|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
16-323 |
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: 592.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 16 TYRRSGRSGLDLPAISLGLWQNFGGTDVFETGRAVLRRAFDRGVTHFDLANNYGPPPGSAEENFGRVLATDFKAHRDELI 95
Cdd:cd19151 1 KYNRCGRSGLKLPAISLGLWHNFGDVDRYENSRAMLRRAFDLGITHFDLANNYGPPPGSAEENFGRILKEDLKPYRDELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 96 VSTKAGYDMWPGPYGSWGSRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGISSYSPE 175
Cdd:cd19151 81 ISTKAGYTMWPGPYGDWGSKKYLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGISNYPPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 176 MTRRAAAILKDLGTPCLIHQPSYSMLNRWIEGGLLDALEETGIGCIAFSPLAQGMLTTKYLNGQPTDARAAKGGT-LKAH 254
Cdd:cd19151 161 EAREAAAILKDLGTPCLIHQPKYSMFNRWVEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYLNGIPEDSRAAKGSSfLKPE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1333942756 255 FLSPENLERVRALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDALKNTAFTPEELA 323
Cdd:cd19151 241 QITEEKLAKVRRLNEIAQARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALDNREFSEEELA 309
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
16-323 |
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: 571.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 16 TYRRSGRSGLDLPAISLGLWQNFGGTDVFETGRAVLRRAFDRGVTHFDLANNYGPPPGSAEENFGRVLATDFKAHRDELI 95
Cdd:cd19150 1 QYRRCGKSGLKLPALSLGLWHNFGDDTPLETQRAILRTAFDLGITHFDLANNYGPPPGSAEENFGRILREDFAGYRDELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 96 VSTKAGYDMWPGPYGSWGSRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGISSYSPE 175
Cdd:cd19150 81 ISTKAGYDMWPGPYGEWGSRKYLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYSPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 176 MTRRAAAILKDLGTPCLIHQPSYSMLNRWIEG-GLLDALEETGIGCIAFSPLAQGMLTTKYLNGQPTDARAAKGGTLKAH 254
Cdd:cd19150 161 RTREAAAILRELGTPLLIHQPSYNMLNRWVEEsGLLDTLQELGVGCIAFTPLAQGLLTDKYLNGIPEGSRASKERSLSPK 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1333942756 255 FLSPENLERVRALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDALKNTAFTPEELA 323
Cdd:cd19150 241 MLTEANLNSIRALNEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGALDNLTFSADELA 309
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
17-323 |
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: 558.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 17 YRRSGRSGLDLPAISLGLWQNFGGTDVFETGRAVLRRAFDRGVTHFDLANNYGPPPGSAEENFGRVLATDFKAHRDELIV 96
Cdd:cd19089 1 YRRCGRSGLHLPAISLGLWHNFGDYTSPEEARELLRTAFDLGITHFDLANNYGPPPGSAEENFGRILKRDLRPYRDELVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 97 STKAGYDMWPGPYGSWGSRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGISSYSPEM 176
Cdd:cd19089 81 STKAGYGMWPGPYGDGGSRKYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPGAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 177 TRRAAAILKDLGTPCLIHQPSYSMLNRWIEGGLLDALEETGIGCIAFSPLAQGMLTTKYLNGQPTDARAAK-GGTLKAHF 255
Cdd:cd19089 161 ARRAIALLRELGVPLIIHQPRYSLLDRWAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKYLNGIPPDSRRAAeSKFLTEEA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333942756 256 LSPENLERVRALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDALKNTAFTPEELA 323
Cdd:cd19089 241 LTPEKLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAALKNLDFSEEELA 308
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
4-342 |
0e+00 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 524.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 4 LYRADPARYTGMTYRRSGRSGLDLPAISLGLWQNFGGTDVFETGRAVLRRAFDRGVTHFDLANNYGPPPGSAEENFGRVL 83
Cdd:PRK09912 2 VWLANPERYGQMQYRYCGKSGLRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGPPPGSAEENFGRLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 84 ATDFKAHRDELIVSTKAGYDMWPGPYGSWGSRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGK 163
Cdd:PRK09912 82 REDFAAYRDELIISTKAGYDMWPGPYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 164 ALYVGISSYSPEMTRRAAAILKDLGTPCLIHQPSYSMLNRWIE-GGLLDALEETGIGCIAFSPLAQGMLTTKYLNGQPTD 242
Cdd:PRK09912 162 ALYVGISSYSPERTQKMVELLREWKIPLLIHQPSYNLLNRWVDkSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 243 ARAAKGGT----LKAHFLSPENLERVRALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDALKNTAFT 318
Cdd:PRK09912 242 SRMHREGNkvrgLTPKMLTEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQALNNLTFS 321
|
330 340
....*....|....*....|....
gi 1333942756 319 PEELAEIDRHAVDGGLNLWQNSSN 342
Cdd:PRK09912 322 TEELAQIDQHIADGELNLWQASSD 345
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
15-329 |
5.73e-138 |
|
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: 394.16 E-value: 5.73e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 15 MTYRRSGRSGLDLPAISLGLWQ---NFGGTDvFETGRAVLRRAFDRGVTHFDLANNYGPppGSAEENFGRVLATDfkaHR 91
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTMTfggPWGGVD-EAEAIAILDAALDAGINFFDTADVYGP--GRSEELLGEALKGR---PR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 92 DELIVSTKAGYDMWPGPYGSWGSRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGISS 171
Cdd:COG0667 75 DDVVIATKVGRRMGPGPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 172 YSPEMTRRAAAILKDLgTPCLIHQPSYSMLNRWIEGGLLDALEETGIGCIAFSPLAQGMLTTKYLNGQPTDARAAKGGTL 251
Cdd:COG0667 155 YSAEQLRRALAIAEGL-PPIVAVQNEYSLLDRSAEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGATFPEGDRAATNF 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333942756 252 KAHFLSPENLERVRALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDALKNTaFTPEELAEIDRHA 329
Cdd:COG0667 234 VQGYLTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADLE-LSAEDLAALDAAL 310
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
24-312 |
8.03e-98 |
|
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: 291.42 E-value: 8.03e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 24 GLDLPAISLGLWQNFGGTDVFETGRAVLRRAFDRGVTHFDLANNYGPppGSAEENFGRVLAtDFKahRDELIVSTKAGYD 103
Cdd:cd19074 1 GLKVSELSLGTWLTFGGQVDDEDAKACVRKAYDLGINFFDTADVYAA--GQAEEVLGKALK-GWP--RESYVISTKVFWP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 104 MWPGPYGSWGSRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGISSYSPEMTRRAAAI 183
Cdd:cd19074 76 TGPGPNDRGLSRKHIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 184 LKDLG-TPCLIHQPSYSMLNRWIEGGLLDALEETGIGCIAFSPLAQGMLTTKYLNGQPTDARAAKGGTLKAHF----LSP 258
Cdd:cd19074 156 ARQFGlIPPVVEQPQYNMLWREIEEEVIPLCEKNGIGLVVWSPLAQGLLTGKYRDGIPPPSRSRATDEDNRDKkrrlLTD 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1333942756 259 ENLERVRALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDAL 312
Cdd:cd19074 236 ENLEKVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKAS 289
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
30-329 |
4.90e-89 |
|
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: 268.80 E-value: 4.90e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 30 ISLGLWQNFGGTDV--FETGRAVLRRAFDRGVTHFDLANNYGPppGSAEENFGRVLAtDFKAHRDELIVSTKagYDMWPG 107
Cdd:pfam00248 1 IGLGTWQLGGGWGPisKEEALEALRAALEAGINFIDTAEVYGD--GKSEELLGEALK-DYPVKRDKVVIATK--VPDGDG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 108 PYGSWGSRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGISSYSPEMTRRAaaiLKDL 187
Cdd:pfam00248 76 PWPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKA---LTKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 188 GTPCLIHQPSYSMLNRWIEGGLLDALEETGIGCIAFSPLAQGMLTTKYLngqpTDARAAKGGTL-KAHFLSPENLERVRA 266
Cdd:pfam00248 153 KIPIVAVQVEYNLLRRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYT----RDPDKGPGERRrLLKKGTPLNLEALEA 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333942756 267 LDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDALKnTAFTPEELAEIDRHA 329
Cdd:pfam00248 229 LEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALE-FPLSDEEVARIDELL 290
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
15-326 |
5.69e-86 |
|
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: 261.74 E-value: 5.69e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 15 MTYRRSGRSGLDLPAISLGLwQNFGGTDVFETGRAVLRRAFDRGVTHFDLANNYGPppGSAEENFGRVLAtdfkAHRDEL 94
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGT-MNFGGRTDEETSFAIMDRALDAGINFFDTADVYGG--GRSEEIIGRWIA----GRRDDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 95 IVSTKAGYDMWPGPYGSWGSRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGISSYSP 174
Cdd:cd19087 74 VLATKVFGPMGDDPNDRGLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 175 EMTRRAAAILKDLGTPCLI-HQPSYSMLNRWIEGGLLDALEETGIGCIAFSPLAQGMLTTKYLNGQ-PTDARAAKGGTLK 252
Cdd:cd19087 154 WQIAKAQGIAARRGLLRFVsEQPMYNLLKRQAELEILPAARAYGLGVIPYSPLAGGLLTGKYGKGKrPESGRLVERARYQ 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333942756 253 AHFLSPENLERVRALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDALKNTaFTPEELAEID 326
Cdd:cd19087 234 ARYGLEEYRDIAERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEIT-LTPELLAEID 306
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
15-326 |
1.38e-83 |
|
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: 255.98 E-value: 1.38e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 15 MTYRRSGRSGLDLPAISLGLWQNFGGTDVFETGRAVLRRAFDRGVTHFDLANNYGPppGSAEENFGRVLAtDFKAHRDEL 94
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSWVTFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYAN--GQSEEIMGQAIK-ELGWPRSDY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 95 IVSTKAgydMWPGPYGSWG----SRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGIS 170
Cdd:cd19143 78 VVSTKI---FWGGGGPPPNdrglSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGTS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 171 SYSPEMTRRAAAILKDLG-TPCLIHQPSYSMLNRW-IEGGLLDALEETGIGCIAFSPLAQGMLTTKYLNGQPTDARAAKG 248
Cdd:cd19143 155 EWSAQQIEEAHEIADRLGlIPPVMEQPQYNLFHRErVEVEYAPLYEKYGLGTTTWSPLASGLLTGKYNNGIPEGSRLALP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 249 G----TLKAHFLSPENLERVRALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDALKNTA-FTPEELA 323
Cdd:cd19143 235 GyewlKDRKEELGQEKIEKVRKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEENLKALEVLPkLTPEVME 314
|
...
gi 1333942756 324 EID 326
Cdd:cd19143 315 KIE 317
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
24-326 |
1.59e-81 |
|
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: 249.75 E-value: 1.59e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 24 GLDLPAISLGLWQ----NFGGTDVFETGRAVlRRAFDRGVTHFDLANNYGPppGSAEENFGRVLatdfKAHRDELIVSTK 99
Cdd:cd19084 1 DLKVSRIGLGTWAiggtWWGEVDDQESIEAI-KAAIDLGINFFDTAPVYGF--GHSEEILGKAL----KGRRDDVVIATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 100 AGYDmWPGPYGSW--GSRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGISSYSPEMT 177
Cdd:cd19084 74 CGLR-WDGGKGVTkdLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 178 RRAAAIlkdlgTPCLIHQPSYSMLNRWIEGGLLDALEETGIGCIAFSPLAQGMLTTKYLNGQ---PTDARAAKggtlkaH 254
Cdd:cd19084 153 EEARKY-----GPIVSLQPPYSMLEREIEEELLPYCRENGIGVLPYGPLAQGLLTGKYKKEPtfpPDDRRSRF------P 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333942756 255 FLSPE----NLERVRALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDALKNTaFTPEELAEID 326
Cdd:cd19084 222 FFRGEnfekNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDWE-LTEEELKEID 296
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
17-326 |
1.39e-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: 245.57 E-value: 1.39e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 17 YRRSGRSGLDLPAISLGLWQnFGGTDV------FETGRAVLRRAFDRGVTHFDLANNYGPppGSAEENFGRVLaTDFkAH 90
Cdd:cd19079 2 YVRLGNSGLKVSRLCLGCMS-FGDPKWrpwvldEEESRPIIKRALDLGINFFDTANVYSG--GASEEILGRAL-KEF-AP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 91 RDELIVSTKAGYDMWPGPYGSWGSRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGIS 170
Cdd:cd19079 77 RDEVVIATKVYFPMGDGPNGRGLSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGAS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 171 SYSPEMTRRAAAILKDLG-TPCLIHQPSYSMLNRWIEGGLLDALEETGIGCIAFSPLAQGMLTTKYLNGQPTDARAAKGG 249
Cdd:cd19079 157 SMYAWQFAKALHLAEKNGwTKFVSMQNHYNLLYREEEREMIPLCEEEGIGVIPWSPLARGRLARPWGDTTERRRSTTDTA 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1333942756 250 TLKAHFLSPENLERVRALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDALkNTAFTPEELAEID 326
Cdd:cd19079 237 KLKYDYFTEADKEIVDRVEEVAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAAL-DIKLSEEEIKYLE 312
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
15-327 |
1.91e-78 |
|
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: 242.90 E-value: 1.91e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 15 MTYRRSGRSGLDLPAISLG---------LWQNFGGTDVFETGRAVlRRAFDRGVTHFDLANNYGPppGSAEENFGRVLat 85
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGtmtfgggggFFGAWGGVDQEEADRLV-DIALDAGINFFDTADVYSE--GESEEILGKAL-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 86 dfKAHRDELIVSTKAGYDMWPGPYGSWGSRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKAL 165
Cdd:cd19091 76 --KGRRDDVLIATKVRGRMGEGPNDVGLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 166 YVGISSYSPEMTRRAAAILKDLG-TPCLIHQPSYSMLNRWIEGGLLDALEETGIGCIAFSPLAQGMLTTKYLNGQPT-DA 243
Cdd:cd19091 154 YIGVSNFSAWQIMKALGISERRGlARFVALQAYYSLLGRDLEHELMPLALDQGVGLLVWSPLAGGLLSGKYRRGQPApEG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 244 RAAKGGTLKAHFLSPENLERV-RALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDALkNTAFTPEEL 322
Cdd:cd19091 234 SRLRRTGFDFPPVDRERGYDVvDALREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGAA-GLSLTPEEI 312
|
....*
gi 1333942756 323 AEIDR 327
Cdd:cd19091 313 ARLDK 317
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
21-326 |
9.38e-76 |
|
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: 235.57 E-value: 9.38e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 21 GRSGLDLPAISLGLWQnFGGTDVFETGRAVLRRAFDRGVTHFDLANNY-----GPPPGSAEENFGRVLATdfKAHRDELI 95
Cdd:cd19081 3 GRTGLSVSPLCLGTMV-FGWTADEETSFALLDAFVDAGGNFIDTADVYsawvpGNAGGESETIIGRWLKS--RGKRDRVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 96 VSTKAGYDMWPGPYGswGSRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGISSYSPE 175
Cdd:cd19081 80 IATKVGFPMGPNGPG--LSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYSAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 176 MTRRAAAILKDLGTP---CLihQPSYSMLNR-WIEGGLLDALEETGIGCIAFSPLAQGMLTTKYLNGQPTDARAAKGGTL 251
Cdd:cd19081 158 RLQEALELSRQHGLPryvSL--QPEYNLVDReSFEGELLPLCREEGIGVIPYSPLAGGFLTGKYRSEADLPGSTRRGEAA 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333942756 252 KAHfLSPENLERVRALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDAlKNTAFTPEELAEID 326
Cdd:cd19081 236 KRY-LNERGLRILDALDEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAA-AGLRLTDEEVARLD 308
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
28-310 |
2.78e-74 |
|
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: 228.94 E-value: 2.78e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 28 PAISLGLWqNFGGTDVFETGRAVLRRAFDRGVTHFDLANNYGPppGSAEENFGRVLATDFKahRDELIVSTKAGYDMWPG 107
Cdd:cd06660 1 SRLGLGTM-TFGGDGDEEEAFALLDAALEAGGNFFDTADVYGD--GRSERLLGRWLKGRGN--RDDVVIATKGGHPPGGD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 108 PYGSWGSRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGISSYSPEMTRRAAAILKDL 187
Cdd:cd06660 76 PSRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKAH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 188 G-TPCLIHQPSYSMLNRW-IEGGLLDALEETGIGCIAFSPLAQGmlttkylngqptdaraakggtlkahflspenlervr 265
Cdd:cd06660 156 GlPGFAAVQPQYSLLDRSpMEEELLDWAEENGLPLLAYSPLARG------------------------------------ 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1333942756 266 aldaiatrrgqtLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLD 310
Cdd:cd06660 200 ------------PAQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
27-327 |
4.99e-74 |
|
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: 230.55 E-value: 4.99e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 27 LPAISLGLWQnFGGTDVF-----ETGRAVLRRAFDRGVTHFDLANNYGPppGSAEENFGRVLatdfKAHRDELIVSTKAG 101
Cdd:cd19085 1 VSRLGLGCWQ-FGGGYWWgdqddEESIATIHAALDAGINFFDTAEAYGD--GHSEEVLGKAL----KGRRDDVVIATKVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 102 YDMwpgpygswGSRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGISSYSPEMTRRAA 181
Cdd:cd19085 74 PDN--------LTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 182 AIlkdlgTPCLIHQPSYSMLNRWIEGGLLDALEETGIGCIAFSPLAQGMLTTKYLNG---QPTDARAakggTLKAHFLsP 258
Cdd:cd19085 146 DA-----GRIDSNQLPYNLLWRAIEYEILPFCREHGIGVLAYSPLAQGLLTGKFSSAedfPPGDART----RLFRHFE-P 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333942756 259 ENLER----VRALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDALkNTAFTPEELAEIDR 327
Cdd:cd19085 216 GAEEEtfeaLEKLKEIADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAV-DLELSPSVLERLDE 287
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
17-325 |
1.27e-69 |
|
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: 219.78 E-value: 1.27e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 17 YRRSGRSGLDLPAISLG---LWQNFGGTDVfETGRAVLRRAFDRGVTHFDLANNYGPppGSAEENFGRVLatdfKAHRDE 93
Cdd:cd19076 2 TRKLGTQGLEVSALGLGcmgMSAFYGPADE-EESIATLHRALELGVTFLDTADMYGP--GTNEELLGKAL----KDRRDE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 94 LIVSTKAGYDMWPGPY--GSWGSRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGISS 171
Cdd:cd19076 75 VVIATKFGIVRDPGSGfrGVDGRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLSE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 172 YSPEMTRRAAAIlkdlgTPCLIHQPSYSMLNRWIEGGLLDALEETGIGCIAFSPLAQGMLTTKYlngQPTDARAAKGGTL 251
Cdd:cd19076 155 ASADTIRRAHAV-----HPITAVQSEYSLWTRDIEDEVLPTCRELGIGFVAYSPLGRGFLTGAI---KSPEDLPEDDFRR 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1333942756 252 KAHFLSPENLER----VRALDAIATRRGQTLAQMAIAWVL-RDPRVTsALVGARNVEQLDNSLDALkNTAFTPEELAEI 325
Cdd:cd19076 227 NNPRFQGENFDKnlklVEKLEAIAAEKGCTPAQLALAWVLaQGDDIV-PIPGTKRIKYLEENVGAL-DVVLTPEELAEI 303
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
18-326 |
7.41e-64 |
|
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: 205.15 E-value: 7.41e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 18 RRSGRSGLDLPAISLGLwQNFG-----GTDvFETGRAVLRRAFDRGVTHFDLANNYgpPPGSAEENFGRVLAtdfkAHRD 92
Cdd:cd19080 1 RLLGRSGLRVSPLALGT-MTFGtewgwGAD-REEARAMFDAYVEAGGNFIDTANNY--TNGTSERLLGEFIA----GNRD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 93 ELIVSTKAGYDMWPG-PYGSWGSRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGISS 171
Cdd:cd19080 73 RIVLATKYTMNRRPGdPNAGGNHRKNLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 172 YSPEMTRRAAAILKDLG-TPCLIHQPSYSMLNRWIEGGLLDALEETGIGCIAFSPLAQGMLTTKYLNGQPTDARAAKGGT 250
Cdd:cd19080 153 TPAWVVARANTLAELRGwSPFVALQIEYSLLERTPERELLPMARALGLGVTPWSPLGGGLLTGKYQRGEEGRAGEAKGVT 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333942756 251 LKAHFLSPENLERVRALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDALkNTAFTPEELAEID 326
Cdd:cd19080 233 VGFGKLTERNWAIVDVVAAVAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGAL-DLTLSPEQLARLD 307
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
17-326 |
3.66e-61 |
|
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: 198.27 E-value: 3.66e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 17 YRRSGRSGLDLPAISLGLWQ-----NFGGTDVFETGRAvLRRAFDRGVTHFDLANNYGPppGSAEENFGRVLatdfKAHR 91
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTWAigggpWWGGSDDNESIRT-IHAALDLGINLIDTAPAYGF--GHSEEIVGKAI----KGRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 92 DELIVSTKAGYdMWPGPYGSWGS-------RKYLTAS-----LDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAV 159
Cdd:cd19149 74 DKVVLATKCGL-RWDREGGSFFFvrdgvtvYKNLSPEsireeVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 160 RQGKALYVGISSYSPEMTRRAAAIlkdlGTPCLIhQPSYSMLNRWIEGGLLDALEETGIGCIAFSPLAQGMLTTKYLNGQ 239
Cdd:cd19149 153 RQGKIRAIGASNVSVEQIKEYVKA----GQLDII-QEKYSMLDRGIEKELLPYCKKNNIAFQAYSPLEQGLLTGKITPDR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 240 ---PTDARAAKggtlkaHFLSPENLERVRALD----AIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQ-LDNSLDA 311
Cdd:cd19149 228 efdAGDARSGI------PWFSPENREKVLALLekwkPLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPEQaEENAKAG 301
|
330
....*....|....*
gi 1333942756 312 lkNTAFTPEELAEID 326
Cdd:cd19149 302 --DIRLSAEDIATMR 314
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
27-327 |
8.64e-60 |
|
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: 194.43 E-value: 8.64e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 27 LPAISLGLWQNFGGTDVFETG-------RAVLRRAFDRGVTHFDLANNYGPppGSAEENFGRVLatdfKAHRDELIVSTK 99
Cdd:cd19102 1 LTTIGLGTWAIGGGGWGGGWGpqddrdsIAAIRAALDLGINWIDTAAVYGL--GHSEEVVGRAL----KGLRDRPIVATK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 100 AGYdMW--PGPYGSWGSRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGISSYSPEMT 177
Cdd:cd19102 75 CGL-LWdeEGRIRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 178 RRAAAIlkdlgTPCLIHQPSYSMLNRWIEGGLLDALEETGIGCIAFSPLAQGMLTTK----YLNGQPTDARAAKGGTLKA 253
Cdd:cd19102 154 KRCQAI-----HPIASLQPPYSLLRRGIEAEILPFCAEHGIGVIVYSPMQSGLLTGKmtpeRVASLPADDWRRRSPFFQE 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333942756 254 HFLSPeNLERVRALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDALKnTAFTPEELAEIDR 327
Cdd:cd19102 229 PNLAR-NLALVDALRPIAERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAAD-LRLTPEELAEIEA 300
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
36-327 |
1.18e-59 |
|
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: 194.71 E-value: 1.18e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 36 QNFGGTDVFETGRAVLRRAFDRGVTHFDLANNYGPPP-----GSAEENFGRVLATdfKAHRDELIVSTK-AGY--DM-WP 106
Cdd:cd19094 9 MTWGEQNTEAEAHEQLDYAFDEGVNFIDTAEMYPVPPspetqGRTEEIIGSWLKK--KGNRDKVVLATKvAGPgeGItWP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 107 GPYGSWGSRKYLTASLDQSLKRMGLDYVDIF------------------YSHRVDPRTPLEETMGALDHAVRQGKALYVG 168
Cdd:cd19094 87 RGGGTRLDRENIREAVEGSLKRLGTDYIDLYqlhwpdrytplfgggyytEPSEEEDSVSFEEQLEALGELVKAGKIRHIG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 169 ISSYSP----EMTRraAAILKDLGTPCLIhQPSYSMLNRWIEGGLLDALEETGIGCIAFSPLAQGMLTTKYLNGQ--PTD 242
Cdd:cd19094 167 LSNETPwgvmKFLE--LAEQLGLPRIVSI-QNPYSLLNRNFEEGLAEACHRENVGLLAYSPLAGGVLTGKYLDGAarPEG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 243 ARAAKGGTLKAHFLSPENLERVRALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDALkNTAFTPEEL 322
Cdd:cd19094 244 GRLNLFPGYMARYRSPQALEAVAEYVKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLKENIDAF-DVPLSDELL 322
|
....*
gi 1333942756 323 AEIDR 327
Cdd:cd19094 323 AEIDA 327
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
18-326 |
1.22e-59 |
|
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: 194.17 E-value: 1.22e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 18 RRSGRSGLDLPAISLGLwQNFGGTDVF-----ETGRAVLRRAFDRGVTHFDLANNYGPppGSAEENFGRVLAtDFKahRD 92
Cdd:cd19083 2 VKLGKSDIDVNPIGLGT-NAVGGHNLYpnldeEEGKDLVREALDNGVNLLDTAFIYGL--GRSEELVGEVLK-EYN--RN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 93 ELIVSTKAGYDMWPGPYGSWGSRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGISSY 172
Cdd:cd19083 76 EVVIATKGAHKFGGDGSVLNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 173 SPEMTRRAAailKDLGTPCLihQPSYSMLNRWIEGGLLDALEETGIGCIAFSPLAQGMLTTKYLNG---QPTDARAAKGG 249
Cdd:cd19083 156 SLEQLKEAN---KDGYVDVL--QGEYNLLQREAEEDILPYCVENNISFIPYFPLASGLLAGKYTKDtkfPDNDLRNDKPL 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1333942756 250 TLKAHFlsPENLERVRALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDALKNTaFTPEELAEID 326
Cdd:cd19083 231 FKGERF--SENLDKVDKLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKALDVT-LTEEEIAFID 304
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
24-328 |
1.78e-58 |
|
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: 190.91 E-value: 1.78e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 24 GLDLPAISLG---LWQNFGGTDVFETGRAVLRRAFDRGVTHFDLANNYGPPpgSAEENFGRVLatdfKAHRDELIVSTKA 100
Cdd:cd19078 1 GLEVSAIGLGcmgMSHGYGPPPDKEEMIELIRKAVELGITFFDTAEVYGPY--TNEELVGEAL----KPFRDQVVIATKF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 101 GYDMWPGPYGSWG---SRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGISSYSPEMT 177
Cdd:cd19078 75 GFKIDGGKPGPLGldsRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 178 RRAAAIlkdlgTPCLIHQPSYSMLNRWIEGGLLDALEETGIGCIAFSPLAQGMLTTKYLNGQ---PTDARAAkggtlkAH 254
Cdd:cd19078 155 RRAHAV-----CPVTAVQSEYSMMWREPEKEVLPTLEELGIGFVPFSPLGKGFLTGKIDENTkfdEGDDRAS------LP 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333942756 255 FLSPENLER----VRALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDALkNTAFTPEELAEIDRH 328
Cdd:cd19078 224 RFTPEALEAnqalVDLLKEFAEEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAA-DIELTPEELREIEDA 300
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
17-313 |
7.25e-57 |
|
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: 186.88 E-value: 7.25e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 17 YRRSGRSGLDLPAISLGLWQNFGGTDVFETGRAVLRRAFDRGVTHFDLANNYGPppGSAEENFGRVLATDfKAHRDELIV 96
Cdd:cd19141 2 YRNLGKSGLRVSCLGLGTWVTFGSQISDEVAEELVTLAYENGINLFDTAEVYAA--GKAEIVLGKILKKK-GWRRSSYVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 97 STKAgydmwpgpygSWG---------SRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYV 167
Cdd:cd19141 79 TTKI----------FWGgkaeterglSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYW 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 168 GISSYSPEMTRRAAAILKDLG-TPCLIHQPSYSMLNR-WIEGGLLDALEETGIGCIAFSPLAQGMLTTKYLNGQPTDARA 245
Cdd:cd19141 149 GTSRWSAMEIMEAYSVARQFNlIPPIVEQAEYHLFQReKVEMQLPELFHKIGVGAMTWSPLACGILSGKYDDGVPEYSRA 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333942756 246 A-KG-GTLKAHFLSPENLE---RVRALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDALK 313
Cdd:cd19141 229 SlKGyQWLKEKILSEEGRRqqaKLKELQIIADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQAIQ 301
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
27-326 |
9.65e-57 |
|
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: 186.28 E-value: 9.65e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 27 LPAISLGLWQ------NFGGTDVFETGRAVLRRAFDRGVTHFDLANNYGPppGSAEENFGRVLATDfkAHRDELIVSTKa 100
Cdd:cd19093 2 VSPLGLGTWQwgdrlwWGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYGT--GRSERLLGRFLKEL--GDRDEVVIATK- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 101 gydmWPGPYGSWGSRKYLTAsLDQSLKRMGLDYVDIFYSHRVDPR-TPLEETMGALDHAVRQGKALYVGISSYSPEMTRR 179
Cdd:cd19093 77 ----FAPLPWRLTRRSVVKA-LKASLERLGLDSIDLYQLHWPGPWySQIEALMDGLADAVEEGLVRAVGVSNYSADQLRR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 180 AAAILKDLGTPCLIHQPSYSMLNRWIE-GGLLDALEETGIGCIAFSPLAQGMLTTKY-LNGQPTDARAAkggtlkahFLS 257
Cdd:cd19093 152 AHKALKERGVPLASNQVEYSLLYRDPEqNGLLPACDELGITLIAYSPLAQGLLTGKYsPENPPPGGRRR--------LFG 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333942756 258 PENLERVR----ALDAIATRRGQTLAQMAIAWVLRDPRVtsALVGARNVEQLDNSLDALKNTaFTPEELAEID 326
Cdd:cd19093 224 RKNLEKVQplldALEEIAEKYGKTPAQVALNWLIAKGVV--PIPGAKNAEQAEENAGALGWR-LSEEEVAELD 293
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
13-326 |
2.64e-55 |
|
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: 183.65 E-value: 2.64e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 13 TGMTYRRSGRSGLDLPAISLGLWQNFGGTDVFETGRAVLRRAFDRGVTHFDLANNYGPppGSAEENFGRVLATDfKAHRD 92
Cdd:cd19160 1 TGMKYRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDLLTVAYEHGVNLFDTAEVYAA--GKAERTLGNILKSK-GWRRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 93 ELIVSTKAgydMWPGPYGSWG--SRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGIS 170
Cdd:cd19160 78 SYVVTTKI---YWGGQAETERglSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 171 SYSPEMTRRAAAILKDLG-TPCLIHQPSYSMLNR-WIEGGLLDALEETGIGCIAFSPLAQGMLTTKYLNGQPTDARAAKG 248
Cdd:cd19160 155 RWSAMEIMEAYSVARQFNlIPPVCEQAEYHLFQReKVEMQLPELYHKIGVGSVTWSPLACGLITGKYDGRVPDTCRAAVK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 249 GT--LKAHFLSPENLE---RVRALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDALKNTA-FTPEEL 322
Cdd:cd19160 235 GYqwLKEKVQSEEGKKqqaKVKELHPIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGSIQVLSqLTPQTV 314
|
....
gi 1333942756 323 AEID 326
Cdd:cd19160 315 MEID 318
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
18-331 |
1.48e-54 |
|
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: 181.49 E-value: 1.48e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 18 RRSGRSGLDLPAI---SLGLWQNFGGTDVFETGRAVLRRAFDRGVTHFDLANNYGPppgsAEENFGRVLATDfKAHRDEL 94
Cdd:cd19144 4 RTLGRNGPSVPALgfgAMGLSAFYGPPKPDEERFAVLDAAFELGCTFWDTADIYGD----SEELIGRWFKQN-PGKREKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 95 IVSTKAGYDMWP--GPYGSWGSRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGISSY 172
Cdd:cd19144 79 FLATKFGIEKNVetGEYSVDGSPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLSEC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 173 SPEMTRRAAAIlkdlgTPCLIHQPSYSMLNRWIE---GGLLDALEETGIGCIAFSPLAQGMLTTKYLNG---QPTDARAA 246
Cdd:cd19144 159 SAETLRRAHAV-----HPIAAVQIEYSPFSLDIErpeIGVLDTCRELGVAIVAYSPLGRGFLTGAIRSPddfEEGDFRRM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 247 KGGTLKAHFlsPENLERVRALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDALKnTAFTPEELAEId 326
Cdd:cd19144 234 APRFQAENF--PKNLELVDKIKAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLGALK-VKLTEEEEKEI- 309
|
....*
gi 1333942756 327 RHAVD 331
Cdd:cd19144 310 REIAE 314
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
24-326 |
1.08e-51 |
|
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: 172.03 E-value: 1.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 24 GLDLPAISLGLWqNFGGTDVFETGR-----AVLRRAFDRGVTHFDLANNYGPppGSAEENFGRVLAtDFKahRDELIVST 98
Cdd:cd19072 1 GEEVPVLGLGTW-GIGGGMSKDYSDdkkaiEALRYAIELGINLIDTAEMYGG--GHAEELVGKAIK-GFD--REDLFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 99 KAgydmWPgpygsWGSRKY-LTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGISSYSPEMT 177
Cdd:cd19072 75 KV----SP-----DHLKYDdVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 178 RRAAAILKDlgTPCLIHQPSYSMLNRWIEGGLLDALEETGIGCIAFSPLAQGMLTTKylngqptdaraakggtlkahfls 257
Cdd:cd19072 146 EEAQSYLKK--GPIVANQVEYNLFDREEESGLLPYCQKNGIAIIAYSPLEKGKLSNA----------------------- 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1333942756 258 penlERVRALDAIATRRGQTLAQMAIAWVLRDPRVTsALVGARNVEQLDNSLDALkNTAFTPEELAEID 326
Cdd:cd19072 201 ----KGSPLLDEIAKKYGKTPAQIALNWLISKPNVI-AIPKASNIEHLEENAGAL-GWELSEEDLQRLD 263
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
15-313 |
1.36e-51 |
|
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: 173.73 E-value: 1.36e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 15 MTYRRSGRSGLDLPAISLGLWQNFGGTDVFETGRAVLRRAFDRGVTHFDLANNYGPppGSAEENFGRVLATDfKAHRDEL 94
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAA--GKAEVVLGNIIKKK-GWRRSSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 95 IVSTKAgydMWPGPYGSWG--SRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGISSY 172
Cdd:cd19158 78 VITTKI---FWGGKAETERglSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 173 SPEMTRRAAAILKDLG-TPCLIHQPSYSMLNRW-IEGGLLDALEETGIGCIAFSPLAQGMLTTKYLNGQPTDARAAKGGT 250
Cdd:cd19158 155 SSMEIMEAYSVARQFNlIPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGY 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333942756 251 --LKAHFLSPENLE---RVRALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDALK 313
Cdd:cd19158 235 qwLKDKILSEEGRRqqaKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQ 302
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
25-311 |
1.24e-50 |
|
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: 168.42 E-value: 1.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 25 LDLPAISLGLWQnFGGTDVF----ETGRAVLRRAFDRGVTHFDLANNYGPppGSAEENFGRVLatdfKAHRDELIVSTKA 100
Cdd:cd19086 1 LEVSEIGFGTWG-LGGDWWGdvddAEAIRALRAALDLGINFFDTADVYGD--GHSERLLGKAL----KGRRDKVVIATKF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 101 GYDMWPGPYGSWG-SRKYLTASLDQSLKRMGLDYVDIFYSHRVDPR-TPLEETMGALDHAVRQGKALYVGISSYSPEMTR 178
Cdd:cd19086 74 GNRFDGGPERPQDfSPEYIREAVEASLKRLGTDYIDLYQLHNPPDEvLDNDELFEALEKLKQEGKIRAYGVSVGDPEEAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 179 RAaaiLKDLGTPCLihQPSYSMLNRWIEGGLLDALEETGIGCIAFSPLAQGMLTTKylngqptdaraakggtlkahflsp 258
Cdd:cd19086 154 AA---LRRGGIDVV--QVIYNLLDQRPEEELFPLAEEHGVGVIARVPLASGLLTGK------------------------ 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1333942756 259 enlervraldaiatrrgqtLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDA 311
Cdd:cd19086 205 -------------------LAQAALRFILSHPAVSTVIPGARSPEQVEENAAA 238
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
15-326 |
1.32e-50 |
|
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: 171.38 E-value: 1.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 15 MTYRRSGRSGLDLPAISLGLWQNFGGTDVFETGRAVLRRAFDRGVTHFDLANNYGPppGSAEENFGRVLATDfKAHRDEL 94
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAA--GKAEVILGSIIKKK-GWRRSSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 95 IVSTKAgydMWPGPYGSWG--SRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGISSY 172
Cdd:cd19159 78 VITTKL---YWGGKAETERglSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 173 SPEMTRRAAAILKDLG-TPCLIHQPSYSMLNRW-IEGGLLDALEETGIGCIAFSPLAQGMLTTKYLNGQPTDARAAKGGT 250
Cdd:cd19159 155 SAMEIMEAYSVARQFNmIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 251 --LKAHFLSPENLE---RVRALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDALKN-TAFTPEELAE 324
Cdd:cd19159 235 qwLKERIVSEEGRKqqnKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlPKMTSHVVNE 314
|
..
gi 1333942756 325 ID 326
Cdd:cd19159 315 ID 316
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
15-327 |
1.55e-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: 171.11 E-value: 1.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 15 MTYRRSGRSGLDLPAISLGLWQNFGGTDVFETGRAVLRRAFDRGVTHFDLANnyGPPPGSAEENFGRVLAtdfKA--HRD 92
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGTWSTFSTAISEEQAEEIVTLAYENGINYFDTSD--AFTSGQAETELGRILK---KKgwKRS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 93 ELIVSTKAGYDMwpGPYGSWGSRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGISSY 172
Cdd:cd19142 76 SYIVSTKIYWSY--GSEERGLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 173 SPEMTRRAAAILKDLGTPCLI-HQPSYSMLNR-WIEGGLLDALEETGIGCIAFSPLAQGMLTTKYLNGQPTDARAAKGGT 250
Cdd:cd19142 154 SPVEIMEAFSIARQFNCPTPIcEQSEYHMFCReKMELYMPELYNKVGVGLITWSPLSLGLDPGISEETRRLVTKLSFKSS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 251 LKAHFLSPENL--------ERVRALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDALK-NTAFTPEE 321
Cdd:cd19142 234 KYKVGSDGNGIheetrrasHKLRELSLIAERLGCDLTQLLIAWSLKNENVQCVLIGASSLEQLYSQLNSLQlLPKLNSAV 313
|
....*.
gi 1333942756 322 LAEIDR 327
Cdd:cd19142 314 MEELER 319
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
37-312 |
3.23e-50 |
|
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: 169.27 E-value: 3.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 37 NFGGTDVFETGRAVLRRAFDRGVTHFDLANNYG--PPPGSAEENFGRVLATDFKahRDELIVSTKAGYDMWPGPYGSWGS 114
Cdd:cd19082 9 DFGTRIDEEEAFALLDAFVELGGNFIDTARVYGdwVERGASERVIGEWLKSRGN--RDKVVIATKGGHPDLEDMSRSRLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 115 RKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGISSYSPEMTRRAAAILKDLGTPCL-I 193
Cdd:cd19082 87 PEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNWSTERIAEANAYAKAHGLPGFaA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 194 HQPSYSmLNRWIEGGLLDA------------LEETGIGCIAFSPLAQGMLTTKYLNGQPTDARAAKggtlkaHFLSPENL 261
Cdd:cd19082 167 SSPQWS-LARPNEPPWPGPtlvamdeemrawHEENQLPVFAYSSQARGFFSKRAAGGAEDDSELRR------VYYSEENF 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1333942756 262 ERVRALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDAL 312
Cdd:cd19082 240 ERLERAKELAEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAAA 290
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
28-327 |
6.50e-50 |
|
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: 168.89 E-value: 6.50e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 28 PAISLG--LWQNFGGTDVFETGRAVLRRAFDRGVTHFDLANNYgpPPGSAEENFGRVLATDFKahrdeLIVSTKAgyDMW 105
Cdd:cd19075 1 PKIILGtmTFGSQGRFTTAEAAAELLDAFLERGHTEIDTARVY--PDGTSEELLGELGLGERG-----FKIDTKA--NPG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 106 PGPygsWGSRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGISSYSPEMTRRAAAILK 185
Cdd:cd19075 72 VGG---GLSPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 186 DLG--TPClIHQPSYSMLNRWIEGGLLDALEETGIGCIAFSPLAQGMLTTKYLNGQPT------DARAAKGGTLKAHFLS 257
Cdd:cd19075 149 ENGwvLPT-VYQGMYNAITRQVETELFPCLRKLGIRFYAYSPLAGGFLTGKYKYSEDKagggrfDPNNALGKLYRDRYWK 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1333942756 258 PENLERVRALDAIATRRGQTLAQMAIAWVLRDprvtSAL---------VGARNVEQLDNSLDALKNTAFTPEELAEIDR 327
Cdd:cd19075 228 PSYFEALEKVEEAAEKEGISLAEAALRWLYHH----SALdgekgdgviLGASSLEQLEENLAALEKGPLPEEVVKAIDE 302
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
49-326 |
1.75e-48 |
|
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: 165.10 E-value: 1.75e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 49 AVLRRAFDRGVTHFDLANNYGPPPGSAEEnfgRVLATDFKAH---RDELIVSTKAGYDmwPGPYGSWGSRKYLTASLDQS 125
Cdd:cd19077 29 ETMKAALDAGSNLWNGGEFYGPPDPHANL---KLLARFFRKYpeyADKVVLSVKGGLD--PDTLRPDGSPEAVRKSIENI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 126 LKRMG-LDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGISSYSPEMTRRAAAIlkdlgTPCLIHQPSYSMLNRW 204
Cdd:cd19077 104 LRALGgTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAETIRRAHAV-----HPIAAVEVEYSLFSRE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 205 IE-GGLLDALEETGIGCIAFSPLAQGMLTtkylnGQPTDARAAKGGTLKAHF--LSPENLER----VRALDAIATRRGQT 277
Cdd:cd19077 179 IEeNGVLETCAELGIPIIAYSPLGRGLLT-----GRIKSLADIPEGDFRRHLdrFNGENFEKnlklVDALQELAEKKGCT 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1333942756 278 LAQMAIAWVLR--DPRVTsALVGARNVEQLDNSLDALkNTAFTPEELAEID 326
Cdd:cd19077 254 PAQLALAWILAqsGPKII-PIPGSTTLERVEENLKAA-NVELTDEELKEIN 302
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-312 |
1.86e-47 |
|
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: 160.83 E-value: 1.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 15 MTYRRSGRSGLDLPAISLGLwqnfGGTDVFETgrAVLRRAFDRGVTHFDLANNYGPppGSAEENFGRVLATdfkAHRDEL 94
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFGG----GGLPRESP--ELLRRALDLGINYFDTAEGYGN--GNSEEIIGEALKG---LRRDKV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 95 IVSTKAGydmwpgPYGSWGSRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPL---EETMGALDHAVRQGKALYVGIS- 170
Cdd:cd19105 70 FLATKAS------PRLDKKDKAELLKSVEESLKRLQTDYIDIYQLHGVDTPEERllnEELLEALEKLKKEGKVRFIGFSt 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 171 -SYSPEMTRRAAailkDLGtpcLIH--QPSYSMLNR-WIEGGLLDALEETGIGCIAFSPLAQGMLttkylngqptdaraa 246
Cdd:cd19105 144 hDNMAEVLQAAI----ESG---WFDviMVAYNFLNQpAELEEALAAAAEKGIGVVAMKTLAGGYL--------------- 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333942756 247 kggtlkahflspenlerVRALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDAL 312
Cdd:cd19105 202 -----------------QPALLSVLKAKGFSLPQAALKWVLSNPRVDTVVPGMRNFAELEENLAAA 250
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
21-325 |
2.48e-47 |
|
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: 162.22 E-value: 2.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 21 GRSGLDLPAISLG---LWQNFGGTDVFETGRAVLRRAFDRGVTHFDLANNYGPppGSAEENFGRVLAtdfKAHRDELIVS 97
Cdd:cd19145 6 GSQGLEVSAQGLGcmgLSGDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYGP--NTNEVLLGKALK---DGPREKVQLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 98 TKAGYdMWPGPYGSW--GSRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGISSYSPE 175
Cdd:cd19145 81 TKFGI-HEIGGSGVEvrGDPAYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSEASAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 176 MTRRAAAIlkdlgTPCLIHQPSYSMLNRWIEGGLLDALEETGIGCIAFSPLAQGmlttkYLNGQPTDARAAKGGTLKAHF 255
Cdd:cd19145 160 TIRRAHAV-----HPITAVQLEWSLWTRDIEEEIIPTCRELGIGIVPYSPLGRG-----FFAGKAKLEELLENSDVRKSH 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333942756 256 --LSPENLERVRAL----DAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDALKnTAFTPEELAEI 325
Cdd:cd19145 230 prFQGENLEKNKVLyervEALAKKKGCTPAQLALAWVLHQGEDVVPIPGTTKIKNLNQNIGALS-VKLTKEDLKEI 304
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
28-311 |
7.04e-46 |
|
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: 156.63 E-value: 7.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 28 PAISLGLWQNFGGTDVFETGRA--VLRRAFDRGVTHFDLANNYGpppgSAEENFGRVLATdfkAHRDELIVSTKAGY-DM 104
Cdd:cd19095 1 SVLGLGTSGIGRVWGVPSEAEAarLLNTALDLGINLIDTAPAYG----RSEERLGRALAG---LRRDDLFIATKVGThGE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 105 WPGPYGSWgSRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGISSYSPEmtrrAAAIL 184
Cdd:cd19095 74 GGRDRKDF-SPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVSGDGEE----LEAAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 185 KDLGTPCLihQPSYSMLNRWIEgGLLDALEETGIGCIAFSPLAQGMLTtkylngqptdaraakggtlKAHFLSPENLERV 264
Cdd:cd19095 149 ASGVFDVV--QLPYNVLDREEE-ELLPLAAEAGLGVIVNRPLANGRLR-------------------RRVRRRPLYADYA 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1333942756 265 RALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDA 311
Cdd:cd19095 207 RRPEFAAEIGGATWAQAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
27-312 |
7.66e-46 |
|
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: 156.61 E-value: 7.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 27 LPAISLGLWQnFGGTDVF------ETGRAVLRRAFDRGVTHFDLANNYGPppGSAEENFGRVLatdfKAHRDELIVSTKA 100
Cdd:cd19088 1 VSRLGYGAMR-LTGPGIWgppadrEEAIAVLRRALELGVNFIDTADSYGP--DVNERLIAEAL----HPYPDDVVIATKG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 101 GYdMWPGPyGSW---GSRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGISSYSPEMT 177
Cdd:cd19088 74 GL-VRTGP-GWWgpdGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 178 RRAAAIlkdlgTPCLIHQPSYSMLNRWIEgGLLDALEETGIGCIAFSPLAqgmlttkylngqptdaraakGGTLkahfls 257
Cdd:cd19088 152 EEARAI-----VRIVSVQNRYNLANRDDE-GVLDYCEAAGIAFIPWFPLG--------------------GGDL------ 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1333942756 258 penLERVRALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDAL 312
Cdd:cd19088 200 ---AQPGGLLAEVAARLGATPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAAA 251
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
28-313 |
9.01e-46 |
|
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: 157.33 E-value: 9.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 28 PAISLG---LWQNFGGTDvFETGRAVLRRAFDRGVTHFDLANNYGPppgsAEENFGRVLAtdfKAHRDELIVSTKAGYDM 104
Cdd:cd19090 1 SALGLGtagLGGVFGGVD-DDEAVATIRAALDLGINYIDTAPAYGD----SEERLGLALA---ELPREPLVLSTKVGRLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 105 -WPGPYgswgSRKYLTASLDQSLKRMGLDYVDIFYSHrvDP-RTPLEETMG------ALDHAVRQGKALYVGISSYSPEM 176
Cdd:cd19090 73 eDTADY----SADRVRRSVEESLERLGRDRIDLLMIH--DPeRVPWVDILApggaleALLELKEEGLIKHIGLGGGPPDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 177 TRRAaaILKDLGTPCLIHQpSYSMLNRWIEGGLLDALEETGIGCIAFSPLAQGMLTTKYLNGQPTDARaakggtlkahFL 256
Cdd:cd19090 147 LRRA--IETGDFDVVLTAN-RYTLLDQSAADELLPAAARHGVGVINASPLGMGLLAGRPPERVRYTYR----------WL 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1333942756 257 SPENLERVRALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDALK 313
Cdd:cd19090 214 SPELLDRAKRLYELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAAE 270
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
23-315 |
1.02e-43 |
|
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: 151.94 E-value: 1.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 23 SGLDLPAISLGLWqnfGGTDVFETGRAVLRR---AFDRGVTHFDLANNYGPppGSAEENFGRVLATDfKAHRDELIVSTK 99
Cdd:cd19092 2 EGLEVSRLVLGCM---RLADWGESAEELLSLieaALELGITTFDHADIYGG--GKCEELFGEALALN-PGLREKIEIQTK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 100 AG-------YDMWPGPYGSwgSRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGISSY 172
Cdd:cd19092 76 CGirlgddpRPGRIKHYDT--SKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 173 SP---EMTRRAaailkdLGTPCLIHQPSYSMLNR-WIEGGLLDALEETGIGCIAFSPLAQGMLTTKYLngqptdaraakg 248
Cdd:cd19092 154 TPsqiELLQSY------LDQPLVTNQIELSLLHTeAIDDGTLDYCQLLDITPMAWSPLGGGRLFGGFD------------ 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333942756 249 gtlkahflspENLERVRA-LDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDALKNT 315
Cdd:cd19092 216 ----------ERFQRLRAaLEELAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALDIE 273
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
15-327 |
3.04e-43 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 153.05 E-value: 3.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 15 MTYRRSGRSGLDLPAISLGLWqNFGGTDvFETGRAVLRRAFDRGVTHFDLANNYGpppGSaEENFGRVLatdfKAHRDEL 94
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGM-RLPRKD-EEEAEALIRRAIDNGINYIDTARGYG---DS-EEFLGKAL----KGPRDKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 95 IVSTKAGydmwpgpygSW-GSRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETM---GALDH---AVRQGKALYV 167
Cdd:COG1453 71 ILATKLP---------PWvRDPEDMRKDLEESLKRLQTDYIDLYLIHGLNTEEDLEKVLkpgGALEAlekAKAEGKIRHI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 168 GISSYSPemtrrAAAILKDLGTP----CLIHqpsYSMLNRWIEGG--LLDALEETGIGCIAFSPLAQGMLTTKylngqpt 241
Cdd:COG1453 142 GFSTHGS-----LEVIKEAIDTGdfdfVQLQ---YNYLDQDNQAGeeALEAAAEKGIGVIIMKPLKGGRLANP------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 242 daraakggtlkahflsPENLERVraldaiaTRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDALKNT-AFTPE 320
Cdd:COG1453 207 ----------------PEKLVEL-------LCPPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENLKTADNLePLTEE 263
|
....*..
gi 1333942756 321 ELAEIDR 327
Cdd:COG1453 264 ELAILER 270
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
28-312 |
4.86e-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: 150.56 E-value: 4.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 28 PAISLGLwQNFGGTDVFETGRAVLRRAFDRGVTHFDLANNY-----GPPPGSAEENFGRVLATdfKAHRDELIVSTKAGY 102
Cdd:cd19752 1 SELCLGT-MYFGTRTDEETSFAILDRYVAAGGNFLDTANNYafwteGGVGGESERLIGRWLKD--RGNRDDVVIATKVGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 103 dMWPGPYGSWGSRKYLTAS-----LDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGISSYSPEMT 177
Cdd:cd19752 78 -GPRDPDGGPESPEGLSAEtieqeIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 178 RRAAAILKDLGTP---CLIHQPSYSMLNRWIEGG--------LLDALEETG-IGCIAFSPLaqgmlttkyLNGQPTDARA 245
Cdd:cd19752 157 ERARQIARQQGWAefsAIQQRHSYLRPRPGADFGvqrivtdeLLDYASSRPdLTLLAYSPL---------LSGAYTRPDR 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1333942756 246 AkggtLKAHFLSPENLERVRALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDAL 312
Cdd:cd19752 228 P----LPEQYDGPDSDARLAVLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAAL 290
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
24-327 |
3.21e-42 |
|
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: 148.61 E-value: 3.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 24 GLDLPAISLGLWQ----NFGGTDVfETGRAVLRRAFDRGVTHFDLANNYGPppGSAEENFGRVLATdfKAHRDELIVSTK 99
Cdd:cd19148 1 DLPVSRIALGTWAiggwMWGGTDE-KEAIETIHKALDLGINLIDTAPVYGF--GLSEEIVGKALKE--YGKRDRVVIATK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 100 AGYDmWP--GPYGSWGSRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGISSYSPE-M 176
Cdd:cd19148 76 VGLE-WDegGEVVRNSSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSPEqM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 177 TR-RAAAilkdlgtPCLIHQPSYSMLNRWIEGGLLDALEETGIGCIAFSPLAQGMLTtkylnGQPTDARAAKGGTLKAH- 254
Cdd:cd19148 155 ETfRKVA-------PLHTVQPPYNLFEREIEKDVLPYARKHNIVTLAYGALCRGLLS-----GKMTKDTKFEGDDLRRTd 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1333942756 255 --FLSP---ENLERVRALDAIATRR-GQTLAQMAIAWVLRDPRVTSALVGARNVEQLDnSLDALKNTAFTPEELAEIDR 327
Cdd:cd19148 223 pkFQEPrfsQYLAAVEELDKLAQERyGKSVIHLAVRWLLDQPGVSIALWGARKPEQLD-AVDEVFGWSLNDEDMKEIDA 300
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-327 |
8.84e-42 |
|
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: 148.18 E-value: 8.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 17 YRRSGRSGLDLPAISLG------LWqnfgGTDVFETGRAVLRRAFDRGVTHFDLANNYGPppGSAEENFGRVLATDfkah 90
Cdd:cd19104 2 YRRFGRTGLKVSELTFGgggiggLM----GRTTREEQIAAVRRALDLGINFFDTAPSYGD--GKSEENLGRALKGL---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 91 RDELIVSTKAGYDmwPGPYGSWGSRkyLTASLDQSLKRMGLDYVDIFYSH-RVDPRTP--------------LEETMGAL 155
Cdd:cd19104 72 PAGPYITTKVRLD--PDDLGDIGGQ--IERSVEKSLKRLKRDSVDLLQLHnRIGDERDkpvggtlsttdvlgLGGVADAF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 156 DHAVRQGKALYVGISSYS-PEMTRRAaailkdLGTPCL-IHQPSYSMLNRW------------IEGGLLDALEETGIGCI 221
Cdd:cd19104 148 ERLRSEGKIRFIGITGLGnPPAIREL------LDSGKFdAVQVYYNLLNPSaaearprgwsaqDYGGIIDAAAEHGVGVM 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 222 AFSPLAQGMLTTkylngqptDARAAKGGTLKAHFLSPENLERVRALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARN 301
Cdd:cd19104 222 GIRVLAAGALTT--------SLDRGREAPPTSDSDVAIDFRRAAAFRALAREWGETLAQLAHRFALSNPGVSTVLVGVKN 293
|
330 340
....*....|....*....|....*.
gi 1333942756 302 VEQLDNSLDALKNTAFTPEELAEIDR 327
Cdd:cd19104 294 REELEEAVAAEAAGPLPAENLARLEA 319
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
15-323 |
2.60e-41 |
|
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: 146.16 E-value: 2.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 15 MTYRRSGRSGLDLPAISLG---LWQNFGGTDVFEtGRAVLRRAFDRGVTHFDLANNYGPppGSAEENFGRVLaTDFKahR 91
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGaspLGGVFGPVDEEE-AIRTVHEALDSGINYIDTAPWYGQ--GRSETVLGKAL-KGIP--R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 92 DELIVSTKAG-YDmwPGPYGSWG-SRKYLTASLDQSLKRMGLDYVDIFYSHRVD--PRTP--LEETMGALDHAVRQGKAL 165
Cdd:cd19163 75 DSYYLATKVGrYG--LDPDKMFDfSAERITKSVEESLKRLGLDYIDIIQVHDIEfaPSLDqiLNETLPALQKLKEEGKVR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 166 YVGISSYSPEMTRRAA--------AILkdlgTPCliHqpsYSMLNRWIEgGLLDALEETGIGCIAFSPLAQGMLTTKyln 237
Cdd:cd19163 153 FIGITGYPLDVLKEVLerspvkidTVL----SYC--H---YTLNDTSLL-ELLPFFKEKGVGVINASPLSMGLLTER--- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 238 gqptdaraakgGTLKAHFLSPENLERVRALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDALKnTAF 317
Cdd:cd19163 220 -----------GPPDWHPASPEIKEACAKAAAYCKSRGVDISKLALQFALSNPDIATTLVGTASPENLRKNLEAAE-EPL 287
|
....*.
gi 1333942756 318 TPEELA 323
Cdd:cd19163 288 DAHLLA 293
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
47-313 |
2.56e-39 |
|
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: 140.57 E-value: 2.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 47 GRAVLRRAFDRGVTHFDLANNYGPppGSAEENFGRVLATdfkAHRDELIVSTKAGYDMWPGPYGSWG--------SRKYL 118
Cdd:cd19162 21 AAATLDAAWDAGIRYFDTAPLYGL--GLSERRLGAALAR---HPRAEYVVSTKVGRLLEPGAAGRPAgadrrfdfSADGI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 119 TASLDQSLKRMGLDYVDIFYSHRVDPR--TPLEETMGALDHAVRQGKALYVGISSYSPEMTRRAAAilkDLGTPCLIHQP 196
Cdd:cd19162 96 RRSIEASLERLGLDRLDLVFLHDPDRHllQALTDAFPALEELRAEGVVGAIGVGVTDWAALLRAAR---RADVDVVMVAG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 197 SYSMLNRWIEGGLLDALEETGIGCIAFSPLAQGMLTTkylnGQPTDARAAKGGtlkahfLSPENLERVRALDAIATRRGQ 276
Cdd:cd19162 173 RYTLLDRRAATELLPLCAAKGVAVVAAGVFNSGILAT----DDPAGDRYDYRP------ATPEVLARARRLAAVCRRYGV 242
|
250 260 270
....*....|....*....|....*....|....*..
gi 1333942756 277 TLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDALK 313
Cdd:cd19162 243 PLPAAALQFPLRHPAVASVVVGAASPAELRDNLALLR 279
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
15-326 |
5.75e-39 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 141.14 E-value: 5.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 15 MTYRRSGRSGLDLPAISLGLwQNFGGTDVFETGRAVLRRAFDRGVTHFDLANNYGPPP-----GSAEENFGRVLATdfKA 89
Cdd:PRK10625 1 MQYHRIPHSSLEVSTLGLGT-MTFGEQNSEADAHAQLDYAVAQGINLIDVAEMYPVPPrpetqGLTETYIGNWLAK--RG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 90 HRDELIVSTKA-----GYDMWPGPYGSWgSRKYLTASLDQSLKRMGLDYVDIFYSH-----------------RVDPRTP 147
Cdd:PRK10625 78 SREKLIIASKVsgpsrNNDKGIRPNQAL-DRKNIREALHDSLKRLQTDYLDLYQVHwpqrptncfgklgyswtDSAPAVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 148 LEETMGALDHAVRQGKALYVGISSYSP--EMTRRAAAILKDLGTPCLIHQPsYSMLNRWIEGGLLDALEETGIGCIAFSP 225
Cdd:PRK10625 157 LLETLDALAEQQRAGKIRYIGVSNETAfgVMRYLHLAEKHDLPRIVTIQNP-YSLLNRSFEVGLAEVSQYEGVELLAYSC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 226 LAQGMLTTKYLNG-QPTDARaakgGTLKAHFL---SPENLERVRALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARN 301
Cdd:PRK10625 236 LAFGTLTGKYLNGaKPAGAR----NTLFSRFTrysGEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLLGATT 311
|
330 340
....*....|....*....|....*
gi 1333942756 302 VEQLDNSLDALkNTAFTPEELAEID 326
Cdd:PRK10625 312 MEQLKTNIESL-HLTLSEEVLAEIE 335
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
23-326 |
2.51e-38 |
|
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: 137.38 E-value: 2.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 23 SGLDLPAISLGLWQNFGGTDVFETGRAVLRRAFDRGVTHFDLANNYGPppGSAEENFGRVLATDfkahRDELIVSTKagy 102
Cdd:cd19138 7 DGTKVPALGQGTWYMGEDPAKRAQEIEALRAGIDLGMTLIDTAEMYGD--GGSEELVGEAIRGR----RDKVFLVSK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 103 dMWPgpygSWGSRKYLTASLDQSLKRMGLDYVDIFYSH-RvdPRTPLEETMGALDHAVRQGKALYVGISSYSPEMTRRAA 181
Cdd:cd19138 78 -VLP----SNASRQGTVRACERSLRRLGTDYLDLYLLHwR--GGVPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELW 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 182 AILKdlGTPCLIHQPSYSMLNRWIEGGLLDALEETGIGCIAFSPLAQGmlttkylngqptdaraakgGTLKAHFLSPEnl 261
Cdd:cd19138 151 AVPG--GGNCAANQVLYNLGSRGIEYDLLPWCREHGVPVMAYSPLAQG-------------------GLLRRGLLENP-- 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333942756 262 ervrALDAIATRRGQTLAQMAIAWVLRDPRVTsALVGARNVEQLDNSLDALkNTAFTPEELAEID 326
Cdd:cd19138 208 ----TLKEIAARHGATPAQVALAWVLRDGNVI-AIPKSGSPEHARENAAAA-DLELTEEDLAELD 266
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-306 |
3.35e-38 |
|
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: 136.07 E-value: 3.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 17 YRRSGRSGLDLPAISLGLWQNFGGTDvfETGRAVLRRAFDRGVTHFDLANNYgpppGSAEENFGRVLatdfKAHRDELIV 96
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPLGRLSQ--EEAAAIIRRALDLGINYFDTAPSY----GDSEEKIGKAL----KGRRDKVFL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 97 STKAgydmwpgpygswGSRKYLTA--SLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMG------ALDHAVRQGKALYVG 168
Cdd:cd19100 71 ATKT------------GARDYEGAkrDLERSLKRLGTDYIDLYQLHAVDTEEDLDQVFGpggaleALLEAKEEGKIRFIG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 169 ISSYSPEMTRRAAAILkdlgtPCLIHQPSYSMLNRWIEG---GLLDALEETGIGCIAFSPLAQGMLttkyLNGQPTDARA 245
Cdd:cd19100 139 ISGHSPEVLLRALETG-----EFDVVLFPINPAGDHIDSfreELLPLAREKGVGVIAMKVLAGGRL----LSGDPLDPEQ 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333942756 246 akggtlkahflspenlervraldaiatrrgqtlaqmAIAWVLRDPRVTSALVGARNVEQLD 306
Cdd:cd19100 210 ------------------------------------ALRYALSLPPVDVVIVGMDSPEELD 234
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
24-326 |
2.40e-36 |
|
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: 131.92 E-value: 2.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 24 GLDLPAISLGLWqNFGGTDVFETGR-----AVLRRAFDRGVTHFDLANNYGPppGSAEENFGRVLaTDFKahRDELIVST 98
Cdd:cd19137 1 GEKIPALGLGTW-GIGGFLTPDYSRdeemvELLKTAIELGYTHIDTAEMYGG--GHTEELVGKAI-KDFP--REDLFIVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 99 KagydMWPGPYgswgSRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGISSYSPEMTR 178
Cdd:cd19137 75 K----VWPTNL----RYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 179 RAAAILKdlgTPCLIHQPSYSMLNR-WIEGGLLDALEETGIGCIAFSPLAQGMLTTKylngqptdaraakggtlkahfls 257
Cdd:cd19137 147 EAISKSQ---TPIVCNQVKYNLEDRdPERDGLLEYCQKNGITVVAYSPLRRGLEKTN----------------------- 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1333942756 258 penlervRALDAIATRRGQTLAQMAIAWVLRDPRVTsALVGARNVEQLDNSLDALkNTAFTPEELAEID 326
Cdd:cd19137 201 -------RTLEEIAKNYGKTIAQIALAWLIQKPNVV-AIPKAGRVEHLKENLKAT-EIKLSEEEMKLLD 260
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
22-327 |
3.61e-36 |
|
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: 131.23 E-value: 3.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 22 RSGLDLPAISLGLWQNFGgtdvfETGRAVLRRAFDRGVTHFDLANNYGpppgsAEENFGRVLAtDFKAHRDELIVSTKag 101
Cdd:cd19140 3 VNGVRIPALGLGTYPLTG-----EECTRAVEHALELGYRHIDTAQMYG-----NEAQVGEAIA-ASGVPRDELFLTTK-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 102 ydMWPGPYgswgSRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGISSYSPEMTRRAA 181
Cdd:cd19140 70 --VWPDNY----SPDDFLASVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 182 AIlkdLGTPCLIHQPSYS-MLNrwiEGGLLDALEETGIGCIAFSPLAQGMLTTKYLngqptdaraakggtlkahflspen 260
Cdd:cd19140 144 EL---SEAPLFTNQVEYHpYLD---QRKLLDAAREHGIALTAYSPLARGEVLKDPV------------------------ 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1333942756 261 lervraLDAIATRRGQTLAQMAIAWVLRDPRVtSALVGARNVEQLDNSLDALkNTAFTPEELAEIDR 327
Cdd:cd19140 194 ------LQEIGRKHGKTPAQVALRWLLQQEGV-AAIPKATNPERLEENLDIF-DFTLSDEEMARIAA 252
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
23-326 |
1.30e-35 |
|
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: 131.78 E-value: 1.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 23 SGLDLPAISLG-LWQNFGGTDVFETGRAVLRRAFDRGVTHFDLANNYgpPPGSAEENFGRVLATdfKAHRDELIVSTK-- 99
Cdd:cd19146 12 SPLCLGAMSFGeAWKSMMGECDKETAFKLLDAFYEQGGNFIDTANNY--QGEESERWVGEWMAS--RGNRDEMVLATKyt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 100 AGYDMW-PGP----YGSwGSRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGISSYSP 174
Cdd:cd19146 88 TGYRRGgPIKiksnYQG-NHAKSLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSDTPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 175 EMTRRAAAILKDLG-TPCLIHQPSYSMLNRWIEGGLLDALEETGIGCIAFSPLAQGMLTTKylngqptDARAAKGGTLKA 253
Cdd:cd19146 167 WVVSKANAYARAHGlTQFVVYQGHWSAAFRDFERDILPMCEAEGMALAPWGVLGQGQFRTE-------EEFKRRGRSGRK 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333942756 254 HFLSPENLERV-RALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDALKnTAFTPEELAEID 326
Cdd:cd19146 240 GGPQTEKERKVsEKLEKVAEEKGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIEALG-ISLSDEEIQEIE 312
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
27-329 |
7.94e-35 |
|
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: 128.99 E-value: 7.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 27 LPAISLGLWQ----NFGGTDVF------ETGRAVLRRAFDRGVTHFDLANNYGPppGSAEENFGRVLaTDFKahRDELIV 96
Cdd:cd19103 4 LPKIALGTWSwgsgGAGGDQVFgnhldeDTLKAVFDKAMAAGLNLWDTAAVYGM--GASEKILGEFL-KRYP--REDYII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 97 STKAGydmwpgPYGSWGSRKYLTASLDQSLKRMGLDYVDIFYSHR---VDPRTPleetmgALDHAVRQGKALYVGISSYS 173
Cdd:cd19103 79 STKFT------PQIAGQSADPVADMLEGSLARLGTDYIDIYWIHNpadVERWTP------ELIPLLKSGKVKHVGVSNHN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 174 PEMTRRAAAILKDLGTPCLIHQPSYSMLNR-WIEGGLLDALEETGIGCIAFSPLAQGMLTTKYLNGQPTDARAAKGGTLK 252
Cdd:cd19103 147 LAEIKRANEILAKAGVSLSAVQNHYSLLYRsSEEAGILDYCKENGITFFAYMVLEQGALSGKYDTKHPLPEGSGRAETYN 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1333942756 253 AHFLSPENLerVRALDAIATRRGQTLAQMAIAWVLrdPRVTSALVGARNVEQLDNSLDALKNTaFTPEELAEIDRHA 329
Cdd:cd19103 227 PLLPQLEEL--TAVMAEIGAKHGASIAQVAIAWAI--AKGTTPIIGVTKPHHVEDAARAASIT-LTDDEIKELEQLA 298
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
33-326 |
1.12e-34 |
|
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: 128.87 E-value: 1.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 33 GLWQ---NFGGTDVFETGRAVLRRAFDRGVTHFDLANNYGPppgsAEENFGRVLAT--DFKAHRDELIVSTKAGYDmwPG 107
Cdd:cd19101 8 GMWQlsgGHGGIRDEDAAVRAMAAYVDAGLTTFDCADIYGP----AEELIGEFRKRlrRERDAADDVQIHTKWVPD--PG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 108 PYGSwgSRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTP-LEETMGALDHAVRQGKALYVGISSYSPEMTRRAAailkD 186
Cdd:cd19101 82 ELTM--TRAYVEAAIDRSLKRLGVDRLDLVQFHWWDYSDPgYLDAAKHLAELQEEGKIRHLGLTNFDTERLREIL----D 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 187 LGTPCLIHQPSYSMLNRWIEGGLLDALEETGIGCIAFSPLAQGMLTTKYLnGQP-------TDARAAKGGTLKAHFLSPE 259
Cdd:cd19101 156 AGVPIVSNQVQYSLLDRRPENGMAALCEDHGIKLLAYGTLAGGLLSEKYL-GVPeptgpalETRSLQKYKLMIDEWGGWD 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333942756 260 NLERV-RALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDALKnTAFTPEELAEID 326
Cdd:cd19101 235 LFQELlRTLKAIADKHGVSIANVAVRWVLDQPGVAGVIVGARNSEHIDDNVRAFS-FRLDDEDRAAID 301
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
23-327 |
2.63e-34 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 126.71 E-value: 2.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 23 SGLDLPAISLGLWQNFGgtdvfETGRAVLRRAFDRGVTHFDLANNYGpppgsAEENFGRVLAtDFKAHRDELIVSTKagy 102
Cdd:COG0656 1 NGVEIPALGLGTWQLPG-----EEAAAAVRTALEAGYRHIDTAAMYG-----NEEGVGEAIA-ASGVPREELFVTTK--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 103 dMWPGPYGswgsRKYLTASLDQSLKRMGLDYVDIFYSHRvdP-RTPLEETMGALDHAVRQGKALYVGISSYSPEMTRRaa 181
Cdd:COG0656 67 -VWNDNHG----YDDTLAAFEESLERLGLDYLDLYLIHW--PgPGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEE-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 182 aILKDLGTPCLIHQPSYSMLNRwiEGGLLDALEETGIGCIAFSPLAQGMLTTkylngQPTdaraakggtlkahflspenl 261
Cdd:COG0656 138 -LLAETGVKPAVNQVELHPYLQ--QRELLAFCREHGIVVEAYSPLGRGKLLD-----DPV-------------------- 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333942756 262 ervraLDAIATRRGQTLAQMAIAWVLRdpRVTSALVGARNVEQLDNSLDALkNTAFTPEELAEIDR 327
Cdd:COG0656 190 -----LAEIAEKHGKTPAQVVLRWHLQ--RGVVVIPKSVTPERIRENLDAF-DFELSDEDMAAIDA 247
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
27-326 |
5.75e-31 |
|
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: 117.37 E-value: 5.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 27 LPAISLGLWQNFGgtdvfETGRAVLRRAFDRGVTHFDLANNYGpppgsAEENFGRVLAtDFKAHRDELIVSTKAGYDMWp 106
Cdd:cd19073 1 IPALGLGTWQLRG-----DDCANAVKEALELGYRHIDTAEIYN-----NEAEVGEAIA-ESGVPREDLFITTKVWRDHL- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 107 gpygswgSRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGISSYSPEMTRRAAAIlkd 186
Cdd:cd19073 69 -------RPEDLKKSVDRSLEKLGTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDI--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 187 LGTPCLIHQPSYS-MLNRWiegGLLDALEETGIGCIAFSPLAQGmlttkylngqptdaraakggtlkahflspeNLERVR 265
Cdd:cd19073 139 SPLPIAVNQVEFHpFLYQA---ELLEYCRENDIVITAYSPLARG------------------------------EVLRDP 185
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333942756 266 ALDAIATRRGQTLAQMAIAWVLRdpRVTSALVGARNVEQLDNSLDALkNTAFTPEELAEID 326
Cdd:cd19073 186 VIQEIAEKYDKTPAQVALRWLVQ--KGIVVIPKASSEDHLKENLAIF-DWELTSEDVAKID 243
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
48-310 |
4.02e-30 |
|
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: 117.03 E-value: 4.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 48 RAVLRRAFDRGVTHFDLANNYGPppGSAEENFGRVLATDFKAH---RDELIVSTKAGY--DMWPGPYGSWGSR------- 115
Cdd:cd19099 24 REALKAALDSGINVIDTAINYRG--GRSERLIGKALRELIEKGgikRDEVVIVTKAGYipGDGDEPLRPLKYLeeklgrg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 116 ----------------KYLTASLDQSLKRMGLDYVDIFYSH----------RVDPRTPLEETMGALDHAVRQGKALYVGI 169
Cdd:cd19099 102 lidvadsaglrhcispAYLEDQIERSLKRLGLDTIDLYLLHnpeeqllelgEEEFYDRLEEAFEALEEAVAEGKIRYYGI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 170 SSYSP-----------EMTRRAAAILKDLG---------TPCLIHQPsYSMLNRWIEGG----LLDALEETGIGCIAFSP 225
Cdd:cd19099 182 STWDGfrappalpghlSLEKLVAAAEEVGGdnhhfkviqLPLNLLEP-EALTEKNTVKGealsLLEAAKELGLGVIASRP 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 226 LAQGMLttkylngqptdaraakggtlkahflspenLERVRALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQL 305
Cdd:cd19099 261 LNQGQL-----------------------------LGELRLADLLALPGGATLAQRALQFARSTPGVDSALVGMRRPEHV 311
|
....*
gi 1333942756 306 DNSLD 310
Cdd:cd19099 312 DENLA 316
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
45-314 |
1.56e-26 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 106.07 E-value: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 45 ETGRAVLRRAFDRGVTHFDLANNYGpppgSAEENFGRVLATDFKAHrdeliVSTKAGydmwPGPYGSWGSRKYLTASLDQ 124
Cdd:cd19097 26 KEAKKILEYALKAGINTLDTAPAYG----DSEKVLGKFLKRLDKFK-----IITKLP----PLKEDKKEDEAAIEASVEA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 125 SLKRMGLDYVDIFYSHRVD----PRTPLEEtmgALDHAVRQGKALYVGISSYSPEMTRRAAAILKdlgtpCLIHQPSYSM 200
Cdd:cd19097 93 SLKRLKVDSLDGLLLHNPDdllkHGGKLVE---ALLELKKEGLIRKIGVSVYSPEELEKALESFK-----IDIIQLPFNI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 201 LN-RWIEGGLLDALEETGIGCIAFSPLAQGMLTTKYLNgqptdaraakggtLKAHFlsPENLERVRALDAIATRRGQTLA 279
Cdd:cd19097 165 LDqRFLKSGLLAKLKKKGIEIHARSVFLQGLLLMEPDK-------------LPAKF--APAKPLLKKLHELAKKLGLSPL 229
|
250 260 270
....*....|....*....|....*....|....*
gi 1333942756 280 QMAIAWVLRDPRVTSALVGARNVEQLDNSLDALKN 314
Cdd:cd19097 230 ELALGFVLSLPEIDKIVVGVDSLEQLKEIIAAFKK 264
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
28-319 |
1.59e-26 |
|
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: 105.72 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 28 PAISLG---LWQNFGGTDVFETGRAVLRRAFDRGVTHFDLANNYGPppGSAEENFGRVLAtdfKAHRDELIVSTKagydm 104
Cdd:cd19096 1 SVLGFGtmrLPESDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGG--GKSEEILGEALK---EGPREKFYLATK----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 105 wpGPYGSWGSRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEET-----MGALDHAVRQGKALYVGISSYSPemtrr 179
Cdd:cd19096 71 --LPPWSVKSAEDFRRILEESLKRLGVDYIDFYLLHGLNSPEWLEKArkgglLEFLEKAKKEGLIRHIGFSFHDS----- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 180 AAAILKDLGTP----CLIHqpsYSMLNRWIEGG--LLDALEETGIGCIAFSPLAQGMLTTKylngqPTDARAakggtlka 253
Cdd:cd19096 144 PELLKEILDSYdfdfVQLQ---YNYLDQENQAGrpGIEYAAKKGMGVIIMEPLKGGGLANN-----PPEALA-------- 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333942756 254 hflspenlervraldaIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDALKNtaFTP 319
Cdd:cd19096 208 ----------------ILCGAPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENIAAADE--FEP 255
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
17-311 |
1.76e-26 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 106.79 E-value: 1.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 17 YRRSGRSGLDLPAISLG---LWQNFGgtDVFE-TGRAVLRRAFDRGVTHFDLANNYGPPpgSAEENFGRVLATdFKAHRD 92
Cdd:PLN02587 1 LRELGSTGLKVSSVGFGaspLGSVFG--PVSEeDAIASVREAFRLGINFFDTSPYYGGT--LSEKVLGKALKA-LGIPRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 93 ELIVSTKAGYdmwpgpYGSwG---SRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRT---PLEETMGALDHAVRQGKALY 166
Cdd:PLN02587 76 KYVVSTKCGR------YGE-GfdfSAERVTKSVDESLARLQLDYVDILHCHDIEFGSldqIVNETIPALQKLKESGKVRF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 167 VGISSYSPEMTR----RAAAilkdlGTPCLIHQPSYSMLNRWIEGGLLDALEETGIGCIAFSPLAQGMLTTkylNGQPtd 242
Cdd:PLN02587 149 IGITGLPLAIFTyvldRVPP-----GTVDVILSYCHYSLNDSSLEDLLPYLKSKGVGVISASPLAMGLLTE---NGPP-- 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1333942756 243 araakggtlKAHFLSPENLERVRALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDA 311
Cdd:PLN02587 219 ---------EWHPAPPELKSACAAAATHCKEKGKNISKLALQYSLSNKDISTTLVGMNSVQQVEENVAA 278
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
23-326 |
2.96e-25 |
|
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: 103.75 E-value: 2.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 23 SGLDLPAISLG-LWQNFGGTDVFETGRAVLRRAFDRGVTHFDLANNYGPPpgSAEENFGRVLATdfKAHRDELIVSTKAG 101
Cdd:cd19147 11 SPLILGAMSIGdAWSGFMGSMDKEQAFELLDAFYEAGGNFIDTANNYQDE--QSETWIGEWMKS--RKNRDQIVIATKFT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 102 YDMWPGPYGS------WG-SRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVRQGKALYVGISSYSP 174
Cdd:cd19147 87 TDYKAYEVGKgkavnyCGnHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDTPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 175 EMTRRAAAILKDLG-TPCLIHQPSYSMLNRWIEGGLLDALEETGIGCIAFSPLAQGMLTTKylngQPTDARAAKGGTLKA 253
Cdd:cd19147 167 WVVSAANYYATAHGkTPFSVYQGRWNVLNRDFERDIIPMARHFGMALAPWDVLGGGKFQSK----KAVEERKKNGEGLRS 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333942756 254 HFL----SPENLERVRALDAIATRRG-QTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDALkNTAFTPEELAEID 326
Cdd:cd19147 243 FVGgteqTPEEVKISEALEKVAEEHGtESVTAIALAYVRSKAPNVFPLVGGRKIEHLKDNIEAL-SIKLTPEEIEYLE 319
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
45-322 |
1.32e-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: 101.63 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 45 ETGRAVLRRAFDRGVTHFDLANNYGPppGSAEENFGRVLAtdfKAHRDELIVSTKAGYDMWPGPYGS------WG----- 113
Cdd:cd19161 20 ADADATLDAAWDSGIRYFDTAPMYGH--GLAEHRLGDFLR---EKPRDEFVLSTKVGRLLKPAREGSvpdpngFVdplpf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 114 ------SRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEE--------TMG----ALDHAVRQGKALYVGISSYSPE 175
Cdd:cd19161 95 eivydySYDGIMRSFEDSLQRLGLNRIDILYVHDIGVYTHGDRkerhhfaqLMSggfkALEELKKAGVIKAFGLGVNEVQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 176 MTRRAaaiLKDLGTPCLIHQPSYSMLNRWIEGGLLDALEETGIGCIAFSPLAQGMLTTKYLNGQPTDARAAkggtlkahf 255
Cdd:cd19161 175 ICLEA---LDEADLDCFLLAGRYSLLDQSAEEEFLPRCEQRGTSLVIGGVFNSGILATGTKSGAKFNYGDA--------- 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1333942756 256 lSPENLERVRALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDALKNTAftPEEL 322
Cdd:cd19161 243 -PAEIISRVMEIEKICDAYNVPLAAAALQFPLRHPAVASVLTGARNPAQLRQNVEAFQTDI--PEEL 306
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
27-326 |
4.20e-22 |
|
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: 93.57 E-value: 4.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 27 LPAISLGLWQnFGGTDVfetgRAVLRRAFDRGVTHFDLANNYGpppgsAEENFGRVLAtDFKAHRDELIVSTKagydMWP 106
Cdd:cd19139 1 IPAFGLGTFR-LKDDVV----IDSVRTALELGYRHIDTAQIYD-----NEAAVGQAIA-ESGVPRDELFITTK----IWI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 107 GPYgswgSRKYLTASLDQSLKRMGLDYVDIFYSHRVDP--RTPLEETMGALDHAVRQGKALYVGISSYSPEMTRRAAAIL 184
Cdd:cd19139 66 DNL----SKDKLLPSLEESLEKLRTDYVDLTLIHWPSPndEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 185 KDLG---TPCLIHqpSYsMLNRwiegGLLDALEETGIGCIAFSPLAQGMLTtkylnGQPTdaraakggtlkahflspenl 261
Cdd:cd19139 142 GAGAiatNQIELS--PY-LQNR----KLVAHCKQHGIHVTSYMTLAYGKVL-----DDPV-------------------- 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333942756 262 ervraLDAIATRRGQTLAQMAIAWVLRdpRVTSALVGARNVEQLDNSLDALkNTAFTPEELAEID 326
Cdd:cd19139 190 -----LAAIAERHGATPAQIALAWAMA--RGYAVIPSSTKREHLRSNLLAL-DLTLDADDMAAIA 246
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
48-315 |
1.14e-21 |
|
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: 93.44 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 48 RAVLRRAFDRGVTHFDLANNYGPppGSAEENFGRVLATdfkAHRDELIVSTKAGYDMWP-------GPYGSWGSRKY--- 117
Cdd:cd19152 23 KATLVAAWDLGIRYFDTAPWYGA--GLSEERLGAALRE---LGREDYVISTKVGRLLVPlqeveptFEPGFWNPLPFdav 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 118 -------LTASLDQSLKRMGLDYVDIFYSHRVDPRTPLEETMGALDHAVR-----------QGKALYVGISSYSPEMTRR 179
Cdd:cd19152 98 fdysydgILRSIEDSLQRLGLSRIDLLSIHDPDEDLAGAESDEHFAQAIKgafraleelreEGVIKAIGLGVNDWEVILR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 180 AAailkDLGTP-CLIHQPSYSMLNRWIEGGLLDALEETGIGCIAFSPLAQGMLTT----KYLNGQPTDaraakggtlkah 254
Cdd:cd19152 178 IL----EEADLdWVMLAGRYTLLDHSAARELLPECEKRGVKVVNAGPFNSGFLAGgdnfDYYEYGPAP------------ 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333942756 255 flsPENLERVRALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLDALKNT 315
Cdd:cd19152 242 ---PELIARRDRIEALCEQHGVSLAAAALQFALAPPAVASVAPGASSPERVEENVALLATE 299
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
27-326 |
3.75e-21 |
|
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: 91.00 E-value: 3.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 27 LPAISLGLWQnfggTDVFETGRAVlRRAFDRGVTHFDLANNYGpppgsAEENFGRVLATDFKAhRDELIVSTKagydMWP 106
Cdd:cd19071 1 MPLIGLGTYK----LKPEETAEAV-LAALEAGYRHIDTAAAYG-----NEAEVGEAIRESGVP-REELFITTK----LWP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 107 GPYGSWGSRKyltaSLDQSLKRMGLDYVDIFYSH------RVDPRTPLEETMGALDHAVRQGKALYVGISSYSPEMTRRa 180
Cdd:cd19071 66 TDHGYERVRE----ALEESLKDLGLDYLDLYLIHwpvpgkEGGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEE- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 181 aaILKDLGTPCLIHQPSYSMLNRWIEggLLDALEETGIGCIAFSPLAQGmlttkylngqptdaraakggtlkahflsPEN 260
Cdd:cd19071 141 --LLAAARIKPAVNQIELHPYLQQKE--LVEFCKEHGIVVQAYSPLGRG----------------------------RRP 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333942756 261 LERVRALDAIATRRGQTLAQMAIAWVLRdpRVTSALVGARNVEQLDNSLDALkNTAFTPEELAEID 326
Cdd:cd19071 189 LLDDPVLKEIAKKYGKTPAQVLLRWALQ--RGVVVIPKSSNPERIKENLDVF-DFELSEEDMAAID 251
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
19-316 |
6.47e-21 |
|
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: 91.06 E-value: 6.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 19 RSGRSGLDLPAISLGlwQNFGGTDVFETGRAVLRRAFDRGVTHFDLANNYGPPpgSAEENFGRVLATdFKAHRDELIVST 98
Cdd:cd19153 9 LGNVSPVGLGTAALG--GVYGDGLEQDEAVAIVAEAFAAGINHFDTSPYYGAE--SSEAVLGKALAA-LQVPRSSYTVAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 99 KAGYdmwpgpYGSWG---SRKYLTASLDQSLKRMGLDYVDIFYSHRV---DPRTPLEETMGALDHAVRQGKALYVGISSY 172
Cdd:cd19153 84 KVGR------YRDSEfdySAERVRASVATSLERLHTTYLDVVYLHDIefvDYDTLVDEALPALRTLKDEGVIKRIGIAGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 173 SPEMTRRAAAILKdLGTPCLIHqpSYSMLNrWIEGGLLDAL----EETGIGCIAFSPLAQGMLTTKylngqptdaraakg 248
Cdd:cd19153 158 PLDTLTRATRRCS-PGSLDAVL--SYCHLT-LQDARLESDApglvRGAGPHVINASPLSMGLLTSQ-------------- 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1333942756 249 GTLKAHFLSPENLERVRALDAIATRRGQTLAQMAIAWVLRD-PRVTSALVGARNVEQLDNSLDALKNTA 316
Cdd:cd19153 220 GPPPWHPASGELRHYAAAADAVCASVEASLPDLALQYSLAAhAGVGTVLLGPSSLAQLRSMLAAVDAVA 288
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
48-311 |
1.70e-19 |
|
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: 87.33 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 48 RAVLRRAFDRGVTHFDLANNYGPppgsAEENFGRVLATDFKAH-RDELIVSTKAG-YDMWPGPYgswgSRKYLTASLDQS 125
Cdd:cd19164 37 VDIVRRALELGIRAFDTSPYYGP----SEIILGRALKALRDEFpRDTYFIITKVGrYGPDDFDY----SPEWIRASVERS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 126 LKRMGLDYVDIFYSHRVDPRTPlEETMGALDHAVR---QGKALYVGISSYS-PEMTRRAAAILKDLGTPcLIHQPSYSML 201
Cdd:cd19164 109 LRRLHTDYLDLVYLHDVEFVAD-EEVLEALKELFKlkdEGKIRNVGISGYPlPVLLRLAELARTTAGRP-LDAVLSYCHY 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 202 NrwIEGGLLDALEETGIGC------IAFSPLAQGMLTTkylngqptdaraakGGTLKAHFLSPENLERVRALDAIATRRG 275
Cdd:cd19164 187 T--LQNTTLLAYIPKFLAAagvkvvLNASPLSMGLLRS--------------QGPPEWHPASPELRAAAAKAAEYCQAKG 250
|
250 260 270
....*....|....*....|....*....|....*..
gi 1333942756 276 QTLAQMAIAWVLR-DPRVTSALVGARNVEQLDNSLDA 311
Cdd:cd19164 251 TDLADVALRYALReWGGEGPTVVGCSNVDELEEAVEA 287
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
24-327 |
2.03e-18 |
|
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: 83.82 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 24 GLDLPAISLGLwqnfgGTDVFETGRAVLRR--------AFDRGVTHFDLANNYGpppgsAEENFGRVLAtDFKAHRDELI 95
Cdd:cd19120 1 GSKIPAIAFGT-----GTAWYKSGDDDIQRdlvdsvklALKAGFRHIDTAEMYG-----NEKEVGEALK-ESGVPREDLF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 96 VSTKAGYDMwPGPYGSwgsrkyltasLDQSLKRMGLDYVDIFYSH---RVDPRTP-LEETMGALDHAVRQGKALYVGISS 171
Cdd:cd19120 70 ITTKVSPGI-KDPREA----------LRKSLAKLGVDYVDLYLIHspfFAKEGGPtLAEAWAELEALKDAGLVRSIGVSN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 172 YSPEMTRRaaaILKDLGTPCLIHQPSYSMLNRWIEGGLLDALEETGIGCIAFSPLAQgmlTTKYLNGqPTDAraakggtl 251
Cdd:cd19120 139 FRIEDLEE---LLDTAKIKPAVNQIEFHPYLYPQQPALLEYCREHGIVVSAYSPLSP---LTRDAGG-PLDP-------- 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1333942756 252 kahflspenlervrALDAIATRRGQTLAQMAIAWVL-RDPRVTSAlvgARNVEQLDNSLDALKNTaFTPEELAEIDR 327
Cdd:cd19120 204 --------------VLEKIAEKYGVTPAQVLLRWALqKGIVVVTT---SSKEERMKEYLEAFDFE-LTEEEVEEIDK 262
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
24-311 |
1.05e-15 |
|
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: 75.87 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 24 GLDLPAISLGLWQNFGgtdvfETGRAVLRRAFDRGVTHFDLANNYGpppgsAEENFGRVLATDFKAhRDELIVSTKagyd 103
Cdd:cd19131 7 GNTIPQLGLGVWQVSN-----DEAASAVREALEVGYRSIDTAAIYG-----NEEGVGKAIRASGVP-REELFITTK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 104 MWPGPYGSWGSRKyltaSLDQSLKRMGLDYVDIFYSHRVDPRTPL-EETMGALDHAVRQGKALYVGISSYSPEMTRRaaa 182
Cdd:cd19131 72 LWNSDQGYDSTLR----AFDESLRKLGLDYVDLYLIHWPVPAQDKyVETWKALIELKKEGRVKSIGVSNFTIEHLQR--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 183 ILKDLGTPCLIHQ----PsysmlnRWIEGGLLDALEETGIGCIAFSPLAQGMLttkylngqptdaraakggtlkahfLSP 258
Cdd:cd19131 145 LIDETGVVPVVNQielhP------RFQQRELRAFHAKHGIQTESWSPLGQGGL------------------------LSD 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1333942756 259 ENLERvraldaIATRRGQTLAQMAIAWVLRD-----PR-VTSALVgARNVEQLDNSLDA 311
Cdd:cd19131 195 PVIGE------IAEKHGKTPAQVVIRWHLQNglvviPKsVTPSRI-AENFDVFDFELDA 246
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
23-326 |
1.09e-14 |
|
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: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 23 SGLDLPAISLGLWQNFGGtdvfETGRAVLRRAFDRGVTHFDLANNYGpppgsAEENFGRVLATDFKA---HRDELIVSTK 99
Cdd:cd19116 7 DGNEIPAIALGTWKLKDD----EGVRQAVKHAIEAGYRHIDTAYLYG-----NEAEVGEAIREKIAEgvvKREDLFITTK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 100 agydMWpgpyGSWGSRKYLTASLDQSLKRMGLDYVDIFYSH------------RVDPRTPLE----ETMGALDHAVRQGK 163
Cdd:cd19116 78 ----LW----NSYHEREQVEPALRESLKRLGLDYVDLYLIHwpvafkenndseSNGDGSLSDidylETWRGMEDLVKLGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 164 ALYVGISSYSPEMTRRaaaILKDLGTPCLIHQ----PSYSMLNrwieggLLDALEETGIGCIAFSPLaqgmlttkylnGQ 239
Cdd:cd19116 150 TRSIGVSNFNSEQINR---LLSNCNIKPAVNQievhPTLTQEK------LVAYCQSNGIVVMAYSPF-----------GR 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 240 PtdarAAKGGTLKAHFLSPEnlervrALDAIATRRGQTLAQMAIAWVLRD-----PRVTSALVGARNVEQLDNSLdalkn 314
Cdd:cd19116 210 L----VPRGQTNPPPRLDDP------TLVAIAKKYGKTTAQIVLRYLIDRgvvpiPKSSNKKRIKENIDIFDFQL----- 274
|
330
....*....|..
gi 1333942756 315 tafTPEELAEID 326
Cdd:cd19116 275 ---TPEEVAALN 283
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
22-326 |
2.21e-14 |
|
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: 71.97 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 22 RSGLDLPAISLGLWQNfGGTDvFEtgrAVLRRAFDRGVTHFDLANNYGpppgsAEENFGRVLATDfKAHRDELIVSTKag 101
Cdd:cd19135 8 SNGVEMPILGLGTSHS-GGYS-HE---AVVYALKECGYRHIDTAKRYG-----CEELLGKAIKES-GVPREDLFLTTK-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 102 ydMWPGPYGSWGSRKyltaSLDQSLKRMGLDYVDIFYSH-------RVDPRTPLEETMGALDHAVRQGKALYVGISSYSP 174
Cdd:cd19135 75 --LWPSDYGYESTKQ----AFEASLKRLGVDYLDLYLLHwpdcpssGKNVKETRAETWRALEELYDEGLCRAIGVSNFLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 175 EMtrraaaiLKDLGTPCLI----HQPSYSMLNRWIEggLLDALEETGIGCIAFSPLAQGmlttKYLNgQPTdaraakggt 250
Cdd:cd19135 149 EH-------LEQLLEDCSVvphvNQVEFHPFQNPVE--LIEYCRDNNIVFEGYCPLAKG----KALE-EPT--------- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 251 lkahflspenlervraLDAIATRRGQTLAQMAIAWVLRD-----PRVTSALVGARNVEQLDNSLdalkntafTPEELAEI 325
Cdd:cd19135 206 ----------------VTELAKKYQKTPAQILIRWSIQNgvvtiPKSTKEERIKENCQVFDFSL--------SEEDMATL 261
|
.
gi 1333942756 326 D 326
Cdd:cd19135 262 D 262
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
23-287 |
3.35e-14 |
|
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: 72.06 E-value: 3.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 23 SGLDLPAISLGLWQNFGgtdvfETGRAVLRRAFDRGVTHFDLANNYgpppgSAEENFGRVLATDF---KAHRDELIVSTK 99
Cdd:cd19154 8 NGVKMPLIGLGTWQSKG-----AEGITAVRTALKAGYRLIDTAFLY-----QNEEAIGEALAELLeegVVKREDLFITTK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 100 AgydmWPGPYgswgSRKYLTASLDQSLKRMGLDYVDIFYSH------RVDPRT-------------PLEETMGALDHAVR 160
Cdd:cd19154 78 L----WTHEH----APEDVEEALRESLKKLQLEYVDLYLIHapaafkDDEGESgtmengmsihdavDVEDVWRGMEKVYD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 161 QGKALYVGISSYSPEMTRRaaaILKDLGTP-------CLIHQPSYSmlnrwieggLLDALEETGIGCIAFSPLaqgmltt 233
Cdd:cd19154 150 EGLTKAIGVSNFNNDQIQR---ILDNARVKphnnqveCHLYFPQKE---------LVEFCKKHNISVTSYATL------- 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1333942756 234 kylnGQPtdARAAkggTLKAHFLSP-ENLERVRALDAIATRRGQTLAQMAIAWVL 287
Cdd:cd19154 211 ----GSP--GRAN---FTKSTGVSPaPNLLQDPIVKAIAEKHGKTPAQVLLRYLL 256
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
22-328 |
3.54e-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: 72.06 E-value: 3.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 22 RSGLDLPAISLGLWQNFGGtdvfETGRAVlRRAFDRGVTHFDLANNYGpppgsAEENFGRVLATDFKA---HRDELIVST 98
Cdd:cd19123 7 SNGDLIPALGLGTWKSKPG----EVGQAV-KQALEAGYRHIDCAAIYG-----NEAEIGAALAEVFKEgkvKREDLWITS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 99 KagydMWpgpyGSWGSRKYLTASLDQSLKRMGLDYVDIFYSH-----RVD---PRT----------PLEETMGALDHAVR 160
Cdd:cd19123 77 K----LW----NNSHAPEDVLPALEKTLADLQLDYLDLYLMHwpvalKKGvgfPESgedllslspiPLEDTWRAMEELVD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 161 QGKALYVGISSYSPEMTRR--AAAILKDLGTPCLIH----QPSysmlnrwieggLLDALEETGIGCIAFSPLAQGmlttk 234
Cdd:cd19123 149 KGLCRHIGVSNFSVKKLEDllATARIKPAVNQVELHpylqQPE-----------LLAFCRDNGIHLTAYSPLGSG----- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 235 ylnGQPTDARAAKGGTLKAHflsPenlervrALDAIATRRGQTLAQMAIAWVLRdpRVTSALVGARNVEQLDNSLDA--L 312
Cdd:cd19123 213 ---DRPAAMKAEGEPVLLED---P-------VINKIAEKHGASPAQVLIAWAIQ--RGTVVIPKSVNPERIQQNLEAaeV 277
|
330
....*....|....*.
gi 1333942756 313 KNTAFTPEELAEIDRH 328
Cdd:cd19123 278 ELDASDMATIAALDRH 293
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
23-312 |
4.31e-14 |
|
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: 71.67 E-value: 4.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 23 SGLDLPAISLGLWQNFGGtdvfETGRAVLRrAFDRGVTHFDLANNYGPPP--GSAEENFgrvLATDFKAHRDELIVSTKA 100
Cdd:cd19118 3 TGNKIPAIGLGTWQAEPG----EVGAAVKI-ALKAGYRHLDLAKVYQNQHevGQALKEL---LKEEPGVKREDLFITSKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 101 gydmwpgpygsWGSR---KYLTASLDQSLKRMGLDYVDIFYSH-----------RVDPRTPLEETMGALDHAV------- 159
Cdd:cd19118 75 -----------WNNShrpEYVEPALDDTLKELGLDYLDLYLIHwpvafkptgdlNPLTAVPTNGGEVDLDLSVslvdtwk 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 160 ------RQGKALYVGISSYSPEMTRraaAILKDLGTPCLIHQPSYSMLnrWIEGGLLDALEETGIGCIAFSPLAQGMLTT 233
Cdd:cd19118 144 amvelkKTGKVKSIGVSNFSIDHLQ---AIIEETGVVPAVNQIEAHPL--LLQDELVDYCKSKNIHITAYSPLGNNLAGL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 234 KYLNGQPTdaraakggtlkahflspenlervraLDAIATRRGQTLAQMAIAWVLRD-----PR-VTSALVGArNVEQLDN 307
Cdd:cd19118 219 PLLVQHPE-------------------------VKAIAAKLGKTPAQVLIAWGIQRghsviPKsVTPSRIRS-NFEQVEL 272
|
....*
gi 1333942756 308 SLDAL 312
Cdd:cd19118 273 SDDEF 277
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
46-287 |
1.26e-13 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 70.05 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 46 TGRAV---LRRAFDRGVTHFDLANNYGpppgsAEENFGRVLATDfKAHRDELIVSTKagydMWPGPYgswgSRKYLTASL 122
Cdd:PRK11172 14 KDQVVidsVKTALELGYRAIDTAQIYD-----NEAAVGQAIAES-GVPRDELFITTK----IWIDNL----AKDKLIPSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 123 DQSLKRMGLDYVDIFYSHRVDPR--TPLEETMGALDHAVRQGKALYVGISSYSPEMTRRAAAIL--KDLGTpcliHQPSY 198
Cdd:PRK11172 80 KESLQKLRTDYVDLTLIHWPSPNdeVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQAIAAVgaENIAT----NQIEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 199 S--MLNRwiegGLLDALEETGIGCIAFSPLAQGmlttKYLnGQPTdaraakggtlkahflspenlervraLDAIATRRGQ 276
Cdd:PRK11172 156 SpyLQNR----KVVAFAKEHGIHVTSYMTLAYG----KVL-KDPV-------------------------IARIAAKHNA 201
|
250
....*....|.
gi 1333942756 277 TLAQMAIAWVL 287
Cdd:PRK11172 202 TPAQVILAWAM 212
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
42-327 |
3.22e-13 |
|
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: 69.02 E-value: 3.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 42 DVFETGRAVlRRAFDRGVTHFDLANNYgpppgSAEENFGRVLATDFKA---HRDELIVSTKAgydmwpgpygsWGSR--- 115
Cdd:cd19129 17 DPSATRNAV-KAALEAGFRHFDCAERY-----RNEAEVGEAMQEVFKAgkiRREDLFVTTKL-----------WNTNhrp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 116 KYLTASLDQSLKRMGLDYVDIFYSH---------RVDPR-----------TPLEETMGALDHAVRQGKALYVGISSYSPE 175
Cdd:cd19129 80 ERVKPAFEASLKRLQLDYLDLYLIHtpfafqpgdEQDPRdangnviyddgVTLLDTWRAMERLVDEGRCKAIGLSDVSLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 176 MTRR--AAAILKdlgtPCLIHQPSYSMLNRWiegGLLDALEETGIGCIAFSPLAQGMlttkylngqptdaraakggtlka 253
Cdd:cd19129 160 KLREifEAARIK----PAVVQVESHPYLPEW---ELLDFCKNHGIVLQAFAPLGHGM----------------------- 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333942756 254 hflSPENLERvRALDAIATRRGQTLAQMAIAWVLRdpRVTSALVGARNVEQLDNSLDAlknTAFTPEELAEIDR 327
Cdd:cd19129 210 ---EPKLLED-PVITAIARRVNKTPAQVLLAWAIQ--RGTALLTTSKTPSRIRENFDI---STLPEDAMREINE 274
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
24-326 |
6.71e-13 |
|
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: 67.68 E-value: 6.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 24 GLDLPAISLGLWQNFGgtdvfETGRAVLRRAFDRGVTHFDLANNYGpppgsAEENFGRVLATDfKAHRDELIVSTKAgyd 103
Cdd:cd19132 4 GTQIPAIGFGTYPLKG-----DEGVEAVVAALQAGYRLLDTAFNYE-----NEGAVGEAVRRS-GVPREELFVTTKL--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 104 mwPGPYGSwgsRKYLTASLDQSLKRMGLDYVDIFYSHRVDPRTPLE-ETMGALDHAVRQGKALYVGISSYSPEMTRRaaa 182
Cdd:cd19132 70 --PGRHHG---YEEALRTIEESLYRLGLDYVDLYLIHWPNPSRDLYvEAWQALIEAREEGLVRSIGVSNFLPEHLDR--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 183 ILKDLGTPCLIHQ----PSYSMLNrwieggLLDALEETGIGCIAFSPLAQGMlttkylngqptdaraakgGTLKAHflsp 258
Cdd:cd19132 142 LIDETGVTPAVNQielhPYFPQAE------QRAYHREHGIVTQSWSPLGRGS------------------GLLDEP---- 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333942756 259 enlervrALDAIATRRGQTLAQMAIAW-----VLRDPRVTSALVGARNVEQLDNSLDalkntaftPEELAEID 326
Cdd:cd19132 194 -------VIKAIAEKHGKTPAQVVLRWhvqlgVVPIPKSANPERQRENLAIFDFELS--------DEDMAAIA 251
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
40-327 |
7.69e-13 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 68.07 E-value: 7.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 40 GTDVF------ETGRAVLRRAFDRGVTHFDLANNYGPPPGSaeenfgRVLATDFKAHRDELIVSTKAGYDMwpGPYGSWG 113
Cdd:PRK10376 29 GPGVFgppkdrDAAIAVLREAVALGVNHIDTSDFYGPHVTN------QLIREALHPYPDDLTIVTKVGARR--GEDGSWL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 114 ---SRKYLTASLDQSLKRMGLDYVDI------FYSHRVDPRtPLEETMGALDHAVRQGKALYVGISSYSPEMTRRAAAIl 184
Cdd:PRK10376 101 pafSPAELRRAVHDNLRNLGLDVLDVvnlrlmGDGHGPAEG-SIEEPLTVLAELQRQGLVRHIGLSNVTPTQVAEARKI- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 185 kdlgTPCLIHQPSYSMLNRwIEGGLLDALEETGIGCIAFSPLaqgmlttkylngqptdaraakGGtlkahfLSPENLErv 264
Cdd:PRK10376 179 ----AEIVCVQNHYNLAHR-ADDALIDALARDGIAYVPFFPL---------------------GG------FTPLQSS-- 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333942756 265 rALDAIATRRGQTLAQMAIAWVLRdpRVTSALV--GARNVEQLDNSLDAlKNTAFTPEELAEIDR 327
Cdd:PRK10376 225 -TLSDVAASLGATPMQVALAWLLQ--RSPNILLipGTSSVAHLRENLAA-AELVLSEEVLAELDG 285
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
23-327 |
4.16e-12 |
|
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: 65.75 E-value: 4.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 23 SGLDLPAISLGLWQNFGGTDvfETGRAVLRrAFDRGVTHFDLANNYGpppgsAEENFGRVLATDFK----AHRDELIVST 98
Cdd:cd19124 1 SGQTMPVIGMGTASDPPSPE--DIKAAVLE-AIEVGYRHFDTAAAYG-----TEEALGEALAEALRlglvKSRDELFVTS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 99 KagydMWPgpygSWGSRKYLTASLDQSLKRMGLDYVDIFYSH---------RVDPRTP-------LEETMGALDHAVRQG 162
Cdd:cd19124 73 K----LWC----SDAHPDLVLPALKKSLRNLQLEYVDLYLIHwpvslkpgkFSFPIEEedflpfdIKGVWEAMEECQRLG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 163 KALYVGISSYSpemtrraAAILKDL----GTPCLIHQpsYSMLNRWIEGGLLDALEETGIGCIAFSPLaqgmlttkylng 238
Cdd:cd19124 145 LTKAIGVSNFS-------CKKLQELlsfaTIPPAVNQ--VEMNPAWQQKKLREFCKANGIHVTAYSPL------------ 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 239 qptdaraakgGTLKAHFLSPENLERvRALDAIATRRGQTLAQMAIAWVLRdpRVTSALVGARNVEQLDNSLDALkNTAFT 318
Cdd:cd19124 204 ----------GAPGTKWGSNAVMES-DVLKEIAAAKGKTVAQVSLRWVYE--QGVSLVVKSFNKERMKQNLDIF-DWELT 269
|
....*....
gi 1333942756 319 PEELAEIDR 327
Cdd:cd19124 270 EEDLEKISE 278
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
23-326 |
4.93e-12 |
|
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: 65.60 E-value: 4.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 23 SGLDLPAISLGLWQNFGGtdvfETGRAVLRrAFDRGVTHFDLANNYGpppgsAEENFGRVLaTDFKAHRDELIVSTKagy 102
Cdd:cd19117 10 TGAEIPAVGLGTWQSKPN----EVAKAVEA-ALKAGYRHIDTAAIYG-----NEEEVGQGI-KDSGVPREEIFITTK--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 103 dMWpgpyGSWGSRkyLTASLDQSLKRMGLDYVDIFYSH---RVDPR----TPLEE--------------TMGALDHAVRQ 161
Cdd:cd19117 76 -LW----CTWHRR--VEEALDQSLKKLGLDYVDLYLMHwpvPLDPDgndfLFKKDdgtkdhepdwdfikTWELMQKLPAT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 162 GKALYVGISSYSpemTRRAAAILKDLGTP-------CLIH----QPSysmlnrwieggLLDALEETGIGCIAFSPLAQgm 230
Cdd:cd19117 149 GKVKAIGVSNFS---IKNLEKLLASPSAKivpavnqIELHpllpQPK-----------LVDFCKSKGIHATAYSPLGS-- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 231 lttkylngqpTDAraakggtlkahflsPenLERVRALDAIATRRGQTLAQMAIAWVLRdpRVTSALVGARNVEQLDNSLD 310
Cdd:cd19117 213 ----------TNA--------------P--LLKEPVIIKIAKKHGKTPAQVIISWGLQ--RGYSVLPKSVTPSRIESNFK 264
|
330
....*....|....*.
gi 1333942756 311 ALkntAFTPEELAEID 326
Cdd:cd19117 265 LF---TLSDEEFKEID 277
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
24-326 |
6.23e-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: 6.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 24 GLDLPAISLGLWQNFGgtdvfETGRAVLRRAFDRGVTHFDLANNYGpppgsAEENFGRVLATDF---KAHRDELIVSTKA 100
Cdd:cd19111 1 GFPMPVIGLGTYQSPP-----EEVRAAVDYALFVGYRHIDTALSYQ-----NEKAIGEALKWWLkngKLKREEVFITTKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 101 gydmWPgpYGSwgSRKYLTASLDQSLKRMGLDYVDIFYSH-------------RVDPRTPLEETMGALDHAVRQGKALYV 167
Cdd:cd19111 71 ----PP--VYL--EFKDTEKSLEKSLENLKLPYVDLYLIHhpcgfvnkkdkgeRELASSDVTSVWRAMEALVSEGKVKSI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 168 GISSYSPEMTRRAAAILK----DLGTPCLIHQPSYSmlnrwieggLLDALEETGIGCIAFSPLaqgmlttkylnGQPTDA 243
Cdd:cd19111 143 GLSNFNPRQINKILAYAKvkpsNLQLECHAYLQQRE---------LRKFCNKKNIVVTAYAPL-----------GSPGRA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 244 RAAKGGTLkahflsPENLERVRALdAIATRRGQTLAQMAIAWVL-RD----PRVTSALVGARNVEQLDNSLdalkntafT 318
Cdd:cd19111 203 NQSLWPDQ------PDLLEDPTVL-AIAKELDKTPAQVLLRFVLqRGtgvlPKSTNKERIEENFEVFDFEL--------T 267
|
....*...
gi 1333942756 319 PEELAEID 326
Cdd:cd19111 268 EEHFKKLK 275
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
24-230 |
7.20e-12 |
|
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: 64.52 E-value: 7.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 24 GLDLPAISLGLWQNfggTDVFETGRAVLRrAFDRGVTHFDLANNYGpppgsAEENFGRVLAtDFKAHRDELIVSTKagyd 103
Cdd:cd19133 6 GVEMPILGFGVFQI---PDPEECERAVLE-AIKAGYRLIDTAAAYG-----NEEAVGRAIK-KSGIPREELFITTK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 104 MWPGPYGSWGSRKyltaSLDQSLKRMGLDYVDIFYSHRvdPRTPLEETMGALDHAVRQGKALYVGISSYSPEmtrraaaI 183
Cdd:cd19133 72 LWIQDAGYEKAKK----AFERSLKRLGLDYLDLYLIHQ--PFGDVYGAWRAMEELYKEGKIRAIGVSNFYPD-------R 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1333942756 184 LKDLgtpcLIHQPSYSMLNRwIE-------GGLLDALEETGIGCIAFSPLAQGM 230
Cdd:cd19133 139 LVDL----ILHNEVKPAVNQ-IEthpfnqqIEAVEFLKKYGVQIEAWGPFAEGR 187
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
28-327 |
7.47e-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: 7.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 28 PAISLGLWQNFGGTDvfetgRAVLRRAFDRGVTHFDLANNYGpppgsAEENFGRVLATDFK---AHRDELIVSTKagydM 104
Cdd:cd19128 2 PRLGFGTYKITESES-----KEAVKNAIKAGYRHIDCAYYYG-----NEAFIGIAFSEIFKdggVKREDLFITSK----L 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 105 WPGPYGSWGSRKyltaSLDQSLKRMGLDYVDIFYSH-------------------RVDPRTPLEETMGALDHAVRQGKAL 165
Cdd:cd19128 68 WPTMHQPENVKE----QLLITLQDLQLEYLDLFLIHwplafdmdtdgdprddnqiQSLSKKPLEDTWRAMEQCVDEKLTK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 166 YVGISSYSPEMtrraaaiLKDLGTPCLIH--------QPsYSMLNRWIEGGLldaleETGIGCIAFSPLaqgmlttkyln 237
Cdd:cd19128 144 NIGVSNYSTKL-------LTDLLNYCKIKpfmnqiecHP-YFQNDKLIKFCI-----ENNIHVTAYRPL----------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 238 gqptdaraakGGTLKAHFLSPENlerVRALDAIATRRGQTLAQMAIAW-VLRDPRVTSALVGARNVEQLDNSLDALKnTA 316
Cdd:cd19128 200 ----------GGSYGDGNLTFLN---DSELKALATKYNTTPPQVIIAWhLQKWPKNYSVIPKSANKSRCQQNFDIND-LA 265
|
330
....*....|.
gi 1333942756 317 FTPEELAEIDR 327
Cdd:cd19128 266 LTKEDMDAINT 276
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
23-312 |
5.59e-11 |
|
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: 62.36 E-value: 5.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 23 SGLDLPAISLGLWQNFGGtdvfETGRAVlRRAFDRGVTHFDLANNYGpppgsAEENFGRVLATDFKA---HRDELIVSTK 99
Cdd:cd19125 7 TGAKIPAVGLGTWQADPG----VVGNAV-KTAIKEGYRHIDCAAIYG-----NEKEIGKALKKLFEDgvvKREDLFITSK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 100 agydMWPGPYGSWGSRKyltaSLDQSLKRMGLDYVDIFYSH---RVD-----------PRTPLEETMGALDHAVRQGKAL 165
Cdd:cd19125 77 ----LWCTDHAPEDVPP----ALEKTLKDLQLDYLDLYLIHwpvRLKkgahmpepeevLPPDIPSTWKAMEKLVDSGKVR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 166 YVGISSYSpemTRRAAAILKDLGTPCLIHQ----PSysmlnrWIEGGLLDALEETGIGCIAFSPLaqgmlttkylnGQPt 241
Cdd:cd19125 149 AIGVSNFS---VKKLEDLLAVARVPPAVNQvechPG------WQQDKLHEFCKSKGIHLSAYSPL-----------GSP- 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333942756 242 DARAAKGGTLKahflSPenlervrALDAIATRRGQTLAQMAIAWVLRdpRVTSALVGARNVEQLDNSLDAL 312
Cdd:cd19125 208 GTTWVKKNVLK----DP-------IVTKVAEKLGKTPAQVALRWGLQ--RGTSVLPKSTNEERIKENIDVF 265
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
24-326 |
1.26e-10 |
|
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: 60.99 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 24 GLDLPAISLGLWQNFGGTdvfETGRAVlRRAFDRGVTHFDLANNYgpppgSAEENFGRVLATDfKAHRDELIVSTKagyd 103
Cdd:cd19156 6 GVEMPRLGLGVWRVQDGA---EAENAV-KWAIEAGYRHIDTAAIY-----KNEEGVGQGIRES-GVPREEVFVTTK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 104 MWPGPYGSWGSrkylTASLDQSLKRMGLDYVDIFYSHRvdPRT-PLEETMGALDHAVRQGKALYVGISSYSPEMtrraaa 182
Cdd:cd19156 72 LWNSDQGYEST----LAAFEESLEKLGLDYVDLYLIHW--PVKgKFKDTWKAFEKLYKEKKVRAIGVSNFHEHH------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 183 iLKDLGTPCLIHqpsySMLNRwIE-------GGLLDALEETGIGCIAFSPLAQGMLttkylngqptdaraakggtLKAHF 255
Cdd:cd19156 140 -LEELLKSCKVA----PMVNQ-IElhplltqEPLRKFCKEKNIAVEAWSPLGQGKL-------------------LSNPV 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333942756 256 LSpenlervraldAIATRRGQTLAQMAIAWVLRDPRVTsaLVGARNVEQLDNSLDALkNTAFTPEELAEID 326
Cdd:cd19156 195 LK-----------AIGKKYGKSAAQVIIRWDIQHGIIT--IPKSVHEERIQENFDVF-DFELTAEEIRQID 251
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
24-327 |
1.36e-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: 60.88 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 24 GLDLPAISLGLWQnfggTDVFETGRAVlRRAFDRGVTHFDLANNYGpppgsAEENFGRVL---ATDfkahRDELIVSTKa 100
Cdd:cd19127 6 GVEMPALGLGVFQ----TPPEETADAV-ATALADGYRLIDTAAAYG-----NEREVGEGIrrsGVD----RSDIFVTTK- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 101 gydMWPGPYGSWGSRKyltaSLDQSLKRMGLDYVDIFYSHRVDPrTPLEETMG---ALDHAVRQGKALYVGISSYSPEmt 177
Cdd:cd19127 71 ---LWISDYGYDKALR----GFDASLRRLGLDYVDLYLLHWPVP-NDFDRTIQaykALEKLLAEGRVRAIGVSNFTPE-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 178 rRAAAILKDLGTPCLIHQ----PSYSmlnrwiEGGLLDALEETGIGCIAFSPLaqgmlttkylngqptdaraakGGTLKa 253
Cdd:cd19127 141 -HLERLIDATTVVPAVNQvelhPYFS------QKDLRAFHRRLGIVTQAWSPI---------------------GGVMR- 191
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1333942756 254 hFLSPENLERVRALD-----AIATRRGQTLAQMAIAWVLRDPRvtSALVGARNVEQLDNSLDALkNTAFTPEELAEIDR 327
Cdd:cd19127 192 -YGASGPTGPGDVLQdptitGLAEKYGKTPAQIVLRWHLQNGV--SAIPKSVHPERIAENIDIF-DFALSAEDMAAIDA 266
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
24-326 |
1.59e-10 |
|
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: 60.69 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 24 GLDLPAISLGLWQnfggTDVFETGRAVlRRAFDRGVTHFDLANNYGpppgsAEENFGRVLATDFKAhRDELIVSTKAGYD 103
Cdd:cd19130 7 GNSIPQLGYGVFK----VPPADTQRAV-ATALEVGYRHIDTAAIYG-----NEEGVGAAIAASGIP-RDELFVTTKLWND 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 104 MWPGpygswgsrKYLTASLDQSLKRMGLDYVDIFYSHRVDP-RTPLEETMGALDHAVRQGKALYVGISSYSPEMTRRaaa 182
Cdd:cd19130 76 RHDG--------DEPAAAFAESLAKLGLDQVDLYLVHWPTPaAGNYVHTWEAMIELRAAGRTRSIGVSNFLPPHLER--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 183 ILKDLGTPCLIHQ----PSYSmlNRWIEggllDALEETGIGCIAFSPLAQGMLttkylngqptdaraakggtlkahFLSP 258
Cdd:cd19130 145 IVAATGVVPAVNQielhPAYQ--QRTIR----DWAQAHDVKIEAWSPLGQGKL-----------------------LGDP 195
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333942756 259 enlervrALDAIATRRGQTLAQMAIAWVLRDPRVTsaLVGARNVEQLDNSLDaLKNTAFTPEELAEID 326
Cdd:cd19130 196 -------PVGAIAAAHGKTPAQIVLRWHLQKGHVV--FPKSVRRERMEDNLD-VFDFDLTDTEIAAID 253
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
23-288 |
4.96e-10 |
|
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: 59.56 E-value: 4.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 23 SGLDLPAISLGLWQNFGGTDvfETGRAVLRrAFDRGVTHFDLANNY--GPPPGSAEENFgrvLATDFKAHRDELIVSTKA 100
Cdd:cd19122 5 NGVKIPAVGFGTFANEGAKG--ETYAAVTK-ALDVGYRHLDCAWFYlnEDEVGDAVRDF---LKENPSVKREDLFICTKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 101 GYDMWPGPYGSWgsrkyltaSLDQSLKRMGLDYVDIFYSH------RVDPRTPL-----------------EETMGALDH 157
Cdd:cd19122 79 WNHLHEPEDVKW--------SIDNSLKNLKLDYIDLFLVHwpiaaeKNDQRSPKlgpdgkyvilkdltenpEPTWRAMEE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 158 AVRQGKALYVGISSYSPEMTRRAAAILKDLGTPCLIHQPSYsMLNRwiegGLLDALEETGIGCIAFSPLAQGmlttkylN 237
Cdd:cd19122 151 IYESGKAKAIGVSNWTIPGLKKLLSFAKVKPHVNQIEIHPF-LPNE----ELVDYCFSNDILPEAYSPLGSQ-------N 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1333942756 238 GQPTDAraakggtlkahflspenlERVR---ALDAIATRRGQTLAQMAIAWVLR 288
Cdd:cd19122 219 QVPSTG------------------ERVSenpTLNEVAEKGGYSLAQVLIAWGLR 254
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
23-226 |
7.62e-10 |
|
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: 59.08 E-value: 7.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 23 SGLDLPAISLGLWQNFGGtdvfETGRAVLRrAFDRGVTHFDLANNYGpppgsAEENFGRVLATDFKA--HRDELIVSTKa 100
Cdd:cd19121 8 TGASIPAVGLGTWQAKAG----EVKAAVAH-ALKIGYRHIDGALCYQ-----NEDEVGEGIKEAIAGgvKREDLFVTTK- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 101 gydMWpgpyGSWGSRkyLTASLDQSLKRMGLDYVDIFYSH--------RVDPRTP-LEETMGALDH-------------A 158
Cdd:cd19121 77 ---LW----STYHRR--VELCLDRSLKSLGLDYVDLYLVHwpvllnpnGNHDLFPtLPDGSRDLDWdwnhvdtwkqmekV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333942756 159 VRQGKALYVGISSYSpemtrraAAILKDLgtpcLIHQPSYSMLNRwIEG-------GLLDALEETGIGCIAFSPL 226
Cdd:cd19121 148 LKTGKTKAIGVSNYS-------IPYLEEL----LKHATVVPAVNQ-VENhpylpqqELVDFCKEKGILIEAYSPL 210
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
22-331 |
1.10e-09 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 58.90 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 22 RSGLDLPA------ISLGLWQNFGGTDVFETGRA----VLRRAFDRGVTHFDLANNYGpppgSAEENFGRVLATDfKAHR 91
Cdd:cd19098 2 RLGLGLAAlgrpgyINLGHAADLGSGRSVEAMRAhthaVLDAAWAAGVRYFDAARSYG----RAEEFLGSWLRSR-NIAP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 92 DELIVSTKAGYDmwpgpY-GSWG-----------SRKYLTASLDQSLKRMGlDYVDIFYSHRVDPRTPL---EETMGALD 156
Cdd:cd19098 77 DAVFVGSKWGYT-----YtADWQvdaavhevkdhSLARLLKQWEETRSLLG-KHLDLYQIHSATLESGVledADVLAALA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 157 HAVRQGKAlyVGISSYSP---EMTRRAAAILKDLGTPCLIHQPSYSMLnrwiEGGLLDALEE---TGIGCIAFSPLAQGM 230
Cdd:cd19098 151 ELKAEGVK--IGLSLSGPqqaETLRRALEIEIDGARLFDSVQATWNLL----EQSAGEALEEaheAGMGVIVKEALANGR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 231 LTtkylngqptdARAAkggtlkahflSPENLERVRALDAIATRRGQTLAQMAIAWVLRDPRVTSALVGARNVEQLDNSLD 310
Cdd:cd19098 225 LT----------DRNP----------SPELAPLMAVLKAVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLR 284
|
330 340
....*....|....*....|.
gi 1333942756 311 ALkNTAFTPEELAEIDRHAVD 331
Cdd:cd19098 285 AL-DVSLDLELLAALADLAEP 304
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
23-178 |
2.66e-09 |
|
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: 57.50 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 23 SGLDLPAISLGLWQNFGGTDvfetgRAVLRRAFDRGVTHFDLANNYGpppgsAEENFGRVLATDFK---AHRDELIVSTK 99
Cdd:cd19112 7 SGHKMPVIGLGVWRMEPGEI-----KELILNAIKIGYRHFDCAADYK-----NEKEVGEALAEAFKtglVKREDLFITTK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 100 agydMWPGPYGswgsrkYLTASLDQSLKRMGLDYVDIFYSH-----------------------RVDPRTPLEETMGALD 156
Cdd:cd19112 77 ----LWNSDHG------HVIEACKDSLKKLQLDYLDLYLVHfpvatkhtgvgttgsalgedgvlDIDVTISLETTWHAME 146
|
170 180
....*....|....*....|..
gi 1333942756 157 HAVRQGKALYVGISSYSPEMTR 178
Cdd:cd19112 147 KLVSAGLVRSIGISNYDIFLTR 168
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
24-326 |
4.26e-09 |
|
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: 56.77 E-value: 4.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 24 GLDLPAISLGLWQnfGGTDVFETGravLRRAFDRGVTHFDLANNYGpppgsAEENFGRVLATDF---KAHRDELIVSTKa 100
Cdd:cd19155 9 GEKMPVVGLGTWQ--SSPEEIETA---VDTALEAGYRHIDTAYVYR-----NEAAIGNVLKKWIdsgKVKREELFIVTK- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 101 gydMWPGPYGSWGSRKYLTASLdqslKRMGLDYVDIFY---------------------SHRVDPRTPLEETMGALDHAV 159
Cdd:cd19155 78 ---LPPGGNRREKVEKFLLKSL----EKLQLDYVDLYLihfpvgslskeddsgkldptgEHKQDYTTDLLDIWKAMEAQV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 160 RQGKALYVGISSYSPEMTRRaaaILKDLGT-PCLIHQPSYSMLNrwiEGGLLDALEETGIGCIAFSPLaqgmlttkylnG 238
Cdd:cd19155 151 DQGLTRSIGLSNFNREQMAR---ILKNARIkPANLQVELHVYLQ---QKDLVDFCSTHSITVTAYAPL-----------G 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 239 QPtdARAAKGGTLKAHFLSPENLERVRALDAIATRRGQTLAQMAIAWVL-RD----PRVTSALVGARNVEQLDNSLdalk 313
Cdd:cd19155 214 SP--GAAHFSPGTGSPSGSSPDLLQDPVVKAIAERHGKSPAQVLLRWLMqRGvvviPKSTNAARIKENFQVFDFEL---- 287
|
330
....*....|...
gi 1333942756 314 ntafTPEELAEID 326
Cdd:cd19155 288 ----TEADMAKLS 296
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
24-293 |
6.97e-09 |
|
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: 55.91 E-value: 6.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 24 GLDLPAISLGLWQNFGGTdvfETGRAVlRRAFDRGVTHFDLANNYgpppgSAEENFGRVLATDFKAhRDELIVSTKagyd 103
Cdd:cd19126 6 GTRMPWLGLGVFQTPDGD---ETERAV-QTALENGYRSIDTAAIY-----KNEEGVGEAIRESGVP-REELFVTTK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 104 MWPGpygSWGSRKYLTAsLDQSLKRMGLDYVDIFYSHRvdP-RTPLEETMGALDHAVRQGKALYVGISSYSPEMTRRaaa 182
Cdd:cd19126 72 LWND---DQRARRTEDA-FQESLDRLGLDYVDLYLIHW--PgKDKFIDTWKALEKLYASGKVKAIGVSNFQEHHLEE--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 183 ILKDLGTPCLIHQPSYS-MLNRwieGGLLDALEETGIGCIAFSPLAQGMLTTKylngqptdaraakggtlkahflspenl 261
Cdd:cd19126 143 LLAHADVVPAVNQVEFHpYLTQ---KELRGYCKSKGIVVEAWSPLGQGGLLSN--------------------------- 192
|
250 260 270
....*....|....*....|....*....|..
gi 1333942756 262 ervRALDAIATRRGQTLAQMAIAWVLRDPRVT 293
Cdd:cd19126 193 ---PVLAAIGEKYGKSAAQVVLRWDIQHGVVT 221
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
24-331 |
8.42e-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: 56.03 E-value: 8.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 24 GLDLPAISLGLWQnfggTDVFETGRAVLRrAFDRGVTHFDLANNYGpppgsAEENFGRVLA---TDFKAHRDELIVSTKa 100
Cdd:cd19114 1 GDKMPLVGFGTAK----IKANETEEVIYN-AIKVGYRLIDGALLYG-----NEAEVGRGIRkaiQEGLVKREDLFIVTK- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 101 gydMWpgpyGSWGSRKYLTASLDQSLKRMGLDYVDIFYSH------RVDPRT-------------------PLEETMGAL 155
Cdd:cd19114 70 ---LW----NNFHGKDHVREAFDRQLKDYGLDYIDLYLIHfpipaaYVDPAEnypflwkdkelkkfpleqsPMQECWREM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 156 DHAVRQGKALYVGISSYSPEMTRraaailkDLGTPCLI--------HQPsYSMLNRwieggLLDALEETGIGCIAFSPLA 227
Cdd:cd19114 143 EKLVDAGLVRNIGIANFNVQLIL-------DLLTYAKIkpavlqieHHP-YLQQKR-----LIDWAKKQGIQITAYSSFG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 228 QGMLT--TKYLngqptdaraakggtlkAHFlspENLERVRALDAIATRRGQTLAQMAIAWVLRdpRVTSALVGARNVEQL 305
Cdd:cd19114 210 NAVYTkvTKHL----------------KHF---TNLLEHPVVKKLADKHKRDTGQVLLRWAVQ--RNITVIPKSVNVERM 268
|
330 340
....*....|....*....|....*.
gi 1333942756 306 DNSLDalkntaFTPEELAEIDRHAVD 331
Cdd:cd19114 269 KTNLD------ITSYKLDEEDMEALY 288
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
27-232 |
9.00e-09 |
|
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: 55.72 E-value: 9.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 27 LPAISLGLWQnFGGTDVFetgRAVLRRAFDRGVTHFDLANNYGpppgsAEENFGRVLATDFKAH---RDELIVSTKagyd 103
Cdd:cd19136 1 MPILGLGTFR-LRGEEEV---RQAVDAALKAGYRLIDTASVYR-----NEADIGKALRDLLPKYglsREDIFITSK---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 104 MWPGPYGSWGSRkyltASLDQSLKRMGLDYVDIFYSH--------RVDPRTPL--EETMGALDHAVRQGKALYVGISSYS 173
Cdd:cd19136 68 LAPKDQGYEKAR----AACLGSLERLGTDYLDLYLIHwpgvqglkPSDPRNAElrRESWRALEDLYKEGKLRAIGVSNYT 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333942756 174 PemtRRAAAILKDLGTPCLIHQ----PSYsmlnrwIEGGLLDALEETGIGCIAFSPLAQGMLT 232
Cdd:cd19136 144 V---RHLEELLKYCEVPPAVNQvefhPHL------VQKELLKFCKDHGIHLQAYSSLGSGDLR 197
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
23-325 |
1.35e-08 |
|
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: 55.53 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 23 SGLDLPAISLGLWQnfggTDVfETGRAVLRRAFDRGVTHFDLANNYGpppgsAEENFGRVLATDFK---AHRDELIVSTK 99
Cdd:cd19113 7 SGYKMPSVGFGCWK----LDN-ATAADQIYQAIKAGYRLFDGAEDYG-----NEKEVGEGVNRAIDeglVKREELFLTSK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 100 agydMWpgpyGSWGSRKYLTASLDQSLKRMGLDYVDIFYSH------------RVDP-------------RTPLEETMGA 154
Cdd:cd19113 77 ----LW----NNFHDPKNVETALNKTLSDLKLDYVDLFLIHfpiafkfvpieeKYPPgfycgdgdnfvyeDVPILDTWKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 155 LDHAVRQGKALYVGISSYSpemtrraAAILKDLGTPCLI--------HQPsYSMLNRWIEgglldALEETGIGCIAFSPL 226
Cdd:cd19113 149 LEKLVDAGKIKSIGVSNFP-------GALILDLLRGATIkpavlqieHHP-YLQQPKLIE-----YAQKAGITITAYSSF 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 227 aqGMLTTKYLNGQptdaRAAKGGTLKAHflspenlervRALDAIATRRGQTLAQMAIAWVLRdpRVTSALVGARNVEQLd 306
Cdd:cd19113 216 --GPQSFVELNQG----RALNTPTLFEH----------DTIKSIAAKHNKTPAQVLLRWATQ--RGIAVIPKSNLPERL- 276
|
330 340
....*....|....*....|.
gi 1333942756 307 nsLDALKNTAF--TPEELAEI 325
Cdd:cd19113 277 --LQNLSVNDFdlTKEDFEEI 295
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
27-332 |
1.64e-08 |
|
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: 54.86 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 27 LPAISLGLWQNfggTDVfETGRAVLRrAFDRGVTHFDLANNYGpppgsAEENFGRVLATDfKAHRDELIVSTKagydMWP 106
Cdd:cd19134 11 MPVIGLGVGEL---SDD-EAERSVSA-ALEAGYRLIDTAAAYG-----NEAAVGRAIAAS-GIPRGELFVTTK----LAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 107 GPYGSWGSRKYLTASLDqslkRMGLDYVDIFYSHRVDPRT-PLEETMGALDHAVRQGKALYVGISSYSPEmtrRAAAILK 185
Cdd:cd19134 76 PDQGFTASQAACRASLE----RLGLDYVDLYLIHWPAGREgKYVDSWGGLMKLREEGLARSIGVSNFTAE---HLENLID 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 186 DLG-TPCLIHQPSYSMLNrwiEGGLLDALEETGIGCIAFSPLAQGMLTTKylngqptdaraakggtlkahflspenlerv 264
Cdd:cd19134 149 LTFfTPAVNQIELHPLLN---QAELRKVNAQHGIVTQAYSPLGVGRLLDN------------------------------ 195
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333942756 265 RALDAIATRRGQTLAQMAIAWVLRDPRVtsALVGARNVEQLDNSLDALKntaFtpeELAEIDRHAVDG 332
Cdd:cd19134 196 PAVTAIAAAHGRTPAQVLLRWSLQLGNV--VISRSSNPERIASNLDVFD---F---ELTADHMDALDG 255
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
24-293 |
5.79e-08 |
|
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: 53.16 E-value: 5.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 24 GLDLPAISLGLWQNFGGTDVFETgravLRRAFDRGVTHFDLANNYGpppgsAEENFGRVLATDFKAhRDELIVSTKA--- 100
Cdd:cd19157 7 GVKMPWLGLGVFKVEEGSEVVNA----VKTALKNGYRSIDTAAIYG-----NEEGVGKGIKESGIP-REELFITSKVwna 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 101 --GYDmwpgpygswgsrKYLTAsLDQSLKRMGLDYVDIFYSHrvdprTPLE----ETMGALDHAVRQGKALYVGISSYSP 174
Cdd:cd19157 77 dqGYD------------STLKA-FEASLERLGLDYLDLYLIH-----WPVKgkykETWKALEKLYKDGRVRAIGVSNFQV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 175 EMtrraaaiLKDLGTPCLIhQPsysMLN------RWIEGGLLDALEETGIGCIAFSPLAQGMLTTKYLngqptdaraakg 248
Cdd:cd19157 139 HH-------LEDLLADAEI-VP---MVNqvefhpRLTQKELRDYCKKQGIQLEAWSPLMQGQLLDNPV------------ 195
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1333942756 249 gtlkahflspenlervraLDAIATRRGQTLAQMAIAWVLRDPRVT 293
Cdd:cd19157 196 ------------------LKEIAEKYNKSVAQVILRWDLQNGVVT 222
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
23-140 |
8.31e-08 |
|
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: 52.88 E-value: 8.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 23 SGLDLPAISLGLWQNfggTDVFETGRAVLRRAFDRGVTHFDLANNYGPPPgSAEENFGRVLATDfKAHRDELIVSTKagy 102
Cdd:cd19119 8 TGASIPALGLGTASP---HEDRAEVKEAVEAAIKEGYRHIDTAYAYETED-FVGEAIKRAIDDG-SIKREELFITTK--- 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 1333942756 103 dMWPGPYgswgsrKYLTASLDQSLKRMGLDYVDIFYSH 140
Cdd:cd19119 80 -VWPTFY------DEVERSLDESLKALGLDYVDLLLVH 110
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
23-326 |
8.91e-08 |
|
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: 52.77 E-value: 8.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 23 SGLDLPAISLGLWQNFGGtdvfETGRAVlRRAFDRGVTHFDLANNYGPPP--GSA-EENFGRVLATDfkahRDELIVSTK 99
Cdd:cd19106 3 TGQKMPLIGLGTWKSKPG----QVKAAV-KYALDAGYRHIDCAAVYGNEQevGEAlKEKVGPGKAVP----REDLFVTSK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 100 AgydmwpgpygsWGSRKY---LTASLDQSLKRMGLDYVDIFYSH------RVD---PR----------TPLEETMGALDH 157
Cdd:cd19106 74 L-----------WNTKHHpedVEPALRKTLKDLQLDYLDLYLIHwpyafeRGDnpfPKnpdgtirydsTHYKETWKAMEK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 158 AVRQGKALYVGISSYSpemTRRAAAILKDLG-TPCLIHQPSYSMLNrwiEGGLLDALEETGIGCIAFSPLaqgmlttkyl 236
Cdd:cd19106 143 LVDKGLVKAIGLSNFN---SRQIDDILSVARiKPAVLQVECHPYLA---QNELIAHCKARGLVVTAYSPL---------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 237 nGQPTDARAAKGgtlkahflSPENLERVRaLDAIATRRGQTLAQMAIAW-----VLRDPR-VTSALVgARNVEQLDNSLd 310
Cdd:cd19106 207 -GSPDRPWAKPD--------EPVLLEEPK-VKALAKKYNKSPAQILLRWqvqrgVVVIPKsVTPSRI-KQNIQVFDFTL- 274
|
330
....*....|....*.
gi 1333942756 311 alkntafTPEELAEID 326
Cdd:cd19106 275 -------SPEEMKQLD 283
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
23-334 |
2.88e-05 |
|
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: 45.10 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 23 SGLDLPAISLGLWQ--NfggtdvfETGRAVLRRAFDRGVTHFDLANNYGpppgsAEENFGRVLATDFK---AHRDELIVS 97
Cdd:cd19115 9 SGYDMPLVGFGLWKvnN-------DTCADQVYNAIKAGYRLFDGACDYG-----NEVEAGQGVARAIKegiVKREDLFIV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 98 TKagydMWpgpyGSWGSRKYLTASLDQSLKRMGLDYVDIFYSH------RVDP------------------RTPLEETMG 153
Cdd:cd19115 77 SK----LW----NTFHDGERVEPICRKQLADWGIDYFDLFLIHfpialkYVDPavryppgwfydgkkvefsNAPIQETWT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 154 ALDHAVRQGKALYVGISSYSPEMTR---RAAAILKdlGTPCLIHQPSYSmlnrwiEGGLLDALEETGIGCIAFSPLaqGM 230
Cdd:cd19115 149 AMEKLVDKGLARSIGVSNFSAQLLMdllRYARIRP--ATLQIEHHPYLT------QPRLVKYAQKEGIAVTAYSSF--GP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 231 LTTKYLNGQptdaraakggtlKAHFLSPenLERVRALDAIATRRGQTLAQMAIAWVLRdpRVTSALVGARNVEQLDNSLD 310
Cdd:cd19115 219 QSFLELDLP------------GAKDTPP--LFEHDVIKSIAEKHGKTPAQVLLRWATQ--RGIAVIPKSNNPKRLAQNLD 282
|
330 340
....*....|....*....|....*.
gi 1333942756 311 AlknTAF--TPEELAEIDrhAVDGGL 334
Cdd:cd19115 283 V---TGFdlEAEEIKAIS--ALDIGL 303
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
27-229 |
5.46e-05 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 44.29 E-value: 5.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 27 LPAISLGLWQnfggTDVFETGRAVLRrAFDRGVTHFDLANNYGpppgsAEENFGRVL-ATDFKahRDELIVSTKAgydmw 105
Cdd:PRK11565 15 MPQLGLGVWQ----ASNEEVITAIHK-ALEVGYRSIDTAAIYK-----NEEGVGKALkEASVA--REELFITTKL----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333942756 106 pgpygsWGSR-KYLTASLDQSLKRMGLDYVDIFYSHRVDPrtpleetmgALDHAV----------RQGKALYVGISSYSP 174
Cdd:PRK11565 78 ------WNDDhKRPREALEESLKKLQLDYVDLYLMHWPVP---------AIDHYVeawkgmielqKEGLIKSIGVCNFQI 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1333942756 175 EMTRRaaaILKDLGTPCLIHQPSysmLNRWIEGGLLDALEET-GIGCIAFSPLAQG 229
Cdd:PRK11565 143 HHLQR---LIDETGVTPVINQIE---LHPLMQQRQLHAWNAThKIQTESWSPLAQG 192
|
|
| |
