|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
14-322 |
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: 658.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 14 TYERCGKSGVQLPAISLGLWHNFGGVDRFSNSRAMVLRAFDLGITHFDLANNYGPPPGSAETTFGRILRRDLASYRDELI 93
Cdd:cd19151 1 KYNRCGRSGLKLPAISLGLWHNFGDVDRYENSRAMLRRAFDLGITHFDLANNYGPPPGSAEENFGRILKEDLKPYRDELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 94 VSTKAGWPMWPGPYGDWGSRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISSYSPE 173
Cdd:cd19151 81 ISTKAGYTMWPGPYGDWGSKKYLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGISNYPPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 174 ETRRAAHLLQTLGTACLIHQPNYSMFNRALEGGLLAVLGDLGIGCIVFSPLAQGLLTDRYLSGIPADSRAAKPHGFLKRE 253
Cdd:cd19151 161 EAREAAAILKDLGTPCLIHQPKYSMFNRWVEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYLNGIPEDSRAAKGSSFLKPE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1125162345 254 QVTEEVLAQVRRLNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAALDKRAFSDDELR 322
Cdd:cd19151 241 QITEEKLAKVRRLNEIAQARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALDNREFSEEELA 309
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
15-321 |
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: 553.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 15 YERCGKSGVQLPAISLGLWHNFGGVDRFSNSRAMVLRAFDLGITHFDLANNYGPPPGSAETTFGRILRRDLASYRDELIV 94
Cdd:cd19089 1 YRRCGRSGLHLPAISLGLWHNFGDYTSPEEARELLRTAFDLGITHFDLANNYGPPPGSAEENFGRILKRDLRPYRDELVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 95 STKAGWPMWPGPYGDWGSRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISSYSPEE 174
Cdd:cd19089 81 STKAGYGMWPGPYGDGGSRKYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPGAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 175 TRRAAHLLQTLGTACLIHQPNYSMFNRALEGGLLAVLGDLGIGCIVFSPLAQGLLTDRYLSGIPADSRAAKPHGFLKREQ 254
Cdd:cd19089 161 ARRAIALLRELGVPLIIHQPRYSLLDRWAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKYLNGIPPDSRRAAESKFLTEEA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1125162345 255 VTEEVLAQVRRLNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAALDKRAFSDDEL 321
Cdd:cd19089 241 LTPEKLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAALKNLDFSEEEL 307
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
14-321 |
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: 540.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 14 TYERCGKSGVQLPAISLGLWHNFGGVDRFSNSRAMVLRAFDLGITHFDLANNYGPPPGSAETTFGRILRRDLASYRDELI 93
Cdd:cd19150 1 QYRRCGKSGLKLPALSLGLWHNFGDDTPLETQRAILRTAFDLGITHFDLANNYGPPPGSAEENFGRILREDFAGYRDELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 94 VSTKAGWPMWPGPYGDWGSRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISSYSPE 173
Cdd:cd19150 81 ISTKAGYDMWPGPYGEWGSRKYLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYSPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 174 ETRRAAHLLQTLGTACLIHQPNYSMFNRALEG-GLLAVLGDLGIGCIVFSPLAQGLLTDRYLSGIPADSRAAKPHGFLKr 252
Cdd:cd19150 161 RTREAAAILRELGTPLLIHQPSYNMLNRWVEEsGLLDTLQELGVGCIAFTPLAQGLLTDKYLNGIPEGSRASKERSLSP- 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1125162345 253 EQVTEEVLAQVRRLNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAALDKRAFSDDEL 321
Cdd:cd19150 240 KMLTEANLNSIRALNEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGALDNLTFSADEL 308
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
1-329 |
5.73e-166 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 466.00 E-value: 5.73e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 1 MPYRPADIRYDAMTYERCGKSGVQLPAISLGLWHNFGGVDRFSNSRAMVLRAFDLGITHFDLANNYGPPPGSAETTFGRI 80
Cdd:PRK09912 1 MVWLANPERYGQMQYRYCGKSGLRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGPPPGSAEENFGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 81 LRRDLASYRDELIVSTKAGWPMWPGPYGDWGSRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSG 160
Cdd:PRK09912 81 LREDFAAYRDELIISTKAGYDMWPGPYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 161 KALYAGISSYSPEETRRAAHLLQTLGTACLIHQPNYSMFNRALE-GGLLAVLGDLGIGCIVFSPLAQGLLTDRYLSGIPA 239
Cdd:PRK09912 161 KALYVGISSYSPERTQKMVELLREWKIPLLIHQPSYNLLNRWVDkSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 240 DSR----AAKPHGfLKREQVTEEVLAQVRRLNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAALDKRA 315
Cdd:PRK09912 241 DSRmhreGNKVRG-LTPKMLTEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQALNNLT 319
|
330
....*....|....
gi 1125162345 316 FSDDELRTIDRILA 329
Cdd:PRK09912 320 FSTEELAQIDQHIA 333
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
13-329 |
2.56e-129 |
|
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: 371.82 E-value: 2.56e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 13 MTYERCGKSGVQLPAISLGLW---HNFGGVDRfSNSRAMVLRAFDLGITHFDLANNYGPppGSAETTFGRILRRDlasYR 89
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTMtfgGPWGGVDE-AEAIAILDAALDAGINFFDTADVYGP--GRSEELLGEALKGR---PR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 90 DELIVSTKAGWPMWPGPYGDWGSRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISS 169
Cdd:COG0667 75 DDVVIATKVGRRMGPGPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 170 YSPEETRRAAHLLQTLgTACLIHQPNYSMFNRALEGGLLAVLGDLGIGCIVFSPLAQGLLTDRYLSG--IPADSRAAkpH 247
Cdd:COG0667 155 YSAEQLRRALAIAEGL-PPIVAVQNEYSLLDRSAEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGatFPEGDRAA--T 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 248 GFLKREqVTEEVLAQVRRLNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAALDKRaFSDDELRTIDRI 327
Cdd:COG0667 232 NFVQGY-LTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADLE-LSAEDLAALDAA 309
|
..
gi 1125162345 328 LA 329
Cdd:COG0667 310 LA 311
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
22-314 |
3.28e-104 |
|
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: 307.21 E-value: 3.28e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 22 GVQLPAISLGLWHNFGGVDRFSNSRAMVLRAFDLGITHFDLANNYGPppGSAETTFGRILRRdlasY-RDELIVSTKAGW 100
Cdd:cd19074 1 GLKVSELSLGTWLTFGGQVDDEDAKACVRKAYDLGINFFDTADVYAA--GQAEEVLGKALKG----WpRESYVISTKVFW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 101 PMWPGPYgDWG-SRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISSYSPEETRRAA 179
Cdd:cd19074 75 PTGPGPN-DRGlSRKHIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 180 HLLQTLGTACLI-HQPNYSMFNRALEGGLLAVLGDLGIGCIVFSPLAQGLLTDRYLSGIPADSRAAKPH---GFLKREQV 255
Cdd:cd19074 154 DLARQFGLIPPVvEQPQYNMLWREIEEEVIPLCEKNGIGLVVWSPLAQGLLTGKYRDGIPPPSRSRATDednRDKKRRLL 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1125162345 256 TEEVLAQVRRLNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAALDKR 314
Cdd:cd19074 234 TDENLEKVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKASGVK 292
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
28-328 |
1.98e-83 |
|
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: 254.16 E-value: 1.98e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 28 ISLGLWHNFGGVDRFS--NSRAMVLRAFDLGITHFDLANNYGPppGSAETTFGRILRRDLAsYRDELIVSTKagWPMWPG 105
Cdd:pfam00248 1 IGLGTWQLGGGWGPISkeEALEALRAALEAGINFIDTAEVYGD--GKSEELLGEALKDYPV-KRDKVVIATK--VPDGDG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 106 PYGDWGSRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISSYSPEETRRAahlLQTL 185
Cdd:pfam00248 76 PWPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKA---LTKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 186 GTACLIHQPNYSMFNRALEGGLLAVLGDLGIGCIVFSPLAQGLLTDRYLSGIPADSRAAKPHgflkREQVTEEVLAQVRR 265
Cdd:pfam00248 153 KIPIVAVQVEYNLLRRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPGERRRL----LKKGTPLNLEALEA 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1125162345 266 LNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAALDKRaFSDDELRTIDRIL 328
Cdd:pfam00248 229 LEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALEFP-LSDEEVARIDELL 290
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
13-312 |
2.36e-82 |
|
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: 252.52 E-value: 2.36e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 13 MTYERCGKSGVQLPAISLGLWHNFGGVDRFSNSRAMVLRAFDLGITHFDLANNYGPppGSAETTFGRILRRdLASYRDEL 92
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSWVTFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYAN--GQSEEIMGQAIKE-LGWPRSDY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 93 IVSTKAGWPMWPGPYGDWG-SRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISSYS 171
Cdd:cd19143 78 VVSTKIFWGGGGPPPNDRGlSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGTSEWS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 172 PEETRRAAHLLQTLG-TACLIHQPNYSMFNRA-LEGGLLAVLGDLGIGCIVFSPLAQGLLTDRYLSGIPADSRAAKPHGF 249
Cdd:cd19143 158 AQQIEEAHEIADRLGlIPPVMEQPQYNLFHRErVEVEYAPLYEKYGLGTTTWSPLASGLLTGKYNNGIPEGSRLALPGYE 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1125162345 250 LKREQVTEEV---LAQVRRLNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAALD 312
Cdd:cd19143 238 WLKDRKEELGqekIEKVRKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEENLKALE 303
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
22-325 |
2.63e-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: 248.98 E-value: 2.63e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 22 GVQLPAISLGLW----HNFGGVDRfSNSRAMVLRAFDLGITHFDLANNYGPppGSAETTFGRILrrdlASYRDELIVSTK 97
Cdd:cd19084 1 DLKVSRIGLGTWaiggTWWGEVDD-QESIEAIKAAIDLGINFFDTAPVYGF--GHSEEILGKAL----KGRRDDVVIATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 98 AGwPMWPGPYGDW--GSRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISSYSPEET 175
Cdd:cd19084 74 CG-LRWDGGKGVTkdLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 176 RRAAHLLQtlgtaCLIHQPNYSMFNRALEGGLLAVLGDLGIGCIVFSPLAQGLLTDRYLSGI---PADSRAAKPhgFLKR 252
Cdd:cd19084 153 EEARKYGP-----IVSLQPPYSMLEREIEEELLPYCRENGIGVLPYGPLAQGLLTGKYKKEPtfpPDDRRSRFP--FFRG 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1125162345 253 EQVtEEVLAQVRRLNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAALDKRaFSDDELRTID 325
Cdd:cd19084 226 ENF-EKNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDWE-LTEEELKEID 296
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
15-325 |
6.96e-73 |
|
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: 227.85 E-value: 6.96e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 15 YERCGKSGVQLPAISLGLWHnFGGVDR------FSNSRAMVLRAFDLGITHFDLANNYGPppGSAETTFGRILRRDLasY 88
Cdd:cd19079 2 YVRLGNSGLKVSRLCLGCMS-FGDPKWrpwvldEEESRPIIKRALDLGINFFDTANVYSG--GASEEILGRALKEFA--P 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 89 RDELIVSTKAGWPMWPGPYGDWGSRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGIS 168
Cdd:cd19079 77 RDEVVIATKVYFPMGDGPNGRGLSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGAS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 169 SYSPEETRRAAHLLQTLGTACLIH-QPNYSMFNRALEGGLLAVLGDLGIGCIVFSPLAQGLLTDRYLSGIPADSRAAKPh 247
Cdd:cd19079 157 SMYAWQFAKALHLAEKNGWTKFVSmQNHYNLLYREEEREMIPLCEEEGIGVIPWSPLARGRLARPWGDTTERRRSTTDT- 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1125162345 248 GFLKREQVTEEVLAQVRRLNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAALDKRaFSDDELRTID 325
Cdd:cd19079 236 AKLKYDYFTEADKEIVDRVEEVAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAALDIK-LSEEEIKYLE 312
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
13-327 |
1.15e-72 |
|
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: 227.46 E-value: 1.15e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 13 MTYERCGKSGVQLPAISLGLWhNFGG-VDRfSNSRAMVLRAFDLGITHFDLANNYGPppGSAETtfgrILRRDLASYRDE 91
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGTM-NFGGrTDE-ETSFAIMDRALDAGINFFDTADVYGG--GRSEE----IIGRWIAGRRDD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 92 LIVSTKAGWPMWPGPYGDWGSRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISSYS 171
Cdd:cd19087 73 IVLATKVFGPMGDDPNDRGLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNFA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 172 PEETRRAAHLLQTLGTACLI-HQPNYSMFNRALEGGLLAVLGDLGIGCIVFSPLAQGLLTDRYLSGIPADSRAAKPHGFL 250
Cdd:cd19087 153 AWQIAKAQGIAARRGLLRFVsEQPMYNLLKRQAELEILPAARAYGLGVIPYSPLAGGLLTGKYGKGKRPESGRLVERARY 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1125162345 251 KREQVTEEVLAQVRRLNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAALDKRaFSDDELRTIDRI 327
Cdd:cd19087 233 QARYGLEEYRDIAERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEIT-LTPELLAEIDEL 308
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
25-327 |
2.68e-68 |
|
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: 215.53 E-value: 2.68e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 25 LPAISLGLW-----HNFGGVDRfSNSRAMVLRAFDLGITHFDLANNYGPppGSAETTFGRILRRDlasyRDELIVSTKAg 99
Cdd:cd19085 1 VSRLGLGCWqfgggYWWGDQDD-EESIATIHAALDAGINFFDTAEAYGD--GHSEEVLGKALKGR----RDDVVIATKV- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 100 wpmwpgpYGDWGSRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISSYSPEETRRAA 179
Cdd:cd19085 73 -------SPDNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 180 hllqTLGTaCLIHQPNYSMFNRALEGGLLAVLGDLGIGCIVFSPLAQGLLTDRYLSGI---PADSRaaKPHGFLKREQVT 256
Cdd:cd19085 146 ----DAGR-IDSNQLPYNLLWRAIEYEILPFCREHGIGVLAYSPLAQGLLTGKFSSAEdfpPGDAR--TRLFRHFEPGAE 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1125162345 257 EEVLAQVRRLNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAALDKRAfSDDELRTIDRI 327
Cdd:cd19085 219 EETFEALEKLKEIADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVDLEL-SPSVLERLDEI 288
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
26-309 |
6.20e-68 |
|
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: 212.38 E-value: 6.20e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 26 PAISLGLWHnFGGVDRFSNSRAMVLRAFDLGITHFDLANNYGPppGSAETTFGRILRRDlaSYRDELIVSTKAGWPMWPG 105
Cdd:cd06660 1 SRLGLGTMT-FGGDGDEEEAFALLDAALEAGGNFFDTADVYGD--GRSERLLGRWLKGR--GNRDDVVIATKGGHPPGGD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 106 PYGDWGSRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISSYSPEETRRAAHLLQTL 185
Cdd:cd06660 76 PSRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKAH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 186 GTACLI-HQPNYSMFNR-ALEGGLLAVLGDLGIGCIVFSPLAQGlltdrylsgipadsraakphgflkreqvteevlaqv 263
Cdd:cd06660 156 GLPGFAaVQPQYSLLDRsPMEEELLDWAEENGLPLLAYSPLARG------------------------------------ 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1125162345 264 rrlnecarargqtLAQMALAWVLRHREVTAALIGASRPGHIEDAVA 309
Cdd:cd06660 200 -------------PAQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
13-327 |
4.93e-63 |
|
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: 202.84 E-value: 4.93e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 13 MTYERCGKSGVQLPAISLG---------LWHNFGGVDRfSNSRAMVLRAFDLGITHFDLANNYGPppGSAEttfgRILRR 83
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGtmtfgggggFFGAWGGVDQ-EEADRLVDIALDAGINFFDTADVYSE--GESE----EILGK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 84 DLASYRDELIVSTKAGWPMWPGPYGDWGSRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKAL 163
Cdd:cd19091 74 ALKGRRDDVLIATKVRGRMGEGPNDVGLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 164 YAGISSYSpeetrrAAHLLQTLGTACL-------IHQPNYSMFNRALEGGLLAVLGDLGIGCIVFSPLAQGLLTDRYLSG 236
Cdd:cd19091 154 YIGVSNFS------AWQIMKALGISERrglarfvALQAYYSLLGRDLEHELMPLALDQGVGLLVWSPLAGGLLSGKYRRG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 237 --IPADSRAAKPHGFLKReqVTEE-VLAQVRRLNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAALDK 313
Cdd:cd19091 228 qpAPEGSRLRRTGFDFPP--VDRErGYDVVDALREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGAAGL 305
|
330
....*....|....
gi 1125162345 314 RaFSDDELRTIDRI 327
Cdd:cd19091 306 S-LTPEEIARLDKV 318
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
19-324 |
2.53e-60 |
|
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: 195.51 E-value: 2.53e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 19 GKSGVQLPAISLG---LWHNFGGVDRfSNSRAMVLRAFDLGITHFDLANNYGPppGSAETTFGRILRRdlasYRDELIVS 95
Cdd:cd19076 6 GTQGLEVSALGLGcmgMSAFYGPADE-EESIATLHRALELGVTFLDTADMYGP--GTNEELLGKALKD----RRDEVVIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 96 TKAGWPMWPGPY--GDWGSRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISSYSPE 173
Cdd:cd19076 79 TKFGIVRDPGSGfrGVDGRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLSEASAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 174 ETRRAA--HLLQTLgtaclihQPNYSMFNRALEGGLLAVLGDLGIGCIVFSPLAQGLLTDRYLSgiPADSRAAKPHGFLK 251
Cdd:cd19076 159 TIRRAHavHPITAV-------QSEYSLWTRDIEDEVLPTCRELGIGFVAYSPLGRGFLTGAIKS--PEDLPEDDFRRNNP 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1125162345 252 REQvtEEV----LAQVRRLNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAALDKRaFSDDELRTI 324
Cdd:cd19076 230 RFQ--GENfdknLKLVEKLEAIAAEKGCTPAQLALAWVLAQGDDIVPIPGTKRIKYLEENVGALDVV-LTPEELAEI 303
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
19-325 |
2.48e-59 |
|
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: 192.81 E-value: 2.48e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 19 GKSGVQLPAISLGLWhNFG-GVDRfSNSRAMVLRAFDLGITHFDLANNY-----GPPPGSAETTFGRILRRDLAsyRDEL 92
Cdd:cd19081 3 GRTGLSVSPLCLGTM-VFGwTADE-ETSFALLDAFVDAGGNFIDTADVYsawvpGNAGGESETIIGRWLKSRGK--RDRV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 93 IVSTKAGWPMWPGPYGdwGSRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISSYSP 172
Cdd:cd19081 79 VIATKVGFPMGPNGPG--LSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYSA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 173 EETRRAAHLLQTLGTA---CLihQPNYSMFNRA-LEGGLLAVLGDLGIGCIVFSPLAQGLLTDRYLSGIPADSRAAKPHG 248
Cdd:cd19081 157 WRLQEALELSRQHGLPryvSL--QPEYNLVDREsFEGELLPLCREEGIGVIPYSPLAGGFLTGKYRSEADLPGSTRRGEA 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1125162345 249 FLKREqvTEEVLAQVRRLNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAALDKRaFSDDELRTID 325
Cdd:cd19081 235 AKRYL--NERGLRILDALDEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAGLR-LTDEEVARLD 308
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
25-328 |
1.00e-57 |
|
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: 188.65 E-value: 1.00e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 25 LPAISLGLW-----HNFGGV----DRfsNSRAMVLRAFDLGITHFDLANNYGPppGSAETTFGRILRRdlasYRDELIVS 95
Cdd:cd19102 1 LTTIGLGTWaigggGWGGGWgpqdDR--DSIAAIRAALDLGINWIDTAAVYGL--GHSEEVVGRALKG----LRDRPIVA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 96 TKAGwPMW--PGPYGDWGSRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISSYSPE 173
Cdd:cd19102 73 TKCG-LLWdeEGRIRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 174 ETRRAA--HLLQTLgtaclihQPNYSMFNRALEGGLLAVLGDLGIGCIVFSPLAQGLLT-----DRYLSGIPADSRAAKP 246
Cdd:cd19102 152 QMKRCQaiHPIASL-------QPPYSLLRRGIEAEILPFCAEHGIGVIVYSPMQSGLLTgkmtpERVASLPADDWRRRSP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 247 hgflkreQVTEEVLAQ----VRRLNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAALDKRaFSDDELR 322
Cdd:cd19102 225 -------FFQEPNLARnlalVDALRPIAERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAADLR-LTPEELA 296
|
....*.
gi 1125162345 323 TIDRIL 328
Cdd:cd19102 297 EIEALL 302
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
30-328 |
3.19e-52 |
|
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: 174.34 E-value: 3.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 30 LGLWHNFGGVDRFSNSRAMVLRAFDLGITHFDLANNYGPPpgSAETTFGRILrrdlASYRDELIVSTKAGWPMWPGPYGD 109
Cdd:cd19078 12 MGMSHGYGPPPDKEEMIELIRKAVELGITFFDTAEVYGPY--TNEELVGEAL----KPFRDQVVIATKFGFKIDGGKPGP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 110 WG--SRKYLI-ASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISSYSPEETRRaAHLLQTLg 186
Cdd:cd19078 86 LGldSRPEHIrKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETIRR-AHAVCPV- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 187 TAClihQPNYSMFNRALEGGLLAVLGDLGIGCIVFSPLAQGLLTDRYLSGI---PADSRAAKPhgflkreQVTEEVLAQ- 262
Cdd:cd19078 164 TAV---QSEYSMMWREPEKEVLPTLEELGIGFVPFSPLGKGFLTGKIDENTkfdEGDDRASLP-------RFTPEALEAn 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1125162345 263 ---VRRLNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAALDKRaFSDDELRTIDRIL 328
Cdd:cd19078 234 qalVDLLKEFAEEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAADIE-LTPEELREIEDAL 301
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
15-311 |
1.98e-51 |
|
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: 172.63 E-value: 1.98e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 15 YERCGKSGVQLPAISLGLWHNFGGvdRFSNSRA--MVLRAFDLGITHFDLANNYGPppGSAETTFGRILRRDlASYRDEL 92
Cdd:cd19141 2 YRNLGKSGLRVSCLGLGTWVTFGS--QISDEVAeeLVTLAYENGINLFDTAEVYAA--GKAEIVLGKILKKK-GWRRSSY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 93 IVSTKAGWpmwpGPYGDWG---SRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISS 169
Cdd:cd19141 77 VITTKIFW----GGKAETErglSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 170 YSPEETRRAAHLLQTLGtacLI----HQPNYSMFNR-ALEGGLLAVLGDLGIGCIVFSPLAQGLLTDRYLSGIPADSRAA 244
Cdd:cd19141 153 WSAMEIMEAYSVARQFN---LIppivEQAEYHLFQReKVEMQLPELFHKIGVGAMTWSPLACGILSGKYDDGVPEYSRAS 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1125162345 245 -KPHGFLKREQVTEEVLAQVRRLNEC---ARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAAL 311
Cdd:cd19141 230 lKGYQWLKEKILSEEGRRQQAKLKELqiiADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQAI 300
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
19-325 |
4.14e-51 |
|
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: 171.63 E-value: 4.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 19 GKSGVQLPAISLGLWhNFG-----GVDRfSNSRAMVLRAFDLGITHFDLANNYgpPPGSAETTFGRILrrdlASYRDELI 93
Cdd:cd19080 4 GRSGLRVSPLALGTM-TFGtewgwGADR-EEARAMFDAYVEAGGNFIDTANNY--TNGTSERLLGEFI----AGNRDRIV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 94 VSTKAGWPMWPG-PYGDWGSRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISSYSP 172
Cdd:cd19080 76 LATKYTMNRRPGdPNAGGNHRKNLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDTPA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 173 EETRRAAHLLQTLGTACLI-HQPNYSMFNRALEGGLLAVLGDLGIGCIVFSPLAQGLLTDRYLSGIPADSRAAKPHGFLK 251
Cdd:cd19080 156 WVVARANTLAELRGWSPFVaLQIEYSLLERTPERELLPMARALGLGVTPWSPLGGGLLTGKYQRGEEGRAGEAKGVTVGF 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1125162345 252 REQvTEEVLAQVRRLNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAALDkRAFSDDELRTID 325
Cdd:cd19080 236 GKL-TERNWAIVDVVAAVAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALD-LTLSPEQLARLD 307
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
13-331 |
4.94e-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: 172.19 E-value: 4.94e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 13 MTYERCGKSGVQLPAISLGLWHNFGGVDRFSNSRAMVLRAFDLGITHFDLANNYGPppGSAETTFGRILRRDlASYRDEL 92
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAA--GKAEVVLGNIIKKK-GWRRSSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 93 IVSTKAGWpmwpGPYGDWG---SRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISS 169
Cdd:cd19158 78 VITTKIFW----GGKAETErglSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 170 YSPEETRRAAHLLQTLG-TACLIHQPNYSMFNR-ALEGGLLAVLGDLGIGCIVFSPLAQGLLTDRYLSGIPADSRAA-KP 246
Cdd:cd19158 154 WSSMEIMEAYSVARQFNlIPPICEQAEYHMFQReKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASlKG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 247 HGFLKREQVTEE---VLAQVRRLNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAALDK-RAFSDDELR 322
Cdd:cd19158 234 YQWLKDKILSEEgrrQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVlPKLSSSIVH 313
|
....*....
gi 1125162345 323 TIDRILaGN 331
Cdd:cd19158 314 EIDSIL-GN 321
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
13-311 |
9.01e-51 |
|
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: 9.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 13 MTYERCGKSGVQLPAISLGLWHNFGGVDRFSNSRAMVLRAFDLGITHFDLANNYGPppGSAETTFGRILRRDlASYRDEL 92
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAA--GKAEVILGSIIKKK-GWRRSSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 93 IVSTKAGWpmwpGPYGDWG---SRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISS 169
Cdd:cd19159 78 VITTKLYW----GGKAETErglSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 170 YSPEETRRA---AHLLQTLGTACliHQPNYSMFNR-ALEGGLLAVLGDLGIGCIVFSPLAQGLLTDRYLSGIPADSRAA- 244
Cdd:cd19159 154 WSAMEIMEAysvARQFNMIPPVC--EQAEYHLFQReKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASl 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 245 KPHGFLKREQVTEEVLAQVRRLNE---CARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAAL 311
Cdd:cd19159 232 KCYQWLKERIVSEEGRKQQNKLKDlspIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAI 301
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
26-327 |
2.11e-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: 169.66 E-value: 2.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 26 PAISLGLwHNFGGVDRFSN--SRAMVLRAF-DLGITHFDLANNYgpPPGSAETTFGRILrrdlASYRDeLIVSTKAgwPM 102
Cdd:cd19075 1 PKIILGT-MTFGSQGRFTTaeAAAELLDAFlERGHTEIDTARVY--PDGTSEELLGELG----LGERG-FKIDTKA--NP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 103 WPGPygdWGSRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISSYSPEETRRAAHLL 182
Cdd:cd19075 71 GVGG---GLSPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEIC 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 183 QTLG----TaclIHQPNYSMFNRALEGGLLAVLGDLGIGCIVFSPLAQGLLTDRYLSG--IPADSR--AAKPHGFLKREQ 254
Cdd:cd19075 148 KENGwvlpT---VYQGMYNAITRQVETELFPCLRKLGIRFYAYSPLAGGFLTGKYKYSedKAGGGRfdPNNALGKLYRDR 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1125162345 255 -VTEEVLAQVRRLNECARARGQTLAQMALAWVLRHREVTAA-----LIGASRPGHIEDAVAALDKRAFSDDELRTIDRI 327
Cdd:cd19075 225 yWKPSYFEALEKVEEAAEKEGISLAEAALRWLYHHSALDGEkgdgvILGASSLEQLEENLAALEKGPLPEEVVKAIDEA 303
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
15-325 |
2.10e-49 |
|
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: 167.45 E-value: 2.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 15 YERCGKSGVQLPAISLGLW-----HNFGGVDRfSNSRAMVLRAFDLGITHFDLANNYGpppgsaettFG---RILRRDLA 86
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTWaigggPWWGGSDD-NESIRTIHAALDLGINLIDTAPAYG---------FGhseEIVGKAIK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 87 SYRDELIVSTKAGWpMWPGPYGDWGS-------RKYLIAS-----LDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALD 154
Cdd:cd19149 71 GRRDKVVLATKCGL-RWDREGGSFFFvrdgvtvYKNLSPEsireeVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 155 HAVRSGKALYAGISSYSPEETRRAahllQTLGTACLIhQPNYSMFNRALEGGLLAVLGDLGIGCIVFSPLAQGLLTDRY- 233
Cdd:cd19149 150 ELKRQGKIRAIGASNVSVEQIKEY----VKAGQLDII-QEKYSMLDRGIEKELLPYCKKNNIAFQAYSPLEQGLLTGKIt 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 234 --LSGIPADSRAAKPhgFLKREQVtEEVLAQVRRLNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAAL 311
Cdd:cd19149 225 pdREFDAGDARSGIP--WFSPENR-EKVLALLEKWKPLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPEQAEENAKAG 301
|
330
....*....|....
gi 1125162345 312 DKRaFSDDELRTID 325
Cdd:cd19149 302 DIR-LSAEDIATMR 314
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
19-327 |
4.71e-49 |
|
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: 166.44 E-value: 4.71e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 19 GKSGVQLPAISLGLwHNFGGVDRFSN-----SRAMVLRAFDLGITHFDLANNYGPppGSAETTFGRILRrdlASYRDELI 93
Cdd:cd19083 5 GKSDIDVNPIGLGT-NAVGGHNLYPNldeeeGKDLVREALDNGVNLLDTAFIYGL--GRSEELVGEVLK---EYNRNEVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 94 VSTKAGWPMWPGPYGDWGSRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISSYSPE 173
Cdd:cd19083 79 IATKGAHKFGGDGSVLNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFSLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 174 ETRRAAH--LLQTLgtaclihQPNYSMFNRALEGGLLAVLGDLGIGCIVFSPLAQGLLTDRYLSGI---PADSRAAKPHg 248
Cdd:cd19083 159 QLKEANKdgYVDVL-------QGEYNLLQREAEEDILPYCVENNISFIPYFPLASGLLAGKYTKDTkfpDNDLRNDKPL- 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1125162345 249 fLKREQVTEEvLAQVRRLNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAALDKRaFSDDELRTIDRI 327
Cdd:cd19083 231 -FKGERFSEN-LDKVDKLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKALDVT-LTEEEIAFIDAL 306
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
24-325 |
1.46e-48 |
|
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: 164.71 E-value: 1.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 24 QLPAISLGLWH------NFGGVDRFSNSRAMVLRAFDLGITHFDLANNYGPppGSAETTFGRILRRDLAsyRDELIVSTK 97
Cdd:cd19093 1 EVSPLGLGTWQwgdrlwWGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYGT--GRSERLLGRFLKELGD--RDEVVIATK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 98 -AGWPmWPGPYGDwgsrkyLIASLDQSLRRMGLEYVDIFYHHRPDP-DTPLEETMGALDHAVRSGKALYAGISSYSPEET 175
Cdd:cd19093 77 fAPLP-WRLTRRS------VVKALKASLERLGLDSIDLYQLHWPGPwYSQIEALMDGLADAVEEGLVRAVGVSNYSADQL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 176 RRAAHLLQTLGTACLIHQPNYSMFNR-ALEGGLLAVLGDLGIGCIVFSPLAQGLLTDRY-LSGIPADSRAAKPhGFLKRE 253
Cdd:cd19093 150 RRAHKALKERGVPLASNQVEYSLLYRdPEQNGLLPACDELGITLIAYSPLAQGLLTGKYsPENPPPGGRRRLF-GRKNLE 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1125162345 254 QVtEEVLAQVRRLnecARARGQTLAQMALAWVLRHREVtaALIGASRPGHIEDAVAALDKRaFSDDELRTID 325
Cdd:cd19093 229 KV-QPLLDALEEI---AEKYGKTPAQVALNWLIAKGVV--PIPGAKNAEQAEENAGALGWR-LSEEEVAELD 293
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
24-310 |
2.65e-48 |
|
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: 162.26 E-value: 2.65e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 24 QLPAISLGLWhNFGG-----VDRfSNSRAMVLRAFDLGITHFDLANNYGPppGSAETTFGRILRRDlasyRDELIVSTKA 98
Cdd:cd19086 2 EVSEIGFGTW-GLGGdwwgdVDD-AEAIRALRAALDLGINFFDTADVYGD--GHSERLLGKALKGR----RDKVVIATKF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 99 GWPMWPGPYGDWG-SRKYLIASLDQSLRRMGLEYVDIFYHHRPDPD-TPLEETMGALDHAVRSGKALYAGISSYSPEEtr 176
Cdd:cd19086 74 GNRFDGGPERPQDfSPEYIREAVEASLKRLGTDYIDLYQLHNPPDEvLDNDELFEALEKLKQEGKIRAYGVSVGDPEE-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 177 rAAHLLQTLGTACLihQPNYSMFNRALEGGLLAVLGDLGIGCIVFSPLAQGLLTDRylsgipadsraakphgflkreqvt 256
Cdd:cd19086 152 -ALAALRRGGIDVV--QVIYNLLDQRPEEELFPLAEEHGVGVIARVPLASGLLTGK------------------------ 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1125162345 257 eevlaqvrrlnecarargqtLAQMALAWVLRHREVTAALIGASRPGHIEDAVAA 310
Cdd:cd19086 205 --------------------LAQAALRFILSHPAVSTVIPGARSPEQVEENAAA 238
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
43-312 |
2.91e-48 |
|
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: 162.77 E-value: 2.91e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 43 SNSRAMVLRAFDLGITHFDLANNYGPppGSAEttfgRILRRDLASYRDELIVSTKAGWpMWPGPyGDW---GSRKYLIAS 119
Cdd:cd19088 24 EEAIAVLRRALELGVNFIDTADSYGP--DVNE----RLIAEALHPYPDDVVIATKGGL-VRTGP-GWWgpdGSPEYLRQA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 120 LDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISSYSPEETRRAAHLLQtlgTACLihQPNYSMF 199
Cdd:cd19088 96 VEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAIVR---IVSV--QNRYNLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 200 NRALEgGLLAVLGDLGIGCIVFSPLAQGLLtdrylsgipadsraakphgflkreqvteevLAQVRRLNECARARGQTLAQ 279
Cdd:cd19088 171 NRDDE-GVLDYCEAAGIAFIPWFPLGGGDL------------------------------AQPGGLLAEVAARLGATPAQ 219
|
250 260 270
....*....|....*....|....*....|...
gi 1125162345 280 MALAWVLRHREVTAALIGASRPGHIEDAVAALD 312
Cdd:cd19088 220 VALAWLLARSPVMLPIPGTSSVEHLEENLAAAG 252
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
13-311 |
4.02e-46 |
|
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: 159.38 E-value: 4.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 13 MTYERCGKSGVQLPAISLGLWHNFGGVDRFSNSRAMVLRAFDLGITHFDLANNYGPppGSAETTFGRILRRDlASYRDEL 92
Cdd:cd19160 3 MKYRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDLLTVAYEHGVNLFDTAEVYAA--GKAERTLGNILKSK-GWRRSSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 93 IVSTKAGWpmwpGPYGDWG---SRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISS 169
Cdd:cd19160 80 VVTTKIYW----GGQAETErglSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 170 YSPEETRRA---AHLLQTLGTACliHQPNYSMFNR-ALEGGLLAVLGDLGIGCIVFSPLAQGLLTDRYLSGIPADSRAA- 244
Cdd:cd19160 156 WSAMEIMEAysvARQFNLIPPVC--EQAEYHLFQReKVEMQLPELYHKIGVGSVTWSPLACGLITGKYDGRVPDTCRAAv 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 245 KPHGFLKREQVTEE---VLAQVRRLNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAAL 311
Cdd:cd19160 234 KGYQWLKEKVQSEEgkkQQAKVKELHPIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGSI 303
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
13-331 |
4.10e-46 |
|
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: 159.17 E-value: 4.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 13 MTYERCGKSGVQLPAISLGLWHNFGGVDRFSNSRAMVLRAFDLGITHFDLANnyGPPPGSAETTFGRILRRDlASYRDEL 92
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGTWSTFSTAISEEQAEEIVTLAYENGINYFDTSD--AFTSGQAETELGRILKKK-GWKRSSY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 93 IVSTKAGWPMwpGPYGDWGSRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISSYSP 172
Cdd:cd19142 78 IVSTKIYWSY--GSEERGLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRWSP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 173 eetrraAHLLQTLGTA----C---LIHQPNYSMFNR-ALEGGLLAVLGDLGIGCIVFSPLAQGLLTDRYLSGIPADSRAA 244
Cdd:cd19142 156 ------VEIMEAFSIArqfnCptpICEQSEYHMFCReKMELYMPELYNKVGVGLITWSPLSLGLDPGISEETRRLVTKLS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 245 KPHGFLKREQVTEEVLAQVRR-------LNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAALDKRA-F 316
Cdd:cd19142 230 FKSSKYKVGSDGNGIHEETRRashklreLSLIAERLGCDLTQLLIAWSLKNENVQCVLIGASSLEQLYSQLNSLQLLPkL 309
|
330
....*....|....*
gi 1125162345 317 SDDELRTIDRILAGN 331
Cdd:cd19142 310 NSAVMEELERILDNK 324
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
35-312 |
1.61e-44 |
|
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: 153.86 E-value: 1.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 35 NFGGVDRFSNSRAMVLRAFDLGITHFDLANNYG--PPPGSAETTFGRILR-RDLasyRDELIVSTKAGWPMWPGPYGDWG 111
Cdd:cd19082 9 DFGTRIDEEEAFALLDAFVELGGNFIDTARVYGdwVERGASERVIGEWLKsRGN---RDKVVIATKGGHPDLEDMSRSRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 112 SRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISSYSPEETRRA-----AHLLQTLg 186
Cdd:cd19082 86 SPEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNWSTERIAEAnayakAHGLPGF- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 187 tacLIHQPNYS---MFNRALEGGLLAVLGD--------LGIGCIVFSPLAQGLLTDRYLSGIPADSRAAKPHGflkreqv 255
Cdd:cd19082 165 ---AASSPQWSlarPNEPPWPGPTLVAMDEemrawheeNQLPVFAYSSQARGFFSKRAAGGAEDDSELRRVYY------- 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1125162345 256 TEEVLAQVRRLNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAALD 312
Cdd:cd19082 235 SEENFERLERAKELAEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAAAD 291
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
26-310 |
2.43e-44 |
|
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: 152.39 E-value: 2.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 26 PAISLGLWHNFGGVDRFS--NSRAMVLRAFDLGITHFDLANNYGpppgSAETTFGRILRRDLasyRDELIVSTKAG--WP 101
Cdd:cd19095 1 SVLGLGTSGIGRVWGVPSeaEAARLLNTALDLGINLIDTAPAYG----RSEERLGRALAGLR---RDDLFIATKVGthGE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 102 MwPGPYGDWgSRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISSYSPEetrrAAHL 181
Cdd:cd19095 74 G-GRDRKDF-SPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVSGDGEE----LEAA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 182 LQTLGTACLihQPNYSMFNRALEgGLLAVLGDLGIGCIVFSPLAQGLLTDRYLSGIPADSRAAKPHGFLKREqvteevla 261
Cdd:cd19095 148 IASGVFDVV--QLPYNVLDREEE-ELLPLAAEAGLGVIVNRPLANGRLRRRVRRRPLYADYARRPEFAAEIG-------- 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1125162345 262 qvrrlnecararGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAA 310
Cdd:cd19095 217 ------------GATWAQAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
35-327 |
7.60e-44 |
|
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: 153.10 E-value: 7.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 35 NFGGVDRFSNSRAMVLRAFDLGITHFDLANNYGPPP-----GSAETTFGRILRRDlaSYRDELIVSTK-AGwpmwPGPYG 108
Cdd:cd19094 10 TWGEQNTEAEAHEQLDYAFDEGVNFIDTAEMYPVPPspetqGRTEEIIGSWLKKK--GNRDKVVLATKvAG----PGEGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 109 DWGS-------RKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPL------------------EETMGALDHAVRSGKAL 163
Cdd:cd19094 84 TWPRgggtrldRENIREAVEGSLKRLGTDYIDLYQLHWPDRYTPLfgggyytepseeedsvsfEEQLEALGELVKAGKIR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 164 YAGISSYSPEETRRAAHLLQTLGT--ACLIhQPNYSMFNRALEGGLLAVLGDLGIGCIVFSPLAQGLLTDRYLSG--IPA 239
Cdd:cd19094 164 HIGLSNETPWGVMKFLELAEQLGLprIVSI-QNPYSLLNRNFEEGLAEACHRENVGLLAYSPLAGGVLTGKYLDGaaRPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 240 DSRAAKPHGFLKREQvTEEVLAQVRRLNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAALDkRAFSDD 319
Cdd:cd19094 243 GGRLNLFPGYMARYR-SPQALEAVAEYVKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLKENIDAFD-VPLSDE 320
|
....*...
gi 1125162345 320 ELRTIDRI 327
Cdd:cd19094 321 LLAEIDAV 328
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
13-312 |
2.05e-43 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 151.46 E-value: 2.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 13 MTYERCGKSGVQLPAISLGLWHnFGGVDrFSNS--RAMVLRAFDLGITHFDLANNYGPppGSAETTFGRILRRDlASYRD 90
Cdd:COG4989 1 MKRIKLGASGLSVSRIVLGCMR-LGEWD-LSPAeaAALIEAALELGITTFDHADIYGG--YTCEALFGEALKLS-PSLRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 91 ELIVSTKAG-------WPMWPGPYgDWgSRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKAL 163
Cdd:COG4989 76 KIELQTKCGirlpseaRDNRVKHY-DT-SKEHIIASVEGSLRRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELKASGKVR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 164 YAGISSYSPEETRraahLLQT-LGTACLIHQPNYSMFNR-ALEGGLLAVLGDLGIGCIVFSPLAQGLLTdrylsgipads 241
Cdd:COG4989 154 HFGVSNFTPSQFE----LLQSaLDQPLVTNQIELSLLHTdAFDDGTLDYCQLNGITPMAWSPLAGGRLF----------- 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1125162345 242 raakpHGFLKREQVTEEVLAQVrrlnecARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAALD 312
Cdd:COG4989 219 -----GGFDEQFPRLRAALDEL------AEKYGVSPEAIALAWLLRHPAGIQPVIGTTNPERIKAAAAALD 278
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
22-325 |
5.20e-42 |
|
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: 146.61 E-value: 5.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 22 GVQLPAISLGLWhNFGGVDRFSNSR-----AMVLRAFDLGITHFDLANNYGPppGSAEttfgRILRRDLASY-RDELIVS 95
Cdd:cd19072 1 GEEVPVLGLGTW-GIGGGMSKDYSDdkkaiEALRYAIELGINLIDTAEMYGG--GHAE----ELVGKAIKGFdREDLFIT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 96 TKAgWPmWPGPYGDwgsrkyLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISSYSPEET 175
Cdd:cd19072 74 TKV-SP-DHLKYDD------VIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 176 RRA-AHLLQTLGTACLIHqpnYSMFNRALEGGLLAVLGDLGIGCIVFSPLAQGLLTdrylsgipadsraakphgflkreq 254
Cdd:cd19072 146 EEAqSYLKKGPIVANQVE---YNLFDREEESGLLPYCQKNGIAIIAYSPLEKGKLS------------------------ 198
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1125162345 255 vteeVLAQVRRLNECARARGQTLAQMALAWVLRHrEVTAALIGASRPGHIEDAVAALDKRaFSDDELRTID 325
Cdd:cd19072 199 ----NAKGSPLLDEIAKKYGKTPAQIALNWLISK-PNVIAIPKASNIEHLEENAGALGWE-LSEEDLQRLD 263
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
26-310 |
6.61e-42 |
|
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: 146.93 E-value: 6.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 26 PAISLG---LWHNFGGVDrFSNSRAMVLRAFDLGITHFDLANNYGPppgsAETTFGRILRRdlaSYRDELIVSTKAGWPm 102
Cdd:cd19090 1 SALGLGtagLGGVFGGVD-DDEAVATIRAALDLGINYIDTAPAYGD----SEERLGLALAE---LPREPLVLSTKVGRL- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 103 wPGPYGDWgSRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETM--GALD--HAVRS-GKALYAGISSYSPEETRR 177
Cdd:cd19090 72 -PEDTADY-SADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILApgGALEalLELKEeGLIKHIGLGGGPPDLLRR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 178 AahlLQT-LGTACLIHQpNYSMFNRALEGGLLAVLGDLGIGCIVFSPLAQGLLTDRYLSGIPAdsraakphgflKREQVT 256
Cdd:cd19090 150 A---IETgDFDVVLTAN-RYTLLDQSAADELLPAAARHGVGVINASPLGMGLLAGRPPERVRY-----------TYRWLS 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1125162345 257 EEVLAQVRRLNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAA 310
Cdd:cd19090 215 PELLDRAKRLYELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAA 268
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
20-312 |
1.33e-41 |
|
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: 146.16 E-value: 1.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 20 KSGVQLPAISLGLWH---NFGGVDRFsnsRAMVLRAFDLGITHFDLANNYGPppGSAETTFGRILRRDlASYRDELIVST 96
Cdd:cd19092 1 PEGLEVSRLVLGCMRladWGESAEEL---LSLIEAALELGITTFDHADIYGG--GKCEELFGEALALN-PGLREKIEIQT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 97 KAG-------WPMWPGPYgDWgSRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISS 169
Cdd:cd19092 75 KCGirlgddpRPGRIKHY-DT-SKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 170 YSPEETRraahLLQTLGTACLI-HQPNYSMFNR-ALEGGLLAVLGDLGIGCIVFSPLAQGLLTDrylsgipadsraakph 247
Cdd:cd19092 153 FTPSQIE----LLQSYLDQPLVtNQIELSLLHTeAIDDGTLDYCQLLDITPMAWSPLGGGRLFG---------------- 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1125162345 248 GFLKREQVTEEVLAQVrrlnecARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAALD 312
Cdd:cd19092 213 GFDERFQRLRAALEEL------AEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALD 271
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
28-328 |
3.53e-41 |
|
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: 145.53 E-value: 3.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 28 ISLGLWH----NFGGVDRfSNSRAMVLRAFDLGITHFDLANNYGPppGSAETTFGRILRRdlASYRDELIVSTKAGWPmW 103
Cdd:cd19148 7 IALGTWAiggwMWGGTDE-KEAIETIHKALDLGINLIDTAPVYGF--GLSEEIVGKALKE--YGKRDRVVIATKVGLE-W 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 104 P--GPYGDWGSRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISSYSPE--ETRRAA 179
Cdd:cd19148 81 DegGEVVRNSSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSPEqmETFRKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 180 HLLQTLgtaclihQPNYSMFNRALEGGLLAVLGDLGIGCIVFSPLAQGLLT-----DRYLSGipADSRAAKPHgFlkREQ 254
Cdd:cd19148 161 APLHTV-------QPPYNLFEREIEKDVLPYARKHNIVTLAYGALCRGLLSgkmtkDTKFEG--DDLRRTDPK-F--QEP 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1125162345 255 VTEEVLAQVRRLNECARAR-GQTLAQMALAWVLRHREVTAALIGASRPGHIeDAVAALDKRAFSDDELRTIDRIL 328
Cdd:cd19148 229 RFSQYLAAVEELDKLAQERyGKSVIHLAVRWLLDQPGVSIALWGARKPEQL-DAVDEVFGWSLNDEDMKEIDAIL 302
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
47-325 |
7.72e-40 |
|
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: 141.99 E-value: 7.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 47 AMVLRAFDLGITHFDLANNYGPPPGSAETtfgRILRRDLASY---RDELIVSTKAGW-PMWPGPYGdwgSRKYLIASLDQ 122
Cdd:cd19077 29 ETMKAALDAGSNLWNGGEFYGPPDPHANL---KLLARFFRKYpeyADKVVLSVKGGLdPDTLRPDG---SPEAVRKSIEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 123 SLRRMG-LEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISSYSPEETRRAAHLLQtlgTACLihQPNYSMFNR 201
Cdd:cd19077 103 ILRALGgTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAETIRRAHAVHP---IAAV--EVEYSLFSR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 202 A-LEGGLLAVLGDLGIGCIVFSPLAQGLLTDRYLSgiPADSRAAKPHGFLKR--EQVTEEVLAQVRRLNECARARGQTLA 278
Cdd:cd19077 178 EiEENGVLETCAELGIPIIAYSPLGRGLLTGRIKS--LADIPEGDFRRHLDRfnGENFEKNLKLVDALQELAEKKGCTPA 255
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1125162345 279 QMALAWVLR-HREVTAALIGASRPGHIEDAVAALDKRaFSDDELRTID 325
Cdd:cd19077 256 QLALAWILAqSGPKIIPIPGSTTLERVEENLKAANVE-LTDEELKEIN 302
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
19-327 |
8.81e-39 |
|
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: 139.89 E-value: 8.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 19 GKSGVQLPAI---SLGLWHNFGGVDRFSNSRAMVLRAFDLGITHFDLANNYGPppgsAETTFGRILRRDLASyRDELIVS 95
Cdd:cd19144 7 GRNGPSVPALgfgAMGLSAFYGPPKPDEERFAVLDAAFELGCTFWDTADIYGD----SEELIGRWFKQNPGK-REKIFLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 96 TKAGWPMWP--GPYGDWGSRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISSYSPE 173
Cdd:cd19144 82 TKFGIEKNVetGEYSVDGSPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLSECSAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 174 ETRRaahllqtlgtACLIH-----QPNYSMFNRALE---GGLLAVLGDLGIGCIVFSPLAQGLLTDRYLSgiPADSRAAK 245
Cdd:cd19144 162 TLRR----------AHAVHpiaavQIEYSPFSLDIErpeIGVLDTCRELGVAIVAYSPLGRGFLTGAIRS--PDDFEEGD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 246 PHGFLKR--EQVTEEVLAQVRRLNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAALDKRaFSDDELRT 323
Cdd:cd19144 230 FRRMAPRfqAENFPKNLELVDKIKAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLGALKVK-LTEEEEKE 308
|
....
gi 1125162345 324 IDRI 327
Cdd:cd19144 309 IREI 312
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
21-327 |
8.88e-38 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 135.18 E-value: 8.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 21 SGVQLPAISLGLWHNfGGVDRfsnsRAMVLRAFDLGITHFDLANNYGpppgsAETTFGRILRR-DLAsyRDELIVSTKag 99
Cdd:COG0656 1 NGVEIPALGLGTWQL-PGEEA----AAAVRTALEAGYRHIDTAAMYG-----NEEGVGEAIAAsGVP--REELFVTTK-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 100 wpMWPGPYGdwgsRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDtPLEETMGALDHAVRSGKALYAGISSYSPEETRRaa 179
Cdd:COG0656 67 --VWNDNHG----YDDTLAAFEESLERLGLDYLDLYLIHWPGPG-PYVETWRALEELYEEGLIRAIGVSNFDPEHLEE-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 180 hLLQTLGTACLIHQPNYSMFNRalEGGLLAVLGDLGIGCIVFSPLAQG-LLTDrylsgipadsraakphgflkreqvteE 258
Cdd:COG0656 138 -LLAETGVKPAVNQVELHPYLQ--QRELLAFCREHGIVVEAYSPLGRGkLLDD--------------------------P 188
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1125162345 259 VLAQVrrlnecARARGQTLAQMALAWVLRHRevTAALIGASRPGHIEDAVAALDkraF--SDDELRTIDRI 327
Cdd:COG0656 189 VLAEI------AEKHGKTPAQVVLRWHLQRG--VVVIPKSVTPERIRENLDAFD---FelSDEDMAAIDAL 248
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
13-312 |
2.53e-37 |
|
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: 134.99 E-value: 2.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 13 MTYERCGKSGVQLPAISLG---LWHNFGGVDRfSNSRAMVLRAFDLGITHFDLANNYGPppGSAETTFGRILRrdlASYR 89
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGaspLGGVFGPVDE-EEAIRTVHEALDSGINYIDTAPWYGQ--GRSETVLGKALK---GIPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 90 DELIVSTKAGwpmwpgPYGDWG------SRKYLIASLDQSLRRMGLEYVDIFYHH----RPDPDTPLEETMGALDHAVRS 159
Cdd:cd19163 75 DSYYLATKVG------RYGLDPdkmfdfSAERITKSVEESLKRLGLDYIDIIQVHdiefAPSLDQILNETLPALQKLKEE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 160 GKALYAGISSYS----PEETRRAAHLLQTLGTAClihqpNYSMFNRALEgGLLAVLGDLGIGCIVFSPLAQGLLTDRyls 235
Cdd:cd19163 149 GKVRFIGITGYPldvlKEVLERSPVKIDTVLSYC-----HYTLNDTSLL-ELLPFFKEKGVGVINASPLSMGLLTER--- 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1125162345 236 GIPADSRAakphgflkreqvTEEVLAQVRRLNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAALD 312
Cdd:cd19163 220 GPPDWHPA------------SPEIKEACAKAAAYCKSRGVDISKLALQFALSNPDIATTLVGTASPENLRKNLEAAE 284
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-311 |
5.19e-36 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 130.40 E-value: 5.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 13 MTYERCGKSGVQLPAISLGlwhnfGGVDRFSNSrAMVLRAFDLGITHFDLANNYGPppGSAETTFGRILRRdlaSYRDEL 92
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFG-----GGGLPRESP-ELLRRALDLGINYFDTAEGYGN--GNSEEIIGEALKG---LRRDKV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 93 IVSTKAGWPMwpgpygDWGSRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPL---EETMGALDHAVRSGKALYAGISS 169
Cdd:cd19105 70 FLATKASPRL------DKKDKAELLKSVEESLKRLQTDYIDIYQLHGVDTPEERllnEELLEALEKLKKEGKVRFIGFST 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 170 YSPEET--RRAAHL--LQTLgtaclihQPNYSMFNR-ALEGGLLAVLGDLGIGCIVFSPLAQGLLTDRYLSGIPadsraa 244
Cdd:cd19105 144 HDNMAEvlQAAIESgwFDVI-------MVAYNFLNQpAELEEALAAAAEKGIGVVAMKTLAGGYLQPALLSVLK------ 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1125162345 245 kphgflkreqvteevlaqvrrlnecarARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAAL 311
Cdd:cd19105 211 ---------------------------AKGFSLPQAALKWVLSNPRVDTVVPGMRNFAELEENLAAA 250
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
21-325 |
1.35e-34 |
|
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: 127.36 E-value: 1.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 21 SGVQLPAISLGLWHNFGGVDRFSNSRAMVLRAFDLGITHFDLANNYGPppGSAETTFGRILRrdlaSYRDELIVSTKagw 100
Cdd:cd19138 7 DGTKVPALGQGTWYMGEDPAKRAQEIEALRAGIDLGMTLIDTAEMYGD--GGSEELVGEAIR----GRRDKVFLVSK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 101 pMWPGPygdwGSRKYLIASLDQSLRRMGLEYVDIFYHHRPDpDTPLEETMGALDHAVRSGKALYAGISSYSPEETRRAAH 180
Cdd:cd19138 78 -VLPSN----ASRQGTVRACERSLRRLGTDYLDLYLLHWRG-GVPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 181 LLqtLGTACLIHQPNYSMFNRALEGGLLAVLGDLGIGCIVFSPLAQGlltdrylsgipadsraakphGFLKREQVTEEVL 260
Cdd:cd19138 152 VP--GGGNCAANQVLYNLGSRGIEYDLLPWCREHGVPVMAYSPLAQG--------------------GLLRRGLLENPTL 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1125162345 261 AQVrrlnecARARGQTLAQMALAWVLRHREVTaALIGASRPGHIEDAVAALDKrAFSDDELRTID 325
Cdd:cd19138 210 KEI------AARHGATPAQVALAWVLRDGNVI-AIPKSGSPEHARENAAAADL-ELTEEDLAELD 266
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-327 |
3.30e-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: 381330 [Multi-domain] Cd Length: 321 Bit Score: 127.77 E-value: 3.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 15 YERCGKSGVQLPAISLG------LWhnfgGVDRFSNSRAMVLRAFDLGITHFDLANNYGPppGSAETTFGRILRRDlasy 88
Cdd:cd19104 2 YRRFGRTGLKVSELTFGgggiggLM----GRTTREEQIAAVRRALDLGINFFDTAPSYGD--GKSEENLGRALKGL---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 89 RDELIVSTKAGWPmwPGPYGDWGSRkyLIASLDQSLRRMGLEYVDIFY-HHRPDPDTP--------------LEETMGAL 153
Cdd:cd19104 72 PAGPYITTKVRLD--PDDLGDIGGQ--IERSVEKSLKRLKRDSVDLLQlHNRIGDERDkpvggtlsttdvlgLGGVADAF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 154 DHAVRSGKALYAGISSYSPEETRRAA------HLLQTLgtACLIHQP----NYSMFNRALEGGLLAVLGDLGIGCIVFSP 223
Cdd:cd19104 148 ERLRSEGKIRFIGITGLGNPPAIRELldsgkfDAVQVY--YNLLNPSaaeaRPRGWSAQDYGGIIDAAAEHGVGVMGIRV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 224 LAQGLLTDRYLSGIPADSRAAKPhgflkreqvTEEVLAQVRRLNECARARGQTLAQMALAWVLRHREVTAALIGASRPGH 303
Cdd:cd19104 226 LAAGALTTSLDRGREAPPTSDSD---------VAIDFRRAAAFRALAREWGETLAQLAHRFALSNPGVSTVLVGVKNREE 296
|
330 340
....*....|....*....|....
gi 1125162345 304 IEDAVAALDKRAFSDDELRTIDRI 327
Cdd:cd19104 297 LEEAVAAEAAGPLPAENLARLEAL 320
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
26-312 |
3.42e-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: 381391 [Multi-domain] Cd Length: 291 Bit Score: 126.68 E-value: 3.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 26 PAISLGLWhNFGGVDRFSNSRAMVLRAFDLGITHFDLANNY-----GPPPGSAETTFGRILRrdLASYRDELIVSTKAGW 100
Cdd:cd19752 1 SELCLGTM-YFGTRTDEETSFAILDRYVAAGGNFLDTANNYafwteGGVGGESERLIGRWLK--DRGNRDDVVIATKVGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 101 PmWPGPYGDWG-----SRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISSYSPEET 175
Cdd:cd19752 78 G-PRDPDGGPEspeglSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 176 RRAAHLLQTLGTA---CLihQPNYSMFNR---ALEGGLLAVLGDL--------GIGCIVFSPLAQGLLTdrylsgipads 241
Cdd:cd19752 157 ERARQIARQQGWAefsAI--QQRHSYLRPrpgADFGVQRIVTDELldyassrpDLTLLAYSPLLSGAYT----------- 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1125162345 242 RAAKPhgflKREQV-TEEVLAQVRRLNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAALD 312
Cdd:cd19752 224 RPDRP----LPEQYdGPDSDARLAVLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAALD 291
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
19-311 |
3.10e-33 |
|
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: 124.47 E-value: 3.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 19 GKSGVQLPAISLG---LWHNFGGVDRFSNSRAMVLRAFDLGITHFDLANNYGPppGSAETTFGRILRrdlASYRDELIVS 95
Cdd:cd19145 6 GSQGLEVSAQGLGcmgLSGDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYGP--NTNEVLLGKALK---DGPREKVQLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 96 TKAGWpMWPGPYGDW--GSRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISSYSPE 173
Cdd:cd19145 81 TKFGI-HEIGGSGVEvrGDPAYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSEASAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 174 ETRRaAHLLQTLgTAClihQPNYSMFNRALEGGLLAVLGDLGIGCIVFSPLAQGLLTDR-YLSGIPADSRAAKPHGFLKR 252
Cdd:cd19145 160 TIRR-AHAVHPI-TAV---QLEWSLWTRDIEEEIIPTCRELGIGIVPYSPLGRGFFAGKaKLEELLENSDVRKSHPRFQG 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1125162345 253 EQVtEEVLAQVRRLNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAAL 311
Cdd:cd19145 235 ENL-EKNKVLYERVEALAKKKGCTPAQLALAWVLHQGEDVVPIPGTTKIKNLNQNIGAL 292
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
26-312 |
2.17e-31 |
|
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: 119.39 E-value: 2.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 26 PAISLGLwHNFGGVDRFSNSRAM--VLRAFDLGITHFDLANNYGPppGSAETTFGRILRRDLasyRDELIVSTKAGWPMW 103
Cdd:cd19162 1 PRLGLGA-ASLGNLARAGEDEAAatLDAAWDAGIRYFDTAPLYGL--GLSERRLGAALARHP---RAEYVVSTKVGRLLE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 104 PGPYGDWG--------SRKYLIASLDQSLRRMGLEYVDIFYHHRPDP--DTPLEETMGALDHAVRSGKALYAGISSYSPE 173
Cdd:cd19162 75 PGAAGRPAgadrrfdfSADGIRRSIEASLERLGLDRLDLVFLHDPDRhlLQALTDAFPALEELRAEGVVGAIGVGVTDWA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 174 ETRRAAhllQTLGTACLIHQPNYSMFNRALEGGLLAVLGDLGIGCIVFSPLAQGLLtdrylsgipaDSRAAKPHGFLKRe 253
Cdd:cd19162 155 ALLRAA---RRADVDVVMVAGRYTLLDRRAATELLPLCAAKGVAVVAAGVFNSGIL----------ATDDPAGDRYDYR- 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1125162345 254 QVTEEVLAQVRRLNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAALD 312
Cdd:cd19162 221 PATPEVLARARRLAAVCRRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLALLR 279
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
22-325 |
2.26e-30 |
|
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: 115.75 E-value: 2.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 22 GVQLPAISLGLWhNFGGVDR--FSNSRAMV---LRAFDLGITHFDLANNYGPppGSAETTFGRILrrdLASYRDELIVST 96
Cdd:cd19137 1 GEKIPALGLGTW-GIGGFLTpdYSRDEEMVellKTAIELGYTHIDTAEMYGG--GHTEELVGKAI---KDFPREDLFIVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 97 KagwpMWPGPYgdwgSRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISSYSPEETR 176
Cdd:cd19137 75 K----VWPTNL----RYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 177 RAAHLLQtlgTACLIHQPNYSMFNRA-LEGGLLAVLGDLGIGCIVFSPLAQGLLTDRylsgipadsraakphgflkreqv 255
Cdd:cd19137 147 EAISKSQ---TPIVCNQVKYNLEDRDpERDGLLEYCQKNGITVVAYSPLRRGLEKTN----------------------- 200
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 256 teevlaqvRRLNECARARGQTLAQMALAWVLRHREVTaALIGASRPGHIEDAVAALDKRaFSDDELRTID 325
Cdd:cd19137 201 --------RTLEEIAKNYGKTIAQIALAWLIQKPNVV-AIPKAGRVEHLKENLKATEIK-LSEEEMKLLD 260
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
26-313 |
8.13e-30 |
|
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: 114.20 E-value: 8.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 26 PAISLG---LWHNFGGVDRFSNSRAMVLRAFDLGITHFDLANNYGPppGSAETTFGRILRRdlaSYRDELIVSTKagwpm 102
Cdd:cd19096 1 SVLGFGtmrLPESDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGG--GKSEEILGEALKE---GPREKFYLATK----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 103 wpGPYGDWGSRKYLIASLDQSLRRMGLEYVDIFYHH---RPDPDTPLEE--TMGALDHAVRSGKALYAGISSYSPEETrr 177
Cdd:cd19096 71 --LPPWSVKSAEDFRRILEESLKRLGVDYIDFYLLHglnSPEWLEKARKggLLEFLEKAKKEGLIRHIGFSFHDSPEL-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 178 aahLLQTLGTA----CLIHqpnYSMFNRALEGG--LLAVLGDLGIGCIVFSPLAQGLLtdrylsgipadsrAAKPHGFLK 251
Cdd:cd19096 147 ---LKEILDSYdfdfVQLQ---YNYLDQENQAGrpGIEYAAKKGMGVIIMEPLKGGGL-------------ANNPPEALA 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1125162345 252 ReqvteevlaqvrrlnecARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAALDK 313
Cdd:cd19096 208 I-----------------LCGAPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENIAAADE 252
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
22-327 |
9.51e-30 |
|
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381366 [Multi-domain] Cd Length: 253 Bit Score: 113.89 E-value: 9.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 22 GVQLPAISLGLWHNFGGvdrfsNSRAMVLRAFDLGITHFDLANNYGpppgsAETTFGRILRRDLASyRDELIVSTKagwp 101
Cdd:cd19140 5 GVRIPALGLGTYPLTGE-----ECTRAVEHALELGYRHIDTAQMYG-----NEAQVGEAIAASGVP-RDELFLTTK---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 102 MWPGPYgdwgSRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISSYSPEETRRAAHL 181
Cdd:cd19140 70 VWPDNY----SPDDFLASVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 182 lqtLGTACLIHQPNYSMFNRalEGGLLAVLGDLGIGCIVFSPLAQGLLTDRYLsgipadsraakphgflkreqvteevla 261
Cdd:cd19140 146 ---SEAPLFTNQVEYHPYLD--QRKLLDAAREHGIALTAYSPLARGEVLKDPV--------------------------- 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1125162345 262 qvrrLNECARARGQTLAQMALAWVLRHREVtAALIGASRPGHIEDAVAALDkRAFSDDELRTIDRI 327
Cdd:cd19140 194 ----LQEIGRKHGKTPAQVALRWLLQQEGV-AAIPKATNPERLEENLDIFD-FTLSDEEMARIAAL 253
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
15-329 |
2.69e-29 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 114.49 E-value: 2.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 15 YERCGKSGVQLPAISLG---LWHNFGGVDRfSNSRAMVLRAFDLGITHFDLANNYGPPpgSAETTFGRILRRdLASYRDE 91
Cdd:PLN02587 1 LRELGSTGLKVSSVGFGaspLGSVFGPVSE-EDAIASVREAFRLGINFFDTSPYYGGT--LSEKVLGKALKA-LGIPREK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 92 LIVSTKAGwpmwpgPYGDwG---SRKYLIASLDQSLRRMGLEYVDIFYHHR---PDPDTPLEETMGALDHAVRSGKALYA 165
Cdd:PLN02587 77 YVVSTKCG------RYGE-GfdfSAERVTKSVDESLARLQLDYVDILHCHDiefGSLDQIVNETIPALQKLKESGKVRFI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 166 GISSYSPEETRRAAHLLQTLGTACLIHQPNYSMFNRALEGgLLAVLGDLGIGCIVFSPLAQGLLTDrylSGIPADSRAak 245
Cdd:PLN02587 150 GITGLPLAIFTYVLDRVPPGTVDVILSYCHYSLNDSSLED-LLPYLKSKGVGVISASPLAMGLLTE---NGPPEWHPA-- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 246 phgflkreqvTEEVLAQVRRLNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAALDKRA-FSDDE--LR 322
Cdd:PLN02587 224 ----------PPELKSACAAAATHCKEKGKNISKLALQYSLSNKDISTTLVGMNSVQQVEENVAAATELEtSGIDEelLS 293
|
....*..
gi 1125162345 323 TIDRILA 329
Cdd:PLN02587 294 EVEAILA 300
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
25-325 |
1.68e-28 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 111.66 E-value: 1.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 25 LPAISLGLWH----NFGGVDRFSNS------RAMVLRAFDLGITHFDLANNYGPppGSAETTFGRILRRdlaSYRDELIV 94
Cdd:cd19103 4 LPKIALGTWSwgsgGAGGDQVFGNHldedtlKAVFDKAMAAGLNLWDTAAVYGM--GASEKILGEFLKR---YPREDYII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 95 STKAGwPMWPGPYGDwgsrkYLIASLDQSLRRMGLEYVDIFYHHRPdpdTPLEETMGALDHAVRSGKALYAGISSYSPEE 174
Cdd:cd19103 79 STKFT-PQIAGQSAD-----PVADMLEGSLARLGTDYIDIYWIHNP---ADVERWTPELIPLLKSGKVKHVGVSNHNLAE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 175 TRRAAHLLQTLGTACLIHQPNYSMFNRALE-GGLLAVLGDLGIGCIVFSPLAQGLLTDRYLSG--IPADSRAAKPHGFLK 251
Cdd:cd19103 150 IKRANEILAKAGVSLSAVQNHYSLLYRSSEeAGILDYCKENGITFFAYMVLEQGALSGKYDTKhpLPEGSGRAETYNPLL 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1125162345 252 REQvteEVLAQVrrLNECARARGQTLAQMALAWVLrhREVTAALIGASRPGHIEDAVAALdKRAFSDDELRTID 325
Cdd:cd19103 230 PQL---EELTAV--MAEIGAKHGASIAQVAIAWAI--AKGTTPIIGVTKPHHVEDAARAA-SITLTDDEIKELE 295
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
49-309 |
9.49e-27 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 107.40 E-value: 9.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 49 VLRAFDLGITHFDLANNYGPppGSAETTFGRILRRDLASY---RDELIVSTKAGWP-----------MWPGPYGDWG--- 111
Cdd:cd19099 27 LKAALDSGINVIDTAINYRG--GRSERLIGKALRELIEKGgikRDEVVIVTKAGYIpgdgdeplrplKYLEEKLGRGlid 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 112 -----------SRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTP----------LEETMGALDHAVRSGKALYAGISSY 170
Cdd:cd19099 105 vadsaglrhciSPAYLEDQIERSLKRLGLDTIDLYLLHNPEEQLLelgeeefydrLEEAFEALEEAVAEGKIRYYGISTW 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 171 SP-------------EETRRAA-------HLLQTLGTACLIHQPNYSMFNRALEGGLLAVL---GDLGIGCIVFSPLAQG 227
Cdd:cd19099 185 DGfrappalpghlslEKLVAAAeevggdnHHFKVIQLPLNLLEPEALTEKNTVKGEALSLLeaaKELGLGVIASRPLNQG 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 228 LLtdrylsgipadsraakphgflkreqvteevLAQVRRLNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDA 307
Cdd:cd19099 265 QL------------------------------LGELRLADLLALPGGATLAQRALQFARSTPGVDSALVGMRRPEHVDEN 314
|
..
gi 1125162345 308 VA 309
Cdd:cd19099 315 LA 316
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
13-327 |
1.16e-26 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 107.63 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 13 MTYERCGKSGVQLPAISLGLWhNFGGVDRFSNSRAMVLRAFDLGITHFDLANNYGPPP-----GSAETTFGRILRRdlAS 87
Cdd:PRK10625 1 MQYHRIPHSSLEVSTLGLGTM-TFGEQNSEADAHAQLDYAVAQGINLIDVAEMYPVPPrpetqGLTETYIGNWLAK--RG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 88 YRDELIVSTKAGWP-------MWPGPYGDwgsRKYLIASLDQSLRRMGLEYVDIFYHHRPD-----------------PD 143
Cdd:PRK10625 78 SREKLIIASKVSGPsrnndkgIRPNQALD---RKNIREALHDSLKRLQTDYLDLYQVHWPQrptncfgklgyswtdsaPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 144 TPLEETMGALDHAVRSGKALYAGISSYSPEETRRAAHLLQT--LGTACLIHQPnYSMFNRALEGGLLAVLGDLGIGCIVF 221
Cdd:PRK10625 155 VSLLETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEKhdLPRIVTIQNP-YSLLNRSFEVGLAEVSQYEGVELLAY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 222 SPLAQGLLTDRYLSGI-PADSRAAKPHGFLKR--EQVTEEVLAQVrrlnECARARGQTLAQMALAWVLRHREVTAALIGA 298
Cdd:PRK10625 234 SCLAFGTLTGKYLNGAkPAGARNTLFSRFTRYsgEQTQKAVAAYV----DIAKRHGLDPAQMALAFVRRQPFVASTLLGA 309
|
330 340
....*....|....*....|....*....
gi 1125162345 299 SRPGHIEDAVAALDkRAFSDDELRTIDRI 327
Cdd:PRK10625 310 TTMEQLKTNIESLH-LTLSEEVLAEIEAV 337
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
31-328 |
2.81e-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: 381327 [Multi-domain] Cd Length: 304 Bit Score: 105.75 E-value: 2.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 31 GLWH---NFGGVDRFSNSRAMVLRAFDLGITHFDLANNYGPppgsAETTFGRILR--RDLASYRDELIVSTKagwpmW-P 104
Cdd:cd19101 8 GMWQlsgGHGGIRDEDAAVRAMAAYVDAGLTTFDCADIYGP----AEELIGEFRKrlRRERDAADDVQIHTK-----WvP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 105 GPYGDWGSRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTP-LEETMGALDHAVRSGKALYAGISSYSpeeTRRAAHLLQ 183
Cdd:cd19101 79 DPGELTMTRAYVEAAIDRSLKRLGVDRLDLVQFHWWDYSDPgYLDAAKHLAELQEEGKIRHLGLTNFD---TERLREILD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 184 tLGTACLIHQPNYSMFNRALEGGLLAVLGDLGIGCIVFSPLAQGLLTDRYLsGIPADSRAAKPH-GFLKREQVTEEV--- 259
Cdd:cd19101 156 -AGVPIVSNQVQYSLLDRRPENGMAALCEDHGIKLLAYGTLAGGLLSEKYL-GVPEPTGPALETrSLQKYKLMIDEWggw 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1125162345 260 -LAQ--VRRLNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAALDkRAFSDDELRTIDRIL 328
Cdd:cd19101 234 dLFQelLRTLKAIADKHGVSIANVAVRWVLDQPGVAGVIVGARNSEHIDDNVRAFS-FRLDDEDRAAIDAVL 304
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-309 |
4.53e-26 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 103.72 E-value: 4.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 19 GKSGVQLPAISLGLWHnFGGVDRfSNSRAMVLRAFDLGITHFDLANNYGpppgSAETTFGRILRRdlasYRDELIVSTKA 98
Cdd:cd19100 5 GRTGLKVSRLGFGGGP-LGRLSQ-EEAAAIIRRALDLGINYFDTAPSYG----DSEEKIGKALKG----RRDKVFLATKT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 99 GwpmwpgpygdwgSRKY--LIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMG------ALDHAVRSGKALYAGISSY 170
Cdd:cd19100 75 G------------ARDYegAKRDLERSLKRLGTDYIDLYQLHAVDTEEDLDQVFGpggaleALLEAKEEGKIRFIGISGH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 171 SPEetrRAAHLLQTLGTACLIHQPNY-SMFNRALEGGLLAVLGDLGIGCIVFSPLAQGLLTDrylsgipadsraakphgf 249
Cdd:cd19100 143 SPE---VLLRALETGEFDVVLFPINPaGDHIDSFREELLPLAREKGVGVIAMKVLAGGRLLS------------------ 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 250 lkreqvteevlaqvrrlnecaraRGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVA 309
Cdd:cd19100 202 -----------------------GDPLDPEQALRYALSLPPVDVVIVGMDSPEELDENLA 238
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
51-313 |
2.28e-24 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 99.91 E-value: 2.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 51 RAFDLGITHFDLANNYGpppgSAETTFGRILRRDlasyrDELIVSTKAGwpmwPGPYGDWGSRKYLIASLDQSLRRMGLE 130
Cdd:cd19097 34 YALKAGINTLDTAPAYG----DSEKVLGKFLKRL-----DKFKIITKLP----PLKEDKKEDEAAIEASVEASLKRLKVD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 131 YVDIFYHHRP-DPDTPLEETMGALDHAVRSGKALYAGISSYSPEETRRAAHLLQtlgtaCLIHQPNYSMFN-RALEGGLL 208
Cdd:cd19097 101 SLDGLLLHNPdDLLKHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKALESFK-----IDIIQLPFNILDqRFLKSGLL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 209 AVLGDLGIGCIVFSPLAQGLLTDRYlSGIPADSRAAKPHgflkreqvteevlaqVRRLNECARARGQTLAQMALAWVLRH 288
Cdd:cd19097 176 AKLKKKGIEIHARSVFLQGLLLMEP-DKLPAKFAPAKPL---------------LKKLHELAKKLGLSPLELALGFVLSL 239
|
250 260
....*....|....*....|....*
gi 1125162345 289 REVTAALIGASRPGHIEDAVAALDK 313
Cdd:cd19097 240 PEIDKIVVGVDSLEQLKEIIAAFKK 264
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
25-325 |
1.18e-23 |
|
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: 97.34 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 25 LPAISLGLWHNFGgvdrfSNSRAMVLRAFDLGITHFDLANNYGPPPGSAETTfgrilrRDLASYRDELIVSTKagwpMWP 104
Cdd:cd19073 1 IPALGLGTWQLRG-----DDCANAVKEALELGYRHIDTAEIYNNEAEVGEAI------AESGVPREDLFITTK----VWR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 105 GPYGDwgsrKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISSYSPEETRRAAHLLQT 184
Cdd:cd19073 66 DHLRP----EDLKKSVDRSLEKLGTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 185 LGTAcliHQPNYSMFNRALEggLLAVLGDLGIGCIVFSPLAQGlltdrylsgipadsraakphgflkreqvteEVLaQVR 264
Cdd:cd19073 142 PIAV---NQVEFHPFLYQAE--LLEYCRENDIVITAYSPLARG------------------------------EVL-RDP 185
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1125162345 265 RLNECARARGQTLAQMALAWVLRHREVtaALIGASRPGHIEDAVAALDkRAFSDDELRTID 325
Cdd:cd19073 186 VIQEIAEKYDKTPAQVALRWLVQKGIV--VIPKASSEDHLKENLAIFD-WELTSEDVAKID 243
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
21-333 |
1.85e-23 |
|
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: 98.65 E-value: 1.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 21 SGVQLPAISLG-LWHNFGGVDRFSNSRAMVLRAFDLGITHFDLANNYgpPPGSAETTFGRIL--RRDlasyRDELIVSTK 97
Cdd:cd19146 12 SPLCLGAMSFGeAWKSMMGECDKETAFKLLDAFYEQGGNFIDTANNY--QGEESERWVGEWMasRGN----RDEMVLATK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 98 --AGW-PMWPGP----YGDwGSRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGIS-- 168
Cdd:cd19146 86 ytTGYrRGGPIKiksnYQG-NHAKSLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSdt 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 169 -----SYSPEETRraAHLLqtlgTACLIHQPNYSMFNRALEGGLLAVLGDLGIGCIVFSPLAQGLLTdrylsgIPADSRA 243
Cdd:cd19146 165 pawvvSKANAYAR--AHGL----TQFVVYQGHWSAAFRDFERDILPMCEAEGMALAPWGVLGQGQFR------TEEEFKR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 244 AKPHGFLKREQvTEEVLAQVRRLNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAALDKrAFSDDELRT 323
Cdd:cd19146 233 RGRSGRKGGPQ-TEKERKVSEKLEKVAEEKGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIEALGI-SLSDEEIQE 310
|
330
....*....|
gi 1125162345 324 IDRILAGNVG 333
Cdd:cd19146 311 IEDAYPFDVG 320
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
25-325 |
3.93e-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: 90.62 E-value: 3.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 25 LPAISLGLWHNFGGVDRfsnsrAMVLRAFDLGITHFDLANNYGpppgsAETTFGRILRRDLASyRDELIVSTKagwpMWP 104
Cdd:cd19071 1 MPLIGLGTYKLKPEETA-----EAVLAALEAGYRHIDTAAAYG-----NEAEVGEAIRESGVP-REELFITTK----LWP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 105 GPYGdwgsRKYLIASLDQSLRRMGLEYVDIFYHHRP------DPDTPLEETMGALDHAVRSGKALYAGISSYSPEETRRa 178
Cdd:cd19071 66 TDHG----YERVREALEESLKDLGLDYLDLYLIHWPvpgkegGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEE- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 179 ahLLQTLGTACLIHQPNYSMFNRALEggLLAVLGDLGIGCIVFSPLAQGlltdrylsgipadsraakphgflKREQVTEE 258
Cdd:cd19071 141 --LLAAARIKPAVNQIELHPYLQQKE--LVEFCKEHGIVVQAYSPLGRG-----------------------RRPLLDDP 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1125162345 259 VlaqvrrLNECARARGQTLAQMALAWVLRHRevTAALIGASRPGHIEDAVAALDkRAFSDDELRTID 325
Cdd:cd19071 194 V------LKEIAKKYGKTPAQVLLRWALQRG--VVVIPKSSNPERIKENLDVFD-FELSEEDMAAID 251
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
45-311 |
2.36e-20 |
|
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: 89.59 E-value: 2.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 45 SRAMVLRAFDLGITHFDLANNYGPppGSAETTFGRILRRdlaSYRDELIVSTKAGWPMWP-------GPYGDWGSRKYLI 117
Cdd:cd19152 22 AKATLVAAWDLGIRYFDTAPWYGA--GLSEERLGAALRE---LGREDYVISTKVGRLLVPlqeveptFEPGFWNPLPFDA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 118 ----------ASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVR-----------SGKALYAGISSYSPEETR 176
Cdd:cd19152 97 vfdysydgilRSIEDSLQRLGLSRIDLLSIHDPDEDLAGAESDEHFAQAIKgafraleelreEGVIKAIGLGVNDWEVIL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 177 RAAHL--LQTLGTAClihqpNYSMFNRALEGGLLAVLGDLGIGCIVFSPLAQGLLTDRylsgipadsraaKPHGFLKREQ 254
Cdd:cd19152 177 RILEEadLDWVMLAG-----RYTLLDHSAARELLPECEKRGVKVVNAGPFNSGFLAGG------------DNFDYYEYGP 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1125162345 255 VTEEVLAQVRRLNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAAL 311
Cdd:cd19152 240 APPELIARRDRIEALCEQHGVSLAAAALQFALAPPAVASVAPGASSPERVEENVALL 296
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
21-325 |
1.46e-19 |
|
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: 87.57 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 21 SGVQLPAISLG-LWHNFGGVDRFSNSRAMVLRAFDLGITHFDLANNYGPPpgSAETTFGRILR-RDLasyRDELIVSTKA 98
Cdd:cd19147 11 SPLILGAMSIGdAWSGFMGSMDKEQAFELLDAFYEAGGNFIDTANNYQDE--QSETWIGEWMKsRKN---RDQIVIATKF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 99 GWPMWPGPYGD------WG-SRKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSGKALYAGISSYS 171
Cdd:cd19147 86 TTDYKAYEVGKgkavnyCGnHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDTP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 172 PEETRRAAHLLQTLG-TACLIHQPNYSMFNRALEGGLLAVLGDLGIGCIVFSPLAQGlltdRYLSGIPADSRAAKPHG-- 248
Cdd:cd19147 166 AWVVSAANYYATAHGkTPFSVYQGRWNVLNRDFERDIIPMARHFGMALAPWDVLGGG----KFQSKKAVEERKKNGEGlr 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1125162345 249 -FLKREQVTEEVLAQVRRLNECARARG-QTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAALDKRaFSDDELRTID 325
Cdd:cd19147 242 sFVGGTEQTPEEVKISEALEKVAEEHGtESVTAIALAYVRSKAPNVFPLVGGRKIEHLKDNIEALSIK-LTPEEIEYLE 319
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
25-325 |
3.80e-19 |
|
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: 85.10 E-value: 3.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 25 LPAISLGLWHNFGGVdrfsnSRAMVLRAFDLGITHFDLANNYGpppgsAETTFGRILRrDLASYRDELIVSTKagwpMWP 104
Cdd:cd19139 1 IPAFGLGTFRLKDDV-----VIDSVRTALELGYRHIDTAQIYD-----NEAAVGQAIA-ESGVPRDELFITTK----IWI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 105 GPYgdwgSRKYLIASLDQSLRRMGLEYVDIFYHHRPDPD--TPLEETMGALDHAVRSGKALYAGISSYSPEETRRAahlL 182
Cdd:cd19139 66 DNL----SKDKLLPSLEESLEKLRTDYVDLTLIHWPSPNdeVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEA---I 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 183 QTLGTACLI-HQPNYSMF--NRAleggLLAVLGDLGIGCIVFSPLAQGLLTDrylsgipadsraakphgflkreqvtEEV 259
Cdd:cd19139 139 AVVGAGAIAtNQIELSPYlqNRK----LVAHCKQHGIHVTSYMTLAYGKVLD-------------------------DPV 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1125162345 260 LAQVrrlnecARARGQTLAQMALAWVLrHREVtAALIGASRPGHIEDAVAALDKRaFSDDELRTID 325
Cdd:cd19139 190 LAAI------AERHGATPAQIALAWAM-ARGY-AVIPSSTKREHLRSNLLALDLT-LDADDMAAIA 246
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
52-313 |
4.33e-18 |
|
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: 83.14 E-value: 4.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 52 AFDLGITHFDLANNYGPppGSAETTFGRILRRdlaSYRDELIVSTKAGWPMWPG------PYGDWG-----------SRK 114
Cdd:cd19161 29 AWDSGIRYFDTAPMYGH--GLAEHRLGDFLRE---KPRDEFVLSTKVGRLLKPAregsvpDPNGFVdplpfeivydySYD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 115 YLIASLDQSLRRMGLEYVDIFYHHRPDPDTPLEETMGALDHAVRSG--KALY----AG-ISSYS--PEETRRAAHLLQTL 185
Cdd:cd19161 104 GIMRSFEDSLQRLGLNRIDILYVHDIGVYTHGDRKERHHFAQLMSGgfKALEelkkAGvIKAFGlgVNEVQICLEALDEA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 186 GTACLIHQPNYSMFNRALEGGLLAVLGDLGIGCIVFSPLAQGLLtdrylsgipadSRAAKPHGFLKREQVTEEVLAQVRR 265
Cdd:cd19161 184 DLDCFLLAGRYSLLDQSAEEEFLPRCEQRGTSLVIGGVFNSGIL-----------ATGTKSGAKFNYGDAPAEIISRVME 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1125162345 266 LNECARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAALDK 313
Cdd:cd19161 253 IEKICDAYNVPLAAAALQFPLRHPAVASVLTGARNPAQLRQNVEAFQT 300
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
21-292 |
3.11e-16 |
|
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: 77.36 E-value: 3.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 21 SGVQLPAISLGLWHNfGGvdrFSNSrAMVLRAFDLGITHFDLANNYGpppgsAETTFGRILRRDLASyRDELIVSTKagw 100
Cdd:cd19135 9 NGVEMPILGLGTSHS-GG---YSHE-AVVYALKECGYRHIDTAKRYG-----CEELLGKAIKESGVP-REDLFLTTK--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 101 pMWPGPYGDwgsrKYLIASLDQSLRRMGLEYVDIFYHHRPDPDTP-------LEETMGALDHAVRSGKALYAGISSYSPE 173
Cdd:cd19135 75 -LWPSDYGY----ESTKQAFEASLKRLGVDYLDLYLLHWPDCPSSgknvketRAETWRALEELYDEGLCRAIGVSNFLIE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 174 ETRRaahLLQTLGTACLIHQPNYSMFNRALEggLLAVLGDLGIGCIVFSPLAQGLLtdrylsgipadsraakphgfLKRE 253
Cdd:cd19135 150 HLEQ---LLEDCSVVPHVNQVEFHPFQNPVE--LIEYCRDNNIVFEGYCPLAKGKA--------------------LEEP 204
|
250 260 270
....*....|....*....|....*....|....*....
gi 1125162345 254 QVTeevlaqvrrlnECARARGQTLAQMALAWVLRHREVT 292
Cdd:cd19135 205 TVT-----------ELAKKYQKTPAQILIRWSIQNGVVT 232
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
17-312 |
5.30e-16 |
|
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: 77.19 E-value: 5.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 17 RCGKSGVQLPAISLGlwHNFGGVDRFSNSRAMVLRAFDLGITHFDLANNYGPPpgSAETTFGRILRRdLASYRDELIVST 96
Cdd:cd19153 9 LGNVSPVGLGTAALG--GVYGDGLEQDEAVAIVAEAFAAGINHFDTSPYYGAE--SSEAVLGKALAA-LQVPRSSYTVAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 97 KAGwpmwpgPYGDWG---SRKYLIASLDQSLRRMGLEYVDIFYHHR---PDPDTPLEETMGALDHAVRSGKALYAGISSY 170
Cdd:cd19153 84 KVG------RYRDSEfdySAERVRASVATSLERLHTTYLDVVYLHDiefVDYDTLVDEALPALRTLKDEGVIKRIGIAGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 171 SPEETRRAAHLLQTLGTACLIHQPNYSMFNRALEGGLLAVLGDLGIGCIVFSPLAQGLLTDRylsgipaDSRAAKP-HGF 249
Cdd:cd19153 158 PLDTLTRATRRCSPGSLDAVLSYCHLTLQDARLESDAPGLVRGAGPHVINASPLSMGLLTSQ-------GPPPWHPaSGE 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1125162345 250 LKReqvteevlAQVRRLNECArARGQTLAQMALAWVL-RHREVTAALIGASRPGHIEDAVAALD 312
Cdd:cd19153 231 LRH--------YAAAADAVCA-SVEASLPDLALQYSLaAHAGVGTVLLGPSSLAQLRSMLAAVD 285
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
22-327 |
8.41e-16 |
|
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: 76.12 E-value: 8.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 22 GVQLPAISLGL---WHNFGGVDRFSNSRAMVLRAFDLGITHFDLANNYGpppgsAETTFGRILRRDLASyRDELIVSTKA 98
Cdd:cd19120 1 GSKIPAIAFGTgtaWYKSGDDDIQRDLVDSVKLALKAGFRHIDTAEMYG-----NEKEVGEALKESGVP-REDLFITTKV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 99 GWPMwPGPYGdwgsrkyliaSLDQSLRRMGLEYVDIFYHHRP----DPDTPLEETMGALDHAVRSGKALYAGISSYSPEE 174
Cdd:cd19120 75 SPGI-KDPRE----------ALRKSLAKLGVDYVDLYLIHSPffakEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIED 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 175 TRRaahLLQTLGTACLIHQPNYSMFNRALEGGLLAVLGDLGIGCIVFSPLAqglltdrylsgiPADSRAAKPhgflkreq 254
Cdd:cd19120 144 LEE---LLDTAKIKPAVNQIEFHPYLYPQQPALLEYCREHGIVVSAYSPLS------------PLTRDAGGP-------- 200
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1125162345 255 vteevLAQVrrLNECARARGQTLAQMALAWVLRHRevTAALIGASRPGHIEDAVAALDkRAFSDDELRTIDRI 327
Cdd:cd19120 201 -----LDPV--LEKIAEKYGVTPAQVLLRWALQKG--IVVVTTSSKEERMKEYLEAFD-FELTEEEVEEIDKA 263
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
22-325 |
1.12e-14 |
|
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: 72.61 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 22 GVQLPAISLGLWHnfggVDRFSNSRAMVLRAFDLGITHFDLANNYGpppgsAETTFGRILRRDLASyRDELIVSTKagwp 101
Cdd:cd19133 6 GVEMPILGFGVFQ----IPDPEECERAVLEAIKAGYRLIDTAAAYG-----NEEAVGRAIKKSGIP-REELFITTK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 102 MWPGPYGDWGSRKyliaSLDQSLRRMGLEYVDIFYHHRPDPDtpLEETMGALDHAVRSGKALYAGISSYSPEetrRAAHL 181
Cdd:cd19133 72 LWIQDAGYEKAKK----AFERSLKRLGLDYLDLYLIHQPFGD--VYGAWRAMEELYKEGKIRAIGVSNFYPD---RLVDL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 182 LQTLGTACLIHQPNYSMFNRALEggLLAVLGDLGIGCIVFSPLAQGlltdrylsgipadsraakphgflKREQVTEEVLA 261
Cdd:cd19133 143 ILHNEVKPAVNQIETHPFNQQIE--AVEFLKKYGVQIEAWGPFAEG-----------------------RNNLFENPVLT 197
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1125162345 262 QVrrlnecARARGQTLAQMALAWVLRhREVtAALIGASRPGHIEDAVAALDkRAFSDDELRTID 325
Cdd:cd19133 198 EI------AEKYGKSVAQVILRWLIQ-RGI-VVIPKSVRPERIAENFDIFD-FELSDEDMEAIA 252
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
49-310 |
1.25e-13 |
|
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: 70.38 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 49 VLRAFDLGITHFDLANNYGPppgsAETTFGRILRRDLASY-RDELIVSTKAgwpmwpGPYGDWG---SRKYLIASLDQSL 124
Cdd:cd19164 40 VRRALELGIRAFDTSPYYGP----SEIILGRALKALRDEFpRDTYFIITKV------GRYGPDDfdySPEWIRASVERSL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 125 RRMGLEYVDIFYHHrpdpD---TPLEETMGALDHAVR---SGKALYAGISSYSPEETRRAAHLLQTLGTACL---IHQPN 195
Cdd:cd19164 110 RRLHTDYLDLVYLH----DvefVADEEVLEALKELFKlkdEGKIRNVGISGYPLPVLLRLAELARTTAGRPLdavLSYCH 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 196 YSMFNRALEGGLLAVLGDLGIGCIV-FSPLAQGLLTdrylSGIPADSRAAKPhgFLKreqvteevlAQVRRLNECARARG 274
Cdd:cd19164 186 YTLQNTTLLAYIPKFLAAAGVKVVLnASPLSMGLLR----SQGPPEWHPASP--ELR---------AAAAKAAEYCQAKG 250
|
250 260 270
....*....|....*....|....*....|....*..
gi 1125162345 275 QTLAQMALAWVLRHRE-VTAALIGASRPGHIEDAVAA 310
Cdd:cd19164 251 TDLADVALRYALREWGgEGPTVVGCSNVDELEEAVEA 287
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
49-286 |
1.39e-13 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 69.67 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 49 VLRAFDLGITHFDLANNYGpppgsAETTFGRILRRDLASyRDELIVSTKagwpMWPGPYgdwgSRKYLIASLDQSLRRMG 128
Cdd:PRK11172 22 VKTALELGYRAIDTAQIYD-----NEAAVGQAIAESGVP-RDELFITTK----IWIDNL----AKDKLIPSLKESLQKLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 129 LEYVDIFYHHRPDPD--TPLEETMGALDHAVRSGKALYAGISSYSPEETRRAahlLQTLGT-ACLIHQPNYSMF--NRAl 203
Cdd:PRK11172 88 TDYVDLTLIHWPSPNdeVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQA---IAAVGAeNIATNQIELSPYlqNRK- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 204 eggLLAVLGDLGIGCIVFSPLAQGlltdrylsgipadsraakphgflkrEQVTEEVLAQVrrlnecARARGQTLAQMALA 283
Cdd:PRK11172 164 ---VVAFAKEHGIHVTSYMTLAYG-------------------------KVLKDPVIARI------AAKHNATPAQVILA 209
|
...
gi 1125162345 284 WVL 286
Cdd:PRK11172 210 WAM 212
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
22-248 |
2.23e-13 |
|
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: 68.94 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 22 GVQLPAISLGLWHNFGGVdrfsnSRAMVLRAFDLGITHFDLANNYGpppgsAETTFGRILRRDlASYRDELIVSTKagwp 101
Cdd:cd19131 7 GNTIPQLGLGVWQVSNDE-----AASAVREALEVGYRSIDTAAIYG-----NEEGVGKAIRAS-GVPREELFITTK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 102 MWPGPYGDWGSRKyliaSLDQSLRRMGLEYVDIFYHHRPDP--DTPLeETMGALDHAVRSGKALYAGISSYSPEETRRaa 179
Cdd:cd19131 72 LWNSDQGYDSTLR----AFDESLRKLGLDYVDLYLIHWPVPaqDKYV-ETWKALIELKKEGRVKSIGVSNFTIEHLQR-- 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1125162345 180 hLLQTLGTACLIHQPN-YSMFNRAlegGLLAVLGDLGIGCIVFSPLAQG-LLTDRYLSGIpadsraAKPHG 248
Cdd:cd19131 145 -LIDETGVVPVVNQIElHPRFQQR---ELRAFHAKHGIQTESWSPLGQGgLLSDPVIGEI------AEKHG 205
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
22-292 |
2.40e-13 |
|
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: 69.00 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 22 GVQLPAISLGLWHNFGGvdrfSNSRAMVLRAFDLGITHFDLANNYgpppgSAETTFGRILRRDLASyRDELIVSTKagwp 101
Cdd:cd19126 6 GTRMPWLGLGVFQTPDG----DETERAVQTALENGYRSIDTAAIY-----KNEEGVGEAIRESGVP-REELFVTTK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 102 MWPGpygDWGSRKYLIAsLDQSLRRMGLEYVDIFYHHRPDPDTpLEETMGALDHAVRSGKALYAGISSYSPeetrraaHL 181
Cdd:cd19126 72 LWND---DQRARRTEDA-FQESLDRLGLDYVDLYLIHWPGKDK-FIDTWKALEKLYASGKVKAIGVSNFQE-------HH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 182 LQTLGTAC----LIHQPNYSMFNRALEggLLAVLGDLGIGCIVFSPLAQGLLtdrylsgipadsraakphgflkreqVTE 257
Cdd:cd19126 140 LEELLAHAdvvpAVNQVEFHPYLTQKE--LRGYCKSKGIVVEAWSPLGQGGL-------------------------LSN 192
|
250 260 270
....*....|....*....|....*....|....*
gi 1125162345 258 EVLAQVrrlnecARARGQTLAQMALAWVLRHREVT 292
Cdd:cd19126 193 PVLAAI------GEKYGKSAAQVVLRWDIQHGVVT 221
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
49-327 |
2.24e-12 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 66.53 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 49 VLR-AFDLGITHFDLANNYGPppgsaETTfGRILRRDLASYRDELIVSTKAGWPMwpGPYGDWG---SRKYLIASLDQSL 124
Cdd:PRK10376 45 VLReAVALGVNHIDTSDFYGP-----HVT-NQLIREALHPYPDDLTIVTKVGARR--GEDGSWLpafSPAELRRAVHDNL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 125 RRMGLEYVDI------FYHHRPDPDtPLEETMGALDHAVRSGKALYAGISSYSPE---ETRRAAHLlqtlgtACLihQPN 195
Cdd:PRK10376 117 RNLGLDVLDVvnlrlmGDGHGPAEG-SIEEPLTVLAELQRQGLVRHIGLSNVTPTqvaEARKIAEI------VCV--QNH 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 196 YSMFNRAlEGGLLAVLGDLGIGCIVFSPLAqglltdrylsgipadsraakphGFLKREQVTeevlaqvrrLNECARARGQ 275
Cdd:PRK10376 188 YNLAHRA-DDALIDALARDGIAYVPFFPLG----------------------GFTPLQSST---------LSDVAASLGA 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1125162345 276 TLAQMALAWVLrHREVTAALI-GASRPGHIEDAVAALDKRaFSDDELRTIDRI 327
Cdd:PRK10376 236 TPMQVALAWLL-QRSPNILLIpGTSSVAHLRENLAAAELV-LSEEVLAELDGI 286
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
22-325 |
3.26e-12 |
|
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: 65.70 E-value: 3.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 22 GVQLPAISLGLWHnfggVDRFSNSRAmVLRAFDLGITHFDLANNYGPPPGSAETtfgrILRRDLAsyRDELIVSTKagwp 101
Cdd:cd19130 7 GNSIPQLGYGVFK----VPPADTQRA-VATALEVGYRHIDTAAIYGNEEGVGAA----IAASGIP--RDELFVTTK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 102 MWPGPYGDWGSRkyliASLDQSLRRMGLEYVDIFYHHRPDPDTPLE-ETMGALDHAVRSGKALYAGISSYSPEETRRaah 180
Cdd:cd19130 72 LWNDRHDGDEPA----AAFAESLAKLGLDQVDLYLVHWPTPAAGNYvHTWEAMIELRAAGRTRSIGVSNFLPPHLER--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 181 LLQTLGTACLIHQ----PNYSmfNRALEGGLLAvlgdLGIGCIVFSPLAQGLLTDRylsgiPADSRAAKPHgflkreqvt 256
Cdd:cd19130 145 IVAATGVVPAVNQielhPAYQ--QRTIRDWAQA----HDVKIEAWSPLGQGKLLGD-----PPVGAIAAAH--------- 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1125162345 257 eevlaqvrrlnecararGQTLAQMALAWVLRHREVTaaLIGASRPGHIEDAVAALDkRAFSDDELRTID 325
Cdd:cd19130 205 -----------------GKTPAQIVLRWHLQKGHVV--FPKSVRRERMEDNLDVFD-FDLTDTEIAAID 253
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
22-325 |
4.10e-12 |
|
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B (DkgB) from Corynebacterium sp. and 2,5-diketo-D-gluconic acid reductase Zymomonas mobilis are founding members of aldo-keto reductase family 5 member D1 (AKR5D1) and E1 (AKR5E1), respectively. DkgB (EC 1.1.1.274), also called 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381358 [Multi-domain] Cd Length: 255 Bit Score: 65.37 E-value: 4.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 22 GVQLPAISLGLWHNFGgvdrfSNSRAMVLRAFDLGITHFDLANNYGpppgsAETTFGRILRRDLASyRDELIVSTKAgwp 101
Cdd:cd19132 4 GTQIPAIGFGTYPLKG-----DEGVEAVVAALQAGYRLLDTAFNYE-----NEGAVGEAVRRSGVP-REELFVTTKL--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 102 mwPGpyGDWGSRKYLiASLDQSLRRMGLEYVDIFYHHRPDPDTPLE-ETMGALDHAVRSGKALYAGISSYSPEETRRaah 180
Cdd:cd19132 70 --PG--RHHGYEEAL-RTIEESLYRLGLDYVDLYLIHWPNPSRDLYvEAWQALIEAREEGLVRSIGVSNFLPEHLDR--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 181 LLQTLGTACLIHQ----PNysmFNRAlegGLLAVLGDLGIGCIVFSPLAQGLltdrylsgipadsraakphgflkrEQVT 256
Cdd:cd19132 142 LIDETGVTPAVNQielhPY---FPQA---EQRAYHREHGIVTQSWSPLGRGS------------------------GLLD 191
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1125162345 257 EEVLAQVrrlnecARARGQTLAQMALAWVLRHREVtaALIGASRPGHIEDAVAALDkRAFSDDELRTID 325
Cdd:cd19132 192 EPVIKAI------AEKHGKTPAQVVLRWHVQLGVV--PIPKSANPERQRENLAIFD-FELSDEDMAAIA 251
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
21-286 |
1.18e-10 |
|
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: 61.53 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 21 SGVQLPAISLGLWhnfGGVDRFSNSRAmVLRAFDLGITHFDLANNYGpppgsAETTFGRILRRDLAS---YRDELIVSTK 97
Cdd:cd19116 7 DGNEIPAIALGTW---KLKDDEGVRQA-VKHAIEAGYRHIDTAYLYG-----NEAEVGEAIREKIAEgvvKREDLFITTK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 98 agwpMWpgpyGDWGSRKYLIASLDQSLRRMGLEYVDIFYHHRP------------DPDTPLE----ETMGALDHAVRSGK 161
Cdd:cd19116 78 ----LW----NSYHEREQVEPALRESLKRLGLDYVDLYLIHWPvafkenndsesnGDGSLSDidylETWRGMEDLVKLGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 162 ALYAGISSYSPEETRRaahLLQTlgtaCLI----HQ----PNYSmfNRAleggLLAVLGDLGIGCIVFSPLaqglltdry 233
Cdd:cd19116 150 TRSIGVSNFNSEQINR---LLSN----CNIkpavNQievhPTLT--QEK----LVAYCQSNGIVVMAYSPF--------- 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1125162345 234 lsGIPADSRAAKPHGFLKREqvteevlaqvrRLNECARARGQTLAQMALAWVL 286
Cdd:cd19116 208 --GRLVPRGQTNPPPRLDDP-----------TLVAIAKKYGKTTAQIVLRYLI 247
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
22-324 |
4.07e-10 |
|
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: 59.73 E-value: 4.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 22 GVQLPAISLGLWHNFGGVdrfsnSRAMVLRAFDLGITHFDLANNYGpppGSAE--TTFGRILRRDLASyRDELIVSTKag 99
Cdd:cd19123 9 GDLIPALGLGTWKSKPGE-----VGQAVKQALEAGYRHIDCAAIYG---NEAEigAALAEVFKEGKVK-REDLWITSK-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 100 wpMWpgpyGDWGSRKYLIASLDQSLRRMGLEYVDIFYHHRP------------------DPDTPLEETMGALDHAVRSGK 161
Cdd:cd19123 78 --LW----NNSHAPEDVLPALEKTLADLQLDYLDLYLMHWPvalkkgvgfpesgedllsLSPIPLEDTWRAMEELVDKGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 162 ALYAGISSYSpeeTRRAAHLLQTLGTACLIHQPNYSMFNRALEggLLAVLGDLGIGCIVFSPLAQGlltDRylsgiPADS 241
Cdd:cd19123 152 CRHIGVSNFS---VKKLEDLLATARIKPAVNQVELHPYLQQPE--LLAFCRDNGIHLTAYSPLGSG---DR-----PAAM 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 242 RAAKphgflkreqvtEEVLAQVRRLNECARARGQTLAQMALAWVLrHREvTAALIGASRPGHIEDAVAALDKRaFSDDEL 321
Cdd:cd19123 219 KAEG-----------EPVLLEDPVINKIAEKHGASPAQVLIAWAI-QRG-TVVIPKSVNPERIQQNLEAAEVE-LDASDM 284
|
...
gi 1125162345 322 RTI 324
Cdd:cd19123 285 ATI 287
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
21-327 |
5.93e-10 |
|
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: 59.05 E-value: 5.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 21 SGVQLPAISLGLWHNFGGvdrfsNSRAMVLRAFDLGITHFDLANNYGpppgsAETTFGRILRrDLASYRDELIVSTKagw 100
Cdd:cd19117 10 TGAEIPAVGLGTWQSKPN-----EVAKAVEAALKAGYRHIDTAAIYG-----NEEEVGQGIK-DSGVPREEIFITTK--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 101 pMWpgpyGDWGSRkyLIASLDQSLRRMGLEYVDIFYHHRP---------------------DPDTPLEETMGALDHAVRS 159
Cdd:cd19117 76 -LW----CTWHRR--VEEALDQSLKKLGLDYVDLYLMHWPvpldpdgndflfkkddgtkdhEPDWDFIKTWELMQKLPAT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 160 GKALYAGISSYSpeeTRRAAHLLQTLGTA-------CLIHQPNYSmfnraleGGLLAVLGDLGIGCIVFSPLAQglltdr 232
Cdd:cd19117 149 GKVKAIGVSNFS---IKNLEKLLASPSAKivpavnqIELHPLLPQ-------PKLVDFCKSKGIHATAYSPLGS------ 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 233 ylSGIPAdsraakphgflkreqVTEEVLAQVrrlnecARARGQTLAQMALAWVL-RHREVTAALIGASRpghIEdavAAL 311
Cdd:cd19117 213 --TNAPL---------------LKEPVIIKI------AKKHGKTPAQVIISWGLqRGYSVLPKSVTPSR---IE---SNF 263
|
330
....*....|....*.
gi 1125162345 312 DKRAFSDDELRTIDRI 327
Cdd:cd19117 264 KLFTLSDEEFKEIDEL 279
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
20-327 |
7.83e-10 |
|
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: 58.96 E-value: 7.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 20 KSGVQLPAISLGLWHNFGgvdrfSNSRAMVLRAFDLGITHFDLANNYgpppgSAETTFGRILRRDLAS---YRDELIVST 96
Cdd:cd19154 7 SNGVKMPLIGLGTWQSKG-----AEGITAVRTALKAGYRLIDTAFLY-----QNEEAIGEALAELLEEgvvKREDLFITT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 97 KAgwpmWPGPYgdwgSRKYLIASLDQSLRRMGLEYVDIFYHHRP-------------------DPDTPLEETMGALDHAV 157
Cdd:cd19154 77 KL----WTHEH----APEDVEEALRESLKKLQLEYVDLYLIHAPaafkddegesgtmengmsiHDAVDVEDVWRGMEKVY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 158 RSGKALYAGISSYSPEETRRA-------AHLLQtlgTACLIHQPNYSmfnraleggLLAVLGDLGIGCIVFSPLaqgllt 230
Cdd:cd19154 149 DEGLTKAIGVSNFNNDQIQRIldnarvkPHNNQ---VECHLYFPQKE---------LVEFCKKHNISVTSYATL------ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 231 drylsGIPADSRAAKPHGFLKREQVTEEVLAQvrrlnECARARGQTLAQMALAWVLRHRevtAALIGAS-RPGHIEDAVA 309
Cdd:cd19154 211 -----GSPGRANFTKSTGVSPAPNLLQDPIVK-----AIAEKHGKTPAQVLLRYLLQRG---IAVIPKSaTPSRIKENFN 277
|
330
....*....|....*...
gi 1125162345 310 ALDkRAFSDDELRTIDRI 327
Cdd:cd19154 278 IFD-FSLSEEDMATLEEI 294
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
21-171 |
1.22e-09 |
|
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: 58.31 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 21 SGVQLPAISLGLWHNFGGVdrfsnSRAMVLRAFDLGITHFDLANNYGpppgsAETTFGRILRRDLAS--YRDELIVSTKA 98
Cdd:cd19121 8 TGASIPAVGLGTWQAKAGE-----VKAAVAHALKIGYRHIDGALCYQ-----NEDEVGEGIKEAIAGgvKREDLFVTTKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 99 gwpmwpgpygdWGS-RKYLIASLDQSLRRMGLEYVDIFYHHRP----------------------DPDTPLEETMGALDH 155
Cdd:cd19121 78 -----------WSTyHRRVELCLDRSLKSLGLDYVDLYLVHWPvllnpngnhdlfptlpdgsrdlDWDWNHVDTWKQMEK 146
|
170
....*....|....*.
gi 1125162345 156 AVRSGKALYAGISSYS 171
Cdd:cd19121 147 VLKTGKTKAIGVSNYS 162
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
21-327 |
1.25e-09 |
|
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: 58.40 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 21 SGVQLPAISLGLWHNFGGVdrfSNSRAMVLRAFDLGITHFDLANNY--GPPPGSAETTFgriLRRDLASYRDELIVSTKA 98
Cdd:cd19122 5 NGVKIPAVGFGTFANEGAK---GETYAAVTKALDVGYRHLDCAWFYlnEDEVGDAVRDF---LKENPSVKREDLFICTKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 99 gWPMWPGPygdwgsrKYLIASLDQSLRRMGLEYVDIFYHHRP------DPDTPL-----------------EETMGALDH 155
Cdd:cd19122 79 -WNHLHEP-------EDVKWSIDNSLKNLKLDYIDLFLVHWPiaaeknDQRSPKlgpdgkyvilkdltenpEPTWRAMEE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 156 AVRSGKALYAGISSYSPEETRRAAHLLQTLGTA--CLIHQ--PNYSMFNRALEGGLLAVlgdlgigciVFSPLAQglltd 231
Cdd:cd19122 151 IYESGKAKAIGVSNWTIPGLKKLLSFAKVKPHVnqIEIHPflPNEELVDYCFSNDILPE---------AYSPLGS----- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 232 rylsgipadsraakphgflkREQV--TEEVLAQVRRLNECARARGQTLAQMALAWVLRHREVTaaLIGASRPGHIEDAVA 309
Cdd:cd19122 217 --------------------QNQVpsTGERVSENPTLNEVAEKGGYSLAQVLIAWGLRRGYVV--LPKSSTPSRIESNFK 274
|
330
....*....|....*...
gi 1125162345 310 ALDkraFSDDELRTIDRI 327
Cdd:cd19122 275 SIE---LSDEDFEAINQV 289
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
22-178 |
1.44e-09 |
|
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: 58.28 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 22 GVQLPAISLGLWHNFGgvdrfSNSRAMVLRAFDLGITHFDLANNYGpppgsAETTFGRILRRDLAS---YRDELIVSTKA 98
Cdd:cd19111 1 GFPMPVIGLGTYQSPP-----EEVRAAVDYALFVGYRHIDTALSYQ-----NEKAIGEALKWWLKNgklKREEVFITTKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 99 gWPMWPGPygdwgsrKYLIASLDQSLRRMGLEYVDIFYHH-------------RPDPDTPLEETMGALDHAVRSGKALYA 165
Cdd:cd19111 71 -PPVYLEF-------KDTEKSLEKSLENLKLPYVDLYLIHhpcgfvnkkdkgeRELASSDVTSVWRAMEALVSEGKVKSI 142
|
170
....*....|...
gi 1125162345 166 GISSYSPEETRRA 178
Cdd:cd19111 143 GLSNFNPRQINKI 155
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
22-327 |
1.66e-09 |
|
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: 57.80 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 22 GVQLPAISLGLwhnfggvdrFSNSR----AMVLRAFDLGITHFDLANNYGpppgsAETTFGRILRRDlASYRDELIVSTK 97
Cdd:cd19127 6 GVEMPALGLGV---------FQTPPeetaDAVATALADGYRLIDTAAAYG-----NEREVGEGIRRS-GVDRSDIFVTTK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 98 agwpMWPGPYGDWGSRKyliaSLDQSLRRMGLEYVDIFYHHRPDPdTPLEETMG---ALDHAVRSGKALYAGISSYSPEE 174
Cdd:cd19127 71 ----LWISDYGYDKALR----GFDASLRRLGLDYVDLYLLHWPVP-NDFDRTIQaykALEKLLAEGRVRAIGVSNFTPEH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 175 TRRaahLLQTLGTACLIHQ----PNYSmfnralEGGLLAVLGDLGIGCIVFSPLAqGLLTDRylsgipadsraaKPHGFL 250
Cdd:cd19127 142 LER---LIDATTVVPAVNQvelhPYFS------QKDLRAFHRRLGIVTQAWSPIG-GVMRYG------------ASGPTG 199
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1125162345 251 KREQVTEEVLAqvrrlnECARARGQTLAQMALAWVLRHRevTAALIGASRPGHIEDAVAALDKRaFSDDELRTIDRI 327
Cdd:cd19127 200 PGDVLQDPTIT------GLAEKYGKTPAQIVLRWHLQNG--VSAIPKSVHPERIAENIDIFDFA-LSAEDMAAIDAL 267
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
21-177 |
1.80e-09 |
|
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: 57.89 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 21 SGVQLPAISLGLWHNfggVDRFSNSRAMVLRAFDLGITHFDLANNYGpppgsAETTFGRILRRDLAS---YRDELIVSTK 97
Cdd:cd19119 8 TGASIPALGLGTASP---HEDRAEVKEAVEAAIKEGYRHIDTAYAYE-----TEDFVGEAIKRAIDDgsiKREELFITTK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 98 agwpMWPGPYgdwgsrKYLIASLDQSLRRMGLEYVDIFYHHRPDP------DTPLE-------------------ETMGA 152
Cdd:cd19119 80 ----VWPTFY------DEVERSLDESLKALGLDYVDLLLVHWPVCfekdsdDSGKPftpvnddgktryaasgdhiTTYKQ 149
|
170 180
....*....|....*....|....*
gi 1125162345 153 LDHAVRSGKALYAGISSYSPEETRR 177
Cdd:cd19119 150 LEKIYLDGRAKAIGVSNYSIVYLER 174
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
22-237 |
3.93e-09 |
|
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: 56.76 E-value: 3.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 22 GVQLPAISLGLWHNFGGvDRFSNSramVLRAFDLGITHFDLANNYgpppgSAETTFGRILRRDlASYRDELIVSTKagwp 101
Cdd:cd19156 6 GVEMPRLGLGVWRVQDG-AEAENA---VKWAIEAGYRHIDTAAIY-----KNEEGVGQGIRES-GVPREEVFVTTK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 102 MWPGpygDWGSRKYLiASLDQSLRRMGLEYVDIFYHHRPDPDTpLEETMGALDHAVRSGKALYAGISSYSPeetrraaHL 181
Cdd:cd19156 72 LWNS---DQGYESTL-AAFEESLEKLGLDYVDLYLIHWPVKGK-FKDTWKAFEKLYKEKKVRAIGVSNFHE-------HH 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1125162345 182 LQTLGTAC----LIHQPN-YSMFNRAlegGLLAVLGDLGIGCIVFSPLAQG-LLTDRYLSGI 237
Cdd:cd19156 140 LEELLKSCkvapMVNQIElHPLLTQE---PLRKFCKEKNIAVEAWSPLGQGkLLSNPVLKAI 198
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
21-173 |
4.96e-09 |
|
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: 56.27 E-value: 4.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 21 SGVQLPAISLGLWHNFGGvdrfsNSRAMVLRAFDLGITHFDLANNYGpppgsAETTFGRILRRDLASY----RDELIVST 96
Cdd:cd19118 3 TGNKIPAIGLGTWQAEPG-----EVGAAVKIALKAGYRHLDLAKVYQ-----NQHEVGQALKELLKEEpgvkREDLFITS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 97 KAgwpmwpgpygdWGSR---KYLIASLDQSLRRMGLEYVDIFYHHRP-----------DPDTPLEETMGALDHAV----- 157
Cdd:cd19118 73 KL-----------WNNShrpEYVEPALDDTLKELGLDYLDLYLIHWPvafkptgdlnpLTAVPTNGGEVDLDLSVslvdt 141
|
170 180
....*....|....*....|....
gi 1125162345 158 --------RSGKALYAGISSYSPE 173
Cdd:cd19118 142 wkamvelkKTGKVKSIGVSNFSID 165
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
21-170 |
7.25e-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: 56.34 E-value: 7.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 21 SGVQLPAISLGLWHNFGGVdrfsnSRAMVLRAFDLGITHFDLANNYGpppgsAETTFGRIL----RRDLASyRDELIVST 96
Cdd:cd19112 7 SGHKMPVIGLGVWRMEPGE-----IKELILNAIKIGYRHFDCAADYK-----NEKEVGEALaeafKTGLVK-REDLFITT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 97 KagwpMWPGPYGdwgsrkYLIASLDQSLRRMGLEYVDIFYHHRP-----------------------DPDTPLEETMGAL 153
Cdd:cd19112 76 K----LWNSDHG------HVIEACKDSLKKLQLDYLDLYLVHFPvatkhtgvgttgsalgedgvldiDVTISLETTWHAM 145
|
170
....*....|....*..
gi 1125162345 154 DHAVRSGKALYAGISSY 170
Cdd:cd19112 146 EKLVSAGLVRSIGISNY 162
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
21-140 |
2.19e-08 |
|
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: 54.58 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 21 SGVQLPAISLGLWHNFGGVDRfsnSRAMVLRAFDLGITHFDLANNYGpppgsAETTFGRIL----RRDLASYRDELIVST 96
Cdd:cd19124 1 SGQTMPVIGMGTASDPPSPED---IKAAVLEAIEVGYRHFDTAAAYG-----TEEALGEALaealRLGLVKSRDELFVTS 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1125162345 97 KagwpMWPgpygDWGSRKYLIASLDQSLRRMGLEYVDIFYHHRP 140
Cdd:cd19124 73 K----LWC----SDAHPDLVLPALKKSLRNLQLEYVDLYLIHWP 108
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
21-191 |
1.23e-07 |
|
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: 52.45 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 21 SGVQLPAISLGLWHnfggVDRfSNSRAMVLRAFDLGITHFDLANNYGpppgsAETTFGRILRRDLAS---YRDELIVSTK 97
Cdd:cd19113 7 SGYKMPSVGFGCWK----LDN-ATAADQIYQAIKAGYRLFDGAEDYG-----NEKEVGEGVNRAIDEglvKREELFLTSK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 98 agwpMWpgpyGDWGSRKYLIASLDQSLRRMGLEYVDIFYHHRP-------------------------DPDTPLEETMGA 152
Cdd:cd19113 77 ----LW----NNFHDPKNVETALNKTLSDLKLDYVDLFLIHFPiafkfvpieekyppgfycgdgdnfvYEDVPILDTWKA 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 1125162345 153 LDHAVRSGKALYAGISSYSpeetrraAHLLQTLGTACLI 191
Cdd:cd19113 149 LEKLVDAGKIKSIGVSNFP-------GALILDLLRGATI 180
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
22-293 |
1.59e-07 |
|
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: 51.62 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 22 GVQLPAISLGLWHnfggVDRFSNSRAMVLRAFDLGITHFDLANNYGPPPGsaettFGRILRRDLASyRDELIVSTKagwp 101
Cdd:cd19157 7 GVKMPWLGLGVFK----VEEGSEVVNAVKTALKNGYRSIDTAAIYGNEEG-----VGKGIKESGIP-REELFITSK---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 102 MWPGpygDWGSRKYLiASLDQSLRRMGLEYVDIFYHHRPDPDTpLEETMGALDHAVRSGKALYAGISSYSpeetrraAHL 181
Cdd:cd19157 73 VWNA---DQGYDSTL-KAFEASLERLGLDYLDLYLIHWPVKGK-YKETWKALEKLYKDGRVRAIGVSNFQ-------VHH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 182 LQTLGTACLIhQPnysMFN------RALEGGLLAVLGDLGIGCIVFSPLAQGLLTDRYLsgipadsraakphgflkreqv 255
Cdd:cd19157 141 LEDLLADAEI-VP---MVNqvefhpRLTQKELRDYCKKQGIQLEAWSPLMQGQLLDNPV--------------------- 195
|
250 260 270
....*....|....*....|....*....|....*...
gi 1125162345 256 teevlaqvrrLNECARARGQTLAQMALAWVLRHREVTA 293
Cdd:cd19157 196 ----------LKEIAEKYNKSVAQVILRWDLQNGVVTI 223
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
25-172 |
2.83e-07 |
|
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: 51.09 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 25 LPAISLGLWHnFGGVDrfsNSRAMVLRAFDLGITHFDLANNYGpppgsAETTFGRILRRDLASY---RDELIVSTKAGwp 101
Cdd:cd19136 1 MPILGLGTFR-LRGEE---EVRQAVDAALKAGYRLIDTASVYR-----NEADIGKALRDLLPKYglsREDIFITSKLA-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 102 mwpgPYGDWGSRKYliASLDQSLRRMGLEYVDIFYHHRP-----DPDTPLE-----ETMGALDHAVRSGKALYAGISSYS 171
Cdd:cd19136 70 ----PKDQGYEKAR--AACLGSLERLGTDYLDLYLIHWPgvqglKPSDPRNaelrrESWRALEDLYKEGKLRAIGVSNYT 143
|
.
gi 1125162345 172 P 172
Cdd:cd19136 144 V 144
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
25-304 |
4.45e-06 |
|
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: 47.54 E-value: 4.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 25 LPAISLGLWhnfggvdRFSNSRA--MVLRAFDLGITHFDLANNYGpppgsAETTFGRILRRDLASyRDELIVSTKagwpM 102
Cdd:cd19134 11 MPVIGLGVG-------ELSDDEAerSVSAALEAGYRLIDTAAAYG-----NEAAVGRAIAASGIP-RGELFVTTK----L 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 103 WPGPYGDWGSRKYLIASLDqslrRMGLEYVDIFYHHRPDPDT-PLEETMGALDHAVRSGKALYAGISSYSPEetrraaHL 181
Cdd:cd19134 74 ATPDQGFTASQAACRASLE----RLGLDYVDLYLIHWPAGREgKYVDSWGGLMKLREEGLARSIGVSNFTAE------HL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 182 LQTLGTACLIHQPN----YSMFNRAlegGLLAVLGDLGIGCIVFSPLAQGLLTDRylsgiPADSRAAKPHgflkreqvte 257
Cdd:cd19134 144 ENLIDLTFFTPAVNqielHPLLNQA---ELRKVNAQHGIVTQAYSPLGVGRLLDN-----PAVTAIAAAH---------- 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1125162345 258 evlaqvrrlnecararGQTLAQMALAWVLRHRevTAALIGASRPGHI 304
Cdd:cd19134 206 ----------------GRTPAQVLLRWSLQLG--NVVISRSSNPERI 234
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
52-171 |
5.28e-06 |
|
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: 47.13 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 52 AFDLGITHFDLANNYGPPPGSAETtFGRILRRDLASyRDELIVSTKagwpMWPGPYgdwgsRKYLIA-SLDQSLRRMGLE 130
Cdd:cd19128 23 AIKAGYRHIDCAYYYGNEAFIGIA-FSEIFKDGGVK-REDLFITSK----LWPTMH-----QPENVKeQLLITLQDLQLE 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 131 YVDIFYHHRP---DPDT----------------PLEETMGALDHAVRSGKALYAGISSYS 171
Cdd:cd19128 92 YLDLFLIHWPlafDMDTdgdprddnqiqslskkPLEDTWRAMEQCVDEKLTKNIGVSNYS 151
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
21-171 |
5.36e-06 |
|
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: 47.38 E-value: 5.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 21 SGVQLPAISLGLWHNFGGvdrfsNSRAMVLRAFDLGITHFDLANNYGpppgsAETTFGRILRRDLASY----RDELIVST 96
Cdd:cd19106 3 TGQKMPLIGLGTWKSKPG-----QVKAAVKYALDAGYRHIDCAAVYG-----NEQEVGEALKEKVGPGkavpREDLFVTS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 97 KAgwpmwpgpygdWGSRKY---LIASLDQSLRRMGLEYVDIFYHHRP------------DPD-------TPLEETMGALD 154
Cdd:cd19106 73 KL-----------WNTKHHpedVEPALRKTLKDLQLDYLDLYLIHWPyafergdnpfpkNPDgtirydsTHYKETWKAME 141
|
170
....*....|....*..
gi 1125162345 155 HAVRSGKALYAGISSYS 171
Cdd:cd19106 142 KLVDKGLVKAIGLSNFN 158
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
28-313 |
3.33e-05 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 45.03 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 28 ISLGLWHNFGG---VDRFSNSRAMVLR-AFDLGITHFDLANNYGpppgSAETTFGRILRRdLASYRDELIVSTKagwpmW 103
Cdd:cd19098 16 INLGHAADLGSgrsVEAMRAHTHAVLDaAWAAGVRYFDAARSYG----RAEEFLGSWLRS-RNIAPDAVFVGSK-----W 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 104 PGPY-GDWG-----------SRKYLIASLDQSLRRMGlEYVDIFYHHRPDPDTPL---EETMGALDHAVRSGKALyaGIS 168
Cdd:cd19098 86 GYTYtADWQvdaavhevkdhSLARLLKQWEETRSLLG-KHLDLYQIHSATLESGVledADVLAALAELKAEGVKI--GLS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 169 SYSPE--ETRRAAhLLQTLGTACLIH--QPNYSMFNRALeGGLLAVLGDLGIGCIVFSPLAQGLLTDRylsgiPADSRAA 244
Cdd:cd19098 163 LSGPQqaETLRRA-LEIEIDGARLFDsvQATWNLLEQSA-GEALEEAHEAGMGVIVKEALANGRLTDR-----NPSPELA 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1125162345 245 KPHGFLKREqvteevlaqvrrlnecARARGQTLAQMALAWVLRHREVTAALIGASRPGHIEDAVAALDK 313
Cdd:cd19098 236 PLMAVLKAV----------------ADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRALDV 288
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
22-332 |
6.54e-05 |
|
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: 43.99 E-value: 6.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 22 GVQLPAISLG-LWHNFggvdrfSNSRAMVLRAFDLGITHFDLANNYgpppgSAETTFGRILRRDLAS---YRDELIVSTK 97
Cdd:cd19129 3 SGAIPALGFGtLIPDP------SATRNAVKAALEAGFRHFDCAERY-----RNEAEVGEAMQEVFKAgkiRREDLFVTTK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 98 agwpMWpgpygDWGSRKYLIA-SLDQSLRRMGLEYVDIFYHHRP--------------------DPDTPLEETMGALDHA 156
Cdd:cd19129 72 ----LW-----NTNHRPERVKpAFEASLKRLQLDYLDLYLIHTPfafqpgdeqdprdangnviyDDGVTLLDTWRAMERL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 157 VRSGKALYAGISSYSPEETRRAAHLLQTLGTACLIHQPNYsmfnrALEGGLLAVLGDLGIGCIVFSPLAQG----LLTDR 232
Cdd:cd19129 143 VDEGRCKAIGLSDVSLEKLREIFEAARIKPAVVQVESHPY-----LPEWELLDFCKNHGIVLQAFAPLGHGmepkLLEDP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 233 YLSGIpadsraakphgflkreqvteevlaqvrrlnecARARGQTLAQMALAWVLRHRevTAALIGASRPGHIEDavaALD 312
Cdd:cd19129 218 VITAI--------------------------------ARRVNKTPAQVLLAWAIQRG--TALLTTSKTPSRIRE---NFD 260
|
330 340
....*....|....*....|
gi 1125162345 313 KRAFSDDELRTIDRILAGNV 332
Cdd:cd19129 261 ISTLPEDAMREINEGIKTRY 280
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
22-171 |
8.17e-05 |
|
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: 43.70 E-value: 8.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 22 GVQLPAISLGLWhnfggvdRFSNSRA--MVLRAFDLGITHFDLANNYGpppgsAETTFGRILRRDLAS---YRDELIVST 96
Cdd:cd19114 1 GDKMPLVGFGTA-------KIKANETeeVIYNAIKVGYRLIDGALLYG-----NEAEVGRGIRKAIQEglvKREDLFIVT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 97 KagwpMWpgpyGDWGSRKYLIASLDQSLRRMGLEYVDIFYHHRP-----------------DPDT--------PLEETMG 151
Cdd:cd19114 69 K----LW----NNFHGKDHVREAFDRQLKDYGLDYIDLYLIHFPipaayvdpaenypflwkDKELkkfpleqsPMQECWR 140
|
170 180
....*....|....*....|
gi 1125162345 152 ALDHAVRSGKALYAGISSYS 171
Cdd:cd19114 141 EMEKLVDAGLVRNIGIANFN 160
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
20-171 |
1.30e-04 |
|
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: 43.10 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 20 KSGVQLPAISLGLWHNFGGVdrFSNSramVLRAFDLGITHFDLANNYGpppgsAETTFGRILR---RDLASYRDELIVST 96
Cdd:cd19125 6 NTGAKIPAVGLGTWQADPGV--VGNA---VKTAIKEGYRHIDCAAIYG-----NEKEIGKALKklfEDGVVKREDLFITS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 97 KagwpMWpgpyGDWGSRKYLIASLDQSLRRMGLEYVDIFYHHRP--------------DPDTPLEETMGALDHAVRSGKA 162
Cdd:cd19125 76 K----LW----CTDHAPEDVPPALEKTLKDLQLDYLDLYLIHWPvrlkkgahmpepeeVLPPDIPSTWKAMEKLVDSGKV 147
|
....*....
gi 1125162345 163 LYAGISSYS 171
Cdd:cd19125 148 RAIGVSNFS 156
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
22-177 |
1.51e-04 |
|
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: 42.90 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 22 GVQLPAISLGLWHNfggvdRFSNSRAMVLRAFDLGITHFDLANNYGpppgsAETTFGRILRRDLAS---YRDELIVSTKA 98
Cdd:cd19155 9 GEKMPVVGLGTWQS-----SPEEIETAVDTALEAGYRHIDTAYVYR-----NEAAIGNVLKKWIDSgkvKREELFIVTKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 99 gwPMWpgpygdwGSRKYLIAS-LDQSLRRMGLEYVDIFYHHRP---------------------DPDTPLEETMGALDHA 156
Cdd:cd19155 79 --PPG-------GNRREKVEKfLLKSLEKLQLDYVDLYLIHFPvgslskeddsgkldptgehkqDYTTDLLDIWKAMEAQ 149
|
170 180
....*....|....*....|.
gi 1125162345 157 VRSGKALYAGISSYSPEETRR 177
Cdd:cd19155 150 VDQGLTRSIGLSNFNREQMAR 170
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
22-193 |
4.50e-04 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 41.21 E-value: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 22 GVQLPAISLGLWhnfggvdRFSN--SRAMVLRAFDLGITHFDLANNYGpppgsAETTFGRILRR-DLAsyRDELIVSTKa 98
Cdd:PRK11565 12 GNVMPQLGLGVW-------QASNeeVITAIHKALEVGYRSIDTAAIYK-----NEEGVGKALKEaSVA--REELFITTK- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125162345 99 gwpMWPGPYGDWGsrkyliASLDQSLRRMGLEYVDIFYHHRPDPdtpleetmgALDHAVRSGKALYA----------GIS 168
Cdd:PRK11565 77 ---LWNDDHKRPR------EALEESLKKLQLDYVDLYLMHWPVP---------AIDHYVEAWKGMIElqkegliksiGVC 138
|
170 180
....*....|....*....|....*
gi 1125162345 169 SYSPEETRRaahLLQTLGTACLIHQ 193
Cdd:PRK11565 139 NFQIHHLQR---LIDETGVTPVINQ 160
|
|
| |
