|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
14-320 |
0e+00 |
|
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: 668.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 14 EYRRCGRSGLKLPAISLGLWHNFGDATLVETSRQLLRRSFDLGITHFDLANNYGPPPGSAESHFGRLLKEDFLPYRDELI 93
Cdd:cd19151 1 KYNRCGRSGLKLPAISLGLWHNFGDVDRYENSRAMLRRAFDLGITHFDLANNYGPPPGSAEENFGRILKEDLKPYRDELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 94 ISTKAGYTMWDGPYGDWGSRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISNYPAD 173
Cdd:cd19151 81 ISTKAGYTMWPGPYGDWGSKKYLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGISNYPPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 174 RAREAIDLLAQLGTPCIIHQPKYSMFERWVEDGLLDLLQEKGVGSIAFSPLAGGQLTDRYLNGIPADSRAASGSRFLNPD 253
Cdd:cd19151 161 EAREAAAILKDLGTPCLIHQPKYSMFNRWVEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYLNGIPEDSRAAKGSSFLKPE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495144968 254 QITPEKLDKVRKLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQIDDAVGMLANRGFSAEE 320
Cdd:cd19151 241 QITEEKLAKVRRLNEIAQARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALDNREFSEEE 307
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
15-320 |
0e+00 |
|
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: 574.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 15 YRRCGRSGLKLPAISLGLWHNFGDATLVETSRQLLRRSFDLGITHFDLANNYGPPPGSAESHFGRLLKEDFLPYRDELII 94
Cdd:cd19089 1 YRRCGRSGLHLPAISLGLWHNFGDYTSPEEARELLRTAFDLGITHFDLANNYGPPPGSAEENFGRILKRDLRPYRDELVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 95 STKAGYTMWDGPYGDWGSRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISNYPADR 174
Cdd:cd19089 81 STKAGYGMWPGPYGDGGSRKYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPGAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 175 AREAIDLLAQLGTPCIIHQPKYSMFERWVEDGLLDLLQEKGVGSIAFSPLAGGQLTDRYLNGIPADSRAASGSRFLNPDQ 254
Cdd:cd19089 161 ARRAIALLRELGVPLIIHQPRYSLLDRWAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKYLNGIPPDSRRAAESKFLTEEA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495144968 255 ITPEKLDKVRKLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQIDDAVGMLANRGFSAEE 320
Cdd:cd19089 241 LTPEKLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAALKNLDFSEEE 306
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
15-320 |
0e+00 |
|
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: 537.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 15 YRRCGRSGLKLPAISLGLWHNFGDATLVETSRQLLRRSFDLGITHFDLANNYGPPPGSAESHFGRLLKEDFLPYRDELII 94
Cdd:cd19150 2 YRRCGKSGLKLPALSLGLWHNFGDDTPLETQRAILRTAFDLGITHFDLANNYGPPPGSAEENFGRILREDFAGYRDELII 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 95 STKAGYTMWDGPYGDWGSRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISNYPADR 174
Cdd:cd19150 82 STKAGYDMWPGPYGEWGSRKYLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYSPER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 175 AREAIDLLAQLGTPCIIHQPKYSMFERWVE-DGLLDLLQEKGVGSIAFSPLAGGQLTDRYLNGIPADSRAASGsRFLNPD 253
Cdd:cd19150 162 TREAAAILRELGTPLLIHQPSYNMLNRWVEeSGLLDTLQELGVGCIAFTPLAQGLLTDKYLNGIPEGSRASKE-RSLSPK 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495144968 254 QITPEKLDKVRKLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQIDDAVGMLANRGFSAEE 320
Cdd:cd19150 241 MLTEANLNSIRALNEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGALDNLTFSADE 307
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
1-325 |
2.54e-173 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 484.49 E-value: 2.54e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 1 MVYQADPARYATMEYRRCGRSGLKLPAISLGLWHNFGDATLVETSRQLLRRSFDLGITHFDLANNYGPPPGSAESHFGRL 80
Cdd:PRK09912 1 MVWLANPERYGQMQYRYCGKSGLRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGPPPGSAEENFGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 81 LKEDFLPYRDELIISTKAGYTMWDGPYGDWGSRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQG 160
Cdd:PRK09912 81 LREDFAAYRDELIISTKAGYDMWPGPYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 161 KALYVGISNYPADRAREAIDLLAQLGTPCIIHQPKYSMFERWVE-DGLLDLLQEKGVGSIAFSPLAGGQLTDRYLNGIPA 239
Cdd:PRK09912 161 KALYVGISSYSPERTQKMVELLREWKIPLLIHQPSYNLLNRWVDkSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 240 DSR---AASGSRFLNPDQITPEKLDKVRKLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQIDDAVGMLANRGF 316
Cdd:PRK09912 241 DSRmhrEGNKVRGLTPKMLTEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQALNNLTF 320
|
....*....
gi 495144968 317 SAEERQAIE 325
Cdd:PRK09912 321 STEELAQID 329
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
13-329 |
1.85e-132 |
|
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: 379.52 E-value: 1.85e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 13 MEYRRCGRSGLKLPAISLGLWhNFGD---ATLVETSRQLLRRSFDLGITHFDLANNYGPppGSAESHFGRLLKEDflpYR 89
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTM-TFGGpwgGVDEAEAIAILDAALDAGINFFDTADVYGP--GRSEELLGEALKGR---PR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 90 DELIISTKAGYTMWDGPYGDWGSRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISN 169
Cdd:COG0667 75 DDVVIATKVGRRMGPGPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 170 YPADRAREAIDLLAQLgTPCIIHQPKYSMFERWVEDGLLDLLQEKGVGSIAFSPLAGGQLTDRYLNG--IPADSRAAsgs 247
Cdd:COG0667 155 YSAEQLRRALAIAEGL-PPIVAVQNEYSLLDRSAEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGatFPEGDRAA--- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 248 RFLNPDQITPEKLDKVRKLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQIDDAVGMLANRgFSAEERQAIEAI 327
Cdd:COG0667 231 TNFVQGYLTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADLE-LSAEDLAALDAA 309
|
..
gi 495144968 328 LA 329
Cdd:COG0667 310 LA 311
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
22-309 |
1.51e-101 |
|
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: 300.28 E-value: 1.51e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 22 GLKLPAISLGLWHNFGDATLVETSRQLLRRSFDLGITHFDLANNYGPppGSAESHFGRLLKEdfLPyRDELIISTKAGYT 101
Cdd:cd19074 1 GLKVSELSLGTWLTFGGQVDDEDAKACVRKAYDLGINFFDTADVYAA--GQAEEVLGKALKG--WP-RESYVISTKVFWP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 102 MWDGPYgDWG-SRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISNYPADRAREAID 180
Cdd:cd19074 76 TGPGPN-DRGlSRKHIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 181 LLAQLG-TPCIIHQPKYSMFERWVEDGLLDLLQEKGVGSIAFSPLAGGQLTDRYLNGIPADSRAA---SGSRFLNPDQIT 256
Cdd:cd19074 155 LARQFGlIPPVVEQPQYNMLWREIEEEVIPLCEKNGIGLVVWSPLAQGLLTGKYRDGIPPPSRSRatdEDNRDKKRRLLT 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 495144968 257 PEKLDKVRKLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQIDDAVG 309
Cdd:cd19074 235 DENLEKVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVK 287
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
13-327 |
2.60e-94 |
|
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: 282.56 E-value: 2.60e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 13 MEYRRCGRSGLKLPAISLGLWHNFGDATLVETSRQLLRRSFDLGITHFDLANNYGPppGSAESHFGRLLKEDFLPyRDEL 92
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSWVTFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYAN--GQSEEIMGQAIKELGWP-RSDY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 93 IISTKAGYTMWDGPYGDWG-SRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISNYP 171
Cdd:cd19143 78 VVSTKIFWGGGGPPPNDRGlSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGTSEWS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 172 ADRAREAIDLLAQLG-TPCIIHQPKYSMFERW-VEDGLLDLLQEKGVGSIAFSPLAGGQLTDRYLNGIPADSRAASGSRF 249
Cdd:cd19143 158 AQQIEEAHEIADRLGlIPPVMEQPQYNLFHRErVEVEYAPLYEKYGLGTTTWSPLASGLLTGKYNNGIPEGSRLALPGYE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 250 LNPDQITPE---KLDKVRKLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQIDDAVGML-ANRGFSAEERQAIE 325
Cdd:cd19143 238 WLKDRKEELgqeKIEKVRKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEENLKALeVLPKLTPEVMEKIE 317
|
..
gi 495144968 326 AI 327
Cdd:cd19143 318 AI 319
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
13-327 |
3.41e-81 |
|
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: 249.03 E-value: 3.41e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 13 MEYRRCGRSGLKLPAISLGLWhNFGDATLVETSRQLLRRSFDLGITHFDLANNYGPppGSAESHFGRLLKEDflpyRDEL 92
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGTM-NFGGRTDEETSFAIMDRALDAGINFFDTADVYGG--GRSEEIIGRWIAGR----RDDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 93 IISTKAGYTMWDGPYGDWGSRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISNYPA 172
Cdd:cd19087 74 VLATKVFGPMGDDPNDRGLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 173 DRAREAIDLLAQLGTPCII-HQPKYSMFERWVEDGLLDLLQEKGVGSIAFSPLAGGQLTDRYLNGIPADSRAASGSRFLN 251
Cdd:cd19087 154 WQIAKAQGIAARRGLLRFVsEQPMYNLLKRQAELEILPAARAYGLGVIPYSPLAGGLLTGKYGKGKRPESGRLVERARYQ 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495144968 252 PDQITPEKLDKVRKLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQIDDAVGMLANRgFSAEERQAIEAI 327
Cdd:cd19087 234 ARYGLEEYRDIAERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEIT-LTPELLAEIDEL 308
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
28-328 |
3.60e-81 |
|
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: 248.38 E-value: 3.60e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 28 ISLGLWHNFGDATLV--ETSRQLLRRSFDLGITHFDLANNYGPppGSAESHFGRLLKEDfLPYRDELIISTKagYTMWDG 105
Cdd:pfam00248 1 IGLGTWQLGGGWGPIskEEALEALRAALEAGINFIDTAEVYGD--GKSEELLGEALKDY-PVKRDKVVIATK--VPDGDG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 106 PYGDWGSRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISNYPADRAREAidlLAQL 185
Cdd:pfam00248 76 PWPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKA---LTKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 186 GTPCIIHQPKYSMFERWVEDGLLDLLQEKGVGSIAFSPLAGGQLTDRYLNGIPADsraaSGSRFLNPDQITPEKLDKVRK 265
Cdd:pfam00248 153 KIPIVAVQVEYNLLRRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKG----PGERRRLLKKGTPLNLEALEA 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495144968 266 LNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQIDDAVGMLANRgFSAEERQAIEAIL 328
Cdd:pfam00248 229 LEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALEFP-LSDEEVARIDELL 290
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
14-325 |
1.08e-79 |
|
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: 245.19 E-value: 1.08e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 14 EYRRCGRSGLKLPAISLGLWHnFGDATL------VETSRQLLRRSFDLGITHFDLANNYGPppGSAESHFGRLLKEdFLP 87
Cdd:cd19079 1 EYVRLGNSGLKVSRLCLGCMS-FGDPKWrpwvldEEESRPIIKRALDLGINFFDTANVYSG--GASEEILGRALKE-FAP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 88 yRDELIISTKAGYTMWDGPYGDWGSRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGI 167
Cdd:cd19079 77 -RDEVVIATKVYFPMGDGPNGRGLSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 168 SNYPADRAREAIDLLAQLG-TPCIIHQPKYSMFERWVEDGLLDLLQEKGVGSIAFSPLAGGQLTDRYLNGIPADSRAASG 246
Cdd:cd19079 156 SSMYAWQFAKALHLAEKNGwTKFVSMQNHYNLLYREEEREMIPLCEEEGIGVIPWSPLARGRLARPWGDTTERRRSTTDT 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495144968 247 SRFLNpDQITPEKLDKVRKLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQIDDAVGMLaNRGFSAEERQAIE 325
Cdd:cd19079 236 AKLKY-DYFTEADKEIVDRVEEVAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAAL-DIKLSEEEIKYLE 312
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
26-309 |
5.90e-75 |
|
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: 230.10 E-value: 5.90e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 26 PAISLGLWHnFGDATLVETSRQLLRRSFDLGITHFDLANNYGPppGSAESHFGRLLKEDflPYRDELIISTKAGYTMWDG 105
Cdd:cd06660 1 SRLGLGTMT-FGGDGDEEEAFALLDAALEAGGNFFDTADVYGD--GRSERLLGRWLKGR--GNRDDVVIATKGGHPPGGD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 106 PYGDWGSRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISNYPADRAREAIDLLAQL 185
Cdd:cd06660 76 PSRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKAH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 186 G-TPCIIHQPKYSMFERWV-EDGLLDLLQEKGVGSIAFSPLAGGqltdrylngipadsraasgsrflnpdqitpekldkv 263
Cdd:cd06660 156 GlPGFAAVQPQYSLLDRSPmEEELLDWAEENGLPLLAYSPLARG------------------------------------ 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 495144968 264 rklndlalqrgqkLSQMALAWVLRDEKVTSVLIGASKTSQIDDAVG 309
Cdd:cd06660 200 -------------PAQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
13-327 |
1.40e-73 |
|
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: 229.81 E-value: 1.40e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 13 MEYRRCGRSGLKLPAISLG---------LWHNFGdATLVETSRQLLRRSFDLGITHFDLANNYGPppGSAESHFGRLLKe 83
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGtmtfgggggFFGAWG-GVDQEEADRLVDIALDAGINFFDTADVYSE--GESEEILGKALK- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 84 dflPYRDELIISTKAGYTMWDGPYGDWGSRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKAL 163
Cdd:cd19091 77 ---GRRDDVLIATKVRGRMGEGPNDVGLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 164 YVGISNYPADRAREAIDLLAQLG-TPCIIHQPKYSMFERWVEDGLLDLLQEKGVGSIAFSPLAGGQLTDRYLNG--IPAD 240
Cdd:cd19091 154 YIGVSNFSAWQIMKALGISERRGlARFVALQAYYSLLGRDLEHELMPLALDQGVGLLVWSPLAGGLLSGKYRRGqpAPEG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 241 SRAASGSRFLNPdqITPEKL-DKVRKLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQIDDAVGMlANRGFSAE 319
Cdd:cd19091 234 SRLRRTGFDFPP--VDRERGyDVVDALREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGA-AGLSLTPE 310
|
....*...
gi 495144968 320 ERQAIEAI 327
Cdd:cd19091 311 EIARLDKV 318
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
22-325 |
5.77e-73 |
|
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: 227.41 E-value: 5.77e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 22 GLKLPAISLGLW----HNFGDATlVETSRQLLRRSFDLGITHFDLANNYGPppGSAESHFGRLLKEdflpYRDELIISTK 97
Cdd:cd19084 1 DLKVSRIGLGTWaiggTWWGEVD-DQESIEAIKAAIDLGINFFDTAPVYGF--GHSEEILGKALKG----RRDDVVIATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 98 AGyTMWDGPYGDW--GSRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISNYPADRA 175
Cdd:cd19084 74 CG-LRWDGGKGVTkdLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 176 REAIDLlaqlgTPCIIHQPKYSMFERWVEDGLLDLLQEKGVGSIAFSPLAGGQLTDRYLNGI---PADSRAAsgSRFLNP 252
Cdd:cd19084 153 EEARKY-----GPIVSLQPPYSMLEREIEEELLPYCRENGIGVLPYGPLAQGLLTGKYKKEPtfpPDDRRSR--FPFFRG 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495144968 253 DQItPEKLDKVRKLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQIDDAVGMLaNRGFSAEERQAIE 325
Cdd:cd19084 226 ENF-EKNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGAL-DWELTEEELKEID 296
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
19-309 |
4.02e-68 |
|
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: 215.54 E-value: 4.02e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 19 GRSGLKLPAISLGLWhNFGDATLVETSRQLLRRSFDLGITHFDLANNY-----GPPPGSAESHFGRLLKEdfLPYRDELI 93
Cdd:cd19081 3 GRTGLSVSPLCLGTM-VFGWTADEETSFALLDAFVDAGGNFIDTADVYsawvpGNAGGESETIIGRWLKS--RGKRDRVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 94 ISTKAGYTMWDGPYGdwGSRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISNYPAD 173
Cdd:cd19081 80 IATKVGFPMGPNGPG--LSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYSAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 174 RAREAIDLLAQLGTPCIIH-QPKYSMFER-WVEDGLLDLLQEKGVGSIAFSPLAGGQLTDRYLNGIPADSRAASGSRFln 251
Cdd:cd19081 158 RLQEALELSRQHGLPRYVSlQPEYNLVDReSFEGELLPLCREEGIGVIPYSPLAGGFLTGKYRSEADLPGSTRRGEAA-- 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 495144968 252 PDQITPEKLDKVRKLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQIDDAVG 309
Cdd:cd19081 236 KRYLNERGLRILDALDEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLA 293
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
19-325 |
3.46e-63 |
|
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: 202.83 E-value: 3.46e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 19 GRSGLKLPAISLG---LWHNFGDATLVETSRQLLRRSFDLGITHFDLANNYgpPPGSAESHFGRLLKEDflpyRDELIIS 95
Cdd:cd19080 4 GRSGLRVSPLALGtmtFGTEWGWGADREEARAMFDAYVEAGGNFIDTANNY--TNGTSERLLGEFIAGN----RDRIVLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 96 TKagYTMWDGP----YGdwG-SRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISNY 170
Cdd:cd19080 78 TK--YTMNRRPgdpnAG--GnHRKNLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 171 PADRAREAiDLLAQL--GTPCIIHQPKYSMFERWVEDGLLDLLQEKGVGSIAFSPLAGGQLTDRYLNGIPADSRAASGSR 248
Cdd:cd19080 154 PAWVVARA-NTLAELrgWSPFVALQIEYSLLERTPERELLPMARALGLGVTPWSPLGGGLLTGKYQRGEEGRAGEAKGVT 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495144968 249 FlNPDQITPEKLDKVRKLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQIDDAVGMLaNRGFSAEERQAIE 325
Cdd:cd19080 233 V-GFGKLTERNWAIVDVVAAVAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGAL-DLTLSPEQLARLD 307
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
15-312 |
5.64e-63 |
|
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: 202.29 E-value: 5.64e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 15 YRRCGRSGLKLPAISLGLWHNFGDATLVETSRQLLRRSFDLGITHFDLANNYGPppGSAESHFGRLLKEDFLpYRDELII 94
Cdd:cd19141 2 YRNLGKSGLRVSCLGLGTWVTFGSQISDEVAEELVTLAYENGINLFDTAEVYAA--GKAEIVLGKILKKKGW-RRSSYVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 95 STKagyTMWDG-PYGDWG-SRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISNYPA 172
Cdd:cd19141 79 TTK---IFWGGkAETERGlSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 173 DRAREAIDLLAQLG-TPCIIHQPKYSMFER-WVEDGLLDLLQEKGVGSIAFSPLAGGQLTDRYLNGIPADSRAA-SGSRF 249
Cdd:cd19141 156 MEIMEAYSVARQFNlIPPIVEQAEYHLFQReKVEMQLPELFHKIGVGAMTWSPLACGILSGKYDDGVPEYSRASlKGYQW 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495144968 250 LNpDQITPEK----LDKVRKLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQIDDAVGMLA 312
Cdd:cd19141 236 LK-EKILSEEgrrqQAKLKELQIIADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQAIQ 301
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
13-311 |
3.44e-60 |
|
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: 195.69 E-value: 3.44e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 13 MEYRRCGRSGLKLPAISLGLWHNFGDATLVETSRQLLRRSFDLGITHFDLANNYGPppGSAESHFGRLLKEDFLpYRDEL 92
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAA--GKAEVVLGNIIKKKGW-RRSSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 93 IISTKagyTMWDGPY-GDWG-SRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISNY 170
Cdd:cd19158 78 VITTK---IFWGGKAeTERGlSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 171 PADRAREAIDLLAQLG-TPCIIHQPKYSMFERW-VEDGLLDLLQEKGVGSIAFSPLAGGQLTDRYLNGIPADSRAA-SGS 247
Cdd:cd19158 155 SSMEIMEAYSVARQFNlIPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASlKGY 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495144968 248 RFLNpDQITPE----KLDKVRKLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQIDDAVGML 311
Cdd:cd19158 235 QWLK-DKILSEegrrQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAI 301
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
13-311 |
1.98e-59 |
|
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: 193.72 E-value: 1.98e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 13 MEYRRCGRSGLKLPAISLGLWHNFGDATLVETSRQLLRRSFDLGITHFDLANNYGPppGSAESHFGRLLKEDFLpYRDEL 92
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAA--GKAEVILGSIIKKKGW-RRSSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 93 IISTKagyTMWDGPY-GDWG-SRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISNY 170
Cdd:cd19159 78 VITTK---LYWGGKAeTERGlSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 171 PADRAREAIDLLAQLG-TPCIIHQPKYSMFERW-VEDGLLDLLQEKGVGSIAFSPLAGGQLTDRYLNGIPADSRAASGSR 248
Cdd:cd19159 155 SAMEIMEAYSVARQFNmIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCY 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495144968 249 FLNPDQITPE----KLDKVRKLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQIDDAVGML 311
Cdd:cd19159 235 QWLKERIVSEegrkQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAI 301
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
25-309 |
5.57e-59 |
|
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: 191.26 E-value: 5.57e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 25 LPAISLGLW-----HNFGDATlVETSRQLLRRSFDLGITHFDLANNYGPppGSAESHFGRLLKedflPYRDELIISTKAG 99
Cdd:cd19085 1 VSRLGLGCWqfgggYWWGDQD-DEESIATIHAALDAGINFFDTAEAYGD--GHSEEVLGKALK----GRRDDVVIATKVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 100 YtmwdgpygDWGSRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISNYPADRAREAI 179
Cdd:cd19085 74 P--------DNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 180 DLlaqlgTPCIIHQPKYSMFERWVEDGLLDLLQEKGVGSIAFSPLAGGQLTDRYLNGI---PADSRaasgSRFLNPDQ-- 254
Cdd:cd19085 146 DA-----GRIDSNQLPYNLLWRAIEYEILPFCREHGIGVLAYSPLAQGLLTGKFSSAEdfpPGDAR----TRLFRHFEpg 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 495144968 255 ITPEKLDKVRKLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQIDDAVG 309
Cdd:cd19085 217 AEEETFEALEKLKEIADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAA 271
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
13-328 |
1.70e-57 |
|
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: 188.66 E-value: 1.70e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 13 MEYRRCGRSGLKLPAISLGLWHNFGDATLVETSRQLLRRSFDLGITHFDLANNYGPppGSAESHFGRLLKEDFLpYRDEL 92
Cdd:cd19160 3 MKYRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDLLTVAYEHGVNLFDTAEVYAA--GKAERTLGNILKSKGW-RRSSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 93 IISTKagyTMWDG-PYGDWG-SRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISNY 170
Cdd:cd19160 80 VVTTK---IYWGGqAETERGlSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 171 PADRAREAIDLLAQLG-TPCIIHQPKYSMFER-WVEDGLLDLLQEKGVGSIAFSPLAGGQLTDRYLNGIPADSRAA-SGS 247
Cdd:cd19160 157 SAMEIMEAYSVARQFNlIPPVCEQAEYHLFQReKVEMQLPELYHKIGVGSVTWSPLACGLITGKYDGRVPDTCRAAvKGY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 248 RFLNPDQITPE---KLDKVRKLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQIDDAVGMLANRG-FSAEERQA 323
Cdd:cd19160 237 QWLKEKVQSEEgkkQQAKVKELHPIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGSIQVLSqLTPQTVME 316
|
....*
gi 495144968 324 IEAIL 328
Cdd:cd19160 317 IDALL 321
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
14-286 |
3.80e-57 |
|
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: 187.04 E-value: 3.80e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 14 EYRRCGRSGLKLPAISLGLW--HNFGDATLVETSRQLLRRSFDLGITHFDLANNYGPppGSAESHFGRLLKEdflpYRDE 91
Cdd:cd19076 1 PTRKLGTQGLEVSALGLGCMgmSAFYGPADEEESIATLHRALELGVTFLDTADMYGP--GTNEELLGKALKD----RRDE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 92 LIISTKAGYTMWDGPY--GDWGSRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISN 169
Cdd:cd19076 75 VVIATKFGIVRDPGSGfrGVDGRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLSE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 170 YPADRAREA-----IDLLaqlgtpciihQPKYSMFERWVEDGLLDLLQEKGVGSIAFSPLAGGQLTDRYlngIPADSRAA 244
Cdd:cd19076 155 ASADTIRRAhavhpITAV----------QSEYSLWTRDIEDEVLPTCRELGIGFVAYSPLGRGFLTGAI---KSPEDLPE 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 495144968 245 SGSRFLNPdQITPEKLDK----VRKLNDLALQRGQKLSQMALAWVL 286
Cdd:cd19076 222 DDFRRNNP-RFQGENFDKnlklVEKLEAIAAEKGCTPAQLALAWVL 266
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
45-328 |
9.68e-53 |
|
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: 175.55 E-value: 9.68e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 45 SRQLLRRSFDLGITHFDLANNYGPppGSAESHFGRLLKEdflpYRDELIISTKAGyTMWD--GPYGDWGSRKYLISSLDQ 122
Cdd:cd19102 28 SIAAIRAALDLGINWIDTAAVYGL--GHSEEVVGRALKG----LRDRPIVATKCG-LLWDeeGRIRRSLKPASIRAECEA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 123 SLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISNYPADRAR--EAIDLLAQLgtpciihQPKYSMFE 200
Cdd:cd19102 101 SLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKrcQAIHPIASL-------QPPYSLLR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 201 RWVEDGLLDLLQEKGVGSIAFSPLAGGQLTDR----YLNGIPADSRAAsGSRFLNPDQITPeKLDKVRKLNDLALQRGQK 276
Cdd:cd19102 174 RGIEAEILPFCAEHGIGVIVYSPMQSGLLTGKmtpeRVASLPADDWRR-RSPFFQEPNLAR-NLALVDALRPIAERHGRT 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 495144968 277 LSQMALAWVLRDEKVTSVLIGASKTSQIDDAVGMlANRGFSAEERQAIEAIL 328
Cdd:cd19102 252 VAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGA-ADLRLTPEELAEIEALL 302
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
15-326 |
1.60e-50 |
|
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: 170.15 E-value: 1.60e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 15 YRRCGRSGLKLPAISLGLW-----HNFGDATlVETSRQLLRRSFDLGITHFDLANNYGPppGSAESHFGRLLKedflPYR 89
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTWaigggPWWGGSD-DNESIRTIHAALDLGINLIDTAPAYGF--GHSEEIVGKAIK----GRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 90 DELIISTKAGyTMWDGPYGDWGS-------RKYL-----ISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIV 157
Cdd:cd19149 74 DKVVLATKCG-LRWDREGGSFFFvrdgvtvYKNLspesiREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 158 RQGKALYVGISNYpadrAREAIDLLAQLGTPCIIhQPKYSMFERWVEDGLLDLLQEKGVGSIAFSPLAGGQLTDRYlngI 237
Cdd:cd19149 153 RQGKIRAIGASNV----SVEQIKEYVKAGQLDII-QEKYSMLDRGIEKELLPYCKKNNIAFQAYSPLEQGLLTGKI---T 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 238 PADSRAASGSRFLNPdQITPEKLDKV----RKLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQIDDAVGMLAN 313
Cdd:cd19149 225 PDREFDAGDARSGIP-WFSPENREKVlallEKWKPLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPEQAEENAKAGDI 303
|
330
....*....|...
gi 495144968 314 RgFSAEERQAIEA 326
Cdd:cd19149 304 R-LSAEDIATMRS 315
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
13-304 |
3.92e-50 |
|
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: 169.57 E-value: 3.92e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 13 MEYRRCGRSGLKLPAISLGLWHNFGDATLVETSRQLLRRSFDLGITHFDLANnyGPPPGSAESHFGRLLKEDFLPyRDEL 92
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGTWSTFSTAISEEQAEEIVTLAYENGINYFDTSD--AFTSGQAETELGRILKKKGWK-RSSY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 93 IISTKagyTMWD-GPYGDWGSRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISNYP 171
Cdd:cd19142 78 IVSTK---IYWSyGSEERGLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRWS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 172 ADRAREAIDLLAQLGTPC-IIHQPKYSMFER-WVEDGLLDLLQEKGVGSIAFSPLA-------GGQLTDRYLNGIPADSR 242
Cdd:cd19142 155 PVEIMEAFSIARQFNCPTpICEQSEYHMFCReKMELYMPELYNKVGVGLITWSPLSlgldpgiSEETRRLVTKLSFKSSK 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495144968 243 AASGSRFLNPDQITPEKLDKVRKLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQI 304
Cdd:cd19142 235 YKVGSDGNGIHEETRRASHKLRELSLIAERLGCDLTQLLIAWSLKNENVQCVLIGASSLEQL 296
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
16-327 |
4.75e-50 |
|
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: 168.75 E-value: 4.75e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 16 RRCGRSGLKLPAISLGL----WHNFGDATLVETSRQLLRRSFDLGITHFDLANNYGPppGSAESHFGRLLKEdflPYRDE 91
Cdd:cd19083 2 VKLGKSDIDVNPIGLGTnavgGHNLYPNLDEEEGKDLVREALDNGVNLLDTAFIYGL--GRSEELVGEVLKE---YNRNE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 92 LIISTKAGYTMWDGPYGDWGSRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISNYP 171
Cdd:cd19083 77 VVIATKGAHKFGGDGSVLNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 172 ADRAREA-----IDLLaqlgtpciihQPKYSMFERWVEDGLLDLLQEKGVGSIAFSPLAGGQLTDRYL-------NGIPA 239
Cdd:cd19083 157 LEQLKEAnkdgyVDVL----------QGEYNLLQREAEEDILPYCVENNISFIPYFPLASGLLAGKYTkdtkfpdNDLRN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 240 DSRAASGSRFlnpdqitPEKLDKVRKLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQ-IDDAVGMLANrgFSA 318
Cdd:cd19083 227 DKPLFKGERF-------SENLDKVDKLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQvIDNLKALDVT--LTE 297
|
....*....
gi 495144968 319 EERQAIEAI 327
Cdd:cd19083 298 EEIAFIDAL 306
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
23-309 |
3.47e-49 |
|
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: 164.19 E-value: 3.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 23 LKLPAISLGLW----HNFGDATlVETSRQLLRRSFDLGITHFDLANNYGPppGSAESHFGRLLKEDflpyRDELIISTKA 98
Cdd:cd19086 1 LEVSEIGFGTWglggDWWGDVD-DAEAIRALRAALDLGINFFDTADVYGD--GHSERLLGKALKGR----RDKVVIATKF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 99 GYTMWDGPYGDWG-SRKYLISSLDQSLKRMGLEYVDIFYHHRPDPE-TPLEETMRALDHIVRQGKALYVGISnypADRAR 176
Cdd:cd19086 74 GNRFDGGPERPQDfSPEYIREAVEASLKRLGTDYIDLYQLHNPPDEvLDNDELFEALEKLKQEGKIRAYGVS---VGDPE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 177 EAIDLLAQLGTPCIIHQpkYSMFERWVEDGLLDLLQEKGVGSIAFSPLAGGQLTDrylngipadsraasgsrflnpdqit 256
Cdd:cd19086 151 EALAALRRGGIDVVQVI--YNLLDQRPEEELFPLAEEHGVGVIARVPLASGLLTG------------------------- 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 495144968 257 pekldkvrklndlalqrgqKLSQMALAWVLRDEKVTSVLIGASKTSQIDDAVG 309
Cdd:cd19086 204 -------------------KLAQAALRFILSHPAVSTVIPGARSPEQVEENAA 237
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
24-325 |
8.71e-49 |
|
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: 165.09 E-value: 8.71e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 24 KLPAISLGLWH------NFGDATLVETSRQLLRRSFDLGITHFDLANNYGPppGSAESHFGRLLKEdfLPYRDELIISTK 97
Cdd:cd19093 1 EVSPLGLGTWQwgdrlwWGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYGT--GRSERLLGRFLKE--LGDRDEVVIATK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 98 -AGYTmWDGPYGDwgsrkyLISSLDQSLKRMGLEYVDIFYHHRPDP-ETPLEETMRALDHIVRQGKALYVGISNYPADRA 175
Cdd:cd19093 77 fAPLP-WRLTRRS------VVKALKASLERLGLDSIDLYQLHWPGPwYSQIEALMDGLADAVEEGLVRAVGVSNYSADQL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 176 REAIDLLAQLGTPCIIHQPKYSMFERWVE-DGLLDLLQEKGVGSIAFSPLAGGQLTDRYlngipADSRAASGSRflnPDQ 254
Cdd:cd19093 150 RRAHKALKERGVPLASNQVEYSLLYRDPEqNGLLPACDELGITLIAYSPLAQGLLTGKY-----SPENPPPGGR---RRL 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495144968 255 ITPEKLDKVR----KLNDLALQRGQKLSQMALAWVLrdEKVTSVLIGASKTSQIDDAVGMLANRgFSAEERQAIE 325
Cdd:cd19093 222 FGRKNLEKVQplldALEEIAEKYGKTPAQVALNWLI--AKGVVPIPGAKNAEQAEENAGALGWR-LSEEEVAELD 293
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
22-328 |
1.02e-48 |
|
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: 165.10 E-value: 1.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 22 GLKLPAISLG---LWHNFGDATLVETSRQLLRRSFDLGITHFDLANNYGPPpgsaesHFGRLLKEDFLPYRDELIISTKA 98
Cdd:cd19078 1 GLEVSAIGLGcmgMSHGYGPPPDKEEMIELIRKAVELGITFFDTAEVYGPY------TNEELVGEALKPFRDQVVIATKF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 99 GYTMWDGPYGDWG--SRKYLI-SSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISNYPADRA 175
Cdd:cd19078 75 GFKIDGGKPGPLGldSRPEHIrKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 176 REAIDLlaqlgTPCIIHQPKYSMFERWVEDGLLDLLQEKGVGSIAFSPLAGGQLTDRYLNGI---PADSRAASgSRFlnp 252
Cdd:cd19078 155 RRAHAV-----CPVTAVQSEYSMMWREPEKEVLPTLEELGIGFVPFSPLGKGFLTGKIDENTkfdEGDDRASL-PRF--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 253 dqiTPEKLDK----VRKLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQIDDAVGMlANRGFSAEERQAIEAIL 328
Cdd:cd19078 226 ---TPEALEAnqalVDLLKEFAEEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGA-ADIELTPEELREIEDAL 301
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
26-327 |
2.00e-48 |
|
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: 164.27 E-value: 2.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 26 PAISLG--LWHNFGDATLVETSRQLLRRSFDLGITHFDLANNYgpPPGSAESHFGRLLKEDflpyrDELIISTKAgytmw 103
Cdd:cd19075 1 PKIILGtmTFGSQGRFTTAEAAAELLDAFLERGHTEIDTARVY--PDGTSEELLGELGLGE-----RGFKIDTKA----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 104 DGPYGDWGSRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISNYPADRAREAIDLLA 183
Cdd:cd19075 69 NPGVGGGLSPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 184 QLG--TPCiIHQPKYSMFERWVEDGLLDLLQEKGVGSIAFSPLAGGQLTDRYLNGipadSRAASGSRFLNPDQI------ 255
Cdd:cd19075 149 ENGwvLPT-VYQGMYNAITRQVETELFPCLRKLGIRFYAYSPLAGGFLTGKYKYS----EDKAGGGRFDPNNALgklyrd 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 256 ---TPEKLDKVRKLNDLALQRGQKLSQMALAWV-----LRDEKVTSVLIGASKTSQIDDAVGMLANRGFSAEERQAIEAI 327
Cdd:cd19075 224 rywKPSYFEALEKVEEAAEKEGISLAEAALRWLyhhsaLDGEKGDGVILGASSLEQLEENLAALEKGPLPEEVVKAIDEA 303
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
21-308 |
1.09e-47 |
|
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: 161.95 E-value: 1.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 21 SGLKLPAISLGLWHNFGDATLVETSRQLLRRSFDLGITHFDLANNYGPppGSAESHFGRLLKEDfLPYRDELIISTKAGY 100
Cdd:cd19092 2 EGLEVSRLVLGCMRLADWGESAEELLSLIEAALELGITTFDHADIYGG--GKCEELFGEALALN-PGLREKIEIQTKCGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 101 TMWDGPYGDWG-----SRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISNYPAdra 175
Cdd:cd19092 79 RLGDDPRPGRIkhydtSKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFTP--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 176 rEAIDLLAQ-LGTPCIIHQPKYSMFER-WVEDGLLDLLQEKGVGSIAFSPLAGGqltdrylngipadsraasgsRFLNPD 253
Cdd:cd19092 156 -SQIELLQSyLDQPLVTNQIELSLLHTeAIDDGTLDYCQLLDITPMAWSPLGGG--------------------RLFGGF 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 495144968 254 QitpEKLDKVRK-LNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQIDDAV 308
Cdd:cd19092 215 D---ERFQRLRAaLEELAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSAV 267
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
22-325 |
1.75e-46 |
|
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase. Escherichia coli YeaE may act as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381298 [Multi-domain] Cd Length: 263 Bit Score: 158.16 E-value: 1.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 22 GLKLPAISLGLW----HNFGDATLVETSRQLLRRSFDLGITHFDLANNYGPppGSAESHFGRLLKeDFLpyRDELIISTK 97
Cdd:cd19072 1 GEEVPVLGLGTWgiggGMSKDYSDDKKAIEALRYAIELGINLIDTAEMYGG--GHAEELVGKAIK-GFD--REDLFITTK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 98 AgytmwdgpYGDWGSRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISNYPADRARE 177
Cdd:cd19072 76 V--------SPDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 178 AIDLLaqLGTPCIIHQPKYSMFERWVEDGLLDLLQEKGVGSIAFSPLAGGQLTDRYLngipadsraasgsrflnpdqitp 257
Cdd:cd19072 148 AQSYL--KKGPIVANQVEYNLFDREEESGLLPYCQKNGIAIIAYSPLEKGKLSNAKG----------------------- 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 258 ekldkVRKLNDLALQRGQKLSQMALAWVLRDEKVTsVLIGASKTSQIDDAVGMLanrGF--SAEERQAIE 325
Cdd:cd19072 203 -----SPLLDEIAKKYGKTPAQIALNWLISKPNVI-AIPKASNIEHLEENAGAL---GWelSEEDLQRLD 263
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
35-327 |
9.01e-45 |
|
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: 155.42 E-value: 9.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 35 NFGDATLVETSRQLLRRSFDLGITHFDLANNYGPPP-----GSAESHFGRLLKEDflPYRDELIISTK-AGYT--MWDGP 106
Cdd:cd19094 10 TWGEQNTEAEAHEQLDYAFDEGVNFIDTAEMYPVPPspetqGRTEEIIGSWLKKK--GNRDKVVLATKvAGPGegITWPR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 107 YGDWG-SRKYLISSLDQSLKRMGLEYVDIFYHHRPD------------------PETPLEETMRALDHIVRQGKALYVGI 167
Cdd:cd19094 88 GGGTRlDRENIREAVEGSLKRLGTDYIDLYQLHWPDrytplfgggyytepseeeDSVSFEEQLEALGELVKAGKIRHIGL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 168 SNYPADRAREAIDLLAQLGTPCIIH-QPKYSMFERWVEDGLLDLLQEKGVGSIAFSPLAGGQLTDRYLNG--IPADSRAA 244
Cdd:cd19094 168 SNETPWGVMKFLELAEQLGLPRIVSiQNPYSLLNRNFEEGLAEACHRENVGLLAYSPLAGGVLTGKYLDGaaRPEGGRLN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 245 SGSRFLnPDQITPEKLDKVRKLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQIDDAVGMLaNRGFSAEERQAI 324
Cdd:cd19094 248 LFPGYM-ARYRSPQALEAVAEYVKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLKENIDAF-DVPLSDELLAEI 325
|
...
gi 495144968 325 EAI 327
Cdd:cd19094 326 DAV 328
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
43-308 |
2.89e-44 |
|
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: 151.99 E-value: 2.89e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 43 ETSRQLLRRSFDLGITHFDLANNYGPppGSAEshfgRLLKEDFLPYRDELIISTKAGYTMwDGPyGDW---GSRKYLISS 119
Cdd:cd19088 24 EEAIAVLRRALELGVNFIDTADSYGP--DVNE----RLIAEALHPYPDDVVIATKGGLVR-TGP-GWWgpdGSPEYLRQA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 120 LDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISNYPADRAREAIDLlaqlgTPCIIHQPKYSMF 199
Cdd:cd19088 96 VEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAI-----VRIVSVQNRYNLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 200 ERwVEDGLLDLLQEKGVGSIAFSPLAGGQLtdrylngipadsrAASGsrflnpdqitpekldkvRKLNDLALQRGQKLSQ 279
Cdd:cd19088 171 NR-DDEGVLDYCEAAGIAFIPWFPLGGGDL-------------AQPG-----------------GLLAEVAARLGATPAQ 219
|
250 260
....*....|....*....|....*....
gi 495144968 280 MALAWVLRDEKVTSVLIGASKTSQIDDAV 308
Cdd:cd19088 220 VALAWLLARSPVMLPIPGTSSVEHLEENL 248
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
35-311 |
5.30e-43 |
|
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: 150.01 E-value: 5.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 35 NFGDATLVETSRQLLRRSFDLGITHFDLANNYG--PPPGSAESHFGRLLKEDFLpyRDELIISTKAGYTMWDGPYGDWGS 112
Cdd:cd19082 9 DFGTRIDEEEAFALLDAFVELGGNFIDTARVYGdwVERGASERVIGEWLKSRGN--RDKVVIATKGGHPDLEDMSRSRLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 113 RKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISNYPADRAREAIDLLAQLG-TPCII 191
Cdd:cd19082 87 PEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNWSTERIAEANAYAKAHGlPGFAA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 192 HQPKYSMF----ERWVEDGL-------LDLLQEKGVGSIAFSPLAGGQLTDRYLNGIPADSRAAsgSRFLNPDQItpEKL 260
Cdd:cd19082 167 SSPQWSLArpnePPWPGPTLvamdeemRAWHEENQLPVFAYSSQARGFFSKRAAGGAEDDSELR--RVYYSEENF--ERL 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 495144968 261 DKVRKlndLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQIDDAVGML 311
Cdd:cd19082 243 ERAKE---LAEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAAA 290
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
26-311 |
5.37e-43 |
|
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: 149.79 E-value: 5.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 26 PAISLGLWhNFGDATLVETSRQLLRRSFDLGITHFDLANNY-----GPPPGSAESHFGRLLKEDFLpyRDELIISTKAGy 100
Cdd:cd19752 1 SELCLGTM-YFGTRTDEETSFAILDRYVAAGGNFLDTANNYafwteGGVGGESERLIGRWLKDRGN--RDDVVIATKVG- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 101 tmwdGPYGDWG---------SRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISNYP 171
Cdd:cd19752 77 ----AGPRDPDggpespeglSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 172 ADRAREAIDLLAQLGTP---CIihQPKYSMF----------ERWVEDGLLDLLQEKGVGSI-AFSPLAGGQLTDrylngi 237
Cdd:cd19752 153 AWRLERARQIARQQGWAefsAI--QQRHSYLrprpgadfgvQRIVTDELLDYASSRPDLTLlAYSPLLSGAYTR------ 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495144968 238 padsraasGSRFLNPDQITPEKLDKVRKLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQIDDAVGML 311
Cdd:cd19752 225 --------PDRPLPEQYDGPDSDARLAVLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAAL 290
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
13-308 |
1.05e-42 |
|
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: 149.24 E-value: 1.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 13 MEYRRCGRSGLKLPAISLG---LWHNFGDATLVEtSRQLLRRSFDLGITHFDLANNYGPppGSAESHFGRLLKEdfLPyR 89
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGaspLGGVFGPVDEEE-AIRTVHEALDSGINYIDTAPWYGQ--GRSETVLGKALKG--IP-R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 90 DELIISTKAG------YTMWDGpygdwgSRKYLISSLDQSLKRMGLEYVDIFYHH----RPDPETPLEETMRALDHIVRQ 159
Cdd:cd19163 75 DSYYLATKVGrygldpDKMFDF------SAERITKSVEESLKRLGLDYIDIIQVHdiefAPSLDQILNETLPALQKLKEE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 160 GKALYVGISNYP-------ADRAREAIDllaqlgtpCIIHQPKYSMFERWVEDgLLDLLQEKGVGSIAFSPLAGGQLTDR 232
Cdd:cd19163 149 GKVRFIGITGYPldvlkevLERSPVKID--------TVLSYCHYTLNDTSLLE-LLPFFKEKGVGVINASPLSMGLLTER 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495144968 233 ylnGIPADSRAasgsrflnpdqiTPEKLDKVRKLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQIDDAV 308
Cdd:cd19163 220 ---GPPDWHPA------------SPEIKEACAKAAAYCKSRGVDISKLALQFALSNPDIATTLVGTASPENLRKNL 280
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
26-305 |
2.67e-42 |
|
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: 147.00 E-value: 2.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 26 PAISLGLWHNFGDATLV--ETSRQLLRRSFDLGITHFDLANNYGpppgSAESHFGRLLKEDFlpyRDELIISTKAGYTmW 103
Cdd:cd19095 1 SVLGLGTSGIGRVWGVPseAEAARLLNTALDLGINLIDTAPAYG----RSEERLGRALAGLR---RDDLFIATKVGTH-G 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 104 DG--PYGDWgSRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISNYPadrarEAIDL 181
Cdd:cd19095 73 EGgrDRKDF-SPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVSGDG-----EELEA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 182 LAQLGTPCIIhQPKYSMFERWvEDGLLDLLQEKGVGSIAFSPLAGGQLTDRYlngipadsraasgsrflnpdQITPEKLD 261
Cdd:cd19095 147 AIASGVFDVV-QLPYNVLDRE-EEELLPLAAEAGLGVIVNRPLANGRLRRRV--------------------RRRPLYAD 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 495144968 262 KVRKLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGaskTSQID 305
Cdd:cd19095 205 YARRPEFAAEIGGATWAQAALRFVLSHPGVSSAIVG---TTNPE 245
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-327 |
2.35e-41 |
|
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: 146.26 E-value: 2.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 14 EYRRCGRSGLKLPAISLG------LWhnfGDATlVETSRQLLRRSFDLGITHFDLANNYGPppGSAESHFGRLLKEDflp 87
Cdd:cd19104 1 KYRRFGRTGLKVSELTFGgggiggLM---GRTT-REEQIAAVRRALDLGINFFDTAPSYGD--GKSEENLGRALKGL--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 88 yRDELIISTKAGYTmwDGPYGDWGSRkyLISSLDQSLKRMGLEYVDIFY-HHRPDPETP--------------LEETMRA 152
Cdd:cd19104 72 -PAGPYITTKVRLD--PDDLGDIGGQ--IERSVEKSLKRLKRDSVDLLQlHNRIGDERDkpvggtlsttdvlgLGGVADA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 153 LDHIVRQGKALYVGIS---NYPAdrAREAID------------LL---AQLGTPciihqPKYSMFErwvEDGLLDLLQEK 214
Cdd:cd19104 147 FERLRSEGKIRFIGITglgNPPA--IRELLDsgkfdavqvyynLLnpsAAEARP-----RGWSAQD---YGGIIDAAAEH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 215 GVGSIAFSPLAGGQLTDRYLNGIPADSRAASgsrflnPDQITPEKLDKVRKLNDlalQRGQKLSQMALAWVLRDEKVTSV 294
Cdd:cd19104 217 GVGVMGIRVLAAGALTTSLDRGREAPPTSDS------DVAIDFRRAAAFRALAR---EWGETLAQLAHRFALSNPGVSTV 287
|
330 340 350
....*....|....*....|....*....|...
gi 495144968 295 LIGASKTSQIDDAVGMLANRGFSAEERQAIEAI 327
Cdd:cd19104 288 LVGVKNREELEEAVAAEAAGPLPAENLARLEAL 320
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-306 |
3.14e-41 |
|
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: 143.88 E-value: 3.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 13 MEYRRCGRSGLKLPAISLGlwhnfGDATLVETSRqLLRRSFDLGITHFDLANNYGPppGSAESHFGRLLKEdflPYRDEL 92
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFG-----GGGLPRESPE-LLRRALDLGINYFDTAEGYGN--GNSEEIIGEALKG---LRRDKV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 93 IISTKAGytmwdgPYGDWGSRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPL---EETMRALDHIVRQGKALYVGIS- 168
Cdd:cd19105 70 FLATKAS------PRLDKKDKAELLKSVEESLKRLQTDYIDIYQLHGVDTPEERllnEELLEALEKLKKEGKVRFIGFSt 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 169 -NYPADRAREAIDllaqlgTPCI-IHQPKYS-MFERWVEDGLLDLLQEKGVGSIAFSPLAGGQLtdrylngipadsRAAS 245
Cdd:cd19105 144 hDNMAEVLQAAIE------SGWFdVIMVAYNfLNQPAELEEALAAAAEKGIGVVAMKTLAGGYL------------QPAL 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495144968 246 GSRFLNPdqitpekldkvrklndlalqrGQKLSQMALAWVLRDEKVTSVLIGASKTSQIDD 306
Cdd:cd19105 206 LSVLKAK---------------------GFSLPQAALKWVLSNPRVDTVVPGMRNFAELEE 245
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
13-327 |
5.40e-40 |
|
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: 142.97 E-value: 5.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 13 MEYRRCGRSGLKLPAI---SLGLWHNFGDATLVETSRQLLRRSFDLGITHFDLANNYGPppgsAESHFGRLLKEDfLPYR 89
Cdd:cd19144 1 IPTRTLGRNGPSVPALgfgAMGLSAFYGPPKPDEERFAVLDAAFELGCTFWDTADIYGD----SEELIGRWFKQN-PGKR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 90 DELIISTKAGYTM--WDGPYGDWGSRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGI 167
Cdd:cd19144 76 EKIFLATKFGIEKnvETGEYSVDGSPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 168 SNYPADRAREAidllaqlgtpCIIH-----QPKYSMFERWVED---GLLDLLQEKGVGSIAFSPLAGGQLTDRYLNgiPA 239
Cdd:cd19144 156 SECSAETLRRA----------HAVHpiaavQIEYSPFSLDIERpeiGVLDTCRELGVAIVAYSPLGRGFLTGAIRS--PD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 240 DSRAASGSRFL---NPDQItPEKLDKVRKLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQIDDAVGMLaNRGF 316
Cdd:cd19144 224 DFEEGDFRRMAprfQAENF-PKNLELVDKIKAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLGAL-KVKL 301
|
330
....*....|.
gi 495144968 317 SAEERQAIEAI 327
Cdd:cd19144 302 TEEEEKEIREI 312
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
22-328 |
7.52e-40 |
|
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: 142.06 E-value: 7.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 22 GLKLPAISLGLWHNFGD---ATLVETSRQLLRRSFDLGITHFDLANNYGPppGSAESHFGRLLKEdfLPYRDELIISTKA 98
Cdd:cd19148 1 DLPVSRIALGTWAIGGWmwgGTDEKEAIETIHKALDLGINLIDTAPVYGF--GLSEEIVGKALKE--YGKRDRVVIATKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 99 GYTmWD--GPYGDWGSRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISNY-PA--D 173
Cdd:cd19148 77 GLE-WDegGEVVRNSSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFsPEqmE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 174 RAREAidllAQLGTpciiHQPKYSMFERWVEDGLLDLLQEKGVGSIAFSPLAGGQLT-----DRYLNGipADSRAA---- 244
Cdd:cd19148 156 TFRKV----APLHT----VQPPYNLFEREIEKDVLPYARKHNIVTLAYGALCRGLLSgkmtkDTKFEG--DDLRRTdpkf 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 245 SGSRFlnpdqitPEKLDKVRKLNDLALQRGQK-LSQMALAWVLRDEKVTSVLIGASKTSQIDDAVGMLanrGFS--AEER 321
Cdd:cd19148 226 QEPRF-------SQYLAAVEELDKLAQERYGKsVIHLAVRWLLDQPGVSIALWGARKPEQLDAVDEVF---GWSlnDEDM 295
|
....*..
gi 495144968 322 QAIEAIL 328
Cdd:cd19148 296 KEIDAIL 302
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
26-308 |
1.98e-39 |
|
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: 140.00 E-value: 1.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 26 PAISLG---LWHNFGDATLvETSRQLLRRSFDLGITHFDLANNYGPppgsAESHFGRLLKEdflPYRDELIISTKAGYTM 102
Cdd:cd19090 1 SALGLGtagLGGVFGGVDD-DEAVATIRAALDLGINYIDTAPAYGD----SEERLGLALAE---LPREPLVLSTKVGRLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 103 wdGPYGDWgSRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMR-----ALDHIVRQGKALYVGISNYPADRARE 177
Cdd:cd19090 73 --EDTADY-SADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILAPggaleALLELKEEGLIKHIGLGGGPPDLLRR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 178 AI-----DllaqlgtpCIIHQPKYSMFERWVEDGLLDLLQEKGVGSIAFSPLAGGQLTDRYLNGIPAdsraasgsrflNP 252
Cdd:cd19090 150 AIetgdfD--------VVLTANRYTLLDQSAADELLPAAARHGVGVINASPLGMGLLAGRPPERVRY-----------TY 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 495144968 253 DQITPEKLDKVRKLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQIDDAV 308
Cdd:cd19090 211 RWLSPELLDRAKRLYELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNV 266
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
21-308 |
3.26e-39 |
|
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this family. It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381364 [Multi-domain] Cd Length: 266 Bit Score: 139.31 E-value: 3.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 21 SGLKLPAISLGLWHNFGDATLVETSRQLLRRSFDLGITHFDLANNYGPppGSAESHFGRLLKedflPYRDELIISTKAgy 100
Cdd:cd19138 7 DGTKVPALGQGTWYMGEDPAKRAQEIEALRAGIDLGMTLIDTAEMYGD--GGSEELVGEAIR----GRRDKVFLVSKV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 101 tmwdgpYGDWGSRKYLISSLDQSLKRMGLEYVDIFYHHRPDpETPLEETMRALDHIVRQGKALYVGISNYPADRAREAID 180
Cdd:cd19138 79 ------LPSNASRQGTVRACERSLRRLGTDYLDLYLLHWRG-GVPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 181 LLAqlGTPCIIHQPKYSMFERWVEDGLLDLLQEKGVGSIAFSPLAGGQLTDRYLNGIPAdsraasgsrflnpdqitpekl 260
Cdd:cd19138 152 VPG--GGNCAANQVLYNLGSRGIEYDLLPWCREHGVPVMAYSPLAQGGLLRRGLLENPT--------------------- 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 495144968 261 dkvrkLNDLALQRGQKLSQMALAWVLRDEKVtsvlIGASKTSQIDDAV 308
Cdd:cd19138 209 -----LKEIAARHGATPAQVALAWVLRDGNV----IAIPKSGSPEHAR 247
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
13-327 |
1.28e-38 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 140.34 E-value: 1.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 13 MEYRRCGRSGLKLPAISLGLWH-NFGDAtlvETSRQLLRRSFDLGITHFDLANNYGpppGSaESHFGRLLKEdflpYRDE 91
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGMRlPRKDE---EEAEALIRRAIDNGINYIDTARGYG---DS-EEFLGKALKG----PRDK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 92 LIISTKAGYTMWDGPygdwGSRKYLisslDQSLKRMGLEYVDIFYHHRPDPETPLEETMR------ALDHIVRQGKALYV 165
Cdd:COG1453 70 VILATKLPPWVRDPE----DMRKDL----EESLKRLQTDYIDLYLIHGLNTEEDLEKVLKpggaleALEKAKAEGKIRHI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 166 GISNY-PADRAREAIDllaqlgTP----CIIHqpkYSMFERWVEDG--LLDLLQEKGVGSIAFSPLAGGQLTdrylngip 238
Cdd:COG1453 142 GFSTHgSLEVIKEAID------TGdfdfVQLQ---YNYLDQDNQAGeeALEAAAEKGIGVIIMKPLKGGRLA-------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 239 adsraasgsrflNPdqitPEKLDKVRKlndlalqrgQKLS--QMALAWVLRDEKVTSVLIGASKTSQIDDAVGMLANRG- 315
Cdd:COG1453 205 ------------NP----PEKLVELLC---------PPLSpaEWALRFLLSHPEVTTVLSGMSTPEQLDENLKTADNLEp 259
|
330
....*....|..
gi 495144968 316 FSAEERQAIEAI 327
Cdd:COG1453 260 LTEEELAILERL 271
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-308 |
9.04e-36 |
|
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: 129.52 E-value: 9.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 15 YRRCGRSGLKLPAISLGLWHnFGDATlVETSRQLLRRSFDLGITHFDLANNYGpppgSAESHFGRLLKedflPYRDELII 94
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGP-LGRLS-QEEAAAIIRRALDLGINYFDTAPSYG----DSEEKIGKALK----GRRDKVFL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 95 STKAGYTMWDGpygdwgSRKylisSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMR---ALDHIVR---QGKALYVGIS 168
Cdd:cd19100 71 ATKTGARDYEG------AKR----DLERSLKRLGTDYIDLYQLHAVDTEEDLDQVFGpggALEALLEakeEGKIRFIGIS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 169 NYPADRAREAID------LLAQLGtPCIIHQPKYsmferwvEDGLLDLLQEKGVGSIAFSPLAGGQLtdrylngipadsr 242
Cdd:cd19100 141 GHSPEVLLRALEtgefdvVLFPIN-PAGDHIDSF-------REELLPLAREKGVGVIAMKVLAGGRL------------- 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495144968 243 aasgsrfLNPDQITPEKldkvrklndlalqrgqklsqmALAWVLRDEKVTSVLIGASKTSQIDDAV 308
Cdd:cd19100 200 -------LSGDPLDPEQ---------------------ALRYALSLPPVDVVIVGMDSPEELDENL 237
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
15-329 |
1.75e-35 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 130.67 E-value: 1.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 15 YRRCGRSGLKLPAISLG---LWHNFGDATlVETSRQLLRRSFDLGITHFDLANNYGPPpgSAESHFGRLLKEDFLPyRDE 91
Cdd:PLN02587 1 LRELGSTGLKVSSVGFGaspLGSVFGPVS-EEDAIASVREAFRLGINFFDTSPYYGGT--LSEKVLGKALKALGIP-REK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 92 LIISTKAGYtmwdgpYGDwG---SRKYLISSLDQSLKRMGLEYVDIFYHHrpDPE-----TPLEETMRALDHIVRQGKAL 163
Cdd:PLN02587 77 YVVSTKCGR------YGE-GfdfSAERVTKSVDESLARLQLDYVDILHCH--DIEfgsldQIVNETIPALQKLKESGKVR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 164 YVGISNYPADRAREAIDLLAQLGTPCIIHQPKYSMFERWVEDgLLDLLQEKGVGSIAFSPLAGGQLTDrylNGiPADSRA 243
Cdd:PLN02587 148 FIGITGLPLAIFTYVLDRVPPGTVDVILSYCHYSLNDSSLED-LLPYLKSKGVGVISASPLAMGLLTE---NG-PPEWHP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 244 ASgsrflnpdqitPEKLDKVRKLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQIDDAVGM---LANRGFSAEE 320
Cdd:PLN02587 223 AP-----------PELKSACAAAATHCKEKGKNISKLALQYSLSNKDISTTLVGMNSVQQVEENVAAateLETSGIDEEL 291
|
....*....
gi 495144968 321 RQAIEAILA 329
Cdd:PLN02587 292 LSEVEAILA 300
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
16-312 |
2.73e-35 |
|
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: 129.86 E-value: 2.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 16 RRCGRSGLKLPAISLG---LWHNFGDATLVETSRQLLRRSFDLGITHFDLANNYGPppGSAESHFGRLLKEdflPYRDEL 92
Cdd:cd19145 3 VKLGSQGLEVSAQGLGcmgLSGDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYGP--NTNEVLLGKALKD---GPREKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 93 IISTKAGYTMWDGPYGDW-GSRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISNYP 171
Cdd:cd19145 78 QLATKFGIHEIGGSGVEVrGDPAYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSEAS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 172 ADRAREAIDLlaqlgTPCIIHQPKYSMFERWVEDGLLDLLQEKGVGSIAFSPLAGGqltdrYLNGIPADSRAASGSRFLN 251
Cdd:cd19145 158 ADTIRRAHAV-----HPITAVQLEWSLWTRDIEEEIIPTCRELGIGIVPYSPLGRG-----FFAGKAKLEELLENSDVRK 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495144968 252 --PdQITPEKLDKVR----KLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQIDDAVGMLA 312
Cdd:cd19145 228 shP-RFQGENLEKNKvlyeRVEALAKKKGCTPAQLALAWVLHQGEDVVPIPGTTKIKNLNQNIGALS 293
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
22-294 |
1.17e-34 |
|
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: 127.30 E-value: 1.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 22 GLKLPAISLGLWHNFG----DATLVETSRQLLRRSFDLGITHFDLANNYGPppGSAESHFGRLLKeDFlpYRDELIISTK 97
Cdd:cd19137 1 GEKIPALGLGTWGIGGfltpDYSRDEEMVELLKTAIELGYTHIDTAEMYGG--GHTEELVGKAIK-DF--PREDLFIVTK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 98 AGYTMWdgpygdwgSRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISNYPADRARE 177
Cdd:cd19137 76 VWPTNL--------RYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 178 AIDLLAqlgTPCIIHQPKYSMFER-WVEDGLLDLLQEKGVGSIAFSPLAGGQLTdrylngipadsraasgsrflnpdqit 256
Cdd:cd19137 148 AISKSQ---TPIVCNQVKYNLEDRdPERDGLLEYCQKNGITVVAYSPLRRGLEK-------------------------- 198
|
250 260 270
....*....|....*....|....*....|....*...
gi 495144968 257 pekldKVRKLNDLALQRGQKLSQMALAWVLRDEKVTSV 294
Cdd:cd19137 199 -----TNRTLEEIAKNYGKTIAQIALAWLIQKPNVVAI 231
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
13-327 |
1.37e-33 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 126.51 E-value: 1.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 13 MEYRRCGRSGLKLPAISLGLWhNFGDATLVETSRQLLRRSFDLGITHFDLANNYGPPP-----GSAESHFGRLLKEDflP 87
Cdd:PRK10625 1 MQYHRIPHSSLEVSTLGLGTM-TFGEQNSEADAHAQLDYAVAQGINLIDVAEMYPVPPrpetqGLTETYIGNWLAKR--G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 88 YRDELIISTKAGytmwdGPY--GDWG-------SRKYLISSLDQSLKRMGLEYVDIFYHHRPDPET-------------- 144
Cdd:PRK10625 78 SREKLIIASKVS-----GPSrnNDKGirpnqalDRKNIREALHDSLKRLQTDYLDLYQVHWPQRPTncfgklgyswtdsa 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 145 ---PLEETMRALDHIVRQGKALYVGISNYPADRAREAIDLLAQLGTPCIIH-QPKYSMFERWVEDGLLDLLQEKGVGSIA 220
Cdd:PRK10625 153 pavSLLETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEKHDLPRIVTiQNPYSLLNRSFEVGLAEVSQYEGVELLA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 221 FSPLAGGQLTDRYLNGI-PADSRAASGSRFLNPDqiTPEKLDKVRKLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGAS 299
Cdd:PRK10625 233 YSCLAFGTLTGKYLNGAkPAGARNTLFSRFTRYS--GEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLLGAT 310
|
330 340
....*....|....*....|....*...
gi 495144968 300 KTSQIDDAVGMLaNRGFSAEERQAIEAI 327
Cdd:PRK10625 311 TMEQLKTNIESL-HLTLSEEVLAEIEAV 337
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
21-325 |
1.73e-33 |
|
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: 125.04 E-value: 1.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 21 SGLKLPAISLGL----WHnfGDATLVETSRQLLRRSFDLGITHFDLANNYGPPPGSAESHfgrLLKEDFL---PYRDELI 93
Cdd:cd19077 1 NGKLVGPIGLGLmgltWR--PNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHANLK---LLARFFRkypEYADKVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 94 ISTKAGYTM-WDGPYGdwgSRKYLISSLDQSLKRMG-LEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISNYP 171
Cdd:cd19077 76 LSVKGGLDPdTLRPDG---SPEAVRKSIENILRALGgTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 172 ADRAREAIDLlaqlgTPCIIHQPKYSMFERWVED-GLLDLLQEKGVGSIAFSPLAGGQLTDRY--LNGIPADSRAASGSR 248
Cdd:cd19077 153 AETIRRAHAV-----HPIAAVEVEYSLFSREIEEnGVLETCAELGIPIIAYSPLGRGLLTGRIksLADIPEGDFRRHLDR 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495144968 249 FlNPDQItPEKLDKVRKLNDLALQRGQKLSQMALAWVLRDEKVTSVLI-GASKTSQIDDAVGmLANRGFSAEERQAIE 325
Cdd:cd19077 228 F-NGENF-EKNLKLVDALQELAEKKGCTPAQLALAWILAQSGPKIIPIpGSTTLERVEENLK-AANVELTDEELKEIN 302
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
23-312 |
2.71e-33 |
|
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: 124.39 E-value: 2.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 23 LKLPAISLGLWHNFGDATLVETsrqlLRRSFDLGITHFDLANNYGPppGSAESHFGRLLKEdfLPyRDELIISTKAGYTM 102
Cdd:cd19162 3 LGLGAASLGNLARAGEDEAAAT----LDAAWDAGIRYFDTAPLYGL--GLSERRLGAALAR--HP-RAEYVVSTKVGRLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 103 WDGPYG-------DWG-SRKYLISSLDQSLKRMGLEYVDIFYHHRPDP--ETPLEETMRALDHIVRQGKALYVGISnypA 172
Cdd:cd19162 74 EPGAAGrpagadrRFDfSADGIRRSIEASLERLGLDRLDLVFLHDPDRhlLQALTDAFPALEELRAEGVVGAIGVG---V 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 173 DRAREAIDLLAQLGTPCIIHQPKYSMFERWVEDGLLDLLQEKGVGSIAFSPLAGGQLtdryLNGIPADSRAASGsrflnp 252
Cdd:cd19162 151 TDWAALLRAARRADVDVVMVAGRYTLLDRRAATELLPLCAAKGVAVVAAGVFNSGIL----ATDDPAGDRYDYR------ 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 253 dQITPEKLDKVRKLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQIDDAVGMLA 312
Cdd:cd19162 221 -PATPEVLARARRLAAVCRRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLALLR 279
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
21-231 |
3.08e-33 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 123.24 E-value: 3.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 21 SGLKLPAISLGLWHNFGDATlvetsRQLLRRSFDLGITHFDLANNYGpppgsAESHFGRLLKEDFLPyRDELIISTKAgy 100
Cdd:COG0656 1 NGVEIPALGLGTWQLPGEEA-----AAAVRTALEAGYRHIDTAAMYG-----NEEGVGEAIAASGVP-REELFVTTKV-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 101 tmwdgpYGDWGSRKYLISSLDQSLKRMGLEYVDIFYHHRPDPEtPLEETMRALDHIVRQGKALYVGISNYPADRAREAID 180
Cdd:COG0656 68 ------WNDNHGYDDTLAAFEESLERLGLDYLDLYLIHWPGPG-PYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLA 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495144968 181 LlaqLGTPCIIHQPKYSMFERwvEDGLLDLLQEKGVGSIAFSPLAGGQLTD 231
Cdd:COG0656 141 E---TGVKPAVNQVELHPYLQ--QRELLAFCREHGIVVEAYSPLGRGKLLD 186
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
49-328 |
2.72e-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: 381327 [Multi-domain] Cd Length: 304 Bit Score: 121.93 E-value: 2.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 49 LRRSFDLGITHFDLANNYGPppgsAESHFGRLLKE--DFLPYRDELIISTKagytmWDGPYGDWG-SRKYLISSLDQSLK 125
Cdd:cd19101 29 MAAYVDAGLTTFDCADIYGP----AEELIGEFRKRlrRERDAADDVQIHTK-----WVPDPGELTmTRAYVEAAIDRSLK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 126 RMGLEYVDIFYHHRPDPETP-LEETMRALDHIVRQGKALYVGISNYPADRAREAIDLlaqlGTPCIIHQPKYSMFERWVE 204
Cdd:cd19101 100 RLGVDRLDLVQFHWWDYSDPgYLDAAKHLAELQEEGKIRHLGLTNFDTERLREILDA----GVPIVSNQVQYSLLDRRPE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 205 DGLLDLLQEKGVGSIAFSPLAGGQLTDRYLnGIPADSRAASGSRFLNPDQITPEK-------LDKVRKLNDLALQRGQKL 277
Cdd:cd19101 176 NGMAALCEDHGIKLLAYGTLAGGLLSEKYL-GVPEPTGPALETRSLQKYKLMIDEwggwdlfQELLRTLKAIADKHGVSI 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 495144968 278 SQMALAWVLRDEKVTSVLIGASKTSQIDDAVgmlanRGFS----AEERQAIEAIL 328
Cdd:cd19101 255 ANVAVRWVLDQPGVAGVIVGARNSEHIDDNV-----RAFSfrldDEDRAAIDAVL 304
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
23-326 |
1.63e-31 |
|
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: 119.75 E-value: 1.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 23 LKLPAISLGLW----------HNFGDATLVETSRQLLRRSFDLGITHFDLANNYGPppGSAESHFGRLLKEdflPYRDEL 92
Cdd:cd19103 2 KKLPKIALGTWswgsggaggdQVFGNHLDEDTLKAVFDKAMAAGLNLWDTAAVYGM--GASEKILGEFLKR---YPREDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 93 IISTKagYTmwdgPYGDWGSRKYLISSLDQSLKRMGLEYVDIFYHHRP-DPETPLEEtmraLDHIVRQGKALYVGISNYP 171
Cdd:cd19103 77 IISTK--FT----PQIAGQSADPVADMLEGSLARLGTDYIDIYWIHNPaDVERWTPE----LIPLLKSGKVKHVGVSNHN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 172 ADRAREAIDLLAQLGTPCIIHQPKYSMFER-WVEDGLLDLLQEKGVGSIAFSPLAGGQLTDRYL--NGIPADS-RAASgs 247
Cdd:cd19103 147 LAEIKRANEILAKAGVSLSAVQNHYSLLYRsSEEAGILDYCKENGITFFAYMVLEQGALSGKYDtkHPLPEGSgRAET-- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 248 rfLNPdqitpeKLDKVRKLND----LALQRGQKLSQMALAWVLrdEKVTSVLIGASKTSQIDDAVGMlANRGFSAEERQA 323
Cdd:cd19103 225 --YNP------LLPQLEELTAvmaeIGAKHGASIAQVAIAWAI--AKGTTPIIGVTKPHHVEDAARA-ASITLTDDEIKE 293
|
...
gi 495144968 324 IEA 326
Cdd:cd19103 294 LEQ 296
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
20-327 |
1.21e-30 |
|
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: 116.20 E-value: 1.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 20 RSGLKLPAISLGLWHNFGdatlvETSRQLLRRSFDLGITHFDLANNYGpppgsAESHFGRLLKEDFLPyRDELIISTKag 99
Cdd:cd19140 3 VNGVRIPALGLGTYPLTG-----EECTRAVEHALELGYRHIDTAQMYG-----NEAQVGEAIAASGVP-RDELFLTTK-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 100 ytMWDGPYgdwgSRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISNYPADRAREAI 179
Cdd:cd19140 70 --VWPDNY----SPDDFLASVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 180 DLLAqlgTPCIIHQPKYSMFERwvEDGLLDLLQEKGVGSIAFSPLAGGQLTDRYLngipadsraasgsrflnpdqitpek 259
Cdd:cd19140 144 ELSE---APLFTNQVEYHPYLD--QRKLLDAAREHGIALTAYSPLARGEVLKDPV------------------------- 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 260 ldkvrkLNDLALQRGQKLSQMALAWVLRDEKVTSVligaSKTSQIDDAVGMLANRGF--SAEERQAIEAI 327
Cdd:cd19140 194 ------LQEIGRKHGKTPAQVALRWLLQQEGVAAI----PKATNPERLEENLDIFDFtlSDEEMARIAAL 253
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
21-328 |
7.87e-29 |
|
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins; Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis.
Pssm-ID: 381372 [Multi-domain] Cd Length: 326 Bit Score: 113.29 E-value: 7.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 21 SGLKLPAISLG-LWHNFGDATLVETSRQLLRRSFDLGITHFDLANNYgpPPGSAESHFGRLLKEDflPYRDELIISTK-- 97
Cdd:cd19146 12 SPLCLGAMSFGeAWKSMMGECDKETAFKLLDAFYEQGGNFIDTANNY--QGEESERWVGEWMASR--GNRDEMVLATKyt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 98 AGYTMWDGP-----YGDwGSRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISNYPA 172
Cdd:cd19146 88 TGYRRGGPIkiksnYQG-NHAKSLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSDTPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 173 -------DRAREAidllaqlG-TPCIIHQPKYSMFERWVEDGLLDLLQEKGVGSIAFSPLAGGQLTdrylngIPADSRAA 244
Cdd:cd19146 167 wvvskanAYARAH-------GlTQFVVYQGHWSAAFRDFERDILPMCEAEGMALAPWGVLGQGQFR------TEEEFKRR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 245 SGSRFlnpdQITP--EKLDKV-RKLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQIDDAVGMLAnRGFSAEER 321
Cdd:cd19146 234 GRSGR----KGGPqtEKERKVsEKLEKVAEEKGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIEALG-ISLSDEEI 308
|
....*..
gi 495144968 322 QAIEAIL 328
Cdd:cd19146 309 QEIEDAY 315
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
43-314 |
7.14e-25 |
|
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: 101.92 E-value: 7.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 43 ETSRQLLRRSFDLGITHFDLANNYGPppGSAESHFGRLLKEdfLPyRDELIISTKAGYTMW----DGPYGDWGSRKYL-- 116
Cdd:cd19152 20 EEAKATLVAAWDLGIRYFDTAPWYGA--GLSEERLGAALRE--LG-REDYVISTKVGRLLVplqeVEPTFEPGFWNPLpf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 117 -----IS------SLDQSLKRMGLEYVDIFYHHRPDPETPLEET-----------MRALDHIVRQGKALYVGI-SN--YP 171
Cdd:cd19152 95 davfdYSydgilrSIEDSLQRLGLSRIDLLSIHDPDEDLAGAESdehfaqaikgaFRALEELREEGVIKAIGLgVNdwEV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 172 ADRAREAID----LLAqlGTPCIIHQPKysmferwvEDGLLDLLQEKGVGSIAFSPLAGGQLtdrylngipadsraASGS 247
Cdd:cd19152 175 ILRILEEADldwvMLA--GRYTLLDHSA--------ARELLPECEKRGVKVVNAGPFNSGFL--------------AGGD 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495144968 248 RFLNP--DQITPEKLDKVRKLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQIDDAVGMLANR 314
Cdd:cd19152 231 NFDYYeyGPAPPELIARRDRIEALCEQHGVSLAAAALQFALAPPAVASVAPGASSPERVEENVALLATE 299
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
21-325 |
2.39e-24 |
|
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: 100.67 E-value: 2.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 21 SGLKLPAISLG-LWHNFGDATLVETSRQLLRRSFDLGITHFDLANNYGPPpgSAESHFGRLLKEDFLpyRDELIISTKAG 99
Cdd:cd19147 11 SPLILGAMSIGdAWSGFMGSMDKEQAFELLDAFYEAGGNFIDTANNYQDE--QSETWIGEWMKSRKN--RDQIVIATKFT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 100 --YTMWDGPYGD----WG-SRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISNYPA 172
Cdd:cd19147 87 tdYKAYEVGKGKavnyCGnHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDTPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 173 DRAREAIDLLAQLG-TPCIIHQPKYSMFERWVEDGLLDLLQEKGVGSIAFSPLAGGQLTDRYLngipADSRAASGS---R 248
Cdd:cd19147 167 WVVSAANYYATAHGkTPFSVYQGRWNVLNRDFERDIIPMARHFGMALAPWDVLGGGKFQSKKA----VEERKKNGEglrS 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495144968 249 FLNPDQITPEKLDKVRKLNDLALQRG-QKLSQMALAWVLRDEKVTSVLIGASKTSQIDDAVGMLANRgFSAEERQAIE 325
Cdd:cd19147 243 FVGGTEQTPEEVKISEALEKVAEEHGtESVTAIALAYVRSKAPNVFPLVGGRKIEHLKDNIEALSIK-LTPEEIEYLE 319
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
25-229 |
2.70e-24 |
|
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: 98.88 E-value: 2.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 25 LPAISLGLWHNFGDatlveTSRQLLRRSFDLGITHFDLANNYGpppgsAESHFGRLLKEDFLPyRDELIISTKAGYTMWD 104
Cdd:cd19073 1 IPALGLGTWQLRGD-----DCANAVKEALELGYRHIDTAEIYN-----NEAEVGEAIAESGVP-REDLFITTKVWRDHLR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 105 gpYGDwgsrkyLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEETMRALDHIVRQGKALYVGISNYPADRAREAIDLlaq 184
Cdd:cd19073 70 --PED------LKKSVDRSLEKLGTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDI--- 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495144968 185 LGTPCIIHQPKYSMFerWVEDGLLDLLQEKGVGSIAFSPLAGGQL 229
Cdd:cd19073 139 SPLPIAVNQVEFHPF--LYQAELLEYCRENDIVITAYSPLARGEV 181
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
43-304 |
5.63e-24 |
|
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: 99.71 E-value: 5.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 43 ETSRQLLRRSFDLGITHFDLANNYGPppGSAESHFGRLLKEdfLPyRDELIISTKAGYTMW---DG---PYGDWG----- 111
Cdd:cd19161 20 ADADATLDAAWDSGIRYFDTAPMYGH--GLAEHRLGDFLRE--KP-RDEFVLSTKVGRLLKparEGsvpDPNGFVdplpf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 112 ------SRKYLISSLDQSLKRMGLEYVDIFYHHRPDPETPLEE--------TM----RALDHIVRQG--KALYVGISNYP 171
Cdd:cd19161 95 eivydySYDGIMRSFEDSLQRLGLNRIDILYVHDIGVYTHGDRkerhhfaqLMsggfKALEELKKAGviKAFGLGVNEVQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 172 A-DRAREAIDLlaqlgtPCIIHQPKYSMFERWVEDGLLDLLQEKGVGSIAFSPLAGGQLtdrylngipadSRAASGSRFL 250
Cdd:cd19161 175 IcLEALDEADL------DCFLLAGRYSLLDQSAEEEFLPRCEQRGTSLVIGGVFNSGIL-----------ATGTKSGAKF 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 495144968 251 NPDQITPEKLDKVRKLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQI 304
Cdd:cd19161 238 NYGDAPAEIISRVMEIEKICDAYNVPLAAAALQFPLRHPAVASVLTGARNPAQL 291
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
46-308 |
2.02e-23 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 98.16 E-value: 2.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 46 RQLLRRSFDLGITHFDLANNYGPppGSAESHFGRLLKE---DFLPYRDELIISTKAGY--TMWDGPYGDWGSR------- 113
Cdd:cd19099 24 REALKAALDSGINVIDTAINYRG--GRSERLIGKALRElieKGGIKRDEVVIVTKAGYipGDGDEPLRPLKYLeeklgrg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 114 ----------------KYLISSLDQSLKRMGLEYVDIFYHHRPDPETP----------LEETMRALDHIVRQGKALYVGI 167
Cdd:cd19099 102 lidvadsaglrhcispAYLEDQIERSLKRLGLDTIDLYLLHNPEEQLLelgeeefydrLEEAFEALEEAVAEGKIRYYGI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 168 SNYPADRAREAIDLLAQLG--------------------TPCIIHQPkYSMFERWVEDG----LLDLLQEKGVGSIAFSP 223
Cdd:cd19099 182 STWDGFRAPPALPGHLSLEklvaaaeevggdnhhfkviqLPLNLLEP-EALTEKNTVKGealsLLEAAKELGLGVIASRP 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 224 LAGGQLtdrylngipadsraasgsrflnpdqitpekLDKVRKLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQ 303
Cdd:cd19099 261 LNQGQL------------------------------LGELRLADLLALPGGATLAQRALQFARSTPGVDSALVGMRRPEH 310
|
....*
gi 495144968 304 IDDAV 308
Cdd:cd19099 311 VDENL 315
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
43-308 |
9.57e-21 |
|
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: 89.54 E-value: 9.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 43 ETSRQLLRRSFDLGITHFDLANNYGPppGSAESHFGRLLKEDflpYRDELIISTKAGYtmWDGPYGDwGSRKYLisslDQ 122
Cdd:cd19096 21 EKAIEMIRYAIDAGINYFDTAYGYGG--GKSEEILGEALKEG---PREKFYLATKLPP--WSVKSAE-DFRRIL----EE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 123 SLKRMGLEYVDIFYHH---RPDPETPLEE--TMRALDHIVRQGKALYVGISNY-PADRAREAIDllaqlGTP---CIIHq 193
Cdd:cd19096 89 SLKRLGVDYIDFYLLHglnSPEWLEKARKggLLEFLEKAKKEGLIRHIGFSFHdSPELLKEILD-----SYDfdfVQLQ- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 194 pkYSMFERWVEDG--LLDLLQEKGVGSIAFSPLAGGQLTdrylngipadsraasgsrflnpdQITPEKLDKVRKLNDLAL 271
Cdd:cd19096 163 --YNYLDQENQAGrpGIEYAAKKGMGVIIMEPLKGGGLA-----------------------NNPPEALAILCGAPLSPA 217
|
250 260 270
....*....|....*....|....*....|....*..
gi 495144968 272 QrgqklsqMALAWVLRDEKVTSVLIGASKTSQIDDAV 308
Cdd:cd19096 218 E-------WALRFLLSHPEVTTVLSGMSTPEQLDENI 247
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
20-229 |
2.54e-20 |
|
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: 88.54 E-value: 2.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 20 RSGLKLPAISLGLWHNFG---DATLVEtsrqlLRrsfDLGITHFDLANNYGpppgsAESHFGRLLKEDFLPyRDELIIST 96
Cdd:cd19135 8 SNGVEMPILGLGTSHSGGyshEAVVYA-----LK---ECGYRHIDTAKRYG-----CEELLGKAIKESGVP-REDLFLTT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 97 KagytMWDGPYGDwgsrKYLISSLDQSLKRMGLEYVDIFYHHRPDPETP-------LEETMRALDHIVRQGKALYVGISN 169
Cdd:cd19135 74 K----LWPSDYGY----ESTKQAFEASLKRLGVDYLDLYLLHWPDCPSSgknvketRAETWRALEELYDEGLCRAIGVSN 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 170 YpadRAREAIDLLAQLGTPCIIHQPKYSMFERWVEdgLLDLLQEKGVGSIAFSPLAGGQL 229
Cdd:cd19135 146 F---LIEHLEQLLEDCSVVPHVNQVEFHPFQNPVE--LIEYCRDNNIVFEGYCPLAKGKA 200
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
43-308 |
3.90e-20 |
|
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: 87.97 E-value: 3.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 43 ETSRQLLRRSFDLGITHFDLANNYGpppgSAESHFGRLLKEDflpyrDELIISTKAGYTMWDGPYgdwgSRKYLISSLDQ 122
Cdd:cd19097 26 KEAKKILEYALKAGINTLDTAPAYG----DSEKVLGKFLKRL-----DKFKIITKLPPLKEDKKE----DEAAIEASVEA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 123 SLKRMGLEYVDIFYHHRPDPET-PLEETMRALDHIVRQGKALYVGISNYpadrAREAIDLLAQLGTPCIIHQPkYSMFE- 200
Cdd:cd19097 93 SLKRLKVDSLDGLLLHNPDDLLkHGGKLVEALLELKKEGLIRKIGVSVY----SPEELEKALESFKIDIIQLP-FNILDq 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 201 RWVEDGLLDLLQEKGVG----SIafsplaggqltdrYLNGIpadsraasgsrFLNPDQITPEKL----DKVRKLNDLALQ 272
Cdd:cd19097 168 RFLKSGLLAKLKKKGIEiharSV-------------FLQGL-----------LLMEPDKLPAKFapakPLLKKLHELAKK 223
|
250 260 270
....*....|....*....|....*....|....*.
gi 495144968 273 RGQKLSQMALAWVLRDEKVTSVLIGASKTSQIDDAV 308
Cdd:cd19097 224 LGLSPLELALGFVLSLPEIDKIVVGVDSLEQLKEII 259
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
21-327 |
1.17e-19 |
|
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: 87.54 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 21 SGLKLPAISLGLWHNFGDATlvetsRQLLRRSFDLGITHFDLANNYGpppgsAESHFGRLLKEDF---LPYRDELIISTK 97
Cdd:cd19112 7 SGHKMPVIGLGVWRMEPGEI-----KELILNAIKIGYRHFDCAADYK-----NEKEVGEALAEAFktgLVKREDLFITTK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 98 agytMWDGPYGdwgsrkYLISSLDQSLKRMGLEYVDIFYHHRP-----------------------DPETPLEETMRALD 154
Cdd:cd19112 77 ----LWNSDHG------HVIEACKDSLKKLQLDYLDLYLVHFPvatkhtgvgttgsalgedgvldiDVTISLETTWHAME 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 155 HIVRQGKALYVGISNYPADRAReaiDLLAQLG-TPCIIHQPKYSMFERwveDGLLDLLQEKGVGSIAFSPLAGGqltdry 233
Cdd:cd19112 147 KLVSAGLVRSIGISNYDIFLTR---DCLAYSKiKPAVNQIETHPYFQR---DSLVKFCQKHGISVTAHTPLGGA------ 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 234 lngipadsrAASGSRFlnpDQITPEKlDKVrkLNDLALQRGQKLSQMALAWVLrdEKVTSVLIGASKTSQIDDAVGMLan 313
Cdd:cd19112 215 ---------AANAEWF---GSVSPLD-DPV--LKDLAKKYGKSAAQIVLRWGI--QRNTAVIPKSSKPERLKENIDVF-- 275
|
330
....*....|....*.
gi 495144968 314 rGF--SAEERQAIEAI 327
Cdd:cd19112 276 -DFqlSKEDMKLIKSL 290
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
25-229 |
1.46e-19 |
|
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: 86.38 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 25 LPAISLGLWHNFGDATlvetsRQLLRRSFDLGITHFDLANNYGpppgsAESHFGRLLKEDFLPyRDELIISTKagytMWD 104
Cdd:cd19071 1 MPLIGLGTYKLKPEET-----AEAVLAALEAGYRHIDTAAAYG-----NEAEVGEAIRESGVP-REELFITTK----LWP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 105 GPYGdwgsRKYLISSLDQSLKRMGLEYVDIFYHHRP------DPETPLEETMRALDHIVRQGKALYVGISNYPAdrarEA 178
Cdd:cd19071 66 TDHG----YERVREALEESLKDLGLDYLDLYLIHWPvpgkegGSKEARLETWRALEELVDEGLVRSIGVSNFNV----EH 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495144968 179 IDLLAQLGT--PCiIHQPKYSMFerWVEDGLLDLLQEKGVGSIAFSPLAGGQL 229
Cdd:cd19071 138 LEELLAAARikPA-VNQIELHPY--LQQKELVEFCKEHGIVVQAYSPLGRGRR 187
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
22-327 |
3.40e-19 |
|
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: 85.75 E-value: 3.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 22 GLKLPAISLGL---WHNFGDATLVETSRQLLRRSFDLGITHFDLANNYGpppgsAESHFGRLLKEDFLPyRDELIISTKA 98
Cdd:cd19120 1 GSKIPAIAFGTgtaWYKSGDDDIQRDLVDSVKLALKAGFRHIDTAEMYG-----NEKEVGEALKESGVP-REDLFITTKV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 99 GYTMWDGPygdwgsrkyliSSLDQSLKRMGLEYVDIFYHHRP----DPETPLEETMRALDHIVRQGKALYVGISNYPADR 174
Cdd:cd19120 75 SPGIKDPR-----------EALRKSLAKLGVDYVDLYLIHSPffakEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIED 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 175 AREaidLLAQLGTPCIIHQPKYSMFERWVEDGLLDLLQEKGVGSIAFSPLAggQLTdrylngipadsraasgsrflnpdQ 254
Cdd:cd19120 144 LEE---LLDTAKIKPAVNQIEFHPYLYPQQPALLEYCREHGIVVSAYSPLS--PLT-----------------------R 195
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495144968 255 ITPEKLDKVrkLNDLALQRGQKLSQMALAWVLrdEKVTSVLIGASKTSQIDDAVGMlANRGFSAEERQAIEAI 327
Cdd:cd19120 196 DAGGPLDPV--LEKIAEKYGVTPAQVLLRWAL--QKGIVVVTTSSKEERMKEYLEA-FDFELTEEEVEEIDKA 263
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
16-308 |
5.91e-18 |
|
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: 82.58 E-value: 5.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 16 RRCGRSGLKLPAISLG---LWHNFGDATLVETSRQLLRRSFDLGITHFDLANNYGPPpgSAESHFGRLLKEDFLPyRDEL 92
Cdd:cd19153 3 ETLEIALGNVSPVGLGtaaLGGVYGDGLEQDEAVAIVAEAFAAGINHFDTSPYYGAE--SSEAVLGKALAALQVP-RSSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 93 IISTKAGYtmwdgpYGDWG---SRKYLISSLDQSLKRMGLEYVDIFYHHR---PDPETPLEETMRALDHIVRQGKALYVG 166
Cdd:cd19153 80 TVATKVGR------YRDSEfdySAERVRASVATSLERLHTTYLDVVYLHDiefVDYDTLVDEALPALRTLKDEGVIKRIG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 167 ISNYPadrareaIDLLAQLGTPCIIHQPK-------YSMFERWVEDGLLDLLQEKGVGSIAFSPLAGGQLTDRylnGIPA 239
Cdd:cd19153 154 IAGYP-------LDTLTRATRRCSPGSLDavlsychLTLQDARLESDAPGLVRGAGPHVINASPLSMGLLTSQ---GPPP 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 240 DSRAASGSRFLNPDQITPEKlDKVRKLNDLALQRgqklsqmALA-WVlrdeKVTSVLIGASKTSQIDDAV 308
Cdd:cd19153 224 WHPASGELRHYAAAADAVCA-SVEASLPDLALQY-------SLAaHA----GVGTVLLGPSSLAQLRSML 281
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
25-286 |
6.74e-17 |
|
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: 78.93 E-value: 6.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 25 LPAISLGLWHNFGDATlvetsRQLLRRSFDLGITHFDLANNYGpppgsAESHFGRLLKEDFLPyRDELIISTKagytMWD 104
Cdd:cd19139 1 IPAFGLGTFRLKDDVV-----IDSVRTALELGYRHIDTAQIYD-----NEAAVGQAIAESGVP-RDELFITTK----IWI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 105 GPYgdwgSRKYLISSLDQSLKRMGLEYVDIFYHHRPDP--ETPLEETMRALDHIVRQGKALYVGISNYPADRAREAIDLL 182
Cdd:cd19139 66 DNL----SKDKLLPSLEESLEKLRTDYVDLTLIHWPSPndEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 183 AqlGTPCIIHQPKYSMFERwvEDGLLDLLQEKGVGSIAFSPLAGGQLTDrylngipadsraasgsrflnpdqitpeklDK 262
Cdd:cd19139 142 G--AGAIATNQIELSPYLQ--NRKLVAHCKQHGIHVTSYMTLAYGKVLD-----------------------------DP 188
|
250 260
....*....|....*....|....
gi 495144968 263 VrkLNDLALQRGQKLSQMALAWVL 286
Cdd:cd19139 189 V--LAAIAERHGATPAQIALAWAM 210
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
49-287 |
1.65e-16 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 78.47 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 49 LRRSFDLGITHFDLANNYGPppgsaesHF-GRLLKEDFLPYRDELIISTKAGYTMwdGPYGDWG---SRKYLISSLDQSL 124
Cdd:PRK10376 46 LREAVALGVNHIDTSDFYGP-------HVtNQLIREALHPYPDDLTIVTKVGARR--GEDGSWLpafSPAELRRAVHDNL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 125 KRMGLEYVDI------FYHHRPDPEtPLEETMRALDHIVRQGKALYVGISNYPADRAREaidllAQLGTPCIIHQPKYSM 198
Cdd:PRK10376 117 RNLGLDVLDVvnlrlmGDGHGPAEG-SIEEPLTVLAELQRQGLVRHIGLSNVTPTQVAE-----ARKIAEIVCVQNHYNL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 199 FERwVEDGLLDLLQEKGVGSIAFSPLAGgqltdrylngipadsraasgsrfLNPDQITpekldkvrKLNDLALQRGQKLS 278
Cdd:PRK10376 191 AHR-ADDALIDALARDGIAYVPFFPLGG-----------------------FTPLQSS--------TLSDVAASLGATPM 238
|
....*....
gi 495144968 279 QMALAWVLR 287
Cdd:PRK10376 239 QVALAWLLQ 247
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
22-229 |
2.62e-16 |
|
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: 77.41 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 22 GLKLPAISLGLWHNFGDATlvetsRQLLRRSFDLGITHFDLANNYGpppgsAESHFGRLLKEDFLPyRDELIISTKagyt 101
Cdd:cd19131 7 GNTIPQLGLGVWQVSNDEA-----ASAVREALEVGYRSIDTAAIYG-----NEEGVGKAIRASGVP-REELFITTK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 102 MWDGPYGDWGSRKylisSLDQSLKRMGLEYVDIFYHHRPDP-ETPLEETMRALDHIVRQGKALYVGISNYPADRAREAID 180
Cdd:cd19131 72 LWNSDQGYDSTLR----AFDESLRKLGLDYVDLYLIHWPVPaQDKYVETWKALIELKKEGRVKSIGVSNFTIEHLQRLID 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495144968 181 llaQLGTPCIIHQpkYSMFERWVEDGLLDLLQEKGVGSIAFSPLAGGQL 229
Cdd:cd19131 148 ---ETGVVPVVNQ--IELHPRFQQRELRAFHAKHGIQTESWSPLGQGGL 191
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
22-237 |
1.99e-15 |
|
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: 74.78 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 22 GLKLPAISLGLWH-NFGDATlvetsRQLLRRSFDLGITHFDLANNYgpppgSAESHFGRLLKEDFLPyRDELIISTKagy 100
Cdd:cd19126 6 GTRMPWLGLGVFQtPDGDET-----ERAVQTALENGYRSIDTAAIY-----KNEEGVGEAIRESGVP-REELFVTTK--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 101 tMWDGpygDWGSRKYLiSSLDQSLKRMGLEYVDIFYHHRPDPETpLEETMRALDHIVRQGKALYVGISNYPADRAREaid 180
Cdd:cd19126 72 -LWND---DQRARRTE-DAFQESLDRLGLDYVDLYLIHWPGKDK-FIDTWKALEKLYASGKVKAIGVSNFQEHHLEE--- 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495144968 181 LLAQLGTPCIIHQPKYSmfERWVEDGLLDLLQEKGVGSIAFSPLAGGQ-LTDRYLNGI 237
Cdd:cd19126 143 LLAHADVVPAVNQVEFH--PYLTQKELRGYCKSKGIVVEAWSPLGQGGlLSNPVLAAI 198
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
23-243 |
2.24e-15 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 74.67 E-value: 2.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 23 LKLPAISLGLWHNFGDAtlVETSrqlLRRSFDLGITHFDLANNYGpppgsAESHFGRLLKEDFLPyRDELIISTKagytM 102
Cdd:PRK11172 1 MSIPAFGLGTFRLKDQV--VIDS---VKTALELGYRAIDTAQIYD-----NEAAVGQAIAESGVP-RDELFITTK----I 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 103 WDGPYgdwgSRKYLISSLDQSLKRMGLEYVDIFYHHRPDP--ETPLEETMRALDHIVRQGKALYVGISNYPADRAREAID 180
Cdd:PRK11172 66 WIDNL----AKDKLIPSLKESLQKLRTDYVDLTLIHWPSPndEVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQAIA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495144968 181 LL--AQLGTpciiHQPKYSMFERwvEDGLLDLLQEKGVGSIAFSPLAGGQ-LTDRYLNGIPADSRA 243
Cdd:PRK11172 142 AVgaENIAT----NQIELSPYLQ--NRKVVAFAKEHGIHVTSYMTLAYGKvLKDPVIARIAAKHNA 201
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
21-294 |
8.25e-15 |
|
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: 73.47 E-value: 8.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 21 SGLKLPAISLGLWHNFGDatlvETSRQLLRRSFDLGITHFDLANNYGpppgsAESHFGRLLKEDF---LPYRDELIISTK 97
Cdd:cd19116 7 DGNEIPAIALGTWKLKDD----EGVRQAVKHAIEAGYRHIDTAYLYG-----NEAEVGEAIREKIaegVVKREDLFITTK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 98 agytMWdgpyGDWGSRKYLISSLDQSLKRMGLEYVDIFYHHRP-------DPETPLE---------ETMRALDHIVRQGK 161
Cdd:cd19116 78 ----LW----NSYHEREQVEPALRESLKRLGLDYVDLYLIHWPvafkennDSESNGDgslsdidylETWRGMEDLVKLGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 162 ALYVGISNYPAdrarEAID-LLAQLGTPCIIHQ----PKYSmferwvEDGLLDLLQEKGVGSIAFSPLaggqltdrylnG 236
Cdd:cd19116 150 TRSIGVSNFNS----EQINrLLSNCNIKPAVNQievhPTLT------QEKLVAYCQSNGIVVMAYSPF-----------G 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 495144968 237 IPAdsraasGSRFLNPdqitPEKLDKvRKLNDLALQRGQKLSQMALAWVLrDEKVTSV 294
Cdd:cd19116 209 RLV------PRGQTNP----PPRLDD-PTLVAIAKKYGKTTAQIVLRYLI-DRGVVPI 254
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
25-308 |
1.36e-14 |
|
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: 73.08 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 25 LPAISLGLW-HNFGDATLVETSR--QLLRRSFDLGITHFDLANNYGPppgsAESHFGRLLKEDFLPY-RDELIISTKAG- 99
Cdd:cd19164 13 LPPLIFGAAtFSYQYTTDPESIPpvDIVRRALELGIRAFDTSPYYGP----SEIILGRALKALRDEFpRDTYFIITKVGr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 100 YTMWDGPYgdwgSRKYLISSLDQSLKRMGLEYVDIFYHHrpDPE-TPLEETMRALDHIVR---QGKALYVGISNYPADR- 174
Cdd:cd19164 89 YGPDDFDY----SPEWIRASVERSLRRLHTDYLDLVYLH--DVEfVADEEVLEALKELFKlkdEGKIRNVGISGYPLPVl 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 175 AREAIDLLAQLGTP--CIIhqpKYSMFErwVEDGLL-----DLLQEKGVGSI--AfSPLAGGQLTDRylnGIPaDSRAAS 245
Cdd:cd19164 163 LRLAELARTTAGRPldAVL---SYCHYT--LQNTTLlayipKFLAAAGVKVVlnA-SPLSMGLLRSQ---GPP-EWHPAS 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495144968 246 gsrflnpdqitPEKLDKVRKLNDLALQRGQKLSQMALAWVLR-DEKVTSVLIGASKTSQIDDAV 308
Cdd:cd19164 233 -----------PELRAAAAKAAEYCQAKGTDLADVALRYALReWGGEGPTVVGCSNVDELEEAV 285
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
22-292 |
1.98e-14 |
|
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: 72.04 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 22 GLKLPAISLGLWhnfgdatLVETSRQL---LRRSFDLGITHFDLANNYGPPPGsaeshFGRLLKEDFLPyRDELIISTKa 98
Cdd:cd19157 7 GVKMPWLGLGVF-------KVEEGSEVvnaVKTALKNGYRSIDTAAIYGNEEG-----VGKGIKESGIP-REELFITSK- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 99 gytMWDGpygDWGSRKYLiSSLDQSLKRMGLEYVDIFYHHRPDpETPLEETMRALDHIVRQGKALYVGISNYpadRAREA 178
Cdd:cd19157 73 ---VWNA---DQGYDSTL-KAFEASLERLGLDYLDLYLIHWPV-KGKYKETWKALEKLYKDGRVRAIGVSNF---QVHHL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 179 IDLLAQLGTPCIIHQPKYSmfERWVEDGLLDLLQEKGVGSIAFSPLAGGQLTDRYLngipadsraasgsrflnpdqitpe 258
Cdd:cd19157 142 EDLLADAEIVPMVNQVEFH--PRLTQKELRDYCKKQGIQLEAWSPLMQGQLLDNPV------------------------ 195
|
250 260 270
....*....|....*....|....*....|....
gi 495144968 259 kldkvrkLNDLALQRGQKLSQMALAWVLRDEKVT 292
Cdd:cd19157 196 -------LKEIAEKYNKSVAQVILRWDLQNGVVT 222
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
20-284 |
6.02e-14 |
|
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: 71.29 E-value: 6.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 20 RSGLKLPAISLGLWhNFGDATLVETsrqlLRRSFDLGITHFDLANNYGpppgsAESHFGRLLKEDF---LPYRDELIIST 96
Cdd:cd19123 7 SNGDLIPALGLGTW-KSKPGEVGQA----VKQALEAGYRHIDCAAIYG-----NEAEIGAALAEVFkegKVKREDLWITS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 97 KagytMWDgpygDWGSRKYLISSLDQSLKRMGLEYVDIFYHHRP------------------DPETPLEETMRALDHIVR 158
Cdd:cd19123 77 K----LWN----NSHAPEDVLPALEKTLADLQLDYLDLYLMHWPvalkkgvgfpesgedllsLSPIPLEDTWRAMEELVD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 159 QGKALYVGISNYPADRAReaiDLLAQLGTPCIIHQPKYSMFERWVEdgLLDLLQEKGVGSIAFSPLAGGqltDRylngiP 238
Cdd:cd19123 149 KGLCRHIGVSNFSVKKLE---DLLATARIKPAVNQVELHPYLQQPE--LLAFCRDNGIHLTAYSPLGSG---DR-----P 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 495144968 239 ADSRAASGSRFLNpdqitpeklDKVrkLNDLALQRGQKLSQMALAW 284
Cdd:cd19123 216 AAMKAEGEPVLLE---------DPV--INKIAEKHGASPAQVLIAW 250
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
21-304 |
1.88e-13 |
|
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: 69.68 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 21 SGLKLPAISLGLWHNFGD--ATLVETSRQLlrrsfdlGITHFDLANNYGpppgsAESHFGRLLKEDF---LPYRDELIIS 95
Cdd:cd19125 7 TGAKIPAVGLGTWQADPGvvGNAVKTAIKE-------GYRHIDCAAIYG-----NEKEIGKALKKLFedgVVKREDLFIT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 96 TKagytMW-------DGPygdwgsrkyliSSLDQSLKRMGLEYVDIFYHHRP--------------DPETPLEETMRALD 154
Cdd:cd19125 75 SK----LWctdhapeDVP-----------PALEKTLKDLQLDYLDLYLIHWPvrlkkgahmpepeeVLPPDIPSTWKAME 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 155 HIVRQGKALYVGISNYPADRAReaiDLLAQLGTPCIIHQpkYSMFERWVEDGLLDLLQEKGVGSIAFSPLaggqltdryl 234
Cdd:cd19125 140 KLVDSGKVRAIGVSNFSVKKLE---DLLAVARVPPAVNQ--VECHPGWQQDKLHEFCKSKGIHLSAYSPL---------- 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 235 ngipadsrAASGSRFLNPDQITPEKLDKVrklndlALQRGQKLSQMALAWVLrdEKVTSVLIGASKTSQI 304
Cdd:cd19125 205 --------GSPGTTWVKKNVLKDPIVTKV------AEKLGKTPAQVALRWGL--QRGTSVLPKSTNEERI 258
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
22-228 |
4.08e-13 |
|
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: 67.98 E-value: 4.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 22 GLKLPAISLGLWHnfgdATLVETSRQLLRRSFDLGITHFDLANNYGpppgsAESHFGRLLKEDFLPyRDELIISTKagyt 101
Cdd:cd19133 6 GVEMPILGFGVFQ----IPDPEECERAVLEAIKAGYRLIDTAAAYG-----NEEAVGRAIKKSGIP-REELFITTK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 102 MWDGPYGDWGSRKylisSLDQSLKRMGLEYVDIFYHHRP--DpetpLEETMRALDHIVRQGKALYVGISNYPADRareAI 179
Cdd:cd19133 72 LWIQDAGYEKAKK----AFERSLKRLGLDYLDLYLIHQPfgD----VYGAWRAMEELYKEGKIRAIGVSNFYPDR---LV 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495144968 180 DLLAQLGTPCIIHQPKYSMFerWVEDGLLDLLQEKGVGSIAFSPLAGGQ 228
Cdd:cd19133 141 DLILHNEVKPAVNQIETHPF--NQQIEAVEFLKKYGVQIEAWGPFAEGR 187
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
21-224 |
7.71e-13 |
|
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: 67.91 E-value: 7.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 21 SGLKLPAISLGLWHNFGD--ATLVETSrqlLRRsfdlGITHFDLANNYGpppgsAESHFGRLLKEDFLPyRDELIISTKa 98
Cdd:cd19117 10 TGAEIPAVGLGTWQSKPNevAKAVEAA---LKA----GYRHIDTAAIYG-----NEEEVGQGIKDSGVP-REEIFITTK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 99 gytMWdgpyGDWGSRkyLISSLDQSLKRMGLEYVDIFYHHRP---------------------DPETPLEETMRALDHIV 157
Cdd:cd19117 76 ---LW----CTWHRR--VEEALDQSLKKLGLDYVDLYLMHWPvpldpdgndflfkkddgtkdhEPDWDFIKTWELMQKLP 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495144968 158 RQGKALYVGISNYPADRAReaiDLLAQLGTPCIIHQPKYSMFERWVEDGLLDLLQEKGVGSIAFSPL 224
Cdd:cd19117 147 ATGKVKAIGVSNFSIKNLE---KLLASPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPL 210
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
25-230 |
1.01e-12 |
|
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: 66.89 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 25 LPAISLGLWHNFGDatlvETSRQLLRRSFDLGITHFDLANNYGpppgsAESHFGRLLKeDFLPY----RDELIISTKAGy 100
Cdd:cd19136 1 MPILGLGTFRLRGE----EEVRQAVDAALKAGYRLIDTASVYR-----NEADIGKALR-DLLPKyglsREDIFITSKLA- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 101 tmwdgPYGDWGSRKYliSSLDQSLKRMGLEYVDIFYHHRP-----DPETPLE-----ETMRALDHIVRQGKALYVGISNY 170
Cdd:cd19136 70 -----PKDQGYEKAR--AACLGSLERLGTDYLDLYLIHWPgvqglKPSDPRNaelrrESWRALEDLYKEGKLRAIGVSNY 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495144968 171 PADRAREaidLLAQLGTPCIIHQpkysmFE---RWVEDGLLDLLQEKGVGSIAFSPLAGGQLT 230
Cdd:cd19136 143 TVRHLEE---LLKYCEVPPAVNQ-----VEfhpHLVQKELLKFCKDHGIHLQAYSSLGSGDLR 197
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
21-305 |
1.58e-12 |
|
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: 66.88 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 21 SGLKLPAISLGLWHNFGDATlvETSRQLLRrSFDLGITHFDLANNY--GPPPGSAESHFgrlLKEDFLPYRDELIISTKa 98
Cdd:cd19122 5 NGVKIPAVGFGTFANEGAKG--ETYAAVTK-ALDVGYRHLDCAWFYlnEDEVGDAVRDF---LKENPSVKREDLFICTK- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 99 gytMWDG--PYGD--WgsrkylisSLDQSLKRMGLEYVDIFYHHRP------DPETPL-----------------EETMR 151
Cdd:cd19122 78 ---VWNHlhEPEDvkW--------SIDNSLKNLKLDYIDLFLVHWPiaaeknDQRSPKlgpdgkyvilkdltenpEPTWR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 152 ALDHIVRQGKALYVGISNYpadrareAIDLLAQLGTPCII--HQPKYSMFERWVEDGLLDLLQEKGVGSIAFSPLaGGQl 229
Cdd:cd19122 147 AMEEIYESGKAKAIGVSNW-------TIPGLKKLLSFAKVkpHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPL-GSQ- 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495144968 230 tdrylNGIPAdsraasgsrflnpdqiTPEKLDKVRKLNDLALQRGQKLSQMALAWVLRDEKVtsVLIGASKTSQID 305
Cdd:cd19122 218 -----NQVPS----------------TGERVSENPTLNEVAEKGGYSLAQVLIAWGLRRGYV--VLPKSSTPSRIE 270
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
22-228 |
3.87e-12 |
|
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: 65.37 E-value: 3.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 22 GLKLPAISLGLWHNFGDAtLVETSRQLLRRSFDLgithFDLANNYGpppgsAESHFGRLLKEDFLPyRDELIISTKAgyt 101
Cdd:cd19132 4 GTQIPAIGFGTYPLKGDE-GVEAVVAALQAGYRL----LDTAFNYE-----NEGAVGEAVRRSGVP-REELFVTTKL--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 102 mwdgPYGDWGSRKYLiSSLDQSLKRMGLEYVDIFYHHRPDPETPLE-ETMRALDHIVRQGKALYVGISNYPAdrarEAID 180
Cdd:cd19132 70 ----PGRHHGYEEAL-RTIEESLYRLGLDYVDLYLIHWPNPSRDLYvEAWQALIEAREEGLVRSIGVSNFLP----EHLD 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495144968 181 -LLAQLGTPCIIHQpkYSMFERWVEDGLLDLLQEKGVGSIAFSPLAGGQ 228
Cdd:cd19132 141 rLIDETGVTPAVNQ--IELHPYFPQAEQRAYHREHGIVTQSWSPLGRGS 187
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
22-170 |
5.00e-12 |
|
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: 65.21 E-value: 5.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 22 GLKLPAISLGLWHNFGDATlvetsRQLLRRSFDLGITHFDLANNYGpppgsAESHFGRLLKEDF---LPYRDELIISTKA 98
Cdd:cd19111 1 GFPMPVIGLGTYQSPPEEV-----RAAVDYALFVGYRHIDTALSYQ-----NEKAIGEALKWWLkngKLKREEVFITTKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 99 gytmWdgPYGDwgSRKYLISSLDQSLKRMGLEYVDIFYHH-------------RPDPETPLEETMRALDHIVRQGKALYV 165
Cdd:cd19111 71 ----P--PVYL--EFKDTEKSLEKSLENLKLPYVDLYLIHhpcgfvnkkdkgeRELASSDVTSVWRAMEALVSEGKVKSI 142
|
....*
gi 495144968 166 GISNY 170
Cdd:cd19111 143 GLSNF 147
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
26-228 |
6.54e-12 |
|
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: 64.85 E-value: 6.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 26 PAISLGLWHnfgdaTLVETSRQLLRRSFDLGITHFDLANNYGpppgsAESHFGRLLKEDF---LPYRDELIISTKAGYTM 102
Cdd:cd19128 2 PRLGFGTYK-----ITESESKEAVKNAIKAGYRHIDCAYYYG-----NEAFIGIAFSEIFkdgGVKREDLFITSKLWPTM 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 103 wdgpygdwgSRKYLIS-SLDQSLKRMGLEYVDIFYHHRP-------------------DPETPLEETMRALDHIVRQGKA 162
Cdd:cd19128 72 ---------HQPENVKeQLLITLQDLQLEYLDLFLIHWPlafdmdtdgdprddnqiqsLSKKPLEDTWRAMEQCVDEKLT 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495144968 163 LYVGISNYpadrareAIDLLAQLGTPCIIhQPKYSMFERWVE---DGLLDLLQEKGVGSIAFSPLAGGQ 228
Cdd:cd19128 143 KNIGVSNY-------STKLLTDLLNYCKI-KPFMNQIECHPYfqnDKLIKFCIENNIHVTAYRPLGGSY 203
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
21-224 |
7.21e-12 |
|
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: 65.13 E-value: 7.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 21 SGLKLPAISLGLWHNFGdatlvETSRQLLRRSFDLGITHFDLANNYgpppgSAESHFGRLLKEDF---LPYRDELIISTK 97
Cdd:cd19154 8 NGVKMPLIGLGTWQSKG-----AEGITAVRTALKAGYRLIDTAFLY-----QNEEAIGEALAELLeegVVKREDLFITTK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 98 AGYTMwdgpygdwGSRKYLISSLDQSLKRMGLEYVDIFYHHRP-------------------DPETPLEETMRALDHIVR 158
Cdd:cd19154 78 LWTHE--------HAPEDVEEALRESLKKLQLEYVDLYLIHAPaafkddegesgtmengmsiHDAVDVEDVWRGMEKVYD 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495144968 159 QGKALYVGISNYPADRAREAIDLlaqlgtpCIIhQPKYSMFE---RWVEDGLLDLLQEKGVGSIAFSPL 224
Cdd:cd19154 150 EGLTKAIGVSNFNNDQIQRILDN-------ARV-KPHNNQVEchlYFPQKELVEFCKKHNISVTSYATL 210
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
21-227 |
9.85e-12 |
|
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: 64.44 E-value: 9.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 21 SGLKLPAISLGLWHNFGDATLVetsRQLLRRSFDLGITHFDLANNYGpppgsAESHFGRLLKEDF---LPYRDELIISTK 97
Cdd:cd19119 8 TGASIPALGLGTASPHEDRAEV---KEAVEAAIKEGYRHIDTAYAYE-----TEDFVGEAIKRAIddgSIKREELFITTK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 98 AGYTMWDgpygdwgsrkYLISSLDQSLKRMGLEYVDIFYHHRP--------------DPETPLEETMRA----------- 152
Cdd:cd19119 80 VWPTFYD----------EVERSLDESLKALGLDYVDLLLVHWPvcfekdsddsgkpfTPVNDDGKTRYAasgdhittykq 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495144968 153 LDHIVRQGKALYVGISNYpadrareAIDLLAQLGTPCIIhQPKYSMFE---RWVEDGLLDLLQEKGVGSIAFSPLAGG 227
Cdd:cd19119 150 LEKIYLDGRAKAIGVSNY-------SIVYLERLIKECKV-VPAVNQVElhpHLPQMDLRDFCFKHGILVTAYSPLGSH 219
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
22-229 |
1.98e-11 |
|
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: 63.31 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 22 GLKLPAISLGLWHnFGDATLVETSrqlLRRSFDLGITHFDLANNYgpppgSAESHFGRLLKEDFLPyRDELIISTKagyt 101
Cdd:cd19156 6 GVEMPRLGLGVWR-VQDGAEAENA---VKWAIEAGYRHIDTAAIY-----KNEEGVGQGIRESGVP-REEVFVTTK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 102 MWDGpygDWGSRKYLiSSLDQSLKRMGLEYVDIFYHHRPDpETPLEETMRALDHIVRQGKALYVGISNYpadRAREAIDL 181
Cdd:cd19156 72 LWNS---DQGYESTL-AAFEESLEKLGLDYVDLYLIHWPV-KGKFKDTWKAFEKLYKEKKVRAIGVSNF---HEHHLEEL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495144968 182 LAQLGTPCIIHQpkYSMFERWVEDGLLDLLQEKGVGSIAFSPLAGGQL 229
Cdd:cd19156 144 LKSCKVAPMVNQ--IELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGKL 189
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
21-229 |
2.40e-11 |
|
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: 63.32 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 21 SGLKLPAISLGLWHnfGDATLVetsRQLLRRSFDLGITHFDLANNYGpppgsAESHFGRLLKEDFLP--YRDELIISTKA 98
Cdd:cd19121 8 TGASIPAVGLGTWQ--AKAGEV---KAAVAHALKIGYRHIDGALCYQ-----NEDEVGEGIKEAIAGgvKREDLFVTTKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 99 GYTMWDGPygdwgsrkylISSLDQSLKRMGLEYVDIFYHHRP--------DPETP-LEETMRALDH-------------I 156
Cdd:cd19121 78 WSTYHRRV----------ELCLDRSLKSLGLDYVDLYLVHWPvllnpngnHDLFPtLPDGSRDLDWdwnhvdtwkqmekV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495144968 157 VRQGKALYVGISNYpadrareAIDLLAQLgTPCIIHQPKYSMFE---RWVEDGLLDLLQEKGVGSIAFSPL--AGGQL 229
Cdd:cd19121 148 LKTGKTKAIGVSNY-------SIPYLEEL-LKHATVVPAVNQVEnhpYLPQQELVDFCKEKGILIEAYSPLgsTGSPL 217
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
21-286 |
3.13e-11 |
|
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: 63.06 E-value: 3.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 21 SGLKLPAISLGLWHNFGDAtlvETSRQLLRRSFDLGITHFDLANNYGpppgsAESHFGRLLKEDF----LPYRDELIIST 96
Cdd:cd19124 1 SGQTMPVIGMGTASDPPSP---EDIKAAVLEAIEVGYRHFDTAAAYG-----TEEALGEALAEALrlglVKSRDELFVTS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 97 KagytMW--DGPYGDwgsrkyLISSLDQSLKRMGLEYVDIF------------YHHRPDPETPL----EETMRALDHIVR 158
Cdd:cd19124 73 K----LWcsDAHPDL------VLPALKKSLRNLQLEYVDLYlihwpvslkpgkFSFPIEEEDFLpfdiKGVWEAMEECQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 159 QGKALYVGISNYPADRAReaiDLLAQLGTPCIIHQpkYSMFERWVEDGLLDLLQEKGVGSIAFSPLAGGqltdrylnGIP 238
Cdd:cd19124 143 LGLTKAIGVSNFSCKKLQ---ELLSFATIPPAVNQ--VEMNPAWQQKKLREFCKANGIHVTAYSPLGAP--------GTK 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 495144968 239 ADSRAASGSRFlnpdqitpekldkvrkLNDLALQRGQKLSQMALAWVL 286
Cdd:cd19124 210 WGSNAVMESDV----------------LKEIAAAKGKTVAQVSLRWVY 241
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
21-226 |
4.97e-11 |
|
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: 62.43 E-value: 4.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 21 SGLKLPAISLGLWH----NFGDATLVetsrqllrrSFDLGITHFDLANNYGPPP--GSAEShfgRLLKEDFLPYRDELII 94
Cdd:cd19118 3 TGNKIPAIGLGTWQaepgEVGAAVKI---------ALKAGYRHLDLAKVYQNQHevGQALK---ELLKEEPGVKREDLFI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 95 STKAgytmwdgpygdWGSR---KYLISSLDQSLKRMGLEYVDIFYHHRP-----------DPETPLEETMRALDHIV--- 157
Cdd:cd19118 71 TSKL-----------WNNShrpEYVEPALDDTLKELGLDYLDLYLIHWPvafkptgdlnpLTAVPTNGGEVDLDLSVslv 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495144968 158 ----------RQGKALYVGISNYPADRAREAIDllAQLGTPCIIhqpKYSMFERWVEDGLLDLLQEKGVGSIAFSPLAG 226
Cdd:cd19118 140 dtwkamvelkKTGKVKSIGVSNFSIDHLQAIIE--ETGVVPAVN---QIEAHPLLLQDELVDYCKSKNIHITAYSPLGN 213
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
21-172 |
6.23e-11 |
|
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: 62.46 E-value: 6.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 21 SGLKLPAISLGLWhNFGDATLVETsrqlLRRSFDLGITHFDLANNYGPPPGSAEShFGRLLKEDfLPYRDELIISTKagy 100
Cdd:cd19113 7 SGYKMPSVGFGCW-KLDNATAADQ----IYQAIKAGYRLFDGAEDYGNEKEVGEG-VNRAIDEG-LVKREELFLTSK--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 101 tMWDgpygDWGSRKYLISSLDQSLKRMGLEYVDIFYHHRP-------------------------DPETPLEETMRALDH 155
Cdd:cd19113 77 -LWN----NFHDPKNVETALNKTLSDLKLDYVDLFLIHFPiafkfvpieekyppgfycgdgdnfvYEDVPILDTWKALEK 151
|
170
....*....|....*..
gi 495144968 156 IVRQGKALYVGISNYPA 172
Cdd:cd19113 152 LVDAGKIKSIGVSNFPG 168
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
22-180 |
1.01e-10 |
|
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: 61.27 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 22 GLKLPAISLGLWHNFGDATLVETSRQLlrrsfDLGITHFDLANNYGpppgsAESHFGRLLKEDFLPyRDELIISTKagyt 101
Cdd:cd19127 6 GVEMPALGLGVFQTPPEETADAVATAL-----ADGYRLIDTAAAYG-----NEREVGEGIRRSGVD-RSDIFVTTK---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 102 MWDGPYGDWGSRKylisSLDQSLKRMGLEYVDIFYHHRPDPeTPLEETM---RALDHIVRQGKALYVGISNYPADRAREA 178
Cdd:cd19127 71 LWISDYGYDKALR----GFDASLRRLGLDYVDLYLLHWPVP-NDFDRTIqayKALEKLLAEGRVRAIGVSNFTPEHLERL 145
|
..
gi 495144968 179 ID 180
Cdd:cd19127 146 ID 147
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
25-231 |
2.17e-10 |
|
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: 60.25 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 25 LPAISLGLWHnFGDAtlvETSRQLLRrSFDLGITHFDLANNYGpppgsAESHFGRLLKEDFLPyRDELIISTKagytMWD 104
Cdd:cd19134 11 MPVIGLGVGE-LSDD---EAERSVSA-ALEAGYRLIDTAAAYG-----NEAAVGRAIAASGIP-RGELFVTTK----LAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 105 GPYGDWGSRKYLISSLDqslkRMGLEYVDIFYHHRPDP-ETPLEETMRALDHIVRQGKALYVGISNYPADRAREAIDLLA 183
Cdd:cd19134 76 PDQGFTASQAACRASLE----RLGLDYVDLYLIHWPAGrEGKYVDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLTF 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495144968 184 QlgTPCIihqPKYSMFERWVEDGLLDLLQEKGVGSIAFSPLAGGQLTD 231
Cdd:cd19134 152 F--TPAV---NQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGRLLD 194
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
22-231 |
2.01e-09 |
|
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: 57.57 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 22 GLKLPAISLGLWHNFGDATlvetsRQLLRRSFDLGITHFDLANNYGpppgsAESHFGRLLK---EDFLPYRDELIISTKa 98
Cdd:cd19114 1 GDKMPLVGFGTAKIKANET-----EEVIYNAIKVGYRLIDGALLYG-----NEAEVGRGIRkaiQEGLVKREDLFIVTK- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 99 gytMWDgpygDWGSRKYLISSLDQSLKRMGLEYVDIFYHHRP-----------------DPET--------PLEETMRAL 153
Cdd:cd19114 70 ---LWN----NFHGKDHVREAFDRQLKDYGLDYIDLYLIHFPipaayvdpaenypflwkDKELkkfpleqsPMQECWREM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 154 DHIVRQGKALYVGISNYpadRAREAIDLLAQLGT-PCII---HQPkYSMFERwvedgLLDLLQEKGVGSIAFSPLAGGQL 229
Cdd:cd19114 143 EKLVDAGLVRNIGIANF---NVQLILDLLTYAKIkPAVLqieHHP-YLQQKR-----LIDWAKKQGIQITAYSSFGNAVY 213
|
..
gi 495144968 230 TD 231
Cdd:cd19114 214 TK 215
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
21-224 |
2.14e-09 |
|
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: 57.78 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 21 SGLKLPAISLGLWHNfgDATLVETSrqlLRRSFDLGITHFDLANNYGpppgsAESHFGRLLKEDFLPY----RDELIIST 96
Cdd:cd19106 3 TGQKMPLIGLGTWKS--KPGQVKAA---VKYALDAGYRHIDCAAVYG-----NEQEVGEALKEKVGPGkavpREDLFVTS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 97 KAgytmwdgpygdWGSRKY---LISSLDQSLKRMGLEYVDIFYHHRP------------DP-------ETPLEETMRALD 154
Cdd:cd19106 73 KL-----------WNTKHHpedVEPALRKTLKDLQLDYLDLYLIHWPyafergdnpfpkNPdgtirydSTHYKETWKAME 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495144968 155 HIVRQGKALYVGISNYPAdrarEAIDLLAQLGTpciiHQPKYSMFE---RWVEDGLLDLLQEKGVGSIAFSPL 224
Cdd:cd19106 142 KLVDKGLVKAIGLSNFNS----RQIDDILSVAR----IKPAVLQVEchpYLAQNELIAHCKARGLVVTAYSPL 206
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
22-227 |
1.36e-08 |
|
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: 55.16 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 22 GLKLPAISLGLWhnFGDATlveTSRQLLRRSFDLGITHFDLANNYgpppgSAESHFGRLLKEDFLP---YRDELIISTKa 98
Cdd:cd19129 3 SGAIPALGFGTL--IPDPS---ATRNAVKAALEAGFRHFDCAERY-----RNEAEVGEAMQEVFKAgkiRREDLFVTTK- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 99 gytMWDGPYgdwgSRKYLISSLDQSLKRMGLEYVDIFYHHRP------DPETP--------------LEETMRALDHIVR 158
Cdd:cd19129 72 ---LWNTNH----RPERVKPAFEASLKRLQLDYLDLYLIHTPfafqpgDEQDPrdangnviyddgvtLLDTWRAMERLVD 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495144968 159 QGKALYVGISNYPADRAREAIDllAQLGTPCIIHQPKYSMFERWvedGLLDLLQEKGVGSIAFSPLAGG 227
Cdd:cd19129 145 EGRCKAIGLSDVSLEKLREIFE--AARIKPAVVQVESHPYLPEW---ELLDFCKNHGIVLQAFAPLGHG 208
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
22-231 |
1.46e-08 |
|
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: 54.92 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 22 GLKLPAISLGLWhNFGDATLVETSRQLLrrsfDLGITHFDLANNYGpppgsAESHFGRLLKEDFLPyRDELIISTKagyt 101
Cdd:cd19130 7 GNSIPQLGYGVF-KVPPADTQRAVATAL----EVGYRHIDTAAIYG-----NEEGVGAAIAASGIP-RDELFVTTK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 102 MWDGPYGDWGSRkyliSSLDQSLKRMGLEYVDIFYHHRPDPETPLE-ETMRALDHIVRQGKALYVGISNY-PADRAReai 179
Cdd:cd19130 72 LWNDRHDGDEPA----AAFAESLAKLGLDQVDLYLVHWPTPAAGNYvHTWEAMIELRAAGRTRSIGVSNFlPPHLER--- 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495144968 180 dLLAQLGTPCIIHQpkYSMFERWVEDGLLDLLQEKGVGSIAFSPLAGGQLTD 231
Cdd:cd19130 145 -IVAATGVVPAVNQ--IELHPAYQQRTIRDWAQAHDVKIEAWSPLGQGKLLG 193
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
21-222 |
2.98e-07 |
|
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: 51.27 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 21 SGLKLPAISLGLWhNFGDATLVETSRQLLRRSFDLgithFDLANNYGpppGSAESHFG--RLLKEDFLPyRDELIISTKA 98
Cdd:cd19115 9 SGYDMPLVGFGLW-KVNNDTCADQVYNAIKAGYRL----FDGACDYG---NEVEAGQGvaRAIKEGIVK-REDLFIVSKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 99 GYTMWDGPYGDWGSRKylissldqSLKRMGLEYVDIFYHHRP------DPE------------------TPLEETMRALD 154
Cdd:cd19115 80 WNTFHDGERVEPICRK--------QLADWGIDYFDLFLIHFPialkyvDPAvryppgwfydgkkvefsnAPIQETWTAME 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495144968 155 HIVRQGKALYVGISNYpadRAREAIDLL--AQL--GTPCIIHQPkYsmferWVEDGLLDLLQEKGVGSIAFS 222
Cdd:cd19115 152 KLVDKGLARSIGVSNF---SAQLLMDLLryARIrpATLQIEHHP-Y-----LTQPRLVKYAQKEGIAVTAYS 214
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
22-170 |
1.39e-06 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 48.92 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 22 GLKLPAISLGLWhnfgdATLVETSRQLLRRSFDLGITHFDLANNYGpppgsAESHFGRLLKEDFLPyRDELIISTKagyt 101
Cdd:PRK11565 12 GNVMPQLGLGVW-----QASNEEVITAIHKALEVGYRSIDTAAIYK-----NEEGVGKALKEASVA-REELFITTK---- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 102 MWDGPYGDwgSRKylisSLDQSLKRMGLEYVDIFYHHRPDPETPLE-ETMRALDHIVRQGKALYVGISNY 170
Cdd:PRK11565 77 LWNDDHKR--PRE----ALEESLKKLQLDYVDLYLMHWPVPAIDHYvEAWKGMIELQKEGLIKSIGVCNF 140
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
24-226 |
3.69e-06 |
|
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: 47.65 E-value: 3.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 24 KLPAISLGLWH-NFGDATlvetsrQLLRRSFDLGITHFDLANNYgpppgSAESHFGRLLKEDF---LPYRDELIISTKag 99
Cdd:cd19110 3 DIPAVGLGTWKaSPGEVT------EAVKVAIDAGYRHFDCAYLY-----HNESEVGAGIREKIkegVVRREDLFIVSK-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 100 ytMWDGPYgdwgsRKYLI-SSLDQSLKRMGLEYVDIFYHHRP------DPETPLEE-------------TMRALDHIVRQ 159
Cdd:cd19110 70 --LWCTCH-----KKSLVkTACTRSLKALKLNYLDLYLIHWPmgfkpgEPDLPLDRsgmvipsdtdfldTWEAMEDLVIE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 160 GKALYVGISNYpadrAREAIDLLaqLGTPCIIHQPKYSMFE---RWVEDGLLDLLQEKGVGSIAFSPLAG 226
Cdd:cd19110 143 GLVKNIGVSNF----NHEQLERL--LNKPGLRVKPVTNQIEchpYLTQKKLISFCQSRNVSVTAYRPLGG 206
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
22-286 |
3.55e-05 |
|
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: 44.82 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 22 GLKLPAISLGLWHnfGDATLVETSrqlLRRSFDLGITHFDLANNYGpppgsAESHFGRLLKEDFLP---YRDELIISTKA 98
Cdd:cd19155 9 GEKMPVVGLGTWQ--SSPEEIETA---VDTALEAGYRHIDTAYVYR-----NEAAIGNVLKKWIDSgkvKREELFIVTKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 99 gytmwdgPYGdwGSRKYLISS-LDQSLKRMGLEYVDIFYHHRP---------------------DPETPLEETMRALDHI 156
Cdd:cd19155 79 -------PPG--GNRREKVEKfLLKSLEKLQLDYVDLYLIHFPvgslskeddsgkldptgehkqDYTTDLLDIWKAMEAQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 157 VRQGKALYVGISNYPADRareaidlLAQLGTPCIIhQPKYSMFERWV---EDGLLDLLQEKGVGSIAFSPLAGgqltdry 233
Cdd:cd19155 150 VDQGLTRSIGLSNFNREQ-------MARILKNARI-KPANLQVELHVylqQKDLVDFCSTHSITVTAYAPLGS------- 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 495144968 234 lNGIPADSRAASGSRFLNPDQITPEKLDKVrklndlALQRGQKLSQMALAWVL 286
Cdd:cd19155 215 -PGAAHFSPGTGSPSGSSPDLLQDPVVKAI------AERHGKSPAQVLLRWLM 260
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
22-224 |
8.14e-05 |
|
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: 43.56 E-value: 8.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 22 GLKLPAISLGLWHN-FGDATlvetsrQLLRRSFDLGITHFDLANNYgpppgSAESHFGRLLKEDF---LPYRDELIISTK 97
Cdd:cd19107 1 GAKMPILGLGTWKSpPGQVT------EAVKVAIDAGYRHIDCAYVY-----QNENEVGEAIQEKIkeqVVKREDLFIVSK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 98 AGYTMWDgpygdwgsRKYLISSLDQSLKRMGLEYVDIFYHHRP------DPETPLEE-------------TMRALDHIVR 158
Cdd:cd19107 70 LWCTFHE--------KGLVKGACQKTLSDLKLDYLDLYLIHWPtgfkpgKELFPLDEsgnvipsdttfldTWEAMEELVD 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495144968 159 QGKALYVGISNYpadrAREAIDLLaqLGTPCIIHQPKYSMFE---RWVEDGLLDLLQEKGVGSIAFSPL 224
Cdd:cd19107 142 EGLVKAIGVSNF----NHLQIERI--LNKPGLKYKPAVNQIEchpYLTQEKLIQYCQSKGIVVTAYSPL 204
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
20-305 |
8.84e-05 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 43.49 E-value: 8.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 20 RSGLKLPA------ISLGLWHNFGDATLVETSR----QLLRRSFDLGITHFDLANNYGpppgSAESHFGRLLKEDFLPyR 89
Cdd:cd19098 2 RLGLGLAAlgrpgyINLGHAADLGSGRSVEAMRahthAVLDAAWAAGVRYFDAARSYG----RAEEFLGSWLRSRNIA-P 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 90 DELIISTKAGYTmwdgpY-GDWG-----------SRKYLISSLDQSLKRMGlEYVDIFYHHRPDPETPL---EETMRALD 154
Cdd:cd19098 77 DAVFVGSKWGYT-----YtADWQvdaavhevkdhSLARLLKQWEETRSLLG-KHLDLYQIHSATLESGVledADVLAALA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144968 155 HIVRQGKAlyVGISNYPADRA---REAIDLLAQLGTPCIIHQPKYSMFERWVEDGLLDLlQEKGVGSIAFSPLAGGQLTD 231
Cdd:cd19098 151 ELKAEGVK--IGLSLSGPQQAetlRRALEIEIDGARLFDSVQATWNLLEQSAGEALEEA-HEAGMGVIVKEALANGRLTD 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495144968 232 RylngipadsraasgsrflnpdQITPEKLDKVRKLNDLALQRGQKLSQMALAWVLRDEKVTSVLIGASKTSQID 305
Cdd:cd19098 228 R---------------------NPSPELAPLMAVLKAVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLR 280
|
|
| Alpha_L_fucos |
pfam01120 |
Alpha-L-fucosidase; |
99-146 |
5.34e-03 |
|
Alpha-L-fucosidase;
Pssm-ID: 460072 Cd Length: 333 Bit Score: 37.96 E-value: 5.34e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 495144968 99 GYTMWDGPYGDW-----GSRKYLISSLDQSLKRMGLEYvdIFYHHRPDPETPL 146
Cdd:pfam01120 110 GFTMWDSKYSDWnsvdvGPKRDLVGELAKAVRKQGLKF--GLYYSLADWFNPD 160
|
|
| |
