|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
7-296 |
0e+00 |
|
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: 517.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 7 NSSATLKLNTGASIPVLGFGTWRSVDNNGYHSVIAALKAGYRHIDAAAIYLNEEEVGRAIKDSGVPREEIFITTKLWGTE 86
Cdd:cd19117 1 PSSKTFKLNTGAEIPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIKDSGVPREEIFITTKLWCTW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 87 QRDPEAALNKSLKRLGLDYVDLYLMHWPVPLKTDRVTDGNvlciptLEDGTVDIDTKEWNFIKTWELMQELPKTGKTKAV 166
Cdd:cd19117 81 HRRVEEALDQSLKKLGLDYVDLYLMHWPVPLDPDGNDFLF------KKDDGTKDHEPDWDFIKTWELMQKLPATGKVKAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 167 GVSNFSINNIKELLESPNNKVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFGSANAPLLKEQAIIDMAKKHGVEP 246
Cdd:cd19117 155 GVSNFSIKNLEKLLASPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTNAPLLKEPVIIKIAKKHGKTP 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 6320576 247 AQLIISWSIQRGYVVLAKSVNPERIVSNFKIFTLPEDDFKTISNLSKVHG 296
Cdd:cd19117 235 AQVIISWGLQRGYSVLPKSVTPSRIESNFKLFTLSDEEFKEIDELHKEYG 284
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
20-288 |
7.60e-125 |
|
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: 357.18 E-value: 7.60e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 20 IPVLGFGTWRSVDNNGYHSVIAALKAGYRHIDAAAIYLNEEEVGRAIKDSGVPREEIFITTKLWGTEQR--DPEAALNKS 97
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESGVPREELFITTKLWPTDHGyeRVREALEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 98 LKRLGLDYVDLYLMHWPVPLKTDRVtdgnvlciptledgtvdidtkEWNFIKTWELMQELPKTGKTKAVGVSNFSINNIK 177
Cdd:cd19071 81 LKDLGLDYLDLYLIHWPVPGKEGGS---------------------KEARLETWRALEELVDEGLVRSIGVSNFNVEHLE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 178 ELLESPnnKVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFGSANAPLLKEQAIIDMAKKHGVEPAQLIISWSIQR 257
Cdd:cd19071 140 ELLAAA--RIKPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRRPLLDDPVLKEIAKKYGKTPAQVLLRWALQR 217
|
250 260 270
....*....|....*....|....*....|...
gi 6320576 258 GYVVLAKSVNPERIVSNFKI--FTLPEDDFKTI 288
Cdd:cd19071 218 GVVVIPKSSNPERIKENLDVfdFELSEEDMAAI 250
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
17-293 |
7.70e-125 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 357.44 E-value: 7.70e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 17 GASIPVLGFGTWRSVDNNGYHSVIAALKAGYRHIDAAAIYLNEEEVGRAIKDSGVPREEIFITTKLWGTEQ--RDPEAAL 94
Cdd:COG0656 2 GVEIPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAASGVPREELFVTTKVWNDNHgyDDTLAAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 95 NKSLKRLGLDYVDLYLMHWPVPlktdrvtdgnvlciptledgtvdidtkeWNFIKTWELMQELPKTGKTKAVGVSNFSIN 174
Cdd:COG0656 82 EESLERLGLDYLDLYLIHWPGP----------------------------GPYVETWRALEELYEEGLIRAIGVSNFDPE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 175 NIKELLEspNNKVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFGSANapLLKEQAIIDMAKKHGVEPAQLIISWS 254
Cdd:COG0656 134 HLEELLA--ETGVKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGRGK--LLDDPVLAEIAEKHGKTPAQVVLRWH 209
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 6320576 255 IQRGYVVLAKSVNPERIVSNFKI--FTLPEDDFKTISNLSK 293
Cdd:COG0656 210 LQRGVVVIPKSVTPERIRENLDAfdFELSDEDMAAIDALDR 250
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
13-291 |
6.33e-124 |
|
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: 356.07 E-value: 6.33e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 13 KLNTGASIPVLGFGTWRSVDNNGYHSVIAALKAGYRHIDAAAIYLNEEEVGRAIKDS---GVPREEIFITTKLWGTEQRD 89
Cdd:cd19121 5 KLNTGASIPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAiagGVKREDLFVTTKLWSTYHRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 90 PEAALNKSLKRLGLDYVDLYLMHWPVPLktdrVTDGNVLCIPTLEDGTVDIDtKEWNFIKTWELMQELPKTGKTKAVGVS 169
Cdd:cd19121 85 VELCLDRSLKSLGLDYVDLYLVHWPVLL----NPNGNHDLFPTLPDGSRDLD-WDWNHVDTWKQMEKVLKTGKTKAIGVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 170 NFSINNIKELLesPNNKVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFGSANAPLLKEQAIIDMAKKHGVEPAQL 249
Cdd:cd19121 160 NYSIPYLEELL--KHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTGSPLISDEPVVEIAKKHNVGPGTV 237
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 6320576 250 IISWSIQRGYVVLAKSVNPERIVSNFKIFTLPEDDFKTISNL 291
Cdd:cd19121 238 LISYQVARGAVVLPKSVTPDRIKSNLEIIDLDDEDMNKLNDI 279
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
14-291 |
1.54e-111 |
|
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: 324.75 E-value: 1.54e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 14 LNTGASIPVLGFGTWRSVDNNGYHSVIAALKAGYRHIDAAAIYLNEEEVGRAIKDS-----GVPREEIFITTKLWGTEQR 88
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELlkeepGVKREDLFITSKLWNNSHR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 89 --DPEAALNKSLKRLGLDYVDLYLMHWPVPLKTdrVTDGNVLCIPTLEDGTVDIDTkEWNFIKTWELMQELPKTGKTKAV 166
Cdd:cd19118 81 peYVEPALDDTLKELGLDYLDLYLIHWPVAFKP--TGDLNPLTAVPTNGGEVDLDL-SVSLVDTWKAMVELKKTGKVKSI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 167 GVSNFSINNIKELLESpnNKVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFG--SANAPLLKEQ-AIIDMAKKHG 243
Cdd:cd19118 158 GVSNFSIDHLQAIIEE--TGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGnnLAGLPLLVQHpEVKAIAAKLG 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 6320576 244 VEPAQLIISWSIQRGYVVLAKSVNPERIVSNFKIFTLPEDDFKTISNL 291
Cdd:cd19118 236 KTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFEQVELSDDEFNAVTAL 283
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
12-291 |
2.10e-111 |
|
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: 324.30 E-value: 2.10e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 12 LKLNTGASIPVLGFGTWRSVDNNGYHSVIAALKAGYRHIDAAAIYLNEEEVGRAIKDSG----VPREEIFITTKLWGTEQ 87
Cdd:cd19125 3 FKLNTGAKIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFedgvVKREDLFITSKLWCTDH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 88 rDPEA---ALNKSLKRLGLDYVDLYLMHWPVPLKTDRVTDGNVLCIPTledgtvDIDTkewnfikTWELMQELPKTGKTK 164
Cdd:cd19125 83 -APEDvppALEKTLKDLQLDYLDLYLIHWPVRLKKGAHMPEPEEVLPP------DIPS-------TWKAMEKLVDSGKVR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 165 AVGVSNFSINNIKELLESPnnKVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFGS-----ANAPLLKEQAIIDMA 239
Cdd:cd19125 149 AIGVSNFSVKKLEDLLAVA--RVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSpgttwVKKNVLKDPIVTKVA 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 6320576 240 KKHGVEPAQLIISWSIQRGYVVLAKSVNPERIVSNFKIF--TLPEDDFKTISNL 291
Cdd:cd19125 227 EKLGKTPAQVALRWGLQRGTSVLPKSTNEERIKENIDVFdwSIPEEDFAKFSSI 280
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
9-295 |
2.65e-103 |
|
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a founding member of aldo-keto reductase family 3 member G1 (AKR3G1). It is an aldo/keto reductase that catalyzes the NADPH-dependent reduction of aldehyde- and ketone-groups of different classes of carbonyl compounds to the corresponding alcohols.
Pssm-ID: 381349 [Multi-domain] Cd Length: 297 Bit Score: 304.33 E-value: 2.65e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 9 SATLKLNTGASIPVLGFGTWRSVDNNGYHSVIAALKAGYRHIDAAAIYLNEEEVGRAI----KDSGVPREEIFITTKLWG 84
Cdd:cd19123 1 MKTLPLSNGDLIPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALaevfKEGKVKREDLWITSKLWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 85 TEQrDPEA---ALNKSLKRLGLDYVDLYLMHWPVPLKTDrvtdgnvlcIPTLEDGTVDIDTKEWNFIKTWELMQELPKTG 161
Cdd:cd19123 81 NSH-APEDvlpALEKTLADLQLDYLDLYLMHWPVALKKG---------VGFPESGEDLLSLSPIPLEDTWRAMEELVDKG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 162 KTKAVGVSNFSINNIKELLESPnnKVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFGSANAP----------LLK 231
Cdd:cd19123 151 LCRHIGVSNFSVKKLEDLLATA--RIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDRPaamkaegepvLLE 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6320576 232 EQAIIDMAKKHGVEPAQLIISWSIQRGYVVLAKSVNPERIVSNF--KIFTLPEDDFKTISNLSKVH 295
Cdd:cd19123 229 DPVINKIAEKHGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLeaAEVELDASDMATIAALDRHH 294
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
20-291 |
5.91e-101 |
|
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: 296.85 E-value: 5.91e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 20 IPVLGFGTWRSVDNNGYHSVI-AALKAGYRHIDAAAIYLNEEEVGRAIKDS----GVPREEIFITTKLWGTEQRDPEA-- 92
Cdd:cd19136 1 MPILGLGTFRLRGEEEVRQAVdAALKAGYRLIDTASVYRNEADIGKALRDLlpkyGLSREDIFITSKLAPKDQGYEKAra 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 93 ALNKSLKRLGLDYVDLYLMHWPVPLKTDRVTDGNVLCiptledgtvdidtkewnFIKTWELMQELPKTGKTKAVGVSNFS 172
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWPGVQGLKPSDPRNAEL-----------------RRESWRALEDLYKEGKLRAIGVSNYT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 173 INNIKELLESPnnKVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFGSANAPLLKEQAIIDMAKKHGVEPAQLIIS 252
Cdd:cd19136 144 VRHLEELLKYC--EVPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGDLRLLEDPTVLAIAKKYGRTPAQVLLR 221
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 6320576 253 WSIQRGYVVLAKSVNPERIVSNFKI--FTLPEDDFKTISNL 291
Cdd:cd19136 222 WALQQGIGVIPKSTNPERIAENIKVfdFELSEEDMAELNAL 262
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
12-291 |
1.76e-100 |
|
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: 295.25 E-value: 1.76e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 12 LKLNTGASIPVLGFGTWR-SVDNNGYHSVIAALKAGYRHIDAAAIYLNEEEVGRAIKDSGVPREEIFITTKLW--GTEQR 88
Cdd:cd19133 1 VTLNNGVEMPILGFGVFQiPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKSGIPREELFITTKLWiqDAGYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 89 DPEAALNKSLKRLGLDYVDLYLMHWPVplktdrvtdGNVLCiptledgtvdidtkewnfikTWELMQELPKTGKTKAVGV 168
Cdd:cd19133 81 KAKKAFERSLKRLGLDYLDLYLIHQPF---------GDVYG--------------------AWRAMEELYKEGKIRAIGV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 169 SNFSINNIKELLesPNNKVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFGSANAPLLKEQAIIDMAKKHGVEPAQ 248
Cdd:cd19133 132 SNFYPDRLVDLI--LHNEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAEGRNNLFENPVLTEIAEKYGKSVAQ 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 6320576 249 LIISWSIQRGYVVLAKSVNPERIVSNFKI--FTLPEDDFKTISNL 291
Cdd:cd19133 210 VILRWLIQRGIVVIPKSVRPERIAENFDIfdFELSDEDMEAIAAL 254
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
11-291 |
2.53e-100 |
|
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: 295.05 E-value: 2.53e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 11 TLKLNTGASIPVLGFGTWRSVDNNGYHSVIAALKAGYRHIDAAAIYLNEEEVGRAIKDSGVPREEIFITTKLWGTEQR-- 88
Cdd:cd19131 1 TITLNDGNTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRASGVPREELFITTKLWNSDQGyd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 89 DPEAALNKSLKRLGLDYVDLYLMHWPVPLKtDRvtdgnvlciptledgtvdidtkewnFIKTWELMQELPKTGKTKAVGV 168
Cdd:cd19131 81 STLRAFDESLRKLGLDYVDLYLIHWPVPAQ-DK-------------------------YVETWKALIELKKEGRVKSIGV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 169 SNFSINNIKELLESpnNKVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFGSANapLLKEQAIIDMAKKHGVEPAQ 248
Cdd:cd19131 135 SNFTIEHLQRLIDE--TGVVPVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGG--LLSDPVIGEIAEKHGKTPAQ 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 6320576 249 LIISWSIQRGYVVLAKSVNPERIVSNFKI--FTLPEDDFKTISNL 291
Cdd:cd19131 211 VVIRWHLQNGLVVIPKSVTPSRIAENFDVfdFELDADDMQAIAGL 255
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
14-293 |
1.17e-99 |
|
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: 295.06 E-value: 1.17e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 14 LNTGASIPVLGFGTWRSVDNNGYHSVIAALKAGYRHIDAAAIYLNEEEVGRAIK-----DSGVPREEIFITTKLWGTEQR 88
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKekvgpGKAVPREDLFVTSKLWNTKHH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 89 --DPEAALNKSLKRLGLDYVDLYLMHWPVPLKTDrvtDGNvlcIPTLEDGTV---DIDTKEwnfikTWELMQELPKTGKT 163
Cdd:cd19106 81 peDVEPALRKTLKDLQLDYLDLYLIHWPYAFERG---DNP---FPKNPDGTIrydSTHYKE-----TWKAMEKLVDKGLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 164 KAVGVSNFSINNIKELLEspNNKVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFGSANAP--------LLKEQAI 235
Cdd:cd19106 150 KAIGLSNFNSRQIDDILS--VARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPDRPwakpdepvLLEEPKV 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 236 IDMAKKHGVEPAQLIISWSIQRGYVVLAKSVNPERIVSNFKI--FTLPEDDFKTISNLSK 293
Cdd:cd19106 228 KALAKKYNKSPAQILLRWQVQRGVVVIPKSVTPSRIKQNIQVfdFTLSPEEMKQLDALNR 287
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
11-301 |
1.36e-99 |
|
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: 294.58 E-value: 1.36e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 11 TLKLNTGASIPVLGFGTWRSVDN-NGYHSVIAALKAGYRHIDAAAIYLNEEEVGRA----IKDSGVPREEIFITTKLWGT 85
Cdd:cd19116 2 TIKLNDGNEIPAIALGTWKLKDDeGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAirekIAEGVVKREDLFITTKLWNS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 86 --EQRDPEAALNKSLKRLGLDYVDLYLMHWPVPLKTdrvtdgNVLCIPTLEDGTVDIDtkewnFIKTWELMQELPKTGKT 163
Cdd:cd19116 82 yhEREQVEPALRESLKRLGLDYVDLYLIHWPVAFKE------NNDSESNGDGSLSDID-----YLETWRGMEDLVKLGLT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 164 KAVGVSNFSINNIKELLEspNNKVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFGSANA-------PLLKEQAII 236
Cdd:cd19116 151 RSIGVSNFNSEQINRLLS--NCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLVPrgqtnppPRLDDPTLV 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6320576 237 DMAKKHGVEPAQLIISWSIQRGYVVLAKSVNPERIVSNFKI--FTLPEDDFKTISNLskvHGTKRVV 301
Cdd:cd19116 229 AIAKKYGKTTAQIVLRYLIDRGVVPIPKSSNKKRIKENIDIfdFQLTPEEVAALNSF---NTNQRVY 292
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
12-291 |
1.19e-97 |
|
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: 288.18 E-value: 1.19e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 12 LKLNTGASIPVLGFGTWRSVDNN-GYHSVIAALKAGYRHIDAAAIYLNEEEVGRAIKDSGVPREEIFITTKLWGTEQRD- 89
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQTPDGDeTERAVQTALENGYRSIDTAAIYKNEEGVGEAIRESGVPREELFVTTKLWNDDQRAr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 90 -PEAALNKSLKRLGLDYVDLYLMHWPVPLKtdrvtdgnvlciptledgtvdidtkewnFIKTWELMQELPKTGKTKAVGV 168
Cdd:cd19126 81 rTEDAFQESLDRLGLDYVDLYLIHWPGKDK----------------------------FIDTWKALEKLYASGKVKAIGV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 169 SNFSINNIKELLESPNnkVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFGSANapLLKEQAIIDMAKKHGVEPAQ 248
Cdd:cd19126 133 SNFQEHHLEELLAHAD--VVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQGG--LLSNPVLAAIGEKYGKSAAQ 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 6320576 249 LIISWSIQRGYVVLAKSVNPERIVSNFKI--FTLPEDDFKTISNL 291
Cdd:cd19126 209 VVLRWDIQHGVVTIPKSVHASRIKENADIfdFELSEDDMTAIDAL 253
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
9-299 |
2.76e-97 |
|
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: 288.63 E-value: 2.76e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 9 SATLKLNTGASIPVLGFGTWRSVDNNGY--HSVIAALKAGYRHIDAAAIYLNEEEVGRAIK----DSGVPREEIFITTKL 82
Cdd:cd19119 1 EISFKLNTGASIPALGLGTASPHEDRAEvkEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKraidDGSIKREELFITTKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 83 WGTEQRDPEAALNKSLKRLGLDYVDLYLMHWPVPLKTDRVTDGNVLcIPTLEDGTVDIDtKEWNFIKTWELMQELPKTGK 162
Cdd:cd19119 81 WPTFYDEVERSLDESLKALGLDYVDLLLVHWPVCFEKDSDDSGKPF-TPVNDDGKTRYA-ASGDHITTYKQLEKIYLDGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 163 TKAVGVSNFSINNIKELLESPnnKVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFGSANAPLLKEQAIIDMAKKH 242
Cdd:cd19119 159 AKAIGVSNYSIVYLERLIKEC--KVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAPNLKNPLVKKIAEKY 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 6320576 243 GVEPAQLIISWSIQRGYVVLAKSVNPERIVSNFKIFTLPEDDFKTISNLSKVHGTKR 299
Cdd:cd19119 237 NVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKIVSLTKEDLQKLDDIGEKYPVRF 293
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
14-292 |
1.54e-92 |
|
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: 275.30 E-value: 1.54e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 14 LNTGASIPVLGFGTWRSVDNNGYHSVIAALKAGYRHIDAAAIYLNEEEVGRAIKDSGVPREEIFITTKLWGTEQRDPEA- 92
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRRSGVPREELFVTTKLPGRHHGYEEAl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 93 -ALNKSLKRLGLDYVDLYLMHWPVPlKTDRvtdgnvlciptledgtvdidtkewnFIKTWELMQELPKTGKTKAVGVSNF 171
Cdd:cd19132 81 rTIEESLYRLGLDYVDLYLIHWPNP-SRDL-------------------------YVEAWQALIEAREEGLVRSIGVSNF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 172 SINNIKELLESPNnkVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFGSANApLLKEQAIIDMAKKHGVEPAQLII 251
Cdd:cd19132 135 LPEHLDRLIDETG--VTPAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLGRGSG-LLDEPVIKAIAEKHGKTPAQVVL 211
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 6320576 252 SWSIQRGYVVLAKSVNPERIVSNFKI--FTLPEDDFKTISNLS 292
Cdd:cd19132 212 RWHVQLGVVPIPKSANPERQRENLAIfdFELSDEDMAAIAALD 254
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
10-292 |
1.95e-92 |
|
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: 275.36 E-value: 1.95e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 10 ATLKLNTGASIPVLGFGTWRSvdnNGY-HS-VIAALK-AGYRHIDAAAIYLNEEEVGRAIKDSGVPREEIFITTKLWGTE 86
Cdd:cd19135 3 PTVRLSNGVEMPILGLGTSHS---GGYsHEaVVYALKeCGYRHIDTAKRYGCEELLGKAIKESGVPREDLFLTTKLWPSD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 87 QRDPEA--ALNKSLKRLGLDYVDLYLMHWPvplktdrvtdgnvlciptleDGTVDIDTKEWNFIKTWELMQELPKTGKTK 164
Cdd:cd19135 80 YGYESTkqAFEASLKRLGVDYLDLYLLHWP--------------------DCPSSGKNVKETRAETWRALEELYDEGLCR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 165 AVGVSNFSINNIKELLESPNnkVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFgsANAPLLKEQAIIDMAKKHGV 244
Cdd:cd19135 140 AIGVSNFLIEHLEQLLEDCS--VVPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPL--AKGKALEEPTVTELAKKYQK 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 6320576 245 EPAQLIISWSIQRGYVVLAKSVNPERIVSNFKI--FTLPEDDFKTISNLS 292
Cdd:cd19135 216 TPAQILIRWSIQNGVVTIPKSTKEERIKENCQVfdFSLSEEDMATLDSLH 265
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
12-295 |
5.66e-92 |
|
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: 274.40 E-value: 5.66e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 12 LKLNTGASIPVLGFGTWRSVDNN-GYHSVIAALKAGYRHIDAAAIYLNEEEVGRAIKDSGVPREEIFITTKLWGTEQ--R 88
Cdd:cd19156 1 VKLANGVEMPRLGLGVWRVQDGAeAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRESGVPREEVFVTTKLWNSDQgyE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 89 DPEAALNKSLKRLGLDYVDLYLMHWPVPLKtdrvtdgnvlciptledgtvdidtkewnFIKTWELMQELPKTGKTKAVGV 168
Cdd:cd19156 81 STLAAFEESLEKLGLDYVDLYLIHWPVKGK----------------------------FKDTWKAFEKLYKEKKVRAIGV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 169 SNFSINNIKELLESPnnKVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFGSANapLLKEQAIIDMAKKHGVEPAQ 248
Cdd:cd19156 133 SNFHEHHLEELLKSC--KVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGK--LLSNPVLKAIGKKYGKSAAQ 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 6320576 249 LIISWSIQRGYVVLAKSVNPERIVSNFKI--FTLPEDDFKTISNLSKVH 295
Cdd:cd19156 209 VIIRWDIQHGIITIPKSVHEERIQENFDVfdFELTAEEIRQIDGLNTDH 257
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
11-295 |
1.22e-90 |
|
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: 270.80 E-value: 1.22e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 11 TLKLNTGASIPVLGFGTWRSVDNN-GYHSVIAALKAGYRHIDAAAIYLNEEEVGRAIKDSGVPREEIFITTKLWGTEQRD 89
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEEGSeVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKESGIPREELFITSKVWNADQGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 90 PE--AALNKSLKRLGLDYVDLYLMHWPVPLKtdrvtdgnvlciptledgtvdidtkewnFIKTWELMQELPKTGKTKAVG 167
Cdd:cd19157 81 DStlKAFEASLERLGLDYLDLYLIHWPVKGK----------------------------YKETWKALEKLYKDGRVRAIG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 168 VSNFSINNIKELLESPnnKVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFGSANapLLKEQAIIDMAKKHGVEPA 247
Cdd:cd19157 133 VSNFQVHHLEDLLADA--EIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQ--LLDNPVLKEIAEKYNKSVA 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 6320576 248 QLIISWSIQRGYVVLAKSVNPERIVSNFKI--FTLPEDDFKTISNLSKVH 295
Cdd:cd19157 209 QVILRWDLQNGVVTIPKSIKEHRIIENADVfdFELSQEDMDKIDALNENL 258
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
11-293 |
1.62e-90 |
|
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: 271.80 E-value: 1.62e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 11 TLKLNTGASIPVLGFGTWRSVDNNGYHSVIA---ALKAGYRHIDAAAIYLNEEEVGRAI----KDSGVPREEIFITTKLW 83
Cdd:cd19108 2 RVKLNDGHFIPVLGFGTYAPEEVPKSKALEAtklAIDAGFRHIDSAYLYQNEEEVGQAIrskiADGTVKREDIFYTSKLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 84 GTEQRdPE---AALNKSLKRLGLDYVDLYLMHWPVPLKTdrvtdGNVLcIPTLEDGTVDIDTKEwnFIKTWELMQELPKT 160
Cdd:cd19108 82 CTFHR-PElvrPALEKSLKKLQLDYVDLYLIHFPVALKP-----GEEL-FPKDENGKLIFDTVD--LCATWEAMEKCKDA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 161 GKTKAVGVSNFSINNIKELLESPNNKVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFGS--------ANAPLLKE 232
Cdd:cd19108 153 GLAKSIGVSNFNRRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSqrdkewvdQNSPVLLE 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6320576 233 QAII-DMAKKHGVEPAQLIISWSIQRGYVVLAKSVNPERIVSNFKI--FTLPEDDFKTISNLSK 293
Cdd:cd19108 233 DPVLcALAKKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVfeFQLTSEDMKALDGLNR 296
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
9-293 |
1.79e-88 |
|
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: 266.59 E-value: 1.79e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 9 SATLKLNTGASIPVLGFGTWRSVDNNGYHSVIAALKAGYRHIDAAAIYLNEEEVGRAIKD---SGV-PREEIFITTKLWG 84
Cdd:cd19154 1 SASITLSNGVKMPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAElleEGVvKREDLFITTKLWT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 85 TEQR--DPEAALNKSLKRLGLDYVDLYLMHWPVPLKTDrvtDGNVLCIPTLEDGTVDIDtkewnFIKTWELMQELPKTGK 162
Cdd:cd19154 81 HEHApeDVEEALRESLKKLQLEYVDLYLIHAPAAFKDD---EGESGTMENGMSIHDAVD-----VEDVWRGMEKVYDEGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 163 TKAVGVSNFSINNIKELLEspNNKVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFGS---ANAP----------L 229
Cdd:cd19154 153 TKAIGVSNFNNDQIQRILD--NARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSpgrANFTkstgvspapnL 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6320576 230 LKEQAIIDMAKKHGVEPAQLIISWSIQRGYVVLAKSVNPERIVSNFKI--FTLPEDDFKTISNLSK 293
Cdd:cd19154 231 LQDPIVKAIAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIfdFSLSEEDMATLEEIEK 296
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
20-288 |
1.56e-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: 262.21 E-value: 1.56e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 20 IPVLGFGTWRSVDNNGYHSVIAALKAGYRHIDAAAIYLNEEEVGRAIKDSGVPREEIFITTKLWGTEQRDP--EAALNKS 97
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAESGVPREDLFITTKVWRDHLRPEdlKKSVDRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 98 LKRLGLDYVDLYLMHWPVPlktdrvtdgnvlciptledgTVDIDtkewnfiKTWELMQELPKTGKTKAVGVSNFSINNIK 177
Cdd:cd19073 81 LEKLGTDYVDLLLIHWPNP--------------------TVPLE-------ETLGALKELKEAGKVKSIGVSNFTIELLE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 178 ELLESPNnkVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFgsANAPLLKEQAIIDMAKKHGVEPAQLIISWSIQR 257
Cdd:cd19073 134 EALDISP--LPIAVNQVEFHPFLYQAELLEYCRENDIVITAYSPL--ARGEVLRDPVIQEIAEKYDKTPAQVALRWLVQK 209
|
250 260 270
....*....|....*....|....*....|...
gi 6320576 258 GYVVLAKSVNPERIVSNFKIF--TLPEDDFKTI 288
Cdd:cd19073 210 GIVVIPKASSEDHLKENLAIFdwELTSEDVAKI 242
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
17-307 |
1.25e-86 |
|
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase (AR, EC 1.1.1.21) from Homo sapiens (AKR1B1), Oryctolagus cuniculus (kidney, AKR1B2), Mus musculus (AKR1B3), Rattus norvegicus (lens, AKR1B4), Bos taurus (lens/testis, AKR1B5), and Sus scrofa (lens, AKR1B6), aldose reductase-related protein 1 (ALD1, EC1.1.1.21) from Mus musculus (AKR1B7), Rattus norvegicus (AKR1B14), and Homo sapiens (AKR1B15), Mus musculus fibroblast growth factor induced protein (FR-1 or AKR1B8, EC 1.1.1.21), Cricetulus griseus aldose reductase-related protein 2 (ALD2 or AKR1B9, EC 1.1.1.21), aldose reductase-like from Homo sapiens (ARL-1 or AKR1B10) and Rattus norvegicus (AKR1B13), aldo-keto reductase from Gallus domesticus (eye, tongue, esophagus, AKR1B12), and Oryctolagus cuniculus AR-like protein (3beta-HSD, AKR1B19). AR, also called aldehyde reductase, catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. ALD1 reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. It may play a role in the metabolism of xenobiotic aromatic aldehydes. FR-1, also called aldose reductase-related protein 2, or fibroblast growth factor-regulated protein (FGFRP), is induced by fibroblast growth factor-1. It may play a role in the regulation of the cell cycle. FR-1 belongs to the NADPH-dependent aldo-keto reductase family. ALD2 is an inducible aldo-keto reductase with a preference for aliphatic substrates. It can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. ARL-1, also called aldose reductase-like, or aldose reductase-related protein (ARP), or small intestine reductase, or SI reductase, acts as all-trans-retinaldehyde reductase that can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). It may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. AKR1B15, also called estradiol 17-beta-dehydrogenase AKR1B15, is a mitochondrial aldo-keto reductase that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. It has a strong selectivity towards NADP(H). AKR1B19 is aldose reductase-like that may show 3-beta-hydroxysteroid dehydrogenase (3beta-HSD) activity.
Pssm-ID: 381333 [Multi-domain] Cd Length: 307 Bit Score: 261.97 E-value: 1.25e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 17 GASIPVLGFGTWRSVDNNGYHSVIAALKAGYRHIDAAAIYLNEEEVGRAI----KDSGVPREEIFITTKLWGT--EQRDP 90
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIqekiKEQVVKREDLFIVSKLWCTfhEKGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 91 EAALNKSLKRLGLDYVDLYLMHWPVPLKTdrvtdGNVLcIPTLEDGTVDidTKEWNFIKTWELMQELPKTGKTKAVGVSN 170
Cdd:cd19107 81 KGACQKTLSDLKLDYLDLYLIHWPTGFKP-----GKEL-FPLDESGNVI--PSDTTFLDTWEAMEELVDEGLVKAIGVSN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 171 FSINNIKELLESPNNKVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFGSANAP--------LLKEQAIIDMAKKH 242
Cdd:cd19107 153 FNHLQIERILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPwakpedpsLLEDPKIKEIAAKH 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6320576 243 GVEPAQLIISWSIQRGYVVLAKSVNPERIVSNFKI--FTLPEDDFKTISNLSKvhgTKRVVDMKWGS 307
Cdd:cd19107 233 NKTTAQVLIRFPIQRNLVVIPKSVTPERIAENFKVfdFELSSEDMATILSFNR---NWRACALLSCS 296
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
12-293 |
3.46e-86 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 260.00 E-value: 3.46e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 12 LKLNTGASIPVLGFGTWRSVDNNGYHSVIAALKAGYRHIDAAAIYLNEEEVGRAIKDSGVPREEIFITTKLWGTEQRDPE 91
Cdd:PRK11565 7 IKLQDGNVMPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKEASVAREELFITTKLWNDDHKRPR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 92 AALNKSLKRLGLDYVDLYLMHWPVPLKTdrvtdgnvlciptledgtvdidtkewNFIKTWELMQELPKTGKTKAVGVSNF 171
Cdd:PRK11565 87 EALEESLKKLQLDYVDLYLMHWPVPAID--------------------------HYVEAWKGMIELQKEGLIKSIGVCNF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 172 SINNIKELLESPNnkVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFGSANAPLLKEQAIIDMAKKHGVEPAQLII 251
Cdd:PRK11565 141 QIHHLQRLIDETG--VTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGKGVFDQKVIRDLADKYGKTPAQIVI 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 6320576 252 SWSIQRGYVVLAKSVNPERIVSNFKI--FTLPEDDFKTISNLSK 293
Cdd:PRK11565 219 RWHLDSGLVVIPKSVTPSRIAENFDVfdFRLDKDELGEIAKLDQ 262
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
17-296 |
1.03e-85 |
|
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: 258.32 E-value: 1.03e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 17 GASIPVLGFGT---WRSVDNNGYH-----SVIAALKAGYRHIDAAAIYLNEEEVGRAIKDSGVPREEIFITTKlWGTEQR 88
Cdd:cd19120 1 GSKIPAIAFGTgtaWYKSGDDDIQrdlvdSVKLALKAGFRHIDTAEMYGNEKEVGEALKESGVPREDLFITTK-VSPGIK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 89 DPEAALNKSLKRLGLDYVDLYLMHWPvplktdrvtdgnvlciPTLEDGTVDIDTkewnfikTWELMQELPKTGKTKAVGV 168
Cdd:cd19120 80 DPREALRKSLAKLGVDYVDLYLIHSP----------------FFAKEGGPTLAE-------AWAELEALKDAGLVRSIGV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 169 SNFSINNIKELLESpnNKVVPATNQIEIHPLL--PQDELIAFCKEKGIVVEAYSPFGS--ANAPLLKEQAIIDMAKKHGV 244
Cdd:cd19120 137 SNFRIEDLEELLDT--AKIKPAVNQIEFHPYLypQQPALLEYCREHGIVVSAYSPLSPltRDAGGPLDPVLEKIAEKYGV 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 6320576 245 EPAQLIISWSIQRGYVVLAKSVNPERIVS--NFKIFTLPEDDFKTISNLSKVHG 296
Cdd:cd19120 215 TPAQVLLRWALQKGIVVVTTSSKEERMKEylEAFDFELTEEEVEEIDKAGKQKH 268
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
12-291 |
1.56e-85 |
|
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: 258.11 E-value: 1.56e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 12 LKLNTGASIPVLGFGTWRSVDNNGYHSVIAALKAGYRHIDAAAIYLNEEEVGRAIKDSGVPREEIFITTKLWGTEQRDPE 91
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRSGVDRSDIFVTTKLWISDYGYDK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 92 A--ALNKSLKRLGLDYVDLYLMHWPVPLKTDRVtdgnvlciptledgtvdidtkewnfIKTWELMQELPKTGKTKAVGVS 169
Cdd:cd19127 81 AlrGFDASLRRLGLDYVDLYLLHWPVPNDFDRT-------------------------IQAYKALEKLLAEGRVRAIGVS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 170 NFSINNIKELLESPNnkVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFG----------SANAPLLKEQAIIDMA 239
Cdd:cd19127 136 NFTPEHLERLIDATT--VVPAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGgvmrygasgpTGPGDVLQDPTITGLA 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 6320576 240 KKHGVEPAQLIISWSIQRGYVVLAKSVNPERIVSNFKI--FTLPEDDFKTISNL 291
Cdd:cd19127 214 EKYGKTPAQIVLRWHLQNGVSAIPKSVHPERIAENIDIfdFALSAEDMAAIDAL 267
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
17-291 |
1.71e-83 |
|
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: 252.18 E-value: 1.71e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 17 GASIPVLGFGTWRSVDNNGYHSVIAALKAGYRHIDAAAIYLNEEEVGRAIKDSGVPREEIFITTKLWGTEQRDP--EAAL 94
Cdd:cd19140 5 GVRIPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIAASGVPRDELFLTTKVWPDNYSPDdfLASV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 95 NKSLKRLGLDYVDLYLMHWPVPlktdrvtdgnvlciptledgtvDIDTKEwnfikTWELMQELPKTGKTKAVGVSNFSIN 174
Cdd:cd19140 85 EESLRKLRTDYVDLLLLHWPNK----------------------DVPLAE-----TLGALNEAQEAGLARHIGVSNFTVA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 175 NIKELLESPNNKVVpaTNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFgsANAPLLKEQAIIDMAKKHGVEPAQLIISWS 254
Cdd:cd19140 138 LLREAVELSEAPLF--TNQVEYHPYLDQRKLLDAAREHGIALTAYSPL--ARGEVLKDPVLQEIGRKHGKTPAQVALRWL 213
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 6320576 255 IQR-GYVVLAKSVNPERIVSNFKI--FTLPEDDFKTISNL 291
Cdd:cd19140 214 LQQeGVAAIPKATNPERLEENLDIfdFTLSDEEMARIAAL 253
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
11-291 |
6.80e-80 |
|
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: 243.22 E-value: 6.80e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 11 TLKLNTGASIPVLGFGTWRSVDNNGYHSVIAALKAGYRHIDAAAIYLNEEEVGRAIKDSGVPREEIFITTKLWGTEQ--R 88
Cdd:cd19134 2 TVTLNDDNTMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAASGIPRGELFVTTKLATPDQgfT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 89 DPEAALNKSLKRLGLDYVDLYLMHWPVPlktdrvtdgnvlciptledgtvdidtKEWNFIKTWELMQELPKTGKTKAVGV 168
Cdd:cd19134 82 ASQAACRASLERLGLDYVDLYLIHWPAG--------------------------REGKYVDSWGGLMKLREEGLARSIGV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 169 SNFSINNIKELLEspNNKVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFGSANapLLKEQAIIDMAKKHGVEPAQ 248
Cdd:cd19134 136 SNFTAEHLENLID--LTFFTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGR--LLDNPAVTAIAAAHGRTPAQ 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 6320576 249 LIISWSIQRGYVVLAKSVNPERIVSNFKI--FTLPEDDFKTISNL 291
Cdd:cd19134 212 VLLRWSLQLGNVVISRSSNPERIASNLDVfdFELTADHMDALDGL 256
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
13-293 |
7.86e-80 |
|
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis.
Pssm-ID: 381348 [Multi-domain] Cd Length: 291 Bit Score: 244.07 E-value: 7.86e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 13 KLNTGASIPVLGFGTWRSVDNNG--YHSVIAALKAGYRHIDAAAIYLNEEEVGRAIKD-----SGVPREEIFITTKLWGT 85
Cdd:cd19122 2 TLNNGVKIPAVGFGTFANEGAKGetYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDflkenPSVKREDLFICTKVWNH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 86 --EQRDPEAALNKSLKRLGLDYVDLYLMHWPVplktdrVTDGNVLCIPTL-EDGTVDI--DTKEwNFIKTWELMQELPKT 160
Cdd:cd19122 82 lhEPEDVKWSIDNSLKNLKLDYIDLFLVHWPI------AAEKNDQRSPKLgPDGKYVIlkDLTE-NPEPTWRAMEEIYES 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 161 GKTKAVGVSNFSINNIKELLESPnnKVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFGSANA-----------PL 229
Cdd:cd19122 155 GKAKAIGVSNWTIPGLKKLLSFA--KVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQvpstgervsenPT 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6320576 230 LKEqaiidMAKKHGVEPAQLIISWSIQRGYVVLAKSVNPERIVSNFKIFTLPEDDFKTISNLSK 293
Cdd:cd19122 233 LNE-----VAEKGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIELSDEDFEAINQVAK 291
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
10-298 |
4.29e-78 |
|
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: 240.47 E-value: 4.29e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 10 ATLKLNTGASIPVLGFGTWRSVDNNGYHSVIAALKAGYRHIDAAAIYLNEEEVGRAIK---DSG-VPREEIFITTKLWGT 85
Cdd:cd19112 1 STITLNSGHKMPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAeafKTGlVKREDLFITTKLWNS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 86 EQRD-PEAALNkSLKRLGLDYVDLYLMHWPVPLKTDRV-TDGNVLCiptlEDGTVDIDTkEWNFIKTWELMQELPKTGKT 163
Cdd:cd19112 81 DHGHvIEACKD-SLKKLQLDYLDLYLVHFPVATKHTGVgTTGSALG----EDGVLDIDV-TISLETTWHAMEKLVSAGLV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 164 KAVGVSNFSINNIKELLESpnNKVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFGSANAPL--------LKEQAI 235
Cdd:cd19112 155 RSIGISNYDIFLTRDCLAY--SKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGGAAANAewfgsvspLDDPVL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6320576 236 IDMAKKHGVEPAQLIISWSIQRGYVVLAKSVNPERIVSNFKI--FTLPEDDFKTISNLSKVHGTK 298
Cdd:cd19112 233 KDLAKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVfdFQLSKEDMKLIKSLDRKYRTN 297
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
16-291 |
5.28e-78 |
|
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: 239.09 E-value: 5.28e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 16 TGASIPVLGFGTwrSVDNNGYHS----VIAALKAGYRHIDAAAIYLNEEEVGRAIK---DSGV--PREEIFITTKLWGTE 86
Cdd:cd19124 1 SGQTMPVIGMGT--ASDPPSPEDikaaVLEAIEVGYRHFDTAAAYGTEEALGEALAealRLGLvkSRDELFVTSKLWCSD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 87 --QRDPEAALNKSLKRLGLDYVDLYLMHWPVPLKTDRVTdgnvlcIPTLEDGTVDIDTKEwnfikTWELMQELPKTGKTK 164
Cdd:cd19124 79 ahPDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKPGKFS------FPIEEEDFLPFDIKG-----VWEAMEECQRLGLTK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 165 AVGVSNFSINNIKELLEspNNKVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFGSANAP-----LLKEQAIIDMA 239
Cdd:cd19124 148 AIGVSNFSCKKLQELLS--FATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTKwgsnaVMESDVLKEIA 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 6320576 240 KKHGVEPAQLIISWSIQRGYVVLAKSVNPERIVSNFKIF--TLPEDDFKTISNL 291
Cdd:cd19124 226 AAKGKTVAQVSLRWVYEQGVSLVVKSFNKERMKQNLDIFdwELTEEDLEKISEI 279
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
8-293 |
1.04e-77 |
|
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: 239.63 E-value: 1.04e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 8 SSATLKLNTGASIPVLGFGTWRSVDNNGYHSVIAALKAGYRHIDAAAIYLNEEEVG----RAIKDSGVPREEIFITTKLW 83
Cdd:cd19115 1 ASPTVKLNSGYDMPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGqgvaRAIKEGIVKREDLFIVSKLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 84 GT--EQRDPEAALNKSLKRLGLDYVDLYLMHWPVPLKtdrVTDGNVLCIPTLEDGTVDIDTKEWNFIKTWELMQELPKTG 161
Cdd:cd19115 81 NTfhDGERVEPICRKQLADWGIDYFDLFLIHFPIALK---YVDPAVRYPPGWFYDGKKVEFSNAPIQETWTAMEKLVDKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 162 KTKAVGVSNFSINNIKELLESPnnKVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFGSAN------------APL 229
Cdd:cd19115 158 LARSIGVSNFSAQLLMDLLRYA--RIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGPQSfleldlpgakdtPPL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6320576 230 LKEQAIIDMAKKHGVEPAQLIISWSIQRGYVVLAKSVNPERIVSNFKI--FTLPEDDFKTISNLSK 293
Cdd:cd19115 236 FEHDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVtgFDLEAEEIKAISALDI 301
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
20-310 |
1.14e-77 |
|
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: 239.09 E-value: 1.14e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 20 IPVLGFGTWRSVDNNGYHSVIAALKAGYRHIDAAAIYLNEEEVGRAI----KDSGVPREEIFITTKLWGTEQRDP--EAA 93
Cdd:cd19110 4 IPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIrekiKEGVVRREDLFIVSKLWCTCHKKSlvKTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 94 LNKSLKRLGLDYVDLYLMHWPV---PLKTDRVTDGNVLCIPTLEDgtvdidtkewnFIKTWELMQELPKTGKTKAVGVSN 170
Cdd:cd19110 84 CTRSLKALKLNYLDLYLIHWPMgfkPGEPDLPLDRSGMVIPSDTD-----------FLDTWEAMEDLVIEGLVKNIGVSN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 171 FSINNIKELLESPNNKVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFG--SANAPLLKEQAIIDMAKKHGVEPAQ 248
Cdd:cd19110 153 FNHEQLERLLNKPGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGgsCEGVDLIDDPVIQRIAKKHGKSPAQ 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6320576 249 LIISWSIQRGYVVLAKSVNPERIVSNFKI--FTLPEDDFKTISNLSKvhgtkrvvDMKWGSFPI 310
Cdd:cd19110 233 ILIRFQIQRNVIVIPKSVTPSRIKENIQVfdFELTEHDMDNLLSLDR--------NLRLATFPI 288
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
15-290 |
8.33e-77 |
|
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family.
Pssm-ID: 381355 [Multi-domain] Cd Length: 295 Bit Score: 236.59 E-value: 8.33e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 15 NTGASIPVLGFGTWRSVDNNGYHSVIAALKAGYRHIDAAAIYLNEEEVGRAIKD----SGVPREEIFITTKLWGTEQRdP 90
Cdd:cd19129 1 NGSGAIPALGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEvfkaGKIRREDLFVTTKLWNTNHR-P 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 91 E---AALNKSLKRLGLDYVDLYLMHWPVPLKTDRVTDgnvlciPTLEDGTVDIDtKEWNFIKTWELMQELPKTGKTKAVG 167
Cdd:cd19129 80 ErvkPAFEASLKRLQLDYLDLYLIHTPFAFQPGDEQD------PRDANGNVIYD-DGVTLLDTWRAMERLVDEGRCKAIG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 168 VSNFSINNIKELLESPNNKvvPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFGSANAP-LLKEQAIIDMAKKHGVEP 246
Cdd:cd19129 153 LSDVSLEKLREIFEAARIK--PAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGMEPkLLEDPVITAIARRVNKTP 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 6320576 247 AQLIISWSIQRGYVVLAKSVNPERIVSNFKIFTLPEDDFKTISN 290
Cdd:cd19129 231 AQVLLAWAIQRGTALLTTSKTPSRIRENFDISTLPEDAMREINE 274
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
20-291 |
2.05e-76 |
|
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: 233.78 E-value: 2.05e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 20 IPVLGFGTWRSVDNNGYHSVIAALKAGYRHIDAAAIYLNEEEVGRAIKDSGVPREEIFITTKLWgTEQRDPEA---ALNK 96
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIW-IDNLSKDKllpSLEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 97 SLKRLGLDYVDLYLMHWPVPlktdrvtdgnvlciptleDGTVDIDtkewnfiKTWELMQELPKTGKTKAVGVSNFSINNI 176
Cdd:cd19139 80 SLEKLRTDYVDLTLIHWPSP------------------NDEVPVE-------EYIGALAEAKEQGLTRHIGVSNFTIALL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 177 KELLESPNNKVVpATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFGSANapLLKEQAIIDMAKKHGVEPAQLIISWSIQ 256
Cdd:cd19139 135 DEAIAVVGAGAI-ATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLAYGK--VLDDPVLAAIAERHGATPAQIALAWAMA 211
|
250 260 270
....*....|....*....|....*....|....*..
gi 6320576 257 RGYVVLAKSVNPERIVSNFKI--FTLPEDDFKTISNL 291
Cdd:cd19139 212 RGYAVIPSSTKREHLRSNLLAldLTLDADDMAAIAAL 248
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
14-284 |
1.54e-75 |
|
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: 232.11 E-value: 1.54e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 14 LNTGASIPVLGFGTWRSVDNNGYHSVIAALKAGYRHIDAAAIYLNEEEVGRAIKDSGVPREEIFITTKLWGTEQR--DPE 91
Cdd:cd19130 4 LNDGNSIPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIAASGIPRDELFVTTKLWNDRHDgdEPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 92 AALNKSLKRLGLDYVDLYLMHWPVPLKTdrvtdgnvlciptledgtvdidtkewNFIKTWELMQELPKTGKTKAVGVSNF 171
Cdd:cd19130 84 AAFAESLAKLGLDQVDLYLVHWPTPAAG--------------------------NYVHTWEAMIELRAAGRTRSIGVSNF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 172 SINNIKELLESpnNKVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFGSANapLLKEQAIIDMAKKHGVEPAQLII 251
Cdd:cd19130 138 LPPHLERIVAA--TGVVPAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQGK--LLGDPPVGAIAAAHGKTPAQIVL 213
|
250 260 270
....*....|....*....|....*....|...
gi 6320576 252 SWSIQRGYVVLAKSVNPERIVSNFKIFTLPEDD 284
Cdd:cd19130 214 RWHLQKGHVVFPKSVRRERMEDNLDVFDFDLTD 246
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
17-293 |
3.32e-73 |
|
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: 227.00 E-value: 3.32e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 17 GASIPVLGFGTWRSVDNNGYHSVIAALKAGYRHIDAAAIYLNEEEVGRAIK---DSG-VPREEIFITTKLW--GTEQRDP 90
Cdd:cd19111 1 GFPMPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKwwlKNGkLKREEVFITTKLPpvYLEFKDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 91 EAALNKSLKRLGLDYVDLYLMHWPVPLKTDrvtdgnvlciptlEDGTVDIDTkEWNFIKTWELMQELPKTGKTKAVGVSN 170
Cdd:cd19111 81 EKSLEKSLENLKLPYVDLYLIHHPCGFVNK-------------KDKGERELA-SSDVTSVWRAMEALVSEGKVKSIGLSN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 171 FSINNIKELLESpnNKVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFGS---------ANAP-LLKEQAIIDMAK 240
Cdd:cd19111 147 FNPRQINKILAY--AKVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSpgranqslwPDQPdLLEDPTVLAIAK 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 6320576 241 KHGVEPAQLIISWSIQRGYVVLAKSVNPERIVSNFKIF--TLPEDDFKTISNLSK 293
Cdd:cd19111 225 ELDKTPAQVLLRFVLQRGTGVLPKSTNKERIEENFEVFdfELTEEHFKKLKTLDR 279
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
17-293 |
1.09e-72 |
|
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: 226.60 E-value: 1.09e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 17 GASIPVLGFGTW----RSVDNNGYHSVIAALKAGYRHIDAAAIYLNEEEVGRAIK----DSGVPREEIFITTKLWGTEQr 88
Cdd:cd19109 1 GNSIPIIGLGTYsepkTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIRekiaEGKVKREDIFYCGKLWNTCH- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 89 DPE---AALNKSLKRLGLDYVDLYLMHWPVPLKTdrvtdGNVLcIPTLEDGTVDIDtkEWNFIKTWELMQELPKTGKTKA 165
Cdd:cd19109 80 PPElvrPTLERTLKVLQLDYVDLYIIEMPMAFKP-----GDEI-YPRDENGKWLYH--KTNLCATWEALEACKDAGLVKS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 166 VGVSNFSINNIKELLESPNNKVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFGSANA---------PLLKEQAII 236
Cdd:cd19109 152 IGVSNFNRRQLELILNKPGLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDpiwvnvsspPLLEDPLLN 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 6320576 237 DMAKKHGVEPAQLIISWSIQRGYVVLAKSVNPERIVSNFKI--FTLPEDDFKTISNLSK 293
Cdd:cd19109 232 SIGKKYNKTAAQVVLRFNIQRGVVVIPKSFNPERIKENFQIfdFSLTEEEMKDIEALNK 290
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
11-291 |
1.47e-71 |
|
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: 223.86 E-value: 1.47e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 11 TLKLNTGASIPVLGFGTWRSVDNNGYHSVIAALKAGYRHIDAAAIYLNEEEVG----RAIKDSGVPREEIFITTKLWGT- 85
Cdd:cd19113 2 DIKLNSGYKMPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGegvnRAIDEGLVKREELFLTSKLWNNf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 86 -EQRDPEAALNKSLKRLGLDYVDLYLMHWPVPLKTdrvtdgnvlcIPTLED---GTVDIDTKEWNF-----IKTWELMQE 156
Cdd:cd19113 82 hDPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKF----------VPIEEKyppGFYCGDGDNFVYedvpiLDTWKALEK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 157 LPKTGKTKAVGVSNFSINNIKELLESPnnKVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFGSAN---------- 226
Cdd:cd19113 152 LVDAGKIKSIGVSNFPGALILDLLRGA--TIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGPQSfvelnqgral 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6320576 227 --APLLKEQAIIDMAKKHGVEPAQLIISWSIQRGYVVLAKSVNPERIVSNFKI--FTLPEDDFKTISNL 291
Cdd:cd19113 230 ntPTLFEHDTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVndFDLTKEDFEEIAKL 298
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
12-293 |
1.98e-70 |
|
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: 220.86 E-value: 1.98e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 12 LKLNTGASIPVLGFGTWRSVDNNGYHSVIAALKAGYRHIDAAAIYLNEEEVGRAIK---DSG-VPREEIFITTKL--WGT 85
Cdd:cd19155 4 VTFNNGEKMPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKkwiDSGkVKREELFIVTKLppGGN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 86 EQRDPEAALNKSLKRLGLDYVDLYLMHWPVPLKTDRvtDGNvlcIPTLEDGTVDIDTKEwNFIKTWELMQELPKTGKTKA 165
Cdd:cd19155 84 RREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLSKE--DDS---GKLDPTGEHKQDYTT-DLLDIWKAMEAQVDQGLTRS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 166 VGVSNFSINNIKELLEspNNKVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFGS---------------ANAPLL 230
Cdd:cd19155 158 IGLSNFNREQMARILK--NARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSpgaahfspgtgspsgSSPDLL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6320576 231 KEQAIIDMAKKHGVEPAQLIISWSIQRGYVVLAKSVNPERIVSNFKI--FTLPEDDFKTISNLSK 293
Cdd:cd19155 236 QDPVVKAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVfdFELTEADMAKLSSLDK 300
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
21-291 |
1.82e-69 |
|
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: 217.39 E-value: 1.82e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 21 PVLGFGTWRSVDNNGYHSVIAALKAGYRHIDAAAIYLNEEEVGRAI----KDSGVPREEIFITTKLWGTEQRDPEAA--L 94
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFseifKDGGVKREDLFITSKLWPTMHQPENVKeqL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 95 NKSLKRLGLDYVDLYLMHWpvPLKTDRVTDGNvlciPTLEDGTVDIDTKewNFIKTWELMQELPKTGKTKAVGVSNFSIN 174
Cdd:cd19128 82 LITLQDLQLEYLDLFLIHW--PLAFDMDTDGD----PRDDNQIQSLSKK--PLEDTWRAMEQCVDEKLTKNIGVSNYSTK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 175 NIKELLESpnNKVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFGSA----NAPLLKEQAIIDMAKKHGVEPAQLI 250
Cdd:cd19128 154 LLTDLLNY--CKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGSygdgNLTFLNDSELKALATKYNTTPPQVI 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 6320576 251 ISWSIQR---GYVVLAKSVNPERIVSNFKI--FTLPEDDFKTISNL 291
Cdd:cd19128 232 IAWHLQKwpkNYSVIPKSANKSRCQQNFDIndLALTKEDMDAINTL 277
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
17-291 |
6.87e-68 |
|
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: 213.96 E-value: 6.87e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 17 GASIPVLGFGTWRSVDNNGYHSVIAALKAGYRHIDAAAIYLNEEEVGR----AIKDSGVPREEIFITTKLWGTEQRDP-- 90
Cdd:cd19114 1 GDKMPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRgirkAIQEGLVKREDLFIVTKLWNNFHGKDhv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 91 EAALNKSLKRLGLDYVDLYLMHWPVPLKtdrVTDGNVLCIPTLEDGtvDIDTKEWNFI---KTWELMQELPKTGKTKAVG 167
Cdd:cd19114 81 REAFDRQLKDYGLDYIDLYLIHFPIPAA---YVDPAENYPFLWKDK--ELKKFPLEQSpmqECWREMEKLVDAGLVRNIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 168 VSNFSINNIKELLESPnnKVVPATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFGSAN-----------APLLKEQAII 236
Cdd:cd19114 156 IANFNVQLILDLLTYA--KIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAVytkvtkhlkhfTNLLEHPVVK 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 6320576 237 DMAKKHGVEPAQLIISWSIQRGYVVLAKSVNPERIVSNFKIFT--LPEDDFKTISNL 291
Cdd:cd19114 234 KLADKHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSykLDEEDMEALYEL 290
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
19-291 |
1.45e-67 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 211.81 E-value: 1.45e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 19 SIPVLGFGTWRSVDNNGYHSVIAALKAGYRHIDAAAIYLNEEEVGRAIKDSGVPREEIFITTKLWgTEQRDPE---AALN 95
Cdd:PRK11172 2 SIPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIW-IDNLAKDkliPSLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 96 KSLKRLGLDYVDLYLMHWPVPlktdrvtdgnvlciptleDGTVDIDtkewnfiktwELMQEL---PKTGKTKAVGVSNFS 172
Cdd:PRK11172 81 ESLQKLRTDYVDLTLIHWPSP------------------NDEVSVE----------EFMQALleaKKQGLTREIGISNFT 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 173 INNIKELLESPNNKVVpATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFGSANAplLKEQAIIDMAKKHGVEPAQLIIS 252
Cdd:PRK11172 133 IALMKQAIAAVGAENI-ATNQIELSPYLQNRKVVAFAKEHGIHVTSYMTLAYGKV--LKDPVIARIAAKHNATPAQVILA 209
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 6320576 253 WSIQRGYVVLAKSVNPERIVSNFKI--FTLPEDDFKTISNL 291
Cdd:PRK11172 210 WAMQLGYSVIPSSTKRENLASNLLAqdLQLDAEDMAAIAAL 250
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
17-289 |
2.56e-59 |
|
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: 190.52 E-value: 2.56e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 17 GASIPVLGFGTW-----RSVDNNGYHSVIAALK----AGYRHIDAAAIY---LNEEEVGRAIKdsGVPREEIFITTKLWG 84
Cdd:cd19072 1 GEEVPVLGLGTWgigggMSKDYSDDKKAIEALRyaieLGINLIDTAEMYgggHAEELVGKAIK--GFDREDLFITTKVSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 85 TEQRDPEA--ALNKSLKRLGLDYVDLYLMHWPVPlktdrvtdgnvlciptledgtvDIDTKEwnfikTWELMQELPKTGK 162
Cdd:cd19072 79 DHLKYDDVikAAKESLKRLGTDYIDLYLIHWPNP----------------------SIPIEE-----TLRAMEELVEEGK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 163 TKAVGVSNFSINNIKELLES-PNNKVVpaTNQIEIHpLL---PQDELIAFCKEKGIVVEAYSPFGSANAPLLKEQAIID- 237
Cdd:cd19072 132 IRYIGVSNFSLEELEEAQSYlKKGPIV--ANQVEYN-LFdreEESGLLPYCQKNGIAIIAYSPLEKGKLSNAKGSPLLDe 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 6320576 238 MAKKHGVEPAQLIISWSIQR-GYVVLAKSVNPERIVSNFKI--FTLPEDDFKTIS 289
Cdd:cd19072 209 IAKKYGKTPAQIALNWLISKpNVIAIPKASNIEHLEENAGAlgWELSEEDLQRLD 263
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
11-288 |
3.71e-55 |
|
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: 180.14 E-value: 3.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 11 TLKLNTGASIPVLGFGTWRSVDNNG-YHSVIAALKA----GYRHIDAAAIY---LNEEEVGRAIKDSgvpREEIFITTKL 82
Cdd:cd19138 2 TVTLPDGTKVPALGQGTWYMGEDPAkRAQEIEALRAgidlGMTLIDTAEMYgdgGSEELVGEAIRGR---RDKVFLVSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 83 WGTE--QRDPEAALNKSLKRLGLDYVDLYLMHWP--VPLKTdrvtdgnvlciptledgtvdidtkewnfikTWELMQELP 158
Cdd:cd19138 79 LPSNasRQGTVRACERSLRRLGTDYLDLYLLHWRggVPLAE------------------------------TVAAMEELK 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 159 KTGKTKAVGVSNFSINNIKELLESPNNKVVpATNQIEIHplLPQD----ELIAFCKEKGIVVEAYSPFGSANAP---LLK 231
Cdd:cd19138 129 KEGKIRAWGVSNFDTDDMEELWAVPGGGNC-AANQVLYN--LGSRgieyDLLPWCREHGVPVMAYSPLAQGGLLrrgLLE 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 232 EQAIIDMAKKHGVEPAQLIISWSIQRGYVV-LAKSVNPERIVSNFKI--FTLPEDDFKTI 288
Cdd:cd19138 206 NPTLKEIAARHGATPAQVALAWVLRDGNVIaIPKSGSPEHARENAAAadLELTEEDLAEL 265
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
23-288 |
2.66e-51 |
|
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: 170.96 E-value: 2.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 23 LGFGTWRSVDNNGYHS-------VIAALKAGYRHIDAAAIY---LNEEEVGRAIKDSGVPREEIFITTKLW--------G 84
Cdd:pfam00248 1 IGLGTWQLGGGWGPISkeealeaLRAALEAGINFIDTAEVYgdgKSEELLGEALKDYPVKRDKVVIATKVPdgdgpwpsG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 85 TEQRDPEAALNKSLKRLGLDYVDLYLMHWPvplktdrvtdgnvlciptleDGTVDIDtkewnfiKTWELMQELPKTGKTK 164
Cdd:pfam00248 81 GSKENIRKSLEESLKRLGTDYIDLYYLHWP--------------------DPDTPIE-------ETWDALEELKKEGKIR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 165 AVGVSNFSINNIKELLESPnnKVVPATNQIEIHPL--LPQDELIAFCKEKGIVVEAYSPFGS------------------ 224
Cdd:pfam00248 134 AIGVSNFDAEQIEKALTKG--KIPIVAVQVEYNLLrrRQEEELLEYCKKNGIPLIAYSPLGGglltgkytrdpdkgpger 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6320576 225 ---------ANAPLLkeQAIIDMAKKHGVEPAQLIISW--SIQRGYVVLAKSVNPERIVSNFKI--FTLPEDDFKTI 288
Cdd:pfam00248 212 rrllkkgtpLNLEAL--EALEEIAKEHGVSPAQVALRWalSKPGVTIPIPGASNPEQLEDNLGAleFPLSDEEVARI 286
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
15-296 |
3.27e-47 |
|
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: 161.11 E-value: 3.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 15 NTGASIPVLGFGTW------RSVDNNGYHSVI-AALKAGYRHIDAAAIY---LNEEEVGRAIKDsgVPREEIFITTKLWG 84
Cdd:COG0667 8 RSGLKVSRLGLGTMtfggpwGGVDEAEAIAILdAALDAGINFFDTADVYgpgRSEELLGEALKG--RPRDDVVIATKVGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 85 TEQRDP----------EAALNKSLKRLGLDYVDLYLMHWPvplktdrvtdgnvlciptleDGTVDIDtkewnfiKTWELM 154
Cdd:COG0667 86 RMGPGPngrglsrehiRRAVEASLRRLGTDYIDLYQLHRP--------------------DPDTPIE-------ETLGAL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 155 QELPKTGKTKAVGVSNFSINNIKELLESPNNKVVPATNQIEIHPL--LPQDELIAFCKEKGIVVEAYSPFGS-------- 224
Cdd:COG0667 139 DELVREGKIRYIGVSNYSAEQLRRALAIAEGLPPIVAVQNEYSLLdrSAEEELLPAARELGVGVLAYSPLAGglltgkyr 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 225 --------------ANAPLLKE------QAIIDMAKKHGVEPAQLIISWSIQRGYVVlakSV-----NPERIVSNFKI-- 277
Cdd:COG0667 219 rgatfpegdraatnFVQGYLTErnlalvDALRAIAAEHGVTPAQLALAWLLAQPGVT---SVipgarSPEQLEENLAAad 295
|
330
....*....|....*....
gi 6320576 278 FTLPEDDFKTISNLSKVHG 296
Cdd:COG0667 296 LELSAEDLAALDAALAAVP 314
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
17-288 |
2.35e-45 |
|
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: 154.65 E-value: 2.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 17 GASIPVLGFGTWR---------SVDNNGYHSVIAALKAGYRHIDAAAIYL---NEEEVGRAIKDsgVPREEIFITTKLWG 84
Cdd:cd19137 1 GEKIPALGLGTWGiggfltpdySRDEEMVELLKTAIELGYTHIDTAEMYGgghTEELVGKAIKD--FPREDLFIVTKVWP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 85 TEQR--DPEAALNKSLKRLGLDYVDLYLMHWPVPlktdrvtdgnvlciptledgtvDIDTKEwnfikTWELMQELPKTGK 162
Cdd:cd19137 79 TNLRydDLLRSLQNSLRRLDTDYIDLYLIHWPNP----------------------NIPLEE-----TLSAMAEGVRQGL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 163 TKAVGVSNFSINNIKELLESPNNKVVpaTNQIE---IHPLLPQDELIAFCKEKGIVVEAYSPFgsANAPLLKEQAIIDMA 239
Cdd:cd19137 132 IRYIGVSNFNRRLLEEAISKSQTPIV--CNQVKynlEDRDPERDGLLEYCQKNGITVVAYSPL--RRGLEKTNRTLEEIA 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 6320576 240 KKHGVEPAQLIISWSIQRGYVV-LAKSVNPERIVSNFKI--FTLPEDDFKTI 288
Cdd:cd19137 208 KNYGKTIAQIALAWLIQKPNVVaIPKAGRVEHLKENLKAteIKLSEEEMKLL 259
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
20-274 |
1.83e-42 |
|
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: 148.14 E-value: 1.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 20 IPVLGFGTW----RSV---DNNGYHSVIAALKAGYRH----IDAAAIY---LNEEEVGRAIKDSGvPREEIFITTKLWGT 85
Cdd:cd19093 2 VSPLGLGTWqwgdRLWwgyGEYGDEDLQAAFDAALEAgvnlFDTAEVYgtgRSERLLGRFLKELG-DRDEVVIATKFAPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 86 ----EQRDPEAALNKSLKRLGLDYVDLYLMHWPVPlktdrvtdgNVLCIPTLedgtvdidtkewnfiktWELMQELPKTG 161
Cdd:cd19093 81 pwrlTRRSVVKALKASLERLGLDSIDLYQLHWPGP---------WYSQIEAL-----------------MDGLADAVEEG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 162 KTKAVGVSNFSINNIKELLESPNNKVVP-ATNQIE---IHPLLPQDELIAFCKEKGIVVEAYSP---------FGSANAP 228
Cdd:cd19093 135 LVRAVGVSNYSADQLRRAHKALKERGVPlASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPlaqglltgkYSPENPP 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6320576 229 ------------LLKEQAIID----MAKKHGVEPAQLIISWSIQRGYVVLAKSVNPERIVSN 274
Cdd:cd19093 215 pggrrrlfgrknLEKVQPLLDaleeIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEEN 276
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
20-293 |
7.62e-42 |
|
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: 146.19 E-value: 7.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 20 IPVLGFGTWRSVDNNGYH--------SVI-AALKAGYRHIDAAAIYLN---EEEVGRAIKDsgvPREEIFITTKLWGTEQ 87
Cdd:cd19085 1 VSRLGLGCWQFGGGYWWGdqddeesiATIhAALDAGINFFDTAEAYGDghsEEVLGKALKG---RRDDVVIATKVSPDNL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 88 R--DPEAALNKSLKRLGLDYVDLYLMHWPvplktdrvtdgnvlciptleDGTVDIDtkewnfiKTWELMQELPKTGKTKA 165
Cdd:cd19085 78 TpeDVRKSCERSLKRLGTDYIDLYQIHWP--------------------SSDVPLE-------ETMEALEKLKEEGKIRA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 166 VGVSNFSINNIKELLESPNnkvvPATNQIEIHPLL--PQDELIAFCKEKGIVVEAYSP---------FGSA--------- 225
Cdd:cd19085 131 IGVSNFGPAQLEEALDAGR----IDSNQLPYNLLWraIEYEILPFCREHGIGVLAYSPlaqglltgkFSSAedfppgdar 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 226 -NAPLLKE-----------QAIIDMAKKHGVEPAQLIISWSIQRGYV--VLAKSVNPERIVSNFKIFT--LPEDDFKTIS 289
Cdd:cd19085 207 tRLFRHFEpgaeeetfealEKLKEIADELGVTMAQLALAWVLQQPGVtsVIVGARNPEQLEENAAAVDleLSPSVLERLD 286
|
....
gi 6320576 290 NLSK 293
Cdd:cd19085 287 EISD 290
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
21-276 |
3.64e-38 |
|
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: 134.95 E-value: 3.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 21 PVLGFGTWR---SVDNNGYHSVI-AALKAGYRHIDAAAIY---LNEEEVGRAIKDSGVpREEIFITTKLWGTEQRDP--- 90
Cdd:cd06660 1 SRLGLGTMTfggDGDEEEAFALLdAALEAGGNFFDTADVYgdgRSERLLGRWLKGRGN-RDDVVIATKGGHPPGGDPsrs 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 91 -------EAALNKSLKRLGLDYVDLYLMHWPvplktdrvtdgnvlciptleDGTVDIDtkewnfiKTWELMQELPKTGKT 163
Cdd:cd06660 80 rlspehiRRDLEESLRRLGTDYIDLYYLHRD--------------------DPSTPVE-------ETLEALNELVREGKI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 164 KAVGVSNFSINNIKELLE--SPNNKVVPATNQIEIHPLLPQ---DELIAFCKEKGIVVEAYSPFGSanapllkeqaiidm 238
Cdd:cd06660 133 RYIGVSNWSAERLAEALAyaKAHGLPGFAAVQPQYSLLDRSpmeEELLDWAEENGLPLLAYSPLAR-------------- 198
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 6320576 239 akkhGvePAQLIISWSIQRGYV--VLAKSVNPERIVSNFK 276
Cdd:cd06660 199 ----G--PAQLALAWLLSQPFVtvPIVGARSPEQLEENLA 232
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
17-288 |
3.59e-37 |
|
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381310 [Multi-domain] Cd Length: 296 Bit Score: 134.19 E-value: 3.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 17 GASIPVLGFGTW-------RSVDNNgyhSVIAALKAGYRH----IDAAAIYLN---EEEVGRAIKDSgvpREEIFITTK- 81
Cdd:cd19084 1 DLKVSRIGLGTWaiggtwwGEVDDQ---ESIEAIKAAIDLginfFDTAPVYGFghsEEILGKALKGR---RDDVVIATKc 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 82 --LWGTEQRD-----PE---AALNKSLKRLGLDYVDLYLMHWPvplktdrvtdgnvlciptleDGTVDIDtkewnfiKTW 151
Cdd:cd19084 75 glRWDGGKGVtkdlsPEsirKEVEQSLRRLQTDYIDLYQIHWP--------------------DPNTPIE-------ETA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 152 ELMQELPKTGKTKAVGVSNFSINNIKELLespnnKVVP-ATNQIEIHPLLPQ--DELIAFCKEKGIVVEAYSPFGS---- 224
Cdd:cd19084 128 EALEKLKKEGKIRYIGVSNFSVEQLEEAR-----KYGPiVSLQPPYSMLEREieEELLPYCRENGIGVLPYGPLAQgllt 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 225 ---------------ANAP------LLKEQAIID----MAKKHGVEPAQLIISWSIQRGYV--VLAKSVNPERIVSNFKI 277
Cdd:cd19084 203 gkykkeptfppddrrSRFPffrgenFEKNLEIVDklkeIAEKYGKSLAQLAIAWTLAQPGVtsAIVGAKNPEQLEENAGA 282
|
330
....*....|...
gi 6320576 278 --FTLPEDDFKTI 288
Cdd:cd19084 283 ldWELTEEELKEI 295
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
20-291 |
1.71e-32 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 122.01 E-value: 1.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 20 IPVLGFGTWRS------------VDNNGYHSVIAALKAGYRHIDAAAIY---LNEEEVGRAIKDSgvpREEIFITTK--- 81
Cdd:cd19102 1 LTTIGLGTWAIggggwgggwgpqDDRDSIAAIRAALDLGINWIDTAAVYglgHSEEVVGRALKGL---RDRPIVATKcgl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 82 LWGTEQR-----DPE---AALNKSLKRLGLDYVDLYLMHWPVPlktdrvtdgnvlciptledgtvDIDTKEwnfikTWEL 153
Cdd:cd19102 78 LWDEEGRirrslKPAsirAECEASLRRLGVDVIDLYQIHWPDP----------------------DEPIEE-----AWGA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 154 MQELPKTGKTKAVGVSNFSINNIKELLespnnKVVP-ATNQIEIHPLLPQDE--LIAFCKEKGIVVEAYSPFGS------ 224
Cdd:cd19102 131 LAELKEEGKVRAIGVSNFSVDQMKRCQ-----AIHPiASLQPPYSLLRRGIEaeILPFCAEHGIGVIVYSPMQSglltgk 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 225 ---------------ANAPLLKEQ------AIID----MAKKHGVEPAQLIISWSIQRGYV--VLAKSVNPERIVSNFKI 277
Cdd:cd19102 206 mtpervaslpaddwrRRSPFFQEPnlarnlALVDalrpIAERHGRTVAQLAIAWVLRRPEVtsAIVGARRPDQIDETVGA 285
|
330
....*....|....*.
gi 6320576 278 --FTLPEDDFKTISNL 291
Cdd:cd19102 286 adLRLTPEELAEIEAL 301
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
15-289 |
5.18e-32 |
|
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: 120.84 E-value: 5.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 15 NTGASIPVLGFGTW---------RSVDNNGYHSVIAALKAGYRHIDAAAIY---LNEEEVGRAIKDSgvpREEIFITTK- 81
Cdd:cd19149 6 KSGIEASVIGLGTWaigggpwwgGSDDNESIRTIHAALDLGINLIDTAPAYgfgHSEEIVGKAIKGR---RDKVVLATKc 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 82 --LWGTEQRD---------------PEA---ALNKSLKRLGLDYVDLYLMHWPvplktdrvtdgnvlciptleDGTVDID 141
Cdd:cd19149 83 glRWDREGGSfffvrdgvtvyknlsPESireEVEQSLKRLGTDYIDLYQTHWQ--------------------DVETPIE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 142 tkewnfiKTWELMQELPKTGKTKAVGVSNFSINNIKELLESPNnkvvPATNQIEIHPLLPQ--DELIAFCKEKGIVVEAY 219
Cdd:cd19149 143 -------ETMEALEELKRQGKIRAIGASNVSVEQIKEYVKAGQ----LDIIQEKYSMLDRGieKELLPYCKKNNIAFQAY 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 220 SPFGS-------------------ANAPLLKE----------QAIIDMAKKHGVEPAQLIISWSI-QRGYV-VLAKSVNP 268
Cdd:cd19149 212 SPLEQglltgkitpdrefdagdarSGIPWFSPenrekvlallEKWKPLCEKYGCTLAQLVIAWTLaQPGITsALCGARKP 291
|
330 340
....*....|....*....|...
gi 6320576 269 ERIVSNFKI--FTLPEDDFKTIS 289
Cdd:cd19149 292 EQAEENAKAgdIRLSAEDIATMR 314
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
15-273 |
4.76e-31 |
|
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: 117.66 E-value: 4.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 15 NTGASIPVLGFGTWRSVDNNG-YHSVI----AALKAGYRHIDAAAIYLN---EEEVGRAIKDSGVPREEIFITTKLwG-- 84
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADWGEsAEELLslieAALELGITTFDHADIYGGgkcEELFGEALALNPGLREKIEIQTKC-Gir 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 85 -TEQRDPE-------------AALNKSLKRLGLDYVDLYLMHWPVPLktdrvtdgnvlciptledgtvdIDTKEwnfikT 150
Cdd:cd19092 80 lGDDPRPGrikhydtskehilASVEGSLKRLGTDYLDLLLLHRPDPL----------------------MDPEE-----V 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 151 WELMQELPKTGKTKAVGVSNFSINNIkELLESP-NNKVVpaTNQIEIHPL---LPQDELIAFCKEKGIVVEAYSPFG--- 223
Cdd:cd19092 133 AEAFDELVKSGKVRYFGVSNFTPSQI-ELLQSYlDQPLV--TNQIELSLLhteAIDDGTLDYCQLLDITPMAWSPLGggr 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 6320576 224 --SANAPLLKE--QAIIDMAKKHGVEPAQLIISWsIQR---GYVVLAKSVNPERIVS 273
Cdd:cd19092 210 lfGGFDERFQRlrAALEELAEEYGVTIEAIALAW-LLRhpaRIQPILGTTNPERIRS 265
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
15-298 |
1.04e-30 |
|
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: 117.93 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 15 NTGASIPVLGFGTW--------RSVDNNGYHSVIAALKAGYRHIDAAAIYL-NEEEVGRAIKDSGVPREEIFITTKLWGT 85
Cdd:cd19144 8 RNGPSVPALGFGAMglsafygpPKPDEERFAVLDAAFELGCTFWDTADIYGdSEELIGRWFKQNPGKREKIFLATKFGIE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 86 EQR---------DPE---AALNKSLKRLGLDYVDLYLMHwpvplktdRVtdgnvlciptleDGTVDIDtkewnfiKTWEL 153
Cdd:cd19144 88 KNVetgeysvdgSPEyvkKACETSLKRLGVDYIDLYYQH--------RV------------DGKTPIE-------KTVAA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 154 MQELPKTGKTKAVGVSNFSINNIKELlespnNKVVP-ATNQIEIHPLL-----PQDELIAFCKEKGIVVEAYSPFGSA-- 225
Cdd:cd19144 141 MAELVQEGKIKHIGLSECSAETLRRA-----HAVHPiAAVQIEYSPFSldierPEIGVLDTCRELGVAIVAYSPLGRGfl 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 226 -----------------NAPLLKEQ----------AIIDMAKKHGVEPAQLIISWSIQRG--YVVLAKSVNPERIVSNFK 276
Cdd:cd19144 216 tgairspddfeegdfrrMAPRFQAEnfpknlelvdKIKAIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLEENLG 295
|
330 340
....*....|....*....|....*..
gi 6320576 277 IFT--LPEDDFKTISNLSK---VHGTK 298
Cdd:cd19144 296 ALKvkLTEEEEKEIREIAEeaeVVGER 322
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
42-258 |
1.68e-29 |
|
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: 113.85 E-value: 1.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 42 ALKAGYRHIDAAAIY---LNEEEVGRAIKDsgvPREEIFITTKlWGTEQRD----------PE---AALNKSLKRLGLDY 105
Cdd:cd19076 41 ALELGVTFLDTADMYgpgTNEELLGKALKD---RRDEVVIATK-FGIVRDPgsgfrgvdgrPEyvrAACEASLKRLGTDV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 106 VDLYLMHwpvplktdRVtdgnvlciptleDGTVDIDtkewnfiKTWELMQELPKTGKTKAVGVSNFSINNIKELlespnN 185
Cdd:cd19076 117 IDLYYQH--------RV------------DPNVPIE-------ETVGAMAELVEEGKVRYIGLSEASADTIRRA-----H 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 186 KVVPATN-QIEIHPLL--PQDELIAFCKEKGIVVEAYSPFG-------------------------------SANAPLLk 231
Cdd:cd19076 165 AVHPITAvQSEYSLWTrdIEDEVLPTCRELGIGFVAYSPLGrgfltgaikspedlpeddfrrnnprfqgenfDKNLKLV- 243
|
250 260
....*....|....*....|....*..
gi 6320576 232 eQAIIDMAKKHGVEPAQLIISWSIQRG 258
Cdd:cd19076 244 -EKLEAIAAEKGCTPAQLALAWVLAQG 269
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-235 |
3.47e-27 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 106.41 E-value: 3.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 15 NTGASIPVLGFGT---WRSVDNNGYHSVIAALKAGYRHIDAAAIYLN-EEEVGRAIKDsgvPREEIFITTKLWGTEQRDP 90
Cdd:cd19100 6 RTGLKVSRLGFGGgplGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKG---RRDKVFLATKTGARDYEGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 91 EAALNKSLKRLGLDYVDLYLMHwpvplktdrvtdgnvlCIPTLEDGTVDIDTKEwnfikTWELMQELPKTGKTKAVGVSN 170
Cdd:cd19100 83 KRDLERSLKRLGTDYIDLYQLH----------------AVDTEEDLDQVFGPGG-----ALEALLEAKEEGKIRFIGISG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 171 FSINNIKELLESPNNKVV-PATNQIEIHPLLPQDELIAFCKEKGIVVEAYSPFG----SANAPLLKEQAI 235
Cdd:cd19100 142 HSPEVLLRALETGEFDVVlFPINPAGDHIDSFREELLPLAREKGVGVIAMKVLAggrlLSGDPLDPEQAL 211
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-277 |
1.07e-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: 381331 [Multi-domain] Cd Length: 250 Bit Score: 105.36 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 15 NTGASIPVLGFGTWRSVDNNGyhSVI-AALKAGYRHIDAAAIYLN---EEEVGRAIKdsGVPREEIFITTK-LWGTEQRD 89
Cdd:cd19105 8 KTGLKVSRLGFGGGGLPRESP--ELLrRALDLGINYFDTAEGYGNgnsEEIIGEALK--GLRRDKVFLATKaSPRLDKKD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 90 PE---AALNKSLKRLGLDYVDLYLMHWPVPLKtDRVTDGNVLciptledgtvdidtkewnfiktwELMQELPKTGKTKAV 166
Cdd:cd19105 84 KAellKSVEESLKRLQTDYIDIYQLHGVDTPE-ERLLNEELL-----------------------EALEKLKKEGKVRFI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 167 GVS-NFSINN-IKELLESPNNKVV-PATNQIEIHPLLpqDELIAFCKEKGIVVEAYSPFGSAnapllKEQAIIDMAKKH- 242
Cdd:cd19105 140 GFStHDNMAEvLQAAIESGWFDVImVAYNFLNQPAEL--EEALAAAAEKGIGVVAMKTLAGG-----YLQPALLSVLKAk 212
|
250 260 270
....*....|....*....|....*....|....*..
gi 6320576 243 GVEPAQLIISWSIQRGYV--VLAKSVNPERIVSNFKI 277
Cdd:cd19105 213 GFSLPQAALKWVLSNPRVdtVVPGMRNFAELEENLAA 249
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
42-261 |
3.94e-26 |
|
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: 104.97 E-value: 3.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 42 ALKAGYRHIDAAAIYLN---EEEVGRAIKDSGvPREEIFITTKLWGTEQRDPE----------AALNKSLKRLGLDYVDL 108
Cdd:cd19079 44 ALDLGINFFDTANVYSGgasEEILGRALKEFA-PRDEVVIATKVYFPMGDGPNgrglsrkhimAEVDASLKRLGTDYIDL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 109 YLMHWPvplktDRVTdgnvlciPTLEdgtvdidtkewnfikTWELMQELPKTGKTKAVGVSNFS------INNIKELLEs 182
Cdd:cd19079 123 YQIHRW-----DYET-------PIEE---------------TLEALHDVVKSGKVRYIGASSMYawqfakALHLAEKNG- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 183 pNNKVVPATNQieiHPLLPQD---ELIAFCKEKGIVVEAYSP------------------------------FGSANAPL 229
Cdd:cd19079 175 -WTKFVSMQNH---YNLLYREeerEMIPLCEEEGIGVIPWSPlargrlarpwgdtterrrsttdtaklkydyFTEADKEI 250
|
250 260 270
....*....|....*....|....*....|..
gi 6320576 230 LKeqAIIDMAKKHGVEPAQLIISWSIQRGYVV 261
Cdd:cd19079 251 VD--RVEEVAKERGVSMAQVALAWLLSKPGVT 280
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
19-224 |
4.66e-26 |
|
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: 103.33 E-value: 4.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 19 SIPVLGFGTWR-------SVDNNGYHSVI-AALKAGYRHIDAAAIY---LNEEEVGRAIKDsgvPREEIFITTKL----- 82
Cdd:cd19086 2 EVSEIGFGTWGlggdwwgDVDDAEAIRALrAALDLGINFFDTADVYgdgHSERLLGKALKG---RRDKVVIATKFgnrfd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 83 -WGTEQRDPEA-----ALNKSLKRLGLDYVDLYLMHwpvplktdrvtdgnvlcIPTLEdgtvDIDTKEWnfiktWELMQE 156
Cdd:cd19086 79 gGPERPQDFSPeyireAVEASLKRLGTDYIDLYQLH-----------------NPPDE----VLDNDEL-----FEALEK 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 157 LPKTGKTKAVGVSNFSINNIKELLESPNNKVVpatnQIEIHPL--LPQDELIAFCKEKGIVVEAYSPFGS 224
Cdd:cd19086 133 LKQEGKIRAYGVSVGDPEEALAALRRGGIDVV----QVIYNLLdqRPEEELFPLAEEHGVGVIARVPLAS 198
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
32-291 |
4.05e-25 |
|
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: 102.50 E-value: 4.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 32 DNNGYHSVIAALKAGYRHIDAAAIY---LNEEEVGRAIKDSGvpREEIFITTK---LWGTEQ----RDPE---AALNKSL 98
Cdd:cd19083 32 EEEGKDLVREALDNGVNLLDTAFIYglgRSEELVGEVLKEYN--RNEVVIATKgahKFGGDGsvlnNSPEflrSAVEKSL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 99 KRLGLDYVDLYLMHWPvplktdrvtDGNvlcipTLEDGTVDIdtkewnfiktwelMQELPKTGKTKAVGVSNFSINNIKE 178
Cdd:cd19083 110 KRLNTDYIDLYYIHFP---------DGE-----TPKAEAVGA-------------LQELKDEGKIRAIGVSNFSLEQLKE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 179 LLESPNNKVVPATnqieiHPLLPQD---ELIAFCKEKGIVVEAYSPFGS-------------------ANAPLLKEQAII 236
Cdd:cd19083 163 ANKDGYVDVLQGE-----YNLLQREaeeDILPYCVENNISFIPYFPLASgllagkytkdtkfpdndlrNDKPLFKGERFS 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6320576 237 ----------DMAKKHGVEPAQLIISWSIQRGYV--VLAKSVNPERIVSNFKIF--TLPEDDFKTISNL 291
Cdd:cd19083 238 enldkvdklkSIADEKGVTVAHLALAWYLTRPAIdvVIPGAKRAEQVIDNLKALdvTLTEEEIAFIDAL 306
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
20-263 |
5.46e-25 |
|
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: 100.75 E-value: 5.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 20 IPVLGFGTWR---------SVDNNGYHSVI-AALKAGYRHIDAAAIY---LNEEEVGRAIKDSGvprEEIFITTKL---- 82
Cdd:cd19088 1 VSRLGYGAMRltgpgiwgpPADREEAIAVLrRALELGVNFIDTADSYgpdVNERLIAEALHPYP---DDVVIATKGglvr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 83 -----WGTEQRdPE---AALNKSLKRLGLDYVDLYLMHWPvplktdrvtdgnvlciptleDGTVDIDtkewnfiKTWELM 154
Cdd:cd19088 78 tgpgwWGPDGS-PEylrQAVEASLRRLGLDRIDLYQLHRI--------------------DPKVPFE-------EQLGAL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 155 QELPKTGKTKAVGVSNFSINNIKELLespnnKVVP-ATNQIEIHPLLPQDE-LIAFCKEKGIVVEAYSPFGSANaPLLKE 232
Cdd:cd19088 130 AELQDEGLIRHIGLSNVTVAQIEEAR-----AIVRiVSVQNRYNLANRDDEgVLDYCEAAGIAFIPWFPLGGGD-LAQPG 203
|
250 260 270
....*....|....*....|....*....|.
gi 6320576 233 QAIIDMAKKHGVEPAQLIISWSIQRGYVVLA 263
Cdd:cd19088 204 GLLAEVAARLGATPAQVALAWLLARSPVMLP 234
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
24-221 |
2.87e-24 |
|
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381374 [Multi-domain] Cd Length: 302 Bit Score: 99.69 E-value: 2.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 24 GFGTWR--------SVDNNGYHSVIAALKAGYRHIDAAAIY---LNEEEVGRAIKDSGvPREEIFITTKL---WGTEQ-- 87
Cdd:cd19148 8 ALGTWAiggwmwggTDEKEAIETIHKALDLGINLIDTAPVYgfgLSEEIVGKALKEYG-KRDRVVIATKVgleWDEGGev 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 88 -RDPEAA-----LNKSLKRLGLDYVDLYLMHWPVPLktdrvtdgnvlciptledgtVDIDtkewnfiKTWELMQELPKTG 161
Cdd:cd19148 87 vRNSSPArirkeVEDSLRRLQTDYIDLYQVHWPDPL--------------------VPIE-------ETAEALKELLDEG 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6320576 162 KTKAVGVSNFSINNIKELLE-SPNNKVVPATNQIEIHpllPQDELIAFCKEKGIVVEAYSP 221
Cdd:cd19148 140 KIRAIGVSNFSPEQMETFRKvAPLHTVQPPYNLFERE---IEKDVLPYARKHNIVTLAYGA 197
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
15-223 |
2.08e-23 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 98.74 E-value: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 15 NTGASIPVLGFGTWR--SVDNNGYHSVI-AALKAGYRHIDAAAIYLNEEE-VGRAIKDsgvPREEIFITTKL--WGTEQR 88
Cdd:COG1453 8 KTGLEVSVLGFGGMRlpRKDEEEAEALIrRAIDNGINYIDTARGYGDSEEfLGKALKG---PRDKVILATKLppWVRDPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 89 DPEAALNKSLKRLGLDYVDLYLMHwpvplktdrvtdgnvlCIPTLEDgtVDIDTKEWNFiktWELMQELPKTGKTKAVGV 168
Cdd:COG1453 85 DMRKDLEESLKRLQTDYIDLYLIH----------------GLNTEED--LEKVLKPGGA---LEALEKAKAEGKIRHIGF 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 169 SNF-SINNIKELLESPNNKVVpatnQIEIHPLL----PQDELIAFCKEKGIVVEAYSPFG 223
Cdd:COG1453 144 STHgSLEVIKEAIDTGDFDFV----QLQYNYLDqdnqAGEEALEAAAEKGIGVIIMKPLK 199
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
17-283 |
2.29e-23 |
|
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: 97.28 E-value: 2.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 17 GASIPVLGFGTWRS----VDNNGYHSVI-AALKAGYRHIDAAAIYLN---EEEVGRAIKdsGVPREEIFITTKL-WGTEQ 87
Cdd:cd19074 1 GLKVSELSLGTWLTfggqVDDEDAKACVrKAYDLGINFFDTADVYAAgqaEEVLGKALK--GWPRESYVISTKVfWPTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 88 RDPEAAL---------NKSLKRLGLDYVDLYLMHWPvplktdrvtdgnvlciptleDGTVDIDtkewnfiKTWELMQELP 158
Cdd:cd19074 79 GPNDRGLsrkhifesiHASLKRLQLDYVDIYYCHRY--------------------DPETPLE-------ETVRAMDDLI 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 159 KTGKTKAVGVSNFSINNIKELLE--SPNNKVVPATNQIEIHPLL--PQDELIAFCKEKGIVVEAYSPF------------ 222
Cdd:cd19074 132 RQGKILYWGTSEWSAEQIAEAHDlaRQFGLIPPVVEQPQYNMLWreIEEEVIPLCEKNGIGLVVWSPLaqglltgkyrdg 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 223 ------GSANAPLLKEQAIIDM--------------AKKHGVEPAQLIISWSIQRGYV--VLAKSVNPERIVSNFK--IF 278
Cdd:cd19074 212 ipppsrSRATDEDNRDKKRRLLtdenlekvkklkpiADELGLTLAQLALAWCLRNPAVssAIIGASRPEQLEENVKasGV 291
|
....*
gi 6320576 279 TLPED 283
Cdd:cd19074 292 KLSPE 296
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
15-292 |
4.46e-22 |
|
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: 94.22 E-value: 4.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 15 NTGASIPVLGFGT------------WRSVDNNGYHSVI-AALKAGYRHIDAAAIYLN---EEEVGRAIKDSgvpREEIFI 78
Cdd:cd19091 8 RSGLKVSELALGTmtfgggggffgaWGGVDQEEADRLVdIALDAGINFFDTADVYSEgesEEILGKALKGR---RDDVLI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 79 TTKLWGTEQRDPE----------AALNKSLKRLGLDYVDLYLMHWPvplktDRVTdgnvlciPTLEdgtvdidtkewnfi 148
Cdd:cd19091 85 ATKVRGRMGEGPNdvglsrhhiiRAVEASLKRLGTDYIDLYQLHGF-----DALT-------PLEE-------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 149 kTWELMQELPKTGKTKAVGVSNFSINNI-KELLESPN-NKVVPATNQIEiHPLLPQD---ELIAFCKEKGIVVEAYSP-- 221
Cdd:cd19091 139 -TLRALDDLVRQGKVRYIGVSNFSAWQImKALGISERrGLARFVALQAY-YSLLGRDlehELMPLALDQGVGLLVWSPla 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 222 ----------------------FGSANAPLLKEQA--IID----MAKKHGVEPAQLIISWSIQRGYV--VLAKSVNPERI 271
Cdd:cd19091 217 ggllsgkyrrgqpapegsrlrrTGFDFPPVDRERGydVVDalreIAKETGATPAQVALAWLLSRPTVssVIIGARNEEQL 296
|
330 340
....*....|....*....|...
gi 6320576 272 VSNFKI--FTLPEDDFKTISNLS 292
Cdd:cd19091 297 EDNLGAagLSLTPEEIARLDKVS 319
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
21-274 |
1.01e-21 |
|
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: 91.91 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 21 PVLGFGTWRSVDNNGYHS------VI-AALKAGYRHIDAAAIYLNEEEV-GRAIkdSGVPREEIFITTKLW--GTEQRDP 90
Cdd:cd19095 1 SVLGLGTSGIGRVWGVPSeaeaarLLnTALDLGINLIDTAPAYGRSEERlGRAL--AGLRRDDLFIATKVGthGEGGRDR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 91 --------EAALNKSLKRLGLDYVDLYLMHWPVPlktdrvtdgnvlciPTLEDGTVdidtkewnfiktwELMQELPKTGK 162
Cdd:cd19095 79 kdfspaaiRASIERSLRRLGTDYIDLLQLHGPSD--------------DELTGEVL-------------ETLEDLKAAGK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 163 TKAVGVSNFSiNNIKELLESPNNKVVpatnQIEIHPLLP-QDELIAFCKEKGIVVEAYSPFgsANAPLLKEQAIIDMAKK 241
Cdd:cd19095 132 VRYIGVSGDG-EELEAAIASGVFDVV----QLPYNVLDReEEELLPLAAEAGLGVIVNRPL--ANGRLRRRVRRRPLYAD 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 6320576 242 H-----------GVEPAQLIISWSIQRGYV--VLAKSVNPERIVSN 274
Cdd:cd19095 205 YarrpefaaeigGATWAQAALRFVLSHPGVssAIVGTTNPEHLEEN 250
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
15-284 |
3.52e-20 |
|
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a founding member of aldo-keto reductase family 9 member C1 (AKR9C1).
Pssm-ID: 381307 [Multi-domain] Cd Length: 308 Bit Score: 88.81 E-value: 3.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 15 NTGASIPVLGFGTWR---SVDNNGYHSVIAA-LKAGYRHIDAAAIY----------LNEEEVGRAIKDSGvPREEIFITT 80
Cdd:cd19081 4 RTGLSVSPLCLGTMVfgwTADEETSFALLDAfVDAGGNFIDTADVYsawvpgnaggESETIIGRWLKSRG-KRDRVVIAT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 81 KL-WGTEQRDP-------EAALNKSLKRLGLDYVDLYLMHWPvplktdrvtdgnvlciptleDGTVDIDtkewnfiKTWE 152
Cdd:cd19081 83 KVgFPMGPNGPglsrkhiRRAVEASLRRLQTDYIDLYQAHWD--------------------DPATPLE-------ETLG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 153 LMQELPKTGKTKAVGVSNFSINNIKELLE--SPNNKVVPATNQIEiHPLLPQD----ELIAFCKEKGIVVEAYSPF---- 222
Cdd:cd19081 136 ALNDLIRQGKVRYIGASNYSAWRLQEALElsRQHGLPRYVSLQPE-YNLVDREsfegELLPLCREEGIGVIPYSPLaggf 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 223 ------------GSANAP-----LLKEQ--AIID----MAKKHGVEPAQLIISWSIQRGYV--VLAKSVNPERIVSNFKI 277
Cdd:cd19081 215 ltgkyrseadlpGSTRRGeaakrYLNERglRILDaldeVAAEHGATPAQVALAWLLARPGVtaPIAGARTVEQLEDLLAA 294
|
....*..
gi 6320576 278 FTLPEDD 284
Cdd:cd19081 295 AGLRLTD 301
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
39-290 |
5.51e-20 |
|
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: 88.06 E-value: 5.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 39 VIAALKAGYRHIDAAAIY---LNEEEVGRAIKDsgvPREEIFITTKL----------WGTEQRDPE---AALNKSLKRLG 102
Cdd:cd19078 31 IRKAVELGITFFDTAEVYgpyTNEELVGEALKP---FRDQVVIATKFgfkidggkpgPLGLDSRPEhirKAVEGSLKRLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 103 LDYVDLYLMHwpvplktdRVtDGNVlcipTLED--GTvdidtkewnfiktwelMQELPKTGKTKAVGVSNFSINNIKELl 180
Cdd:cd19078 108 TDYIDLYYQH--------RV-DPNV----PIEEvaGT----------------MKELIKEGKIRHWGLSEAGVETIRRA- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 181 espnNKVVPATN-QIEIHPLL--PQDELIAFCKEKGIVVEAYSPFGS-------------------------------AN 226
Cdd:cd19078 158 ----HAVCPVTAvQSEYSMMWrePEKEVLPTLEELGIGFVPFSPLGKgfltgkidentkfdegddraslprftpealeAN 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6320576 227 APLLkeQAIIDMAKKHGVEPAQLIISWSI-QRGYVV-LAKSVNPERIVSNFKI--FTLPEDDFKTISN 290
Cdd:cd19078 234 QALV--DLLKEFAEEKGATPAQIALAWLLaKKPWIVpIPGTTKLSRLEENIGAadIELTPEELREIED 299
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
15-284 |
5.28e-19 |
|
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: 85.30 E-value: 5.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 15 NTGASIPVLGFGT------WRSVD-NNGYHSVIAALKAGYRHIDAAAIY---LNEEEVGRAIKdsGVPREEIFITTKLWG 84
Cdd:cd19163 8 KTGLKVSKLGFGAsplggvFGPVDeEEAIRTVHEALDSGINYIDTAPWYgqgRSETVLGKALK--GIPRDSYYLATKVGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 85 TEQRDPE----------AALNKSLKRLGLDYVDLYLMHWP--VPLkTDRVTDGnvlCIPTLedgtvdidtkewnfiktwe 152
Cdd:cd19163 86 YGLDPDKmfdfsaeritKSVEESLKRLGLDYIDIIQVHDIefAPS-LDQILNE---TLPAL------------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 153 lmQELPKTGKTKAVGVSNFSINNIKELLESpnnkvvpATNQIEI------HPLLPQ--DELIAFCKEKGIVVEAYSPFGS 224
Cdd:cd19163 143 --QKLKEEGKVRFIGITGYPLDVLKEVLER-------SPVKIDTvlsychYTLNDTslLELLPFFKEKGVGVINASPLSM 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6320576 225 ---ANAPL---------LKE--QAIIDMAKKHGVEPAQLIISWSIQ--RGYVVLAKSVNPERIVSNFKIFTLPEDD 284
Cdd:cd19163 214 gllTERGPpdwhpaspeIKEacAKAAAYCKSRGVDISKLALQFALSnpDIATTLVGTASPENLRKNLEAAEEPLDA 289
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
42-258 |
8.42e-19 |
|
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: 84.79 E-value: 8.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 42 ALKAGYRHIDAAAIY---LNEEEVGRAIKDSgvPREEIFITTKL-------WGTEQR-DPE---AALNKSLKRLGLDYVD 107
Cdd:cd19145 42 AFNSGVTFLDTSDIYgpnTNEVLLGKALKDG--PREKVQLATKFgiheiggSGVEVRgDPAyvrAACEASLKRLDVDYID 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 108 LYLMHwpvplktdRVtdgnvlciptleDGTVDIDTkewnfikTWELMQELPKTGKTKAVGVSNFSINNIKELlespnNKV 187
Cdd:cd19145 120 LYYQH--------RI------------DTTVPIEI-------TMGELKKLVEEGKIKYIGLSEASADTIRRA-----HAV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 188 VPATN-QIEiHPLLPQD---ELIAFCKEKGIVVEAYSPFGS---ANAPLLKE--------------------------QA 234
Cdd:cd19145 168 HPITAvQLE-WSLWTRDieeEIIPTCRELGIGIVPYSPLGRgffAGKAKLEEllensdvrkshprfqgenleknkvlyER 246
|
250 260
....*....|....*....|....
gi 6320576 235 IIDMAKKHGVEPAQLIISWSIQRG 258
Cdd:cd19145 247 VEALAKKKGCTPAQLALAWVLHQG 270
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
21-283 |
1.12e-18 |
|
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: 84.14 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 21 PVLGFGT------WRSVDN-NGYHSVIAALKAGYRHIDAAAIYLNEEE-VGRAIKdsGVPREEIFITTKLwGTEQRDP-- 90
Cdd:cd19090 1 SALGLGTaglggvFGGVDDdEAVATIRAALDLGINYIDTAPAYGDSEErLGLALA--ELPREPLVLSTKV-GRLPEDTad 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 91 ------EAALNKSLKRLGLDYVDLYLMHWPvplktDRVTDGNVLciptLEDGTVdidtkewnfiktwELMQELPKTGKTK 164
Cdd:cd19090 78 ysadrvRRSVEESLERLGRDRIDLLMIHDP-----ERVPWVDIL----APGGAL-------------EALLELKEEGLIK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 165 AVGVSNFSINNIKELLEspnnkvvpaTNQIEI------HPLLPQ---DELIAFCKEKGIVVEAYSPFGS----------- 224
Cdd:cd19090 136 HIGLGGGPPDLLRRAIE---------TGDFDVvltanrYTLLDQsaaDELLPAAARHGVGVINASPLGMgllagrpperv 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 225 --ANAPLLKE-----QAIIDMAKKHGVEPAQLII--SWSIQRGYVVLAKSVNPERIVSNFKIFT--LPED 283
Cdd:cd19090 207 ryTYRWLSPElldraKRLYELCDEHGVPLPALALrfLLRDPRISTVLVGASSPEELEQNVAAAEgpLPEE 276
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
15-276 |
1.24e-18 |
|
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: 84.23 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 15 NTGASIPVLGFGTWRsvdNNGYHS--------VIAALKAGYRHIDAAAIYLN-----EEEVGRAIK-DSGVPREEIFITT 80
Cdd:cd19089 6 RSGLHLPAISLGLWH---NFGDYTspeearelLRTAFDLGITHFDLANNYGPppgsaEENFGRILKrDLRPYRDELVIST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 81 KL-----------WGTEQRdPEAALNKSLKRLGLDYVDLYLMHWP---VPLKtdrvtdgnvlciptledgtvdidtkewn 146
Cdd:cd19089 83 KAgygmwpgpygdGGSRKY-LLASLDQSLKRMGLDYVDIFYHHRYdpdTPLE---------------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 147 fiktwELMQELP---KTGKTKAVGVSNFSINNIKELLESPNNKVVP-ATNQIEIHpLL---PQDELIAFCKEKGIVVEAY 219
Cdd:cd19089 134 -----ETMTALAdavRSGKALYVGISNYPGAKARRAIALLRELGVPlIIHQPRYS-LLdrwAEDGLLEVLEEAGIGFIAF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 220 SP------------------FGSANAPLLKEQAIID-----------MAKKHGVEPAQLIISWSIQRGYV--VLAKSVNP 268
Cdd:cd19089 208 SPlaqglltdkylngippdsRRAAESKFLTEEALTPekleqlrklnkIAAKRGQSLAQLALSWVLRDPRVtsVLIGASSP 287
|
....*...
gi 6320576 269 ERIVSNFK 276
Cdd:cd19089 288 SQLEDNVA 295
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
21-223 |
2.37e-18 |
|
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381322 [Multi-domain] Cd Length: 255 Bit Score: 82.61 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 21 PVLGFGTWR-------SVD-NNGYHSVIAALKAGYRHIDAAAIYLN---EEEVGRAIKDsgVPREEIFITTKL--WGTEQ 87
Cdd:cd19096 1 SVLGFGTMRlpesdddSIDeEKAIEMIRYAIDAGINYFDTAYGYGGgksEEILGEALKE--GPREKFYLATKLppWSVKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 88 R-DPEAALNKSLKRLGLDYVDLYLMHWpvplktdrvtdgnvLCIPTLEDGTVDIDTKEWnfiktwelMQELPKTGKTKAV 166
Cdd:cd19096 79 AeDFRRILEESLKRLGVDYIDFYLLHG--------------LNSPEWLEKARKGGLLEF--------LEKAKKEGLIRHI 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6320576 167 GVSnF--SINNIKELLESPNNKVVpatnQIEIHPL----LPQDELIAFCKEKGIVVEAYSPFG 223
Cdd:cd19096 137 GFS-FhdSPELLKEILDSYDFDFV----QLQYNYLdqenQAGRPGIEYAAKKGMGVIIMEPLK 194
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
42-260 |
1.19e-17 |
|
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the prototype of this family. It is an NADP(H)-dependent aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NADP(H) as a hydride donor.
Pssm-ID: 381320 [Multi-domain] Cd Length: 328 Bit Score: 81.84 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 42 ALKAGYRHIDAAAIY----------LNEEEVGRAIKDSGvPREEIFITTKLWGTEQR-----------DPE---AALNKS 97
Cdd:cd19094 27 AFDEGVNFIDTAEMYpvppspetqgRTEEIIGSWLKKKG-NRDKVVLATKVAGPGEGitwprgggtrlDREnirEAVEGS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 98 LKRLGLDYVDLYLMHWPvplktDRvtdgNVLCIPTLEDGTVDIDTKEWNFIKTWELMQELPKTGKTKAVGVSN------F 171
Cdd:cd19094 106 LKRLGTDYIDLYQLHWP-----DR----YTPLFGGGYYTEPSEEEDSVSFEEQLEALGELVKAGKIRHIGLSNetpwgvM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 172 SINNIKELLESPnnKVVPATNQieiHPLLPQ---DELIAFCKEKGIVVEAYSPFG----------SANAP---------- 228
Cdd:cd19094 177 KFLELAEQLGLP--RIVSIQNP---YSLLNRnfeEGLAEACHRENVGLLAYSPLAggvltgkyldGAARPeggrlnlfpg 251
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 6320576 229 ----LLKEQAI------IDMAKKHGVEPAQLIISWSIQRGYV 260
Cdd:cd19094 252 ymarYRSPQALeavaeyVKLARKHGLSPAQLALAWVRSRPFV 293
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
41-291 |
9.91e-17 |
|
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: 78.91 E-value: 9.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 41 AALKAGYRHIDAAAIY---LNEEEVGRAIKDsgVPREEIFITTKLwgTEQ-----RDP-EAALNKSLKRLGLDYVDLYLM 111
Cdd:cd19103 40 KAMAAGLNLWDTAAVYgmgASEKILGEFLKR--YPREDYIISTKF--TPQiagqsADPvADMLEGSLARLGTDYIDIYWI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 112 HWPVplktdrvtdgnvlciptledgtvdiDTKEWnfikTWELMqELPKTGKTKAVGVSNFSINNIK---ELLESPNNKVV 188
Cdd:cd19103 116 HNPA-------------------------DVERW----TPELI-PLLKSGKVKHVGVSNHNLAEIKranEILAKAGVSLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 189 PATNQIE-IHPLLPQDELIAFCKEKGIVVEAYS-----------------PFGSANA----PLLKE-----QAIIDMAKK 241
Cdd:cd19103 166 AVQNHYSlLYRSSEEAGILDYCKENGITFFAYMvleqgalsgkydtkhplPEGSGRAetynPLLPQleeltAVMAEIGAK 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 6320576 242 HGVEPAQLIISWSIQRGYVVLAKSVNPERIVSNFKI--FTLPEDDFKTISNL 291
Cdd:cd19103 246 HGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAasITLTDDEIKELEQL 297
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
15-116 |
1.67e-16 |
|
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: 78.41 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 15 NTGASIPVLGFGTW----RSVDNNGYHSVI-AALKAGYRHIDAAAIYLN---EEEVGRAIKDSGVPREEIFITTKL-WGT 85
Cdd:cd19143 8 RSGLKVSALSFGSWvtfgNQVDVDEAKECMkAAYDAGVNFFDNAEVYANgqsEEIMGQAIKELGWPRSDYVVSTKIfWGG 87
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 6320576 86 EQRDPEA----------ALNKSLKRLGLDYVDLYLMHWPVP 116
Cdd:cd19143 88 GGPPPNDrglsrkhiveGTKASLKRLQLDYVDLVFCHRPDP 128
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-249 |
1.95e-16 |
|
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: 78.46 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 15 NTGASIPVLGFG------TW-RSVDNNGYHSVIAALKAGYRHIDAAAIYLN---EEEVGRAIKdsGVPrEEIFITTKLWG 84
Cdd:cd19104 7 RTGLKVSELTFGgggiggLMgRTTREEQIAAVRRALDLGINFFDTAPSYGDgksEENLGRALK--GLP-AGPYITTKVRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 85 TEQRDP------EAALNKSLKRLGLDYVDLYLMHwpvplktDRVTDGnvlcipTLEDGTVDIDTKEWNF-IKTWELMQEL 157
Cdd:cd19104 84 DPDDLGdiggqiERSVEKSLKRLKRDSVDLLQLH-------NRIGDE------RDKPVGGTLSTTDVLGlGGVADAFERL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 158 PKTGKTKAVGVSNFS-INNIKELLESPnnkvVPATNQI--------------EIHPLLPQDELIAFCKEKGIVVEAYSPF 222
Cdd:cd19104 151 RSEGKIRFIGITGLGnPPAIRELLDSG----KFDAVQVyynllnpsaaearpRGWSAQDYGGIIDAAAEHGVGVMGIRVL 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 6320576 223 ------GSANAPLL--------------KEQAIIDMAKKHGVEPAQL 249
Cdd:cd19104 227 aagaltTSLDRGREapptsdsdvaidfrRAAAFRALAREWGETLAQL 273
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
41-253 |
3.71e-16 |
|
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, Saccharopolyspora erythraea EryBII, and Streptomyces avermitilis aveBVIII are founding members of aldo-keto reductase family 12 member A1 (AKR12A1), B1 (AKR12B1), and C1(AKR12C1), respectively. TylCII acts as a NDP-hexose 2,3-enoyl reductase. EryBII is a mycarose/desosamine reductase involved in L-mycarose and D-desosamine production. aveBVIII functions as a dTDP-4-keto-6-deoxy-L-hexose-2,3-reductase.
Pssm-ID: 381313 [Multi-domain] Cd Length: 310 Bit Score: 77.23 E-value: 3.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 41 AALKAGYRHIDAAAIY---LNEEEVGRAIKDSgvpREEIFITTKLWGTEQRDPEA----------ALNKSLKRLGLDYVD 107
Cdd:cd19087 38 RALDAGINFFDTADVYgggRSEEIIGRWIAGR---RDDIVLATKVFGPMGDDPNDrglsrrhirrAVEASLRRLQTDYID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 108 LYLMHWPvplktDRVTDgnvlciptledgtvdidtkewnFIKTWELMQELPKTGKTKAVGVSNFSINNIKELLE------ 181
Cdd:cd19087 115 LYQMHHF-----DRDTP----------------------LEETLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGiaarrg 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 182 --------SPNNKVVpatNQIEihpllpqDELIAFCKEKGIVVEAYSPFGS------------------------ANAPL 229
Cdd:cd19087 168 llrfvseqPMYNLLK---RQAE-------LEILPAARAYGLGVIPYSPLAGglltgkygkgkrpesgrlveraryQARYG 237
|
250 260
....*....|....*....|....*....
gi 6320576 230 LKE-----QAIIDMAKKHGVEPAQLIISW 253
Cdd:cd19087 238 LEEyrdiaERFEALAAEAGLTPASLALAW 266
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
41-288 |
1.80e-15 |
|
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: 75.33 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 41 AALKAGYRHIDAAAIYLN---EEEVGRAIKDSgvpREEIFITTKL-WGTEQRDPEA----------ALNKSLKRLGLDYV 106
Cdd:cd19080 39 AYVEAGGNFIDTANNYTNgtsERLLGEFIAGN---RDRIVLATKYtMNRRPGDPNAggnhrknlrrSVEASLRRLQTDYI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 107 DLYLMHWPvplktdrvtdgnvlciptleDGTVDIDtkewnfiktwELMQ---ELPKTGKTKAVGVSNF------SINNIK 177
Cdd:cd19080 116 DLLYVHAW--------------------DFTTPVE----------EVMRaldDLVRAGKVLYVGISDTpawvvaRANTLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 178 ELlespNNKVVPATNQIEiHPLL---PQDELIAFCKEKGIVVEAYSPFGS----------------------ANAPLLKE 232
Cdd:cd19080 166 EL----RGWSPFVALQIE-YSLLertPERELLPMARALGLGVTPWSPLGGglltgkyqrgeegrageakgvtVGFGKLTE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6320576 233 Q--AIID----MAKKHGVEPAQLIISWSIQRGYVV--LAKSVNPERIVSNFKI--FTLPEDDFKTI 288
Cdd:cd19080 241 RnwAIVDvvaaVAEELGRSAAQVALAWVRQKPGVVipIIGARTLEQLKDNLGAldLTLSPEQLARL 306
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
41-253 |
4.04e-15 |
|
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: 74.13 E-value: 4.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 41 AALKAGYRHIDAAAIY-------LNEEEVGRAIKDSGVpREEIFITTK-----LWGTEQR--DPE---AALNKSLKRLGL 103
Cdd:cd19082 25 AFVELGGNFIDTARVYgdwvergASERVIGEWLKSRGN-RDKVVIATKgghpdLEDMSRSrlSPEdirADLEESLERLGT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 104 DYVDLYLMHwpvplktdRvtdgnvlciptlEDGTVDIDtkewnfiktwELM---QELPKTGKTKAVGVSNFSINNIKELL 180
Cdd:cd19082 104 DYIDLYFLH--------R------------DDPSVPVG----------EIVdtlNELVRAGKIRAFGASNWSTERIAEAN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 181 E--SPNNKVVPATNQIE---IHPLLPQ----------DELIAFCKEKGIVVEAYSP--------FGSANAPLLKEQA--- 234
Cdd:cd19082 154 AyaKAHGLPGFAASSPQwslARPNEPPwpgptlvamdEEMRAWHEENQLPVFAYSSqargffskRAAGGAEDDSELRrvy 233
|
250 260 270
....*....|....*....|....*....|
gi 6320576 235 -----------IIDMAKKHGVEPAQLIISW 253
Cdd:cd19082 234 yseenferlerAKELAEEKGVSPTQIALAY 263
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
23-255 |
6.71e-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: 381325 [Multi-domain] Cd Length: 316 Bit Score: 73.89 E-value: 6.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 23 LGFGTWR--SVDNNGYH---SVIAALKAGYRHIDAAAIY---LNEEEVGRAIK----DSGVPREEIFITTK-----LWGT 85
Cdd:cd19099 6 LGLGTYRgdSDDETDEEyreALKAALDSGINVIDTAINYrggRSERLIGKALRelieKGGIKRDEVVIVTKagyipGDGD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 86 EQRDP------------------------------EAALNKSLKRLGLDYVDLYLMHWPvplktdrvtdgnvlciptlED 135
Cdd:cd19099 86 EPLRPlkyleeklgrglidvadsaglrhcispaylEDQIERSLKRLGLDTIDLYLLHNP-------------------EE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 136 GTVDIDTKE--WNFIKTWELMQELPKTGKTKAVGVS--NFSINNIKELLESPNNKVVPATN------------QIEIHPL 199
Cdd:cd19099 147 QLLELGEEEfyDRLEEAFEALEEAVAEGKIRYYGIStwDGFRAPPALPGHLSLEKLVAAAEevggdnhhfkviQLPLNLL 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6320576 200 LPQ------------DELIAFCKEKGIVVEAYSPFGSANapLLKEQAIIDMAKKHGVEP-AQLIISWSI 255
Cdd:cd19099 227 EPEaltekntvkgeaLSLLEAAKELGLGVIASRPLNQGQ--LLGELRLADLLALPGGATlAQRALQFAR 293
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
20-295 |
7.57e-15 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 74.12 E-value: 7.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 20 IPVLGFGTWRSVDNNGYHSVIA----ALKAGYRHIDAAAIY----------LNEEEVGRAIKDSGvPREEIFITTKLWGT 85
Cdd:PRK10625 13 VSTLGLGTMTFGEQNSEADAHAqldyAVAQGINLIDVAEMYpvpprpetqgLTETYIGNWLAKRG-SREKLIIASKVSGP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 86 --------------EQRDPEAALNKSLKRLGLDYVDLYLMHWPvplktDRVTDgnvlCIPTLEDGTVDiDTKEWNFIKTW 151
Cdd:PRK10625 92 srnndkgirpnqalDRKNIREALHDSLKRLQTDYLDLYQVHWP-----QRPTN----CFGKLGYSWTD-SAPAVSLLETL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 152 ELMQELPKTGKTKAVGVSN---------------------FSINNIKELLESPNNKVVPATNQIEIHPLLPQDELiAFCK 210
Cdd:PRK10625 162 DALAEQQRAGKIRYIGVSNetafgvmrylhlaekhdlpriVTIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCL-AFGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 211 EKGIVVEAYSPFGSANAPLLK---------EQAI---IDMAKKHGVEPAQLIISWSIQRGYV--VLAKSVNPERIVSNFK 276
Cdd:PRK10625 241 LTGKYLNGAKPAGARNTLFSRftrysgeqtQKAVaayVDIAKRHGLDPAQMALAFVRRQPFVasTLLGATTMEQLKTNIE 320
|
330 340
....*....|....*....|.
gi 6320576 277 IF--TLPEDdfkTISNLSKVH 295
Cdd:PRK10625 321 SLhlTLSEE---VLAEIEAVH 338
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-288 |
9.15e-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: 381327 [Multi-domain] Cd Length: 304 Bit Score: 73.40 E-value: 9.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 19 SIPVLGFGTWRSVDNNGYHS----VIAALK----AGYRHIDAAAIYLNEEE-VGRAIK---DSGVPREEIFITTKlW--- 83
Cdd:cd19101 1 TISRVINGMWQLSGGHGGIRdedaAVRAMAayvdAGLTTFDCADIYGPAEElIGEFRKrlrRERDAADDVQIHTK-Wvpd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 84 -GTEQRDP---EAALNKSLKRLGLDYVDLYLMHWpvplktdrvtdgnvlciptledgtvdIDTKEWNFIKTWELMQELPK 159
Cdd:cd19101 80 pGELTMTRayvEAAIDRSLKRLGVDRLDLVQFHW--------------------------WDYSDPGYLDAAKHLAELQE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 160 TGKTKAVGVSNFSINNIKELLESPnnkVVPATNQIEiHPLL---PQDELIAFCKEKGIVVEAY----------------S 220
Cdd:cd19101 134 EGKIRHLGLTNFDTERLREILDAG---VPIVSNQVQ-YSLLdrrPENGMAALCEDHGIKLLAYgtlaggllsekylgvpE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 221 PFGSA--NAPLLKEQAIID-----------------MAKKHGVEPAQLIISWSIQR----GYVVLAKsvNPERIVSNFKI 277
Cdd:cd19101 210 PTGPAleTRSLQKYKLMIDewggwdlfqellrtlkaIADKHGVSIANVAVRWVLDQpgvaGVIVGAR--NSEHIDDNVRA 287
|
330
....*....|...
gi 6320576 278 F--TLPEDDFKTI 288
Cdd:cd19101 288 FsfRLDDEDRAAI 300
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
41-252 |
1.40e-14 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 72.17 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 41 AALKAGYRHIDAAAIYLNEEEV-GRAIKDSgvprEEIFITTKL------WGTEQRDPEAALNKSLKRLGLDYVDLYLMHW 113
Cdd:cd19097 34 YALKAGINTLDTAPAYGDSEKVlGKFLKRL----DKFKIITKLpplkedKKEDEAAIEASVEASLKRLKVDSLDGLLLHN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 114 PvplkTDRVTDGNVLciptledgtvdidtkewnfiktWELMQELPKTGKTKAVGVSNFSINNIKELLESPNNKVVpatnQ 193
Cdd:cd19097 110 P----DDLLKHGGKL----------------------VEALLELKKEGLIRKIGVSVYSPEELEKALESFKIDII----Q 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6320576 194 IEIHPL---LPQDELIAFCKEKGIVV---------------EAYSPFGSANAPLLKeqAIIDMAKKHGVEPAQLIIS 252
Cdd:cd19097 160 LPFNILdqrFLKSGLLAKLKKKGIEIharsvflqglllmepDKLPAKFAPAKPLLK--KLHELAKKLGLSPLELALG 234
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
22-221 |
3.09e-14 |
|
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: 71.82 E-value: 3.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 22 VLGFGTW----RSVDNNGYHSVIAALKA-GYRHIDAAAIYLN---EEEVGRAikdsGVPREEIFITTKL--WGTEQRDPE 91
Cdd:cd19075 4 ILGTMTFgsqgRFTTAEAAAELLDAFLErGHTEIDTARVYPDgtsEELLGEL----GLGERGFKIDTKAnpGVGGGLSPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 92 ---AALNKSLKRLGLDYVDLYLMHWPvplktDRVTDgnvlciptLEDgtvdidtkewnfikTWELMQELPKTGKTKAVGV 168
Cdd:cd19075 80 nvrKQLETSLKRLKVDKVDVFYLHAP-----DRSTP--------LEE--------------TLAAIDELYKEGKFKEFGL 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6320576 169 SNFSINNIKELLE--SPNNKVVPA---------TNQIEihpllpqDELIAFCKEKGIVVEAYSP 221
Cdd:cd19075 133 SNYSAWEVAEIVEicKENGWVLPTvyqgmynaiTRQVE-------TELFPCLRKLGIRFYAYSP 189
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
43-257 |
6.06e-14 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 70.82 E-value: 6.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 43 LKAGYRHIDAAAIYL----------NEEEVGRAIKDSGVpREEIFITTKLwGTEQRDP---------------EAALNKS 97
Cdd:cd19752 27 VAAGGNFLDTANNYAfwteggvggeSERLIGRWLKDRGN-RDDVVIATKV-GAGPRDPdggpespeglsaetiEQEIDKS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 98 LKRLGLDYVDLYLMHwpvplKTDRVTDgnvlciptLEDgtvdidtkewnfikTWELMQELPKTGKTKAVGVSNFSINNIK 177
Cdd:cd19752 105 LRRLGTDYIDLYYAH-----VDDRDTP--------LEE--------------TLEAFNELVKAGKVRAIGASNFAAWRLE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 178 ELLESPNNKVVPATNQIEIH-------PLLP-------QDELIAFCKEKG-IVVEAYSP-----FGSANAPLLKE----- 232
Cdd:cd19752 158 RARQIARQQGWAEFSAIQQRhsylrprPGADfgvqrivTDELLDYASSRPdLTLLAYSPllsgaYTRPDRPLPEQydgpd 237
|
250 260 270
....*....|....*....|....*....|
gi 6320576 233 -----QAIIDMAKKHGVEPAQLIISWSIQR 257
Cdd:cd19752 238 sdarlAVLEEVAGELGATPNQVVLAWLLHR 267
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
21-248 |
1.58e-13 |
|
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: 69.70 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 21 PVLGFGT------WRSVDNNGYHSVIAALKAGYRHIDAAAIY---LNEEEVGRAIKdsGVPREEIFITTKLwGTEQRDPE 91
Cdd:cd19162 1 PRLGLGAaslgnlARAGEDEAAATLDAAWDAGIRYFDTAPLYglgLSERRLGAALA--RHPRAEYVVSTKV-GRLLEPGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 92 AA-------------------LNKSLKRLGLDYVDLYLMHWPVPLKTDRVTDGnvlciptledgtvdidtkewnfiktWE 152
Cdd:cd19162 78 AGrpagadrrfdfsadgirrsIEASLERLGLDRLDLVFLHDPDRHLLQALTDA-------------------------FP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 153 LMQELPKTGKTKAVGVsnfSINNIKELLESPNNKVVPATNQIEIHPLL---PQDELIAFCKEKGIVVEAYSPFGS----- 224
Cdd:cd19162 133 ALEELRAEGVVGAIGV---GVTDWAALLRAARRADVDVVMVAGRYTLLdrrAATELLPLCAAKGVAVVAAGVFNSgilat 209
|
250 260 270
....*....|....*....|....*....|....*..
gi 6320576 225 ------------ANAPLL-KEQAIIDMAKKHGVEPAQ 248
Cdd:cd19162 210 ddpagdrydyrpATPEVLaRARRLAAVCRRYGVPLPA 246
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
24-288 |
6.00e-12 |
|
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding members of aldo-keto reductase family 8 member A1-2 (AKR8A1-2), respectively. PLR (EC 1.1.1.65), also called PL reductase (PL-red), catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+).
Pssm-ID: 381303 [Multi-domain] Cd Length: 302 Bit Score: 64.95 E-value: 6.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 24 GFG----TWRSV---DNNGYHSVIAALKAGYRHIDAAAIY------LNEEEVGRAIKDSGVPREEIFITTK---LWGTEQ 87
Cdd:cd19077 9 GLGlmglTWRPNptpDEEAFETMKAALDAGSNLWNGGEFYgppdphANLKLLARFFRKYPEYADKVVLSVKgglDPDTLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 88 RD--PEA---ALNKSLKRLG-LDYVDLYLMHwpvplktdRVtdgnvlciptleDGTVDIDTkewnfikTWELMQELPKTG 161
Cdd:cd19077 89 PDgsPEAvrkSIENILRALGgTKKIDIFEPA--------RV------------DPNVPIEE-------TIKALKELVKEG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 162 KTKAVGVSNFSINNIKELlespnNKVVP-ATNQIEIHPL---LPQDELIAFCKEKGIVVEAYSPFG-------------- 223
Cdd:cd19077 142 KIRGIGLSEVSAETIRRA-----HAVHPiAAVEVEYSLFsreIEENGVLETCAELGIPIIAYSPLGrglltgriksladi 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 224 -----------------SANAPLLkeQAIIDMAKKHGVEPAQLIISWSIQRGY---VVLAKSVNPERIVSNFKIF--TLP 281
Cdd:cd19077 217 pegdfrrhldrfngenfEKNLKLV--DALQELAEKKGCTPAQLALAWILAQSGpkiIPIPGSTTLERVEENLKAAnvELT 294
|
....*..
gi 6320576 282 EDDFKTI 288
Cdd:cd19077 295 DEELKEI 301
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
15-181 |
3.68e-10 |
|
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: 59.86 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 15 NTGASIPVLGFGT--WRSVDNNGYHSVIA------ALKAGYRHIDAAAIY---LNEEEVGRAIKDSGVPREEIFITTKL- 82
Cdd:cd19153 7 IALGNVSPVGLGTaaLGGVYGDGLEQDEAvaivaeAFAAGINHFDTSPYYgaeSSEAVLGKALAALQVPRSSYTVATKVg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 83 -WGTEQRDPEA-----ALNKSLKRLGLDYVDLYLMHwpvplktdrvtdgnvlcipTLEDGTVDIDTKEwnfikTWELMQE 156
Cdd:cd19153 87 rYRDSEFDYSAervraSVATSLERLHTTYLDVVYLH-------------------DIEFVDYDTLVDE-----ALPALRT 142
|
170 180
....*....|....*....|....*
gi 6320576 157 LPKTGKTKAVGVSNFSINNIKELLE 181
Cdd:cd19153 143 LKDEGVIKRIGIAGYPLDTLTRATR 167
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
21-247 |
3.80e-10 |
|
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381378 [Multi-domain] Cd Length: 308 Bit Score: 59.93 E-value: 3.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 21 PVLGFGT------WRSVDNNGYHSVI-AALKAGYRHIDAAAIY---LNEEEVGRAIKDsgVPREEIFITTKL-------- 82
Cdd:cd19152 1 PKLGFGTaplgnlYEAVSDEEAKATLvAAWDLGIRYFDTAPWYgagLSEERLGAALRE--LGREDYVISTKVgrllvplq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 83 ----------WGTEQRDP---------EAALNKSLKRLGLDYVDLYLMHwpvplktDrvtdgnvlciptLEDGTVDIDTK 143
Cdd:cd19152 79 eveptfepgfWNPLPFDAvfdysydgiLRSIEDSLQRLGLSRIDLLSIH-------D------------PDEDLAGAESD 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 144 EWNFIKTWELM---QELPKTGKTKAVGV-SNFSINNIKELLESPNNKVVPAT-----NQIEIHPLLPQdeliafCKEKGI 214
Cdd:cd19152 140 EHFAQAIKGAFralEELREEGVIKAIGLgVNDWEVILRILEEADLDWVMLAGrytllDHSAARELLPE------CEKRGV 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 6320576 215 VVEAYSPFGS----------------ANAPLL-KEQAIIDMAKKHGVEPA 247
Cdd:cd19152 214 KVVNAGPFNSgflaggdnfdyyeygpAPPELIaRRDRIEALCEQHGVSLA 263
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
15-274 |
2.75e-09 |
|
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2).
Pssm-ID: 381377 [Multi-domain] Cd Length: 309 Bit Score: 57.03 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 15 NTGASIPVLGFGTWRS---VDN--NGYHSVIAALKAGYRHIDAAAIY-----LNEEEVGRAIKDSGVP-REEIFITTKL- 82
Cdd:cd19151 7 RSGLKLPAISLGLWHNfgdVDRyeNSRAMLRRAFDLGITHFDLANNYgpppgSAEENFGRILKEDLKPyRDELIISTKAg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 83 ----------WGTeQRDPEAALNKSLKRLGLDYVDLYLMHWPVPlktdrvtdgnvlciptledgtvDIDTKEwnfikTWE 152
Cdd:cd19151 87 ytmwpgpygdWGS-KKYLIASLDQSLKRMGLDYVDIFYHHRPDP----------------------ETPLEE-----TMG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 153 LMQELPKTGKTKAVGVSNFSINNIKE------------LLESPNNKVVPATNQIEIHPLLPQDEL--IAFCK-EKGIVVE 217
Cdd:cd19151 139 ALDQIVRQGKALYVGISNYPPEEAREaaailkdlgtpcLIHQPKYSMFNRWVEEGLLDVLEEEGIgcIAFSPlAQGLLTD 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6320576 218 AY-------SPFGSANAPLLKEQAIID----------MAKKHGVEPAQLIISWSIQRGYV--VLAKSVNPERIVSN 274
Cdd:cd19151 219 RYlngipedSRAAKGSSFLKPEQITEEklakvrrlneIAQARGQKLAQMALAWVLRNKRVtsVLIGASKPSQIEDA 294
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
16-288 |
7.28e-09 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 56.15 E-value: 7.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 16 TGASIPVLGFGTWRSVD-NNGYHSVIAALKA----GYRHIDAAAIY-----LNEEEVGRAIKDSGVP-REEIFITTK--- 81
Cdd:PRK09912 21 SGLRLPALSLGLWHNFGhVNALESQRAILRKafdlGITHFDLANNYgpppgSAEENFGRLLREDFAAyRDELIISTKagy 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 82 -LW------GTEQRDPEAALNKSLKRLGLDYVDLYLMHwpvplktdRVtDGNVlciPTLEdgtvdidtkewnfikTWELM 154
Cdd:PRK09912 101 dMWpgpygsGGSRKYLLASLDQSLKRMGLEYVDIFYSH--------RV-DENT---PMEE---------------TASAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 155 QELPKTGKTKAVGVSNFSINNIKELLESPNNKVVPATNQIEIHPLL----PQDELIAFCKEKGIVVEAYSPFGS------ 224
Cdd:PRK09912 154 AHAVQSGKALYVGISSYSPERTQKMVELLREWKIPLLIHQPSYNLLnrwvDKSGLLDTLQNNGVGCIAFTPLAQglltgk 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 225 --------------------------ANAPLLKEQAIIDMAKKHGVEPAQLIISWSIQRGYV--VLAKSVNPERIVSN-- 274
Cdd:PRK09912 234 ylngipqdsrmhregnkvrgltpkmlTEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDERVtsVLIGASRAEQLEENvq 313
|
330
....*....|....*
gi 6320576 275 -FKIFTLPEDDFKTI 288
Cdd:PRK09912 314 aLNNLTFSTEELAQI 328
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
16-246 |
8.18e-08 |
|
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: 52.85 E-value: 8.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 16 TGASIPVLGFGTWRS----VDNNGYHSVI-AALKAGYRHIDAAAIYLN---EEEVGRAIKDSGVPREEIFITTKL-WGTe 86
Cdd:cd19142 9 SGLRVSNVGLGTWSTfstaISEEQAEEIVtLAYENGINYFDTSDAFTSgqaETELGRILKKKGWKRSSYIVSTKIyWSY- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 87 qRDPEAALNK---------SLKRLGLDYVDLYLMHwpvplKTDrvtdgnVLCiPTLEdgtvdidtkewnFIKTwelMQEL 157
Cdd:cd19142 88 -GSEERGLSRkhiiesvraSLRRLQLDYIDIVIIH-----KAD------PMC-PMEE------------VVRA---MSYL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 158 PKTGKTKAVGVSNFSINNIKELLESPN--NKVVPATNQIEIHPllpqdeliaFCKEK------------GIVVEAYSPFG 223
Cdd:cd19142 140 IDNGLIMYWGTSRWSPVEIMEAFSIARqfNCPTPICEQSEYHM---------FCREKmelympelynkvGVGLITWSPLS 210
|
250 260
....*....|....*....|....*.
gi 6320576 224 SANAP---LLKEQAIIDMAKKHGVEP 246
Cdd:cd19142 211 LGLDPgisEETRRLVTKLSFKSSKYK 236
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
16-276 |
5.53e-07 |
|
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
Pssm-ID: 381376 [Multi-domain] Cd Length: 309 Bit Score: 50.15 E-value: 5.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 16 TGASIPVLGFGTWRSVDNNGYHSV-----IAALKAGYRHIDAAAIY-----LNEEEVGRAIKDSGVP-REEIFITTKL-- 82
Cdd:cd19150 8 SGLKLPALSLGLWHNFGDDTPLETqrailRTAFDLGITHFDLANNYgpppgSAEENFGRILREDFAGyRDELIISTKAgy 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 83 ---------WGTeQRDPEAALNKSLKRLGLDYVDLYLMHwpvplktdrvtdgnvlciptledgTVDIDTKewnFIKTWEL 153
Cdd:cd19150 88 dmwpgpygeWGS-RKYLLASLDQSLKRMGLDYVDIFYSH------------------------RFDPDTP---LEETMGA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 154 MQELPKTGKTKAVGVSNFSINNIKELLESPNNKVVPatnqIEIHP--------LLPQDELIAFCKEKGIVVEAYSPF--- 222
Cdd:cd19150 140 LDHAVRSGKALYVGISSYSPERTREAAAILRELGTP----LLIHQpsynmlnrWVEESGLLDTLQELGVGCIAFTPLaqg 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 223 -------------------GSANAPLLKEQ------AIIDMAKKHGVEPAQLIISWSIQRGYV--VLAKSVNPERIVSNF 275
Cdd:cd19150 216 lltdkylngipegsraskeRSLSPKMLTEAnlnsirALNEIAQKRGQSLAQMALAWVLRDGRVtsALIGASRPEQLEENV 295
|
.
gi 6320576 276 K 276
Cdd:cd19150 296 G 296
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
15-221 |
1.22e-06 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 49.39 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 15 NTGASIPVLGFGT--WRSV-----DNNGYHSVIAALKAGYRHIDAAAIY---LNEEEVGRAIKDSGVPREEIFITTKLwG 84
Cdd:PLN02587 6 STGLKVSSVGFGAspLGSVfgpvsEEDAIASVREAFRLGINFFDTSPYYggtLSEKVLGKALKALGIPREKYVVSTKC-G 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 85 --TEQRDPEA-----ALNKSLKRLGLDYVDLYLMHwpvplktdrvtdgnvlcipTLEDGTVDIDTKEwnfikTWELMQEL 157
Cdd:PLN02587 85 ryGEGFDFSAervtkSVDESLARLQLDYVDILHCH-------------------DIEFGSLDQIVNE-----TIPALQKL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6320576 158 PKTGKTKAVGVSNFSINNIKELLEspnnKVVPAT------------NQIEIHPLLPqdeliaFCKEKGIVVEAYSP 221
Cdd:PLN02587 141 KESGKVRFIGITGLPLAIFTYVLD----RVPPGTvdvilsychyslNDSSLEDLLP------YLKSKGVGVISASP 206
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
18-112 |
1.64e-06 |
|
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: 48.81 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 18 ASIPVLGFGTwrSVDNNGYHS----------VIAALKAGYRHIDAAAIYLNEEEV-GRAIKD--SGVPREEIFITTKL-- 82
Cdd:cd19164 11 AGLPPLIFGA--ATFSYQYTTdpesippvdiVRRALELGIRAFDTSPYYGPSEIIlGRALKAlrDEFPRDTYFIITKVgr 88
|
90 100 110
....*....|....*....|....*....|....*
gi 6320576 83 WGTEQRD--PE---AALNKSLKRLGLDYVDLYLMH 112
Cdd:cd19164 89 YGPDDFDysPEwirASVERSLRRLHTDYLDLVYLH 123
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
21-167 |
3.14e-06 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 48.09 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 21 PVLGFGT------WRSVDNNGYHSVI-AALKAGYRHIDAAAIY---LNEEEVGRAIKDsgVPREEIFITTKLwG---TEQ 87
Cdd:cd19161 1 SELGLGTaglgnlYTAVSNADADATLdAAWDSGIRYFDTAPMYghgLAEHRLGDFLRE--KPRDEFVLSTKV-GrllKPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 88 RDPEA-------------------------ALNKSLKRLGLDYVDLYLMHwpvplKTDRVTDGnvlciptledgtvdiDT 142
Cdd:cd19161 78 REGSVpdpngfvdplpfeivydysydgimrSFEDSLQRLGLNRIDILYVH-----DIGVYTHG---------------DR 137
|
170 180 190
....*....|....*....|....*....|
gi 6320576 143 KEWNFIKT-----WELMQELPKTGKTKAVG 167
Cdd:cd19161 138 KERHHFAQlmsggFKALEELKKAGVIKAFG 167
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
16-116 |
5.63e-06 |
|
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381367 [Multi-domain] Cd Length: 310 Bit Score: 47.06 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 16 TGASIPVLGFGTWRSV-----DNNGYHSVIAALKAGYRHIDAAAIYLN---EEEVGRAIKDSGVPREEIFITTKL-WG-- 84
Cdd:cd19141 8 SGLRVSCLGLGTWVTFgsqisDEVAEELVTLAYENGINLFDTAEVYAAgkaEIVLGKILKKKGWRRSSYVITTKIfWGgk 87
|
90 100 110
....*....|....*....|....*....|....*...
gi 6320576 85 --TEQ----RDPEAALNKSLKRLGLDYVDLYLMHWPVP 116
Cdd:cd19141 88 aeTERglsrKHIIEGLKASLERLQLEYVDIVFANRPDP 125
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
16-298 |
1.11e-05 |
|
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo sapiens, Mus musculus, Mustela putorius, Rattus norvegicus, and Kvb1.1, Kvb1.2 from Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A3 (AKR6A3), A8 (AKR6A8), A10a (AKR6A10a), A13 (AKR6A13), A7 (AKR6A7) and A10b (AKR6A10b), respectively. KCAB1B, also called Shaker channel b-subunit 1(Kvb1), K(+) channel subunit beta-1, or Kv-beta-1, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It modulates action potentials via its effect on the pore-forming alpha subunits.
Pssm-ID: 381385 [Multi-domain] Cd Length: 323 Bit Score: 46.19 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 16 TGASIPVLGFGTWRSV-----DNNGYHSVIAALKAGYRHIDAAAIYL-NEEEV--GRAIKDSGVPREEIFITTKLWGTEQ 87
Cdd:cd19159 9 SGLRVSCLGLGTWVTFggqisDEVAERLMTIAYESGVNLFDTAEVYAaGKAEVilGSIIKKKGWRRSSLVITTKLYWGGK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 88 RDPEAALNK---------SLKRLGLDYVDLYLMHWPvplktdrvtdgnvlciptledgtvDIDTKEWNFIKTwelMQELP 158
Cdd:cd19159 89 AETERGLSRkhiieglkgSLQRLQLEYVDVVFANRP------------------------DSNTPMEEIVRA---MTHVI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 159 KTGKTKAVGVSNFSINNIKELLESPN--NKVVPATNQIEIHplLPQDE-----LIAFCKEKGIVVEAYSPFG-------- 223
Cdd:cd19159 142 NQGMAMYWGTSRWSAMEIMEAYSVARqfNMIPPVCEQAEYH--LFQREkvevqLPELYHKIGVGAMTWSPLAcgiisgky 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 224 ------SANAPL-----LKEQAI--------------IDMAKKHGVEPAQLIISWSIQRGYV--VLAKSVNPERIVSNF- 275
Cdd:cd19159 220 gngvpeSSRASLkcyqwLKERIVseegrkqqnklkdlSPIAERLGCTLPQLAVAWCLRNEGVssVLLGSSTPEQLIENLg 299
|
330 340
....*....|....*....|...
gi 6320576 276 KIFTLPEDDFKTISNLSKVHGTK 298
Cdd:cd19159 300 AIQVLPKMTSHVVNEIDNILRNK 322
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
16-108 |
1.59e-05 |
|
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo sapiens, Rattus norvegicus, and Mus musculus, are founding members of aldo-keto reductase family 6 member A9 (AKR6A9), A12 (AKR6A12), A14 (AKR6A14), respectively. KCAB3B, also called Shaker channel b-subunit 3 (Kvb3), K(+) channel subunit beta-3, or Kv-beta-3, is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. It alters the functional properties of Kv1.5.
Pssm-ID: 381386 [Multi-domain] Cd Length: 325 Bit Score: 45.75 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 16 TGASIPVLGFGTWRSV-----DNNGYHSVIAALKAGYRHIDAAAIYLN---EEEVGRAIKDSGVPREEIFITTKLWGTEQ 87
Cdd:cd19160 11 SGLRVSCLGLGTWVTFgsqisDETAEDLLTVAYEHGVNLFDTAEVYAAgkaERTLGNILKSKGWRRSSYVVTTKIYWGGQ 90
|
90 100 110
....*....|....*....|....*....|
gi 6320576 88 RDPEAALNK---------SLKRLGLDYVDL 108
Cdd:cd19160 91 AETERGLSRkhiieglrgSLDRLQLEYVDI 120
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
16-116 |
1.72e-04 |
|
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: 42.76 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 16 TGASIPVLGFGTWRS-----VDNNGYHSVIAALKAGYRHIDAAAIYLN---EEEVGRAIKDSGVPREEIFITTKLWGTEQ 87
Cdd:cd19158 9 SGLRVSCLGLGTWVTfggqiTDEMAEHLMTLAYDNGINLFDTAEVYAAgkaEVVLGNIIKKKGWRRSSLVITTKIFWGGK 88
|
90 100 110
....*....|....*....|....*....|....*...
gi 6320576 88 RDPEAALNK---------SLKRLGLDYVDLYLMHWPVP 116
Cdd:cd19158 89 AETERGLSRkhiieglkaSLERLQLEYVDVVFANRPDP 126
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
45-113 |
3.07e-03 |
|
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: 38.65 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320576 45 AGYRHIDAAAIYLNEEE---VGRAIKDSGVpREEIFITTKL-----------------WGTEQRDPEAALNKSLKRLGLD 104
Cdd:cd19147 46 AGGNFIDTANNYQDEQSetwIGEWMKSRKN-RDQIVIATKFttdykayevgkgkavnyCGNHKRSLHVSVRDSLRKLQTD 124
|
....*....
gi 6320576 105 YVDLYLMHW 113
Cdd:cd19147 125 WIDILYVHW 133
|
|
| |
