtkpdgsrnldwdWDQAKTwaqME 145
Cdd:cd19092 81 gddprpGRIKHydtskEHILASVEGSLKRLGTDYLDLLLLHRP--------DPLMdP------------EEVAEA---FD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 146 DVLKKGKVKAIGLSNAGIPIIEHIIKTGKVTPAALQVELHPYCPQHA---LLKYCKEKGIILEAYSPLGS---TSSPLHE 219
Cdd:cd19092 138 ELVKSGKVRYFGVSNFTPSQIELLQSYLDQPLVTNQIELSLLHTEAIddgTLDYCQLLDITPMAWSPLGGgrlFGGFDER 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2781183762 220 DPDLVA----VAKKHNVPTATVLISYqVNR---GVVVLPKSVTPARIESNLK--TIKLDEED 272
Cdd:cd19092 218 FQRLRAaleeLAEEYGVTIEAIALAW-LLRhpaRIQPILGTTNPERIRSAVKalDIELTREE 278
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
10-279 |
2.28e-17 |
|
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: 81.12 E-value: 2.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 10 NTGATIPAVGLGT--------WQAKAGEVRQA-----VAHALKAGYRHIDGALCY---QNEEEVGLGIKDSgipRSEIFL 73
Cdd:cd19091 8 RSGLKVSELALGTmtfgggggFFGAWGGVDQEeadrlVDIALDAGINFFDTADVYsegESEEILGKALKGR---RDDVLI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 74 TSKVW-----------SSYHDRVEEClDTTLKSLQTDYLDLYLIHWpvrlvpngthplfptkpdgsrnldwdWDQA---- 138
Cdd:cd19091 85 ATKVRgrmgegpndvgLSRHHIIRAV-EASLKRLGTDYIDLYQLHG--------------------------FDALtple 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 139 KTWAQMEDVLKKGKVKAIGLSN-AGipiiEHIIKT-------GKVTPAALQV-------ELhpycpQHALLKYCKEKGII 203
Cdd:cd19091 138 ETLRALDDLVRQGKVRYIGVSNfSA----WQIMKAlgiserrGLARFVALQAyysllgrDL-----EHELMPLALDQGVG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 204 LEAYSPLG--------STSSPLHED----------PD------------LVAVAKKHNVPTATVLISYQVNRGVVVlpkS 253
Cdd:cd19091 209 LLVWSPLAggllsgkyRRGQPAPEGsrlrrtgfdfPPvdrergydvvdaLREIAKETGATPAQVALAWLLSRPTVS---S 285
|
330 340 350
....*....|....*....|....*....|...
gi 2781183762 254 V-----TPARIESNLKT--IKLDEEDMNRLDKL 279
Cdd:cd19091 286 ViigarNEEQLEDNLGAagLSLTPEEIARLDKV 318
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
18-210 |
3.07e-17 |
|
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: 80.43 E-value: 3.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 18 VGLGTWqAKAG------EVRQAVA---HALKAGYRHIDGALCY---QNEEEVGLGIKDSGiPRSEIFLTSKV---WS--- 79
Cdd:cd19148 7 IALGTW-AIGGwmwggtDEKEAIEtihKALDLGINLIDTAPVYgfgLSEEIVGKALKEYG-KRDRVVIATKVgleWDegg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 80 -----SYHDRVEECLDTTLKSLQTDYLDLYLIHWPVRLVPngthplfptkpdgsrnLDwdwdqaKTWAQMEDVLKKGKVK 154
Cdd:cd19148 85 evvrnSSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVP----------------IE------ETAEALKELLDEGKIR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2781183762 155 AIGLSNAGIPIIEHIIKTgkvtpAALQVELHPY-----CPQHALLKYCKEKGIILEAYSPL 210
Cdd:cd19148 143 AIGVSNFSPEQMETFRKV-----APLHTVQPPYnlferEIEKDVLPYARKHNIVTLAYGAL 198
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
34-278 |
3.36e-16 |
|
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: 77.66 E-value: 3.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 34 VAHALKAGYRHIDGALCY---QNEEEVGLGIKDsgiPRSEIFLTSK----------VWS---SYHDRVEECLDTTLKSLQ 97
Cdd:cd19078 31 IRKAVELGITFFDTAEVYgpyTNEELVGEALKP---FRDQVVIATKfgfkidggkpGPLgldSRPEHIRKAVEGSLKRLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 98 TDYLDLYLIHwpvRLVPNgthplfpTKPDgsrnldwdwDQAKTwaqMEDVLKKGKVKAIGLSNAGipiIEHIIKTGKVTP 177
Cdd:cd19078 108 TDYIDLYYQH---RVDPN-------VPIE---------EVAGT---MKELIKEGKIRHWGLSEAG---VETIRRAHAVCP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 178 -AALQVELHPYC--PQHALLKYCKEKGIILEAYSPLGS-------------------TSSP------LHEDPDLV----A 225
Cdd:cd19078 163 vTAVQSEYSMMWrePEKEVLPTLEELGIGFVPFSPLGKgfltgkidentkfdegddrASLPrftpeaLEANQALVdllkE 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2781183762 226 VAKKHNVPTATVLISYQVNRG--VVVLPKSVTPARIESNLKT--IKLDEEDMNRLDK 278
Cdd:cd19078 243 FAEEKGATPAQIALAWLLAKKpwIVPIPGTTKLSRLEENIGAadIELTPEELREIED 299
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
15-269 |
9.51e-16 |
|
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: 75.72 E-value: 9.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 15 IPAVGLGTWQAKAGEVR-------QAVA---HALKAGYRHIDGALCY---QNEEEVGLGIKDSGiprSEIFLTSKV---- 77
Cdd:cd19088 1 VSRLGYGAMRLTGPGIWgppadreEAIAvlrRALELGVNFIDTADSYgpdVNERLIAEALHPYP---DDVVIATKGglvr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 78 ----WSSYHDRVEE---CLDTTLKSLQTDYLDLYLIHWPvrlvpngthplfptkpDGSRNLDwdwDQAKTWAQMEDvlkK 150
Cdd:cd19088 78 tgpgWWGPDGSPEYlrqAVEASLRRLGLDRIDLYQLHRI----------------DPKVPFE---EQLGALAELQD---E 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 151 GKVKAIGLSNAGIPIIEHIIKTGKVtpAALQVELHPYCPQH-ALLKYCKEKGIILEAYSPLGStSSPLHEDPDLVAVAKK 229
Cdd:cd19088 136 GLIRHIGLSNVTVAQIEEARAIVRI--VSVQNRYNLANRDDeGVLDYCEAAGIAFIPWFPLGG-GDLAQPGGLLAEVAAR 212
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2781183762 230 HNVPTATVLISYQVNRG--VVVLPKSVTPARIESNLK--TIKLD 269
Cdd:cd19088 213 LGATPAQVALAWLLARSpvMLPIPGTSSVEHLEENLAaaGLRLS 256
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
11-279 |
1.04e-15 |
|
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1).
Pssm-ID: 381309 [Multi-domain] Cd Length: 307 Bit Score: 76.30 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 11 TGATIPAVGLGTwQAKAG----------EVRQAVAHALKAGYRHIDGALCY---QNEEEVGLGIKDSGipRSEIFLTSK- 76
Cdd:cd19083 7 SDIDVNPIGLGT-NAVGGhnlypnldeeEGKDLVREALDNGVNLLDTAFIYglgRSEELVGEVLKEYN--RNEVVIATKg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 77 ---------VWSSYHDRVEECLDTTLKSLQTDYLDLYLIHWPvrlvpngthplfptkpdgsrnlDWDWDQAKTWAQMEDV 147
Cdd:cd19083 84 ahkfggdgsVLNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFP----------------------DGETPKAEAVGALQEL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 148 LKKGKVKAIGLSNAGIPIIEHIIKTGKVTpaALQvelHPYCPQH-----ALLKYCKEKGIILEAYSPLGST--------- 213
Cdd:cd19083 142 KDEGKIRAIGVSNFSLEQLKEANKDGYVD--VLQ---GEYNLLQreaeeDILPYCVENNISFIPYFPLASGllagkytkd 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 214 --------------------SSPLHEDPDLVAVAKKHNVPTATVLISYQVNRGVV--VLPKSVTPARIESNLKT--IKLD 269
Cdd:cd19083 217 tkfpdndlrndkplfkgerfSENLDKVDKLKSIADEKGVTVAHLALAWYLTRPAIdvVIPGAKRAEQVIDNLKAldVTLT 296
|
330
....*....|
gi 2781183762 270 EEDMNRLDKL 279
Cdd:cd19083 297 EEEIAFIDAL 306
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
10-277 |
2.10e-15 |
|
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: 75.33 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 10 NTGATIPAVGLGTWQ--AKAGEVRqavAHAL-----KAGYRHIDGALCY----------QNEEEVGLGIKDSGiPRSEIF 72
Cdd:cd19081 4 RTGLSVSPLCLGTMVfgWTADEET---SFALldafvDAGGNFIDTADVYsawvpgnaggESETIIGRWLKSRG-KRDRVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 73 LTSKVWSSYHDR--------VEECLDTTLKSLQTDYLDLYLIHWPVRLVPngthplfptkpdgsrnldwdwdQAKTWAQM 144
Cdd:cd19081 80 IATKVGFPMGPNgpglsrkhIRRAVEASLRRLQTDYIDLYQAHWDDPATP----------------------LEETLGAL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 145 EDVLKKGKVKAIGLSNAGIPIIEHII----KTGKVTPAALQVELHPYCPQH---ALLKYCKEKGIILEAYSPLGS----- 212
Cdd:cd19081 138 NDLIRQGKVRYIGASNYSAWRLQEALelsrQHGLPRYVSLQPEYNLVDRESfegELLPLCREEGIGVIPYSPLAGgfltg 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 213 --------TSSP-------LHEDPD-------LVAVAKKHNVPTATVLISYQVNRGVV--VLPKSVTPARIESNLK--TI 266
Cdd:cd19081 218 kyrseadlPGSTrrgeaakRYLNERglrildaLDEVAAEHGATPAQVALAWLLARPGVtaPIAGARTVEQLEDLLAaaGL 297
|
330
....*....|.
gi 2781183762 267 KLDEEDMNRLD 277
Cdd:cd19081 298 RLTDEEVARLD 308
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
18-160 |
2.20e-15 |
|
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the prototype of this family. It is an NADP(H)-dependent aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NADP(H) as a hydride donor.
Pssm-ID: 381320 [Multi-domain] Cd Length: 328 Bit Score: 75.68 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 18 VGLGT--W--QAKAGEVRQAVAHALKAGYRHIDGALCY---QNEEEVGLG-------IKDSGiPRSEIFLTSKV------ 77
Cdd:cd19094 4 ICLGTmtWgeQNTEAEAHEQLDYAFDEGVNFIDTAEMYpvpPSPETQGRTeeiigswLKKKG-NRDKVVLATKVagpgeg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 78 --WSSY------HDRVEECLDTTLKSLQTDYLDLYLIHWPVRLVPNgthplfptkpdGSRNLDWDWDQAKTWAQMEDVL- 148
Cdd:cd19094 83 itWPRGggtrldRENIREAVEGSLKRLGTDYIDLYQLHWPDRYTPL-----------FGGGYYTEPSEEEDSVSFEEQLe 151
|
170
....*....|....*...
gi 2781183762 149 ------KKGKVKAIGLSN 160
Cdd:cd19094 152 algelvKAGKIRHIGLSN 169
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-281 |
3.09e-15 |
|
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: 74.68 E-value: 3.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 14 TIPAVGLGTWQAKAG---------------EVRQAVAHALKAGYRHIDGALCY---QNEEEVGLGIKDsgIPRSEIFLTS 75
Cdd:cd19103 3 KLPKIALGTWSWGSGgaggdqvfgnhldedTLKAVFDKAMAAGLNLWDTAAVYgmgASEKILGEFLKR--YPREDYIIST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 76 K----VWSSYHDRVEECLDTTLKSLQTDYLDLYLIHWPVrlvpngthplfptkpDGSRNLdwdwdqaktwAQMEDVLKKG 151
Cdd:cd19103 81 KftpqIAGQSADPVADMLEGSLARLGTDYIDIYWIHNPA---------------DVERWT----------PELIPLLKSG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 152 KVKAIGLSN---AGIPIIEHIIKTGKVTPAALQVE---LHPYCPQHALLKYCKEKGIILEAYSPLG--------STSSPL 217
Cdd:cd19103 136 KVKHVGVSNhnlAEIKRANEILAKAGVSLSAVQNHyslLYRSSEEAGILDYCKENGITFFAYMVLEqgalsgkyDTKHPL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 218 HEDPD------------------LVAVAKKHNVPTATVLISYQVNRGVVVLPKSVTPARIESNLKT--IKLDEEDMNRLD 277
Cdd:cd19103 216 PEGSGraetynpllpqleeltavMAEIGAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAasITLTDDEIKELE 295
|
....
gi 2781183762 278 KLAE 281
Cdd:cd19103 296 QLAD 299
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
16-211 |
9.40e-15 |
|
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: 72.59 E-value: 9.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 16 PAVGLGT------WQAKAGE--VRQAVAHALKAGYRHIDGALCY---QNEEEVGLGIKDsgIPRSEIFLTSK--VWS-SY 81
Cdd:cd19096 1 SVLGFGTmrlpesDDDSIDEekAIEMIRYAIDAGINYFDTAYGYgggKSEEILGEALKE--GPREKFYLATKlpPWSvKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 82 HDRVEECLDTTLKSLQTDYLDLYLIHWPvrlvpngthplfptkpdGSRNLDWDWDQAKTWAQMEDVLKKGKVKAIGLS-N 160
Cdd:cd19096 79 AEDFRRILEESLKRLGVDYIDFYLLHGL-----------------NSPEWLEKARKGGLLEFLEKAKKEGLIRHIGFSfH 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2781183762 161 AGIPIIEHIIKTGKVtpAALQVELH----PYCPQHALLKYCKEKGIILEAYSPLG 211
Cdd:cd19096 142 DSPELLKEILDSYDF--DFVQLQYNyldqENQAGRPGIEYAAKKGMGVIIMEPLK 194
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
18-277 |
9.41e-15 |
|
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: 73.43 E-value: 9.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 18 VGLG----TWQAKAGEVRQAVA---HALKAGYRHIDGALCY--------------------QNEEEVGLGIKDSGIPrse 70
Cdd:cd19077 8 IGLGlmglTWRPNPTPDEEAFEtmkAALDAGSNLWNGGEFYgppdphanlkllarffrkypEYADKVVLSVKGGLDP--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 71 iflTSKVWSSYHDRVEECLDTTLKSL-QTDYLDLYLihwPVRLVPNgtHPLfptkpdgsrnldwdwdqAKTWAQMEDVLK 149
Cdd:cd19077 85 ---DTLRPDGSPEAVRKSIENILRALgGTKKIDIFE---PARVDPN--VPI-----------------EETIKALKELVK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 150 KGKVKAIGLSNAGIPIIEHIIKTGKVtpAALQVELHPYC---PQHALLKYCKEKGIILEAYSPLGS-----TSSPLHEDP 221
Cdd:cd19077 140 EGKIRGIGLSEVSAETIRRAHAVHPI--AAVEVEYSLFSreiEENGVLETCAELGIPIIAYSPLGRglltgRIKSLADIP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 222 D------------------------LVAVAKKHNVPTATVLIS---YQVNRGVVVLPKSVTPARIESNLKT--IKLDEED 272
Cdd:cd19077 218 EgdfrrhldrfngenfeknlklvdaLQELAEKKGCTPAQLALAwilAQSGPKIIPIPGSTTLERVEENLKAanVELTDEE 297
|
....*
gi 2781183762 273 MNRLD 277
Cdd:cd19077 298 LKEIN 302
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
16-271 |
1.04e-14 |
|
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: 72.97 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 16 PAVGLGTWQ----AKAGEVRQAVA---HALKAGYRHIDGALCYQNEEEVgLGIKDSGIPRSEIFLTSKV---------WS 79
Cdd:cd19090 1 SALGLGTAGlggvFGGVDDDEAVAtirAALDLGINYIDTAPAYGDSEER-LGLALAELPREPLVLSTKVgrlpedtadYS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 80 syHDRVEECLDTTLKSLQTDYLDLYLIHWPVRLvpngtHPLFPTKPDGSrnLDwdwdqaktwaQMEDVLKKGKVKAIGLS 159
Cdd:cd19090 80 --ADRVRRSVEESLERLGRDRIDLLMIHDPERV-----PWVDILAPGGA--LE----------ALLELKEEGLIKHIGLG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 160 NAGIPIIEHIIKTGKV-------------TPAALQvelhpycpqhaLLKYCKEKGI-ILEAySPLGS-----------TS 214
Cdd:cd19090 141 GGPPDLLRRAIETGDFdvvltanrytlldQSAADE-----------LLPAAARHGVgVINA-SPLGMgllagrppervRY 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 215 SPLHEDPD-------LVAVAKKHNVPTATVLISYQVN----RGVVVLPKSvtPARIESNLKTIK--LDEE 271
Cdd:cd19090 209 TYRWLSPElldrakrLYELCDEHGVPLPALALRFLLRdpriSTVLVGASS--PEELEQNVAAAEgpLPEE 276
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-182 |
8.13e-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: 381330 [Multi-domain] Cd Length: 321 Bit Score: 70.76 E-value: 8.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 10 NTGATIPAVGLG------TW-QAKAGEVRQAVAHALKAGYRHIDGALCY-QNEEEVGLGIKDSGIPrSEIFLTSKV---- 77
Cdd:cd19104 7 RTGLKVSELTFGgggiggLMgRTTREEQIAAVRRALDLGINFFDTAPSYgDGKSEENLGRALKGLP-AGPYITTKVrldp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 78 --WSSYHDRVEECLDTTLKSLQTDYLDLYLIHwpvrlvpNGTHPLFPTKPDGSRNLDWDWDQAKTWAQMEDVLKKGKVKA 155
Cdd:cd19104 86 ddLGDIGGQIERSVEKSLKRLKRDSVDLLQLH-------NRIGDERDKPVGGTLSTTDVLGLGGVADAFERLRSEGKIRF 158
|
170 180
....*....|....*....|....*...
gi 2781183762 156 IGLSNAG-IPIIEHIIKTGKvtPAALQV 182
Cdd:cd19104 159 IGITGLGnPPAIRELLDSGK--FDAVQV 184
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
10-267 |
2.69e-13 |
|
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: 69.12 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 10 NTGATIPAVGLGT-------WQAKAGEVRQAVAHALKAGYRHIDGALCY-QNEEEVGLGIKDSGIPRSEIFLTSKV---- 77
Cdd:cd19163 8 KTGLKVSKLGFGAsplggvfGPVDEEEAIRTVHEALDSGINYIDTAPWYgQGRSETVLGKALKGIPRDSYYLATKVgryg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 78 ------WSSYHDRVEECLDTTLKSLQTDYLDLYLIHwPVRLVPngthplfptkpdgsrnldwDWDQA--KTWAQMEDVLK 149
Cdd:cd19163 88 ldpdkmFDFSAERITKSVEESLKRLGLDYIDIIQVH-DIEFAP-------------------SLDQIlnETLPALQKLKE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 150 KGKVKAIGLSNAGIPIIEHIIKTgkvTPAALQVELhPYCpqH---------ALLKYCKEKGIILEAYSPLG----STSSP 216
Cdd:cd19163 148 EGKVRFIGITGYPLDVLKEVLER---SPVKIDTVL-SYC--HytlndtsllELLPFFKEKGVGVINASPLSmgllTERGP 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2781183762 217 LHEDP----------DLVAVAKKHNVPTATVLISYQVN--RGVVVLPKSVTPARIESNLKTIK 267
Cdd:cd19163 222 PDWHPaspeikeacaKAAAYCKSRGVDISKLALQFALSnpDIATTLVGTASPENLRKNLEAAE 284
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-277 |
2.75e-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: 381327 [Multi-domain] Cd Length: 304 Bit Score: 69.16 E-value: 2.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 14 TIPAVGLGTWQAKAG--------EVRQAVAHALKAGYRHIDGALCYQNEEE-VGLGIKDSG---------------IPRS 69
Cdd:cd19101 1 TISRVINGMWQLSGGhggirdedAAVRAMAAYVDAGLTTFDCADIYGPAEElIGEFRKRLRrerdaaddvqihtkwVPDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 70 EIFLTSKVWssyhdrVEECLDTTLKSLQTDYLDLYLIHWpvrlvpngthplfptkpdgsrnldWDWDQAK---TWAQMED 146
Cdd:cd19101 81 GELTMTRAY------VEAAIDRSLKRLGVDRLDLVQFHW------------------------WDYSDPGyldAAKHLAE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 147 VLKKGKVKAIGLSNAGIPIIEHIIKTGkVTPAALQVElhpYC-----PQHALLKYCKEKGIILEAYSPLGS--------- 212
Cdd:cd19101 131 LQEEGKIRHLGLTNFDTERLREILDAG-VPIVSNQVQ---YSlldrrPENGMAALCEDHGIKLLAYGTLAGgllsekylg 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 213 TSSPLHEDPD--------------------------LVAVAKKHNVPTATVLISYQVNR----GVVVlpkSVTPAR-IES 261
Cdd:cd19101 207 VPEPTGPALEtrslqkyklmidewggwdlfqellrtLKAIADKHGVSIANVAVRWVLDQpgvaGVIV---GARNSEhIDD 283
|
330
....*....|....*...
gi 2781183762 262 NLK--TIKLDEEDMNRLD 277
Cdd:cd19101 284 NVRafSFRLDDEDRAAID 301
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
12-210 |
4.16e-13 |
|
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: 68.39 E-value: 4.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 12 GATIPAVGLGTWQAKAGEVRQAVAH-----ALKAGYRHIDGALCY---QNEEEVGLGIKdsGIPRSEIFLTSKV-WS--- 79
Cdd:cd19074 1 GLKVSELSLGTWLTFGGQVDDEDAKacvrkAYDLGINFFDTADVYaagQAEEVLGKALK--GWPRESYVISTKVfWPtgp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 80 SYHDR------VEECLDTTLKSLQTDYLDLYLIHwpvrlvpngthplfptKPDGSRNLDwdwdqaKTWAQMEDVLKKGKV 153
Cdd:cd19074 79 GPNDRglsrkhIFESIHASLKRLQLDYVDIYYCH----------------RYDPETPLE------ETVRAMDDLIRQGKI 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2781183762 154 KAIGLSNAGIPIIEH----IIKTGKVTPAALQVELHPYC--PQHALLKYCKEKGIILEAYSPL 210
Cdd:cd19074 137 LYWGTSEWSAEQIAEahdlARQFGLIPPVVEQPQYNMLWreIEEEVIPLCEKNGIGLVVWSPL 199
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
10-279 |
9.99e-13 |
|
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: 67.60 E-value: 9.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 10 NTGATIPAVGLGTW----QAKAGEVRQAVAHALKAGYRHIDGALCYQN---EEEVGLGIKDSgipRSEIFLTSKVWSSYH 82
Cdd:cd19087 8 RTGLKVSRLCLGTMnfggRTDEETSFAIMDRALDAGINFFDTADVYGGgrsEEIIGRWIAGR---RDDIVLATKVFGPMG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 83 DRVEE----------CLDTTLKSLQTDYLDLYLIHWPVRLVPngthplfptkpdgsrnldwdWDQakTWAQMEDVLKKGK 152
Cdd:cd19087 85 DDPNDrglsrrhirrAVEASLRRLQTDYIDLYQMHHFDRDTP--------------------LEE--TLRALDDLVRQGK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 153 VKAIGLSN-AGIPIIEHIIKTGKVTPAALQVELHPY--CPQHA---LLKYCKEKGIILEAYSPLG-------------ST 213
Cdd:cd19087 143 IRYIGVSNfAAWQIAKAQGIAARRGLLRFVSEQPMYnlLKRQAeleILPAARAYGLGVIPYSPLAgglltgkygkgkrPE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 214 SSPLHEDP----------------DLVAVAKKHNVPTATVLISYQVNRGVVVLP--KSVTPARIESNLK--TIKLDEEDM 273
Cdd:cd19087 223 SGRLVERAryqarygleeyrdiaeRFEALAAEAGLTPASLALAWVLSHPAVTSPiiGPRTLEQLEDSLAalEITLTPELL 302
|
....*.
gi 2781183762 274 NRLDKL 279
Cdd:cd19087 303 AEIDEL 308
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
20-277 |
8.84e-12 |
|
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD), are founding members of aldo-keto reductase family 9 member A1-3 (AKR9A1-3), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis. AAD (EC1.1.1.91) is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). The AKR9B family includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381306 [Multi-domain] Cd Length: 307 Bit Score: 64.55 E-value: 8.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 20 LGT------WQAKAG--EVRQAVAHALKAGYRHIDGALCYQN---EEEVGLGIKDSgipRSEIFLTSKVWSSYHD----- 83
Cdd:cd19080 15 LGTmtfgteWGWGADreEARAMFDAYVEAGGNFIDTANNYTNgtsERLLGEFIAGN---RDRIVLATKYTMNRRPgdpna 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 84 --------RVEecLDTTLKSLQTDYLDLYLIHWPVRLVPngthplfptKPDGSRNLDwdwdqaktwaqmeDVLKKGKVKA 155
Cdd:cd19080 92 ggnhrknlRRS--VEASLRRLQTDYIDLLYVHAWDFTTP---------VEEVMRALD-------------DLVRAGKVLY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 156 IGLSNAgiP---------IIEHiikTGKVTPAALQVE--LHPYCPQHALLKYCKEKGIILEAYSPLGS------------ 212
Cdd:cd19080 148 VGISDT--PawvvarantLAEL---RGWSPFVALQIEysLLERTPERELLPMARALGLGVTPWSPLGGglltgkyqrgee 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 213 ----TSSPLHEDPD------------LVAVAKKHNVPTATVLISYQVNRGVVVLP--KSVTPARIESNLK--TIKLDEED 272
Cdd:cd19080 223 gragEAKGVTVGFGklternwaivdvVAAVAEELGRSAAQVALAWVRQKPGVVIPiiGARTLEQLKDNLGalDLTLSPEQ 302
|
....*
gi 2781183762 273 MNRLD 277
Cdd:cd19080 303 LARLD 307
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
15-160 |
5.41e-11 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 62.56 E-value: 5.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 15 IPAVGLGTW----QAKAGEVRQAVAHALKAGYRHIDGALCYQ----------NEEEVGLGIKDSGiPRSEIFLTSKVWSS 80
Cdd:PRK10625 13 VSTLGLGTMtfgeQNSEADAHAQLDYAVAQGINLIDVAEMYPvpprpetqglTETYIGNWLAKRG-SREKLIIASKVSGP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 81 YH------------DR--VEECLDTTLKSLQTDYLDLYLIHWPVRlvpngthplfPTKPDGSRNLDWDWDQA-----KTW 141
Cdd:PRK10625 92 SRnndkgirpnqalDRknIREALHDSLKRLQTDYLDLYQVHWPQR----------PTNCFGKLGYSWTDSAPavsllETL 161
|
170
....*....|....*....
gi 2781183762 142 AQMEDVLKKGKVKAIGLSN 160
Cdd:PRK10625 162 DALAEQQRAGKIRYIGVSN 180
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-204 |
8.44e-11 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 61.39 E-value: 8.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 19 GLGTWQ--------AKAG-----EVRQAVAHALKAGYRHIDGALCYQNEEEVgLGikDSGIPRSEIFLTSKV------WS 79
Cdd:cd19097 4 ALGTAQfgldygiaNKSGkpsekEAKKILEYALKAGINTLDTAPAYGDSEKV-LG--KFLKRLDKFKIITKLpplkedKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 80 SYHDRVEECLDTTLKSLQTDYLDLYLIHWPvrlvpngthplfptkpdgsrnLDWDWDQAKTWAQMEDVLKKGKVKAIGLS 159
Cdd:cd19097 81 EDEAAIEASVEASLKRLKVDSLDGLLLHNP---------------------DDLLKHGGKLVEALLELKKEGLIRKIGVS 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2781183762 160 NAGIPIIEHIIKTGKvtPAALQVelhPY------CPQHALLKYCKEKGIIL 204
Cdd:cd19097 140 VYSPEELEKALESFK--IDIIQL---PFnildqrFLKSGLLAKLKKKGIEI 185
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
4-188 |
9.63e-11 |
|
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: 61.40 E-value: 9.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 4 PTSFKLNTGATIPAVGLGTwqAKAGEVRQA----------VAHALKAGYRHIDGALCYQN---EEEVGLGIKDSGIPRSE 70
Cdd:cd19153 1 FGETLEIALGNVSPVGLGT--AALGGVYGDgleqdeavaiVAEAFAAGINHFDTSPYYGAessEAVLGKALAALQVPRSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 71 IFLTSKVW---SSYHD----RVEECLDTTLKSLQTDYLDLYLIHwPVRLVpngthplfptkpdgsrnlDWDWDQAKTWAQ 143
Cdd:cd19153 79 YTVATKVGryrDSEFDysaeRVRASVATSLERLHTTYLDVVYLH-DIEFV------------------DYDTLVDEALPA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2781183762 144 MEDVLKKGKVKAIGLSNAGIPIIEHIIKtgKVTPAALQVELhPYC 188
Cdd:cd19153 140 LRTLKDEGVIKRIGIAGYPLDTLTRATR--RCSPGSLDAVL-SYC 181
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
16-263 |
1.26e-10 |
|
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: 61.22 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 16 PAVGLGTWQ----AKAGE--VRQAVAHALKAGYRHIDGALCY---QNEEEVGLGIKdsGIPRSEIFLTSKV--------- 77
Cdd:cd19162 1 PRLGLGAASlgnlARAGEdeAAATLDAAWDAGIRYFDTAPLYglgLSERRLGAALA--RHPRAEYVVSTKVgrllepgaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 78 ---------WSSYHDRVEECLDTTLKSLQTDYLDLYLIHwpvrlvpngthplfptkpdgsrNLDWDWDQAKTWAQ--MED 146
Cdd:cd19162 79 grpagadrrFDFSADGIRRSIEASLERLGLDRLDLVFLH----------------------DPDRHLLQALTDAFpaLEE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 147 VLKKGKVKAIGLSNAGIPIIEHIIKTGK---VTPAALQVELHPYcPQHALLKYCKEKGIILEAYSPLGS----TSSPlhe 219
Cdd:cd19162 137 LRAEGVVGAIGVGVTDWAALLRAARRADvdvVMVAGRYTLLDRR-AATELLPLCAAKGVAVVAAGVFNSgilaTDDP--- 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2781183762 220 DPD-----------------LVAVAKKHNVPTATVLISYQVN----RGVVVLPKSvtPARIESNL 263
Cdd:cd19162 213 AGDrydyrpatpevlararrLAAVCRRYGVPLPAAALQFPLRhpavASVVVGAAS--PAELRDNL 275
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
19-212 |
2.66e-10 |
|
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: 60.26 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 19 GLGTW-----QAKAGEVRQAVAHALKAGYRHIDGALCYQNEE-EVGLGIKDSGIPRSEIflTSKVWSSY-----HDRVEE 87
Cdd:cd19075 6 GTMTFgsqgrFTTAEAAAELLDAFLERGHTEIDTARVYPDGTsEELLGELGLGERGFKI--DTKANPGVggglsPENVRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 88 CLDTTLKSLQTDYLDLYLIHWPVRlvpngTHPLfptkpdgsrnldwdwdqAKTWAQMEDVLKKGKVKAIGLSNAGIPIIE 167
Cdd:cd19075 84 QLETSLKRLKVDKVDVFYLHAPDR-----STPL-----------------EETLAAIDELYKEGKFKEFGLSNYSAWEVA 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2781183762 168 HIIKT----GKVTPAALQVELHPYCPQH--ALLKYCKEKGIILEAYSPLGS 212
Cdd:cd19075 142 EIVEIckenGWVLPTVYQGMYNAITRQVetELFPCLRKLGIRFYAYSPLAG 192
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
38-264 |
3.68e-10 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 59.65 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 38 LKAGYRHIDGALCYQ--------NEEEVGLG--IKDSGIpRSEIFLTSKVWSSY--------------HDRVEECLDTTL 93
Cdd:cd19752 27 VAAGGNFLDTANNYAfwteggvgGESERLIGrwLKDRGN-RDDVVIATKVGAGPrdpdggpespeglsAETIEQEIDKSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 94 KSLQTDYLDLYLIHWPVRLVPngthplfptkpdgsrnldwdwdqaktwaqMEDVL-------KKGKVKAIGLSNAgipii 166
Cdd:cd19752 106 RRLGTDYIDLYYAHVDDRDTP-----------------------------LEETLeafnelvKAGKVRAIGASNF----- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 167 eHIIKTGKVTPAALQVELHPYC---PQHA-------------------LLKYCKEKGII-LEAYSPL--GSTSSP----- 216
Cdd:cd19752 152 -AAWRLERARQIARQQGWAEFSaiqQRHSylrprpgadfgvqrivtdeLLDYASSRPDLtLLAYSPLlsGAYTRPdrplp 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2781183762 217 ---LHEDPD-----LVAVAKKHNVPTATVLISYQVNRGVVVLP--KSVTPARIESNLK 264
Cdd:cd19752 231 eqyDGPDSDarlavLEEVAGELGATPNQVVLAWLLHRTPAIIPllGASTVEQLEENLA 288
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
10-274 |
4.47e-10 |
|
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo. Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2). It catalyzes the conversion of 3-hydroxybutanal (3-HB) to 1,3-butanediol (1,3-BDO) by using NADPH as a cofactor.
Pssm-ID: 381315 [Multi-domain] Cd Length: 308 Bit Score: 59.58 E-value: 4.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 10 NTGATIPAVGLGTWQ-----AKAGEVRQAVAHALKAGYRHIDGALCY-----QNEEEVGLGIKDSGIP-RSEIFLTSKV- 77
Cdd:cd19089 6 RSGLHLPAISLGLWHnfgdyTSPEEARELLRTAFDLGITHFDLANNYgpppgSAEENFGRILKRDLRPyRDELVISTKAg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 78 ----------WSSyHDRVEECLDTTLKSLQTDYLDLYLIHwpvRLVPNGthPLfptkpdgsrnldwdwdqAKTWAQMEDV 147
Cdd:cd19089 86 ygmwpgpygdGGS-RKYLLASLDQSLKRMGLDYVDIFYHH---RYDPDT--PL-----------------EETMTALADA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 148 LKKGKVKAIGLSNAGIPIIEHIIKT---GKVTPAALQVELHPYC--PQHALLKYCKEKGIILEAYSPLGS---TSSPLHE 219
Cdd:cd19089 143 VRSGKALYVGISNYPGAKARRAIALlreLGVPLIIHQPRYSLLDrwAEDGLLEVLEEAGIGFIAFSPLAQgllTDKYLNG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 220 DPD--------------------------LVAVAKKHNVPTATVLISYQVNRGVV--VLPKSVTPARIESNLKTIK---L 268
Cdd:cd19089 223 IPPdsrraaeskflteealtpekleqlrkLNKIAAKRGQSLAQLALSWVLRDPRVtsVLIGASSPSQLEDNVAALKnldF 302
|
....*.
gi 2781183762 269 DEEDMN 274
Cdd:cd19089 303 SEEELA 308
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-241 |
1.14e-09 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 58.48 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 14 TIPAVGLGTWQAKAG-----EVRQAVAHALKAGYRHIDGALCYQN---EEEVGLGIK----DSGIPRSEIFLTSKV---- 77
Cdd:cd19099 2 TLSSLGLGTYRGDSDdetdeEYREALKAALDSGINVIDTAINYRGgrsERLIGKALRelieKGGIKRDEVVIVTKAgyip 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 78 ------------------------------WSSYHDR-VEECLDTTLKSLQTDYLDLYLIHWPVRLVPngthplfptkPD 126
Cdd:cd19099 82 gdgdeplrplkyleeklgrglidvadsaglRHCISPAyLEDQIERSLKRLGLDTIDLYLLHNPEEQLL----------EL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 127 GSRNLDWDWDQAktWAQMEDVLKKGKVKAIGLSN-----AGIPIIEHIIKTGKVTPA-----------ALQVELHPYCPQ 190
Cdd:cd19099 152 GEEEFYDRLEEA--FEALEEAVAEGKIRYYGISTwdgfrAPPALPGHLSLEKLVAAAeevggdnhhfkVIQLPLNLLEPE 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2781183762 191 ------------HALLKYCKEKGIILEAYSPLGSTsSPLHEDPDLVAVAKKHNVPTATVLISY 241
Cdd:cd19099 230 altekntvkgeaLSLLEAAKELGLGVIASRPLNQG-QLLGELRLADLLALPGGATLAQRALQF 291
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
8-230 |
5.50e-09 |
|
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: 56.29 E-value: 5.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 8 KLNT-GATIPAVGLG-----TWQAKAGEVRQAVA---HALKAGYRHIDGALCY---QNEEEVGLGIKDSgiPRSEIFLTS 75
Cdd:cd19145 4 KLGSqGLEVSAQGLGcmglsGDYGAPKPEEEGIAlihHAFNSGVTFLDTSDIYgpnTNEVLLGKALKDG--PREKVQLAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 76 KVWSSYHDR-----------VEECLDTTLKSLQTDYLDLYLIHWPVRLVPngthplfptkpdgsrnldwdwdQAKTWAQM 144
Cdd:cd19145 82 KFGIHEIGGsgvevrgdpayVRAACEASLKRLDVDYIDLYYQHRIDTTVP----------------------IEITMGEL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 145 EDVLKKGKVKAIGLSNAGipiIEHIIKTGKVTP-AALQVE--LHPYCPQHALLKYCKEKGIILEAYSPLG----STSSPL 217
Cdd:cd19145 140 KKLVEEGKIKYIGLSEAS---ADTIRRAHAVHPiTAVQLEwsLWTRDIEEEIIPTCRELGIGIVPYSPLGrgffAGKAKL 216
|
250
....*....|...
gi 2781183762 218 HEDPDLVAVAKKH 230
Cdd:cd19145 217 EELLENSDVRKSH 229
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
10-114 |
4.32e-08 |
|
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: 53.75 E-value: 4.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 10 NTGATIPAVGLGTW-----QAKAGEVRQAVAHALKAGYRHIDGALCYQN---EEEVGLGIKDSGIPRSEIFLTSKV-W-- 78
Cdd:cd19143 8 RSGLKVSALSFGSWvtfgnQVDVDEAKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIKELGWPRSDYVVSTKIfWgg 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2781183762 79 ----------SSYHdrVEECLDTTLKSLQTDYLDLYLIHWPVRLVP 114
Cdd:cd19143 88 ggpppndrglSRKH--IVEGTKASLKRLQLDYVDLVFCHRPDPATP 131
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
40-264 |
9.84e-08 |
|
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: 52.56 E-value: 9.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 40 AGYRHIDGALCYQNEEEVG-----LG--IKDSGIpRSEIFLTSK--------VWSS--YHDRVEECLDTTLKSLQTDYLD 102
Cdd:cd19082 29 LGGNFIDTARVYGDWVERGaservIGewLKSRGN-RDKVVIATKgghpdledMSRSrlSPEDIRADLEESLERLGTDYID 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 103 LYLIHwpvRlvPNgthplfPTKPDGSRnLDWdwdqaktwaqMEDVLKKGKVKAIGLSNAGIPIIEHII----KTGKVTPA 178
Cdd:cd19082 108 LYFLH---R--DD------PSVPVGEI-VDT----------LNELVRAGKIRAFGASNWSTERIAEANayakAHGLPGFA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 179 ALQVEL-------HPY------CPQHALLKYCKEKGIILEAYSPLGS------TSSPLHEDPDLVAV------------- 226
Cdd:cd19082 166 ASSPQWslarpnePPWpgptlvAMDEEMRAWHEENQLPVFAYSSQARgffskrAAGGAEDDSELRRVyyseenferlera 245
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2781183762 227 ---AKKHNVPTATVLISYQVNRGVVVLP--KSVTPARIESNLK 264
Cdd:cd19082 246 kelAEEKGVSPTQIALAYVLNQPFPTVPiiGPRTPEQLRDSLA 288
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
11-107 |
4.07e-07 |
|
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: 50.93 E-value: 4.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 11 TGATIPAVGLGTWQAKAGEVRQAVAH-----ALKAGYRHIDGALCYQNEE-EVGLG--IKDSGIPRSEIFLTSKVWSSY- 81
Cdd:cd19142 9 SGLRVSNVGLGTWSTFSTAISEEQAEeivtlAYENGINYFDTSDAFTSGQaETELGriLKKKGWKRSSYIVSTKIYWSYg 88
|
90 100 110
....*....|....*....|....*....|...
gi 2781183762 82 -HDR------VEECLDTTLKSLQTDYLDLYLIH 107
Cdd:cd19142 89 sEERglsrkhIIESVRASLRRLQLDYIDIVIIH 121
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
10-210 |
1.80e-06 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 48.62 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 10 NTGATIPAVGLGTwqAKAGEV---------RQAVAHALKAGYRHIDGALCYQN---EEEVGLGIKDSGIPRSEIFLTSKV 77
Cdd:PLN02587 6 STGLKVSSVGFGA--SPLGSVfgpvseedaIASVREAFRLGINFFDTSPYYGGtlsEKVLGKALKALGIPREKYVVSTKC 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 78 wSSYHD-------RVEECLDTTLKSLQTDYLDLYLIHwpvrlvpngthplfptkpdgsrNLDW-DWDQ--AKTWAQMEDV 147
Cdd:PLN02587 84 -GRYGEgfdfsaeRVTKSVDESLARLQLDYVDILHCH----------------------DIEFgSLDQivNETIPALQKL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2781183762 148 LKKGKVKAIGLSNAGIPIIEHIIKtgKVTPAALQVELhPYCpqH---------ALLKYCKEKGIILEAYSPL 210
Cdd:PLN02587 141 KESGKVRFIGITGLPLAIFTYVLD--RVPPGTVDVIL-SYC--HyslndssleDLLPYLKSKGVGVISASPL 207
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
23-201 |
2.57e-05 |
|
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins; Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis.
Pssm-ID: 381372 [Multi-domain] Cd Length: 326 Bit Score: 45.11 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 23 WQAKAGEVRQAVAHAL-----KAGYRHIDGALCYQNEEE---VGLGIKDSGIpRSEIFLTSKVWSSYHDRVEE------- 87
Cdd:cd19146 25 WKSMMGECDKETAFKLldafyEQGGNFIDTANNYQGEESerwVGEWMASRGN-RDEMVLATKYTTGYRRGGPIkiksnyq 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 88 ---------CLDTTLKSLQTDYLDLYLIHWpvrlvpngthplfptkpdgsrnldWDWDQA--KTWAQMEDVLKKGKVKAI 156
Cdd:cd19146 104 gnhakslrlSVEASLKKLQTSYIDILYVHW------------------------WDYTTSipELMQSLNHLVAAGKVLYL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2781183762 157 GLSNagipiiehiiktgkvTPAALQVELHPYCPQHALLKYCKEKG 201
Cdd:cd19146 160 GVSD---------------TPAWVVSKANAYARAHGLTQFVVYQG 189
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
29-211 |
1.43e-04 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 43.03 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 29 EVRQAVAHALKAGYRHIDGALCYQNEEEV---GLGIKDSGIPRSEIFLTSKV---------WSSyhDRVEECLDTTLKSL 96
Cdd:cd19164 35 PPVDIVRRALELGIRAFDTSPYYGPSEIIlgrALKALRDEFPRDTYFIITKVgrygpddfdYSP--EWIRASVERSLRRL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 97 QTDYLDLYLIHwPVRLVPngthplfptkpdgsrnlDWD-WDQAKTWAQMEDvlkKGKVKAIGLSNAGIPII----EHIIK 171
Cdd:cd19164 113 HTDYLDLVYLH-DVEFVA-----------------DEEvLEALKELFKLKD---EGKIRNVGISGYPLPVLlrlaELART 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2781183762 172 TGKVTPAALQVELHpYCPQH-ALLKY------CKEKGIILEAySPLG 211
Cdd:cd19164 172 TAGRPLDAVLSYCH-YTLQNtTLLAYipkflaAAGVKVVLNA-SPLS 216
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
21-161 |
7.06e-04 |
|
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; Phanerochaete chrysosporium ADD (EC1.1.1.91) is a founding member of aldo-keto reductase family 9 member A3. It is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). This family also includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381373 [Multi-domain] Cd Length: 319 Bit Score: 40.96 E-value: 7.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 21 GTWQAKAGEVRQAVAHAL-----KAGYRHIDGALCYQNEEE---VGLGIKDSGIpRSEIFLTSKVWSSY----------- 81
Cdd:cd19147 22 DAWSGFMGSMDKEQAFELldafyEAGGNFIDTANNYQDEQSetwIGEWMKSRKN-RDQIVIATKFTTDYkayevgkgkav 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 82 -----HDR-VEECLDTTLKSLQTDYLDLYLIHWpvrlvpngthplfptkpdgsrnldWDWDQA--KTWAQMEDVLKKGKV 153
Cdd:cd19147 101 nycgnHKRsLHVSVRDSLRKLQTDWIDILYVHW------------------------WDYTTSieEVMDSLHILVQQGKV 156
|
....*...
gi 2781183762 154 KAIGLSNA 161
Cdd:cd19147 157 LYLGVSDT 164
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
11-109 |
1.18e-03 |
|
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: 40.03 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 11 TGATIPAVGLGTWQAKAGEVRQAVAH-----ALKAGYRHIDGALCY-QNEEEVGLG--IKDSGIPRSEIFLTSKVWSSYH 82
Cdd:cd19159 9 SGLRVSCLGLGTWVTFGGQISDEVAErlmtiAYESGVNLFDTAEVYaAGKAEVILGsiIKKKGWRRSSLVITTKLYWGGK 88
|
90 100 110
....*....|....*....|....*....|....*.
gi 2781183762 83 DRVE---------ECLDTTLKSLQTDYLDLYLIHWP 109
Cdd:cd19159 89 AETErglsrkhiiEGLKGSLQRLQLEYVDVVFANRP 124
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
11-109 |
8.06e-03 |
|
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.
Pssm-ID: 381384 [Multi-domain] Cd Length: 324 Bit Score: 37.37 E-value: 8.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781183762 11 TGATIPAVGLGTWQAKAGEVRQAVAHAL-----KAGYRHIDGALCY-QNEEEVGLG--IKDSGIPRSEIFLTSKVWSSYH 82
Cdd:cd19158 9 SGLRVSCLGLGTWVTFGGQITDEMAEHLmtlayDNGINLFDTAEVYaAGKAEVVLGniIKKKGWRRSSLVITTKIFWGGK 88
|
90 100 110
....*....|....*....|....*....|....*.
gi 2781183762 83 DRVE---------ECLDTTLKSLQTDYLDLYLIHWP 109
Cdd:cd19158 89 AETErglsrkhiiEGLKASLERLQLEYVDVVFANRP 124
|
|
| |
