|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
1-346 |
0e+00 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 773.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 1 MVWLANPERYGQMQYRYCGKSGLRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGPPPGSAEENFGRL 80
Cdd:PRK09912 1 MVWLANPERYGQMQYRYCGKSGLRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGPPPGSAEENFGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 81 LREDFAAYRDELIISTKAGYDMWPGPYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSG 160
Cdd:PRK09912 81 LREDFAAYRDELIISTKAGYDMWPGPYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 161 KALYVGISSYSPERTQKMVELLREWKIPLLIHQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQ 240
Cdd:PRK09912 161 KALYVGISSYSPERTQKMVELLREWKIPLLIHQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 241 DSRMHREGNKVRGLTPKMLTEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQALNNLTF 320
Cdd:PRK09912 241 DSRMHREGNKVRGLTPKMLTEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQALNNLTF 320
|
330 340
....*....|....*....|....*.
4AST_G 321 STKELAQIDQHIADGELNLWQASSDK 346
Cdd:PRK09912 321 STEELAQIDQHIADGELNLWQASSDK 346
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
14-326 |
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: 626.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 14 QYRYCGKSGLRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGPPPGSAEENFGRLLREDFAAYRDELI 93
Cdd:cd19150 1 QYRRCGKSGLKLPALSLGLWHNFGDDTPLETQRAILRTAFDLGITHFDLANNYGPPPGSAEENFGRILREDFAGYRDELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 94 ISTKAGYDMWPGPYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPE 173
Cdd:cd19150 81 ISTKAGYDMWPGPYGEWGSRKYLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYSPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 174 RTQKMVELLREWKIPLLIHQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSRMHREgnkvRG 253
Cdd:cd19150 161 RTREAAAILRELGTPLLIHQPSYNMLNRWVEESGLLDTLQELGVGCIAFTPLAQGLLTDKYLNGIPEGSRASKE----RS 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
4AST_G 254 LTPKMLTEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQALNNLTFSTKELA 326
Cdd:cd19150 237 LSPKMLTEANLNSIRALNEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGALDNLTFSADELA 309
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
15-326 |
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: 562.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 15 YRYCGKSGLRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGPPPGSAEENFGRLLREDFAAYRDELII 94
Cdd:cd19089 1 YRRCGRSGLHLPAISLGLWHNFGDYTSPEEARELLRTAFDLGITHFDLANNYGPPPGSAEENFGRILKRDLRPYRDELVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 95 STKAGYDMWPGPYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPER 174
Cdd:cd19089 81 STKAGYGMWPGPYGDGGSRKYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPGAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 175 TQKMVELLREWKIPLLIHQPSYNLLNRWVDKsGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSRMHREGnkvRGL 254
Cdd:cd19089 161 ARRAIALLRELGVPLIIHQPRYSLLDRWAED-GLLEVLEEAGIGFIAFSPLAQGLLTDKYLNGIPPDSRRAAES---KFL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
4AST_G 255 TPKMLTEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQALNNLTFSTKELA 326
Cdd:cd19089 237 TEEALTPEKLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAALKNLDFSEEELA 308
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
14-326 |
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: 548.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 14 QYRYCGKSGLRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGPPPGSAEENFGRLLREDFAAYRDELI 93
Cdd:cd19151 1 KYNRCGRSGLKLPAISLGLWHNFGDVDRYENSRAMLRRAFDLGITHFDLANNYGPPPGSAEENFGRILKEDLKPYRDELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 94 ISTKAGYDMWPGPYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPE 173
Cdd:cd19151 81 ISTKAGYTMWPGPYGDWGSKKYLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGISNYPPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 174 RTQKMVELLREWKIPLLIHQPSYNLLNRWVDKsGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSRMHREGnkvRG 253
Cdd:cd19151 161 EAREAAAILKDLGTPCLIHQPKYSMFNRWVEE-GLLDVLEEEGIGCIAFSPLAQGLLTDRYLNGIPEDSRAAKGS---SF 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
4AST_G 254 LTPKMLTEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQALNNLTFSTKELA 326
Cdd:cd19151 237 LKPEQITEEKLAKVRRLNEIAQARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALDNREFSEEELA 309
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
13-335 |
3.69e-131 |
|
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: 376.83 E-value: 3.69e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 13 MQYRYCGKSGLRLPALSLGLW---HNFGHVNALESqRAILRKAFDLGITHFDLANNYGPppGSAEENFGRLLREDfaaYR 89
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTMtfgGPWGGVDEAEA-IAILDAALDAGINFFDTADVYGP--GRSEELLGEALKGR---PR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 90 DELIISTKAGYDMWPGPYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISS 169
Cdd:COG0667 75 DDVVIATKVGRRMGPGPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 170 YSPERTQKMVELLREWkIPLLIHQPSYNLLNRWVDKsGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNG--IPQDSRMHRE 247
Cdd:COG0667 155 YSAEQLRRALAIAEGL-PPIVAVQNEYSLLDRSAEE-ELLPAARELGVGVLAYSPLAGGLLTGKYRRGatFPEGDRAATN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 248 gnkvrgLTPKMLTEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQALnNLTFSTKELAQ 327
Cdd:COG0667 233 ------FVQGYLTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAA-DLELSAEDLAA 305
|
....*...
4AST_G 328 IDQHIADG 335
Cdd:COG0667 306 LDAALAAV 313
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
28-332 |
5.29e-101 |
|
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: 299.23 E-value: 5.29e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 28 LSLGLWHNFGH--VNALESQRAILRKAFDLGITHFDLANNYGPppGSAEENFGRLLREDfAAYRDELIISTKagYDMWPG 105
Cdd:pfam00248 1 IGLGTWQLGGGwgPISKEEALEALRAALEAGINFIDTAEVYGD--GKSEELLGEALKDY-PVKRDKVVIATK--VPDGDG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 106 PYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPERTQKMvelLREW 185
Cdd:pfam00248 76 PWPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKA---LTKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 186 KIPLLIHQPSYNLLnRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSRMHREGNKVRgltpkmlTEANLN 265
Cdd:pfam00248 153 KIPIVAVQVEYNLL-RRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPGERRRLLKKG-------TPLNLE 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
4AST_G 266 SLRLLNEMAQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQALnNLTFSTKELAQIDQHI 332
Cdd:pfam00248 225 ALEALEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGAL-EFPLSDEEVARIDELL 290
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
22-316 |
2.44e-97 |
|
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: 290.26 E-value: 2.44e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 22 GLRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGPppGSAEENFGRLLREdfaaY-RDELIISTKAGY 100
Cdd:cd19074 1 GLKVSELSLGTWLTFGGQVDDEDAKACVRKAYDLGINFFDTADVYAA--GQAEEVLGKALKG----WpRESYVISTKVFW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 101 DMWPGPYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPERTQKMVE 180
Cdd:cd19074 75 PTGPGPNDRGLSRKHIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 181 LLREW-KIPLLIHQPSYNLLNRWVDkSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSRMHREGNKVRGLTPKML 259
Cdd:cd19074 155 LARQFgLIPPVVEQPQYNMLWREIE-EEVIPLCEKNGIGLVVWSPLAQGLLTGKYRDGIPPPSRSRATDEDNRDKKRRLL 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
4AST_G 260 TEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQALN 316
Cdd:cd19074 234 TDENLEKVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKASG 290
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
13-330 |
1.73e-84 |
|
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: 258.29 E-value: 1.73e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 13 MQYRYCGKSGLRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGPppGSAEENFGRLLREdFAAYRDEL 92
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSWVTFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYAN--GQSEEIMGQAIKE-LGWPRSDY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 93 IISTKAgydMW----PGPYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGIS 168
Cdd:cd19143 78 VVSTKI---FWggggPPPNDRGLSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGTS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 169 SYSPERTQKMVELLREWK-IPLLIHQPSYNLLNRW---VDKSGLLdtlQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSRM 244
Cdd:cd19143 155 EWSAQQIEEAHEIADRLGlIPPVMEQPQYNLFHRErveVEYAPLY---EKYGLGTTTWSPLASGLLTGKYNNGIPEGSRL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 245 HREGNKVRGLTPKMLTEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQALNNLTFSTKE 324
Cdd:cd19143 232 ALPGYEWLKDRKEELGQEKIEKVRKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEENLKALEVLPKLTPE 311
|
....*..
4AST_G 325 -LAQIDQ 330
Cdd:cd19143 312 vMEKIEA 318
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
19-324 |
1.95e-81 |
|
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: 250.19 E-value: 1.95e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 19 GKSGLRLPALSLGLWHnFG-------HVNALESqRAILRKAFDLGITHFDLANNYGPppGSAEENFGRLLREdfAAYRDE 91
Cdd:cd19079 6 GNSGLKVSRLCLGCMS-FGdpkwrpwVLDEEES-RPIIKRALDLGINFFDTANVYSG--GASEEILGRALKE--FAPRDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 92 LIISTKAGYDMWPGPYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYS 171
Cdd:cd19079 80 VVIATKVYFPMGDGPNGRGLSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGASSMY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 172 PERTQKMVEL--LREWkIPLLIHQPSYNLLNRwVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKY------LNGIPQDSR 243
Cdd:cd19079 160 AWQFAKALHLaeKNGW-TKFVSMQNHYNLLYR-EEEREMIPLCEEEGIGVIPWSPLARGRLARPWgdtterRRSTTDTAK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 244 MHREGnkvrgltpkmLTEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQALN-NLTFST 322
Cdd:cd19079 238 LKYDY----------FTEADKEIVDRVEEVAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAALDiKLSEEE 307
|
..
4AST_G 323 KE 324
Cdd:cd19079 308 IK 309
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
22-329 |
1.38e-74 |
|
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: 232.03 E-value: 1.38e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 22 GLRLPALSLGLW----HNFGHVNALESQRAIlRKAFDLGITHFDLANNYGPppGSAEENFGRLLREdfaaYRDELIISTK 97
Cdd:cd19084 1 DLKVSRIGLGTWaiggTWWGEVDDQESIEAI-KAAIDLGINFFDTAPVYGF--GHSEEILGKALKG----RRDDVVIATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 98 AGYDmWPGPYGSG--GSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPERT 175
Cdd:cd19084 74 CGLR-WDGGKGVTkdLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 176 QKMVELlrewkIPLLIHQPSYNLLNRWVDKSgLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGI---PQDSRmhREGNKVR 252
Cdd:cd19084 153 EEARKY-----GPIVSLQPPYSMLEREIEEE-LLPYCRENGIGVLPYGPLAQGLLTGKYKKEPtfpPDDRR--SRFPFFR 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
4AST_G 253 GltPKMltEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQALnNLTFSTKELAQID 329
Cdd:cd19084 225 G--ENF--EKNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGAL-DWELTEEELKEID 296
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
26-313 |
3.01e-72 |
|
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: 223.93 E-value: 3.01e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 26 PALSLGLWHnFGHVNALESQRAILRKAFDLGITHFDLANNYGPppGSAEENFGRLLREDFAayRDELIISTKAGYDMWPG 105
Cdd:cd06660 1 SRLGLGTMT-FGGDGDEEEAFALLDAALEAGGNFFDTADVYGD--GRSERLLGRWLKGRGN--RDDVVIATKGGHPPGGD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 106 PYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPERTQKMVELLREW 185
Cdd:cd06660 76 PSRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKAH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 186 -KIPLLIHQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLltgkylngipqdsrmhregnkvrgltpkmlteanl 264
Cdd:cd06660 156 gLPGFAAVQPQYSLLDRSPMEEELLDWAEENGLPLLAYSPLARGP----------------------------------- 200
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
4AST_G 265 nslrllnemaqqrgqsmAQMALSWLLKDDRVTSVLIGASRAEQLEENVQ 313
Cdd:cd06660 201 -----------------AQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
13-329 |
2.86e-71 |
|
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: 223.99 E-value: 2.86e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 13 MQYRYCGKSGLRLPALSLGLWhNFGHVNALESQRAILRKAFDLGITHFDLANNYGPppGSAEENFGRLLREDfaayRDEL 92
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGTM-NFGGRTDEETSFAIMDRALDAGINFFDTADVYGG--GRSEEIIGRWIAGR----RDDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 93 IISTKAGYDMWPGPYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSP 172
Cdd:cd19087 74 VLATKVFGPMGDDPNDRGLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 173 ERTQKMVELLREWKIPLLI-HQPSYNLLNRWVDKSgLLDTLQNNGVGCIAFTPLAQGLLTGKYLNG--IPQDSRMHREGN 249
Cdd:cd19087 154 WQIAKAQGIAARRGLLRFVsEQPMYNLLKRQAELE-ILPAARAYGLGVIPYSPLAGGLLTGKYGKGkrPESGRLVERARY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 250 KVRGLTPKMLTEAnlnslRLLNEMAQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQALnNLTFSTKELAQID 329
Cdd:cd19087 233 QARYGLEEYRDIA-----ERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAAL-EITLTPELLAEID 306
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
19-329 |
2.36e-70 |
|
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: 221.70 E-value: 2.36e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 19 GKSGLRLPALSLGLWhNFGHVNALESQRAILRKAFDLGITHFDLANNY-----GPPPGSAEENFGRLLREDFAayRDELI 93
Cdd:cd19081 3 GRTGLSVSPLCLGTM-VFGWTADEETSFALLDAFVDAGGNFIDTADVYsawvpGNAGGESETIIGRWLKSRGK--RDRVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 94 ISTKAGYDMWPGpyGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPE 173
Cdd:cd19081 80 IATKVGFPMGPN--GPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYSAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 174 RTQKMVELLREWKIPLLIH-QPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSRMHREGNkvr 252
Cdd:cd19081 158 RLQEALELSRQHGLPRYVSlQPEYNLVDRESFEGELLPLCREEGIGVIPYSPLAGGFLTGKYRSEADLPGSTRRGEA--- 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
4AST_G 253 glTPKMLTEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQAlNNLTFSTKELAQID 329
Cdd:cd19081 235 --AKRYLNERGLRILDALDEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAA-AGLRLTDEEVARLD 308
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
13-330 |
4.07e-70 |
|
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: 221.33 E-value: 4.07e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 13 MQYRYCGKSGLRLPALSLG---------LWHNFGHVNALESQRaILRKAFDLGITHFDLANNYGPppGSAEENFGRLLRe 83
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGtmtfgggggFFGAWGGVDQEEADR-LVDIALDAGINFFDTADVYSE--GESEEILGKALK- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 84 dfaAYRDELIISTKAGYDMWPGPYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKAL 163
Cdd:cd19091 77 ---GRRDDVLIATKVRGRMGEGPNDVGLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 164 YVGISSYSPERTQKMVEL--LREWkIPLLIHQPSYNLLNRWVDKSgLLDTLQNNGVGCIAFTPLAQGLLTGKYLNG--IP 239
Cdd:cd19091 154 YIGVSNFSAWQIMKALGIseRRGL-ARFVALQAYYSLLGRDLEHE-LMPLALDQGVGLLVWSPLAGGLLSGKYRRGqpAP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 240 QDSRMHREGnkvrGLTPKMLTEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQALnNLT 319
Cdd:cd19091 232 EGSRLRRTG----FDFPPVDRERGYDVVDALREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGAA-GLS 306
|
330
....*....|.
4AST_G 320 FSTKELAQIDQ 330
Cdd:cd19091 307 LTPEEIARLDK 317
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
25-330 |
2.11e-66 |
|
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: 210.91 E-value: 2.11e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 25 LPALSLGLW-----HNFGHVNALESqRAILRKAFDLGITHFDLANNYGPppGSAEENFGRLLREDfaayRDELIISTKAG 99
Cdd:cd19085 1 VSRLGLGCWqfgggYWWGDQDDEES-IATIHAALDAGINFFDTAEAYGD--GHSEEVLGKALKGR----RDDVVIATKVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 100 YDMwpgpygsgGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPERTQKMV 179
Cdd:cd19085 74 PDN--------LTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 180 ELlrewkIPLLIHQPSYNLLNRWVDKsGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSRMHREGNKVRGLtPKML 259
Cdd:cd19085 146 DA-----GRIDSNQLPYNLLWRAIEY-EILPFCREHGIGVLAYSPLAQGLLTGKFSSAEDFPPGDARTRLFRHFE-PGAE 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
4AST_G 260 TEAnLNSLRLLNEMAQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQALnNLTFSTKELAQIDQ 330
Cdd:cd19085 219 EET-FEALEKLKEIADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAV-DLELSPSVLERLDE 287
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
14-328 |
3.26e-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: 3.26e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 14 QYRYCGKSGLRLPALSLG---LWHNFGHVNALESqRAILRKAFDLGITHFDLANNYGPppGSAEENFGRLLREdfaaYRD 90
Cdd:cd19076 1 PTRKLGTQGLEVSALGLGcmgMSAFYGPADEEES-IATLHRALELGVTFLDTADMYGP--GTNEELLGKALKD----RRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 91 ELIISTKAGYDMWPGPYGSG--GSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGIS 168
Cdd:cd19076 74 EVVIATKFGIVRDPGSGFRGvdGRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 169 SYSPErtqkmvELLREWKI-PLLIHQPSYNLLNRWVDKsGLLDTLQNNGVGCIAFTPLAQGLLTGKYlngipqDSRMHRE 247
Cdd:cd19076 154 EASAD------TIRRAHAVhPITAVQSEYSLWTRDIED-EVLPTCRELGIGFVAYSPLGRGFLTGAI------KSPEDLP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 248 GNKVRGLTPKMLTEA---NLNSLRLLNEMAQQRGQSMAQMALSWLL-KDDRVtsVLI-GASRAEQLEENVQALnNLTFST 322
Cdd:cd19076 221 EDDFRRNNPRFQGENfdkNLKLVEKLEAIAAEKGCTPAQLALAWVLaQGDDI--VPIpGTKRIKYLEENVGAL-DVVLTP 297
|
....*.
4AST_G 323 KELAQI 328
Cdd:cd19076 298 EELAEI 303
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
15-315 |
1.28e-59 |
|
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: 194.20 E-value: 1.28e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 15 YRYCGKSGLRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGPppGSAEENFGRLLREDfAAYRDELII 94
Cdd:cd19141 2 YRNLGKSGLRVSCLGLGTWVTFGSQISDEVAEELVTLAYENGINLFDTAEVYAA--GKAEIVLGKILKKK-GWRRSSYVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 95 STKAgydMWPGPYGS--GGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSP 172
Cdd:cd19141 79 TTKI---FWGGKAETerGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 173 ERTQKMVELLREWK-IPLLIHQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSRMHREGnkV 251
Cdd:cd19141 156 MEIMEAYSVARQFNlIPPIVEQAEYHLFQREKVEMQLPELFHKIGVGAMTWSPLACGILSGKYDDGVPEYSRASLKG--Y 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
4AST_G 252 RGLTPKMLTEANLNSLRLLNEM---AQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQAL 315
Cdd:cd19141 234 QWLKEKILSEEGRRQQAKLKELqiiADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQAI 300
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
19-329 |
2.24e-59 |
|
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: 193.59 E-value: 2.24e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 19 GKSGLRLPALSLG---LWHNFGHVNALESQRAILRKAFDLGITHFDLANNYgpPPGSAEENFGRLLREDfaayRDELIIS 95
Cdd:cd19080 4 GRSGLRVSPLALGtmtFGTEWGWGADREEARAMFDAYVEAGGNFIDTANNY--TNGTSERLLGEFIAGN----RDRIVLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 96 TKAGYDMWPG-PYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPER 174
Cdd:cd19080 78 TKYTMNRRPGdPNAGGNHRKNLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDTPAWV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 175 TQKMVEL--LREWKiPLLIHQPSYNLLNRWVDKSgLLDTLQNNGVGCIAFTPLAQGLLTGKYLngiPQDSRMHREGNKVR 252
Cdd:cd19080 158 VARANTLaeLRGWS-PFVALQIEYSLLERTPERE-LLPMARALGLGVTPWSPLGGGLLTGKYQ---RGEEGRAGEAKGVT 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
4AST_G 253 GLTPKmLTEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQALnNLTFSTKELAQID 329
Cdd:cd19080 233 VGFGK-LTERNWAIVDVVAAVAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGAL-DLTLSPEQLARLD 307
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
13-329 |
7.09e-58 |
|
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: 190.25 E-value: 7.09e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 13 MQYRYCGKSGLRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGPppGSAEENFGRLLREDfAAYRDEL 92
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAA--GKAEVILGSIIKKK-GWRRSSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 93 IISTKAgydMWPGPYGS--GGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSY 170
Cdd:cd19159 78 VITTKL---YWGGKAETerGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 171 SPERTQKMVELLREWK-IPLLIHQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSRMHREGn 249
Cdd:cd19159 155 SAMEIMEAYSVARQFNmIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKC- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 250 kVRGLTPKMLTE---ANLNSLRLLNEMAQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQALNNL-TFSTKEL 325
Cdd:cd19159 234 -YQWLKERIVSEegrKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLpKMTSHVV 312
|
....
4AST_G 326 AQID 329
Cdd:cd19159 313 NEID 316
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
24-329 |
1.45e-56 |
|
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: 185.89 E-value: 1.45e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 24 RLPALSLGLWH------NFGHVNALESQRAILRKAFDLGITHFDLANNYGPppGSAEENFGRLLREDfaAYRDELIISTK 97
Cdd:cd19093 1 EVSPLGLGTWQwgdrlwWGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYGT--GRSERLLGRFLKEL--GDRDEVVIATK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 98 agydMWPGPYGsgGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDEN-TPMEETASALAHAVQSGKALYVGISSYSPERTQ 176
Cdd:cd19093 77 ----FAPLPWR--LTRRSVVKALKASLERLGLDSIDLYQLHWPGPWySQIEALMDGLADAVEEGLVRAVGVSNYSADQLR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 177 KMVELLREWKIPLLIHQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKYlngipqdSRMHREGNKVRGL-T 255
Cdd:cd19093 151 RAHKALKERGVPLASNQVEYSLLYRDPEQNGLLPACDELGITLIAYSPLAQGLLTGKY-------SPENPPPGGRRRLfG 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
4AST_G 256 PKMLTEanLNSLR-LLNEMAQQRGQSMAQMALSWLLKDDRVtsVLIGASRAEQLEENVQALnNLTFSTKELAQID 329
Cdd:cd19093 224 RKNLEK--VQPLLdALEEIAEKYGKTPAQVALNWLIAKGVV--PIPGAKNAEQAEENAGAL-GWRLSEEEVAELD 293
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
13-330 |
5.32e-56 |
|
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: 185.19 E-value: 5.32e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 13 MQYRYCGKSGLRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGPppGSAEENFGRLLREDfAAYRDEL 92
Cdd:cd19160 3 MKYRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDLLTVAYEHGVNLFDTAEVYAA--GKAERTLGNILKSK-GWRRSSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 93 IISTKAgydMWPGPYGS--GGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSY 170
Cdd:cd19160 80 VVTTKI---YWGGQAETerGLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 171 SPERTQKMVELLREWK-IPLLIHQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSRMHREGn 249
Cdd:cd19160 157 SAMEIMEAYSVARQFNlIPPVCEQAEYHLFQREKVEMQLPELYHKIGVGSVTWSPLACGLITGKYDGRVPDTCRAAVKG- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 250 kVRGLTPKMLTE---ANLNSLRLLNEMAQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQALNNLTFSTKELA 326
Cdd:cd19160 236 -YQWLKEKVQSEegkKQQAKVKELHPIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGSIQVLSQLTPQTV 314
|
....*
4AST_G 327 Q-IDQ 330
Cdd:cd19160 315 MeIDA 319
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
22-332 |
7.84e-55 |
|
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: 181.66 E-value: 7.84e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 22 GLRLPALSLG---LWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGPPpgSAEEnfgrLLREDFAAYRDELIISTKA 98
Cdd:cd19078 1 GLEVSAIGLGcmgMSHGYGPPPDKEEMIELIRKAVELGITFFDTAEVYGPY--TNEE----LVGEALKPFRDQVVIATKF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 99 GYDMWPGPYGSGG---SRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPERT 175
Cdd:cd19078 75 GFKIDGGKPGPLGldsRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 176 QKMVELLrewkiPLLIHQPSYNLLNRWVDKSgLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSRMHRegNKVRGLT 255
Cdd:cd19078 155 RRAHAVC-----PVTAVQSEYSMMWREPEKE-VLPTLEELGIGFVPFSPLGKGFLTGKIDENTKFDEGDDR--ASLPRFT 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
4AST_G 256 PKMLtEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQALnNLTFSTKELAQIDQHI 332
Cdd:cd19078 227 PEAL-EANQALVDLLKEFAEEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAA-DIELTPEELREIEDAL 301
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
19-329 |
8.22e-55 |
|
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: 181.46 E-value: 8.22e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 19 GKSGLRLPALSLGLWHNFGH---VNALESQ-RAILRKAFDLGITHFDLANNYGPppGSAEENFGRLLREdfaAYRDELII 94
Cdd:cd19083 5 GKSDIDVNPIGLGTNAVGGHnlyPNLDEEEgKDLVREALDNGVNLLDTAFIYGL--GRSEELVGEVLKE---YNRNEVVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 95 STKAGYDMWPGPYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPER 174
Cdd:cd19083 80 ATKGAHKFGGDGSVLNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFSLEQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 175 TQK-----MVELLrewkipllihQPSYNLLNRWVDKsGLLDTLQNNGVGCIAFTPLAQGLLTGKYlngiPQDSRMHRegN 249
Cdd:cd19083 160 LKEankdgYVDVL----------QGEYNLLQREAEE-DILPYCVENNISFIPYFPLASGLLAGKY----TKDTKFPD--N 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 250 KVRGLTPKMLTEA---NLNSLRLLNEMAQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQALnNLTFSTKELA 326
Cdd:cd19083 223 DLRNDKPLFKGERfseNLDKVDKLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKAL-DVTLTEEEIA 301
|
...
4AST_G 327 QID 329
Cdd:cd19083 302 FID 304
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
13-329 |
7.01e-54 |
|
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: 179.90 E-value: 7.01e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 13 MQYRYCGKSGLRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGPppGSAEENFGRLLREDfAAYRDEL 92
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAA--GKAEVVLGNIIKKK-GWRRSSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 93 IISTKAgydMWPGPYGS--GGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSY 170
Cdd:cd19158 78 VITTKI---FWGGKAETerGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 171 SPERTQKMVELLREWK-IPLLIHQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSRMHREGn 249
Cdd:cd19158 155 SSMEIMEAYSVARQFNlIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKG- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 250 kVRGLTPKMLTEANLNS---LRLLNEMAQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQALNNL-TFSTKEL 325
Cdd:cd19158 234 -YQWLKDKILSEEGRRQqakLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVLpKLSSSIV 312
|
....
4AST_G 326 AQID 329
Cdd:cd19158 313 HEID 316
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
35-329 |
8.12e-52 |
|
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: 174.29 E-value: 8.12e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 35 NFGHVNALESQRAILRKAFDLGITHFDLANNYGPPP-----GSAEENFGRLLREDfaAYRDELIISTK-AGY--DM-WPG 105
Cdd:cd19094 10 TWGEQNTEAEAHEQLDYAFDEGVNFIDTAEMYPVPPspetqGRTEEIIGSWLKKK--GNRDKVVLATKvAGPgeGItWPR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 106 PYGSGGSRKYLLASLDQSLKRMGLEYVDIF------------------YSHRVDENTPMEETASALAHAVQSGKALYVGI 167
Cdd:cd19094 88 GGGTRLDRENIREAVEGSLKRLGTDYIDLYqlhwpdrytplfgggyytEPSEEEDSVSFEEQLEALGELVKAGKIRHIGL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 168 SSYSPERTQKMVELLREWKIPLLIH-QPSYNLLNRwVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNG--IPQDSRM 244
Cdd:cd19094 168 SNETPWGVMKFLELAEQLGLPRIVSiQNPYSLLNR-NFEEGLAEACHRENVGLLAYSPLAGGVLTGKYLDGaaRPEGGRL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 245 hregNKVRGLTPKMLTEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQALnNLTFSTKE 324
Cdd:cd19094 247 ----NLFPGYMARYRSPQALEAVAEYVKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLKENIDAF-DVPLSDEL 321
|
....*
4AST_G 325 LAQID 329
Cdd:cd19094 322 LAEID 326
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
26-315 |
6.16e-51 |
|
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: 171.59 E-value: 6.16e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 26 PALSLGLwHNFGHVNA---LESQRAILRKAFDLGITHFDLANNYgpPPGSAEENFGRLLREDfaayrDELIISTKAgyDM 102
Cdd:cd19075 1 PKIILGT-MTFGSQGRfttAEAAAELLDAFLERGHTEIDTARVY--PDGTSEELLGELGLGE-----RGFKIDTKA--NP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 103 WPGPygsGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPERTQKMVELL 182
Cdd:cd19075 71 GVGG---GLSPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEIC 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 183 RE--WKIPlLIHQPSYNLLNRWVDKSgLLDTLQNNGVGCIAFTPLAQGLLTGKY--LNGIPQDSRMhREGNKVRGLTPKM 258
Cdd:cd19075 148 KEngWVLP-TVYQGMYNAITRQVETE-LFPCLRKLGIRFYAYSPLAGGFLTGKYkySEDKAGGGRF-DPNNALGKLYRDR 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
4AST_G 259 -LTEANLNSLRLLNEMAQQRGQSMAQMALSWL-----LKDDRVTSVLIGASRAEQLEENVQAL 315
Cdd:cd19075 225 yWKPSYFEALEKVEEAAEKEGISLAEAALRWLyhhsaLDGEKGDGVILGASSLEQLEENLAAL 287
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
13-315 |
8.02e-51 |
|
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.
Pssm-ID: 381368 [Multi-domain] Cd Length: 325 Bit Score: 171.88 E-value: 8.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 13 MQYRYCGKSGLRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANnyGPPPGSAEENFGRLLREDfAAYRDEL 92
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGTWSTFSTAISEEQAEEIVTLAYENGINYFDTSD--AFTSGQAETELGRILKKK-GWKRSSY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 93 IISTKAGYDMwpGPYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSP 172
Cdd:cd19142 78 IVSTKIYWSY--GSEERGLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRWSP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 173 ERTQKMVELLREWKIPLLI-HQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSRM-HREGNK 250
Cdd:cd19142 156 VEIMEAFSIARQFNCPTPIcEQSEYHMFCREKMELYMPELYNKVGVGLITWSPLSLGLDPGISEETRRLVTKLsFKSSKY 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
4AST_G 251 VRGLTPKML---TEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQAL 315
Cdd:cd19142 236 KVGSDGNGIheeTRRASHKLRELSLIAERLGCDLTQLLIAWSLKNENVQCVLIGASSLEQLYSQLNSL 303
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
23-314 |
7.31e-49 |
|
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase YqkF is a founding member of aldo-keto reductase family 11 member C1 (AKR11C1). It may function as oxidoreductase. This family also includes Bacillus halodurans AKR11C1, an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase.
Pssm-ID: 381312 [Multi-domain] Cd Length: 238 Bit Score: 163.80 E-value: 7.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 23 LRLPALSLGLW----HNFGHVNALESQRAIlRKAFDLGITHFDLANNYGPppGSAEENFGRLLREDfaayRDELIISTKA 98
Cdd:cd19086 1 LEVSEIGFGTWglggDWWGDVDDAEAIRAL-RAALDLGINFFDTADVYGD--GHSERLLGKALKGR----RDKVVIATKF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 99 GYDMWPGPYGSGG-SRKYLLASLDQSLKRMGLEYVDIFYSHRV-DENTPMEETASALAHAVQSGKALYVGISSYSPERtq 176
Cdd:cd19086 74 GNRFDGGPERPQDfSPEYIREAVEASLKRLGTDYIDLYQLHNPpDEVLDNDELFEALEKLKQEGKIRAYGVSVGDPEE-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 177 kMVELLREWKIPLLihQPSYNLLNRWVDKsGLLDTLQNNGVGCIAFTPLAQGLLTGKylngipqdsrmhregnkvrgltp 256
Cdd:cd19086 152 -ALAALRRGGIDVV--QVIYNLLDQRPEE-ELFPLAEEHGVGVIARVPLASGLLTGK----------------------- 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
4AST_G 257 kmlteanlnslrllnemaqqrgqsMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQA 314
Cdd:cd19086 205 ------------------------LAQAALRFILSHPAVSTVIPGARSPEQVEENAAA 238
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
31-330 |
1.17e-47 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 162.84 E-value: 1.17e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 31 GLWHNFGHVNALESQRAIlRKAFDLGITHFDLANNYGPppGSAEENFGRLLREdfaaYRDELIISTKAGYdMW--PGPYG 108
Cdd:cd19102 15 GWGGGWGPQDDRDSIAAI-RAALDLGINWIDTAAVYGL--GHSEEVVGRALKG----LRDRPIVATKCGL-LWdeEGRIR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 109 SGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPErtqkmvELLREWKI- 187
Cdd:cd19102 87 RSLKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVD------QMKRCQAIh 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 188 PLLIHQPSYNLLNRWVDKSgLLDTLQNNGVGCIAFTPLAQGLLTGK----YLNGIPQDSRMHREgnkvrgltpKMLTEAN 263
Cdd:cd19102 161 PIASLQPPYSLLRRGIEAE-ILPFCAEHGIGVIVYSPMQSGLLTGKmtpeRVASLPADDWRRRS---------PFFQEPN 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
4AST_G 264 LN-SLRLLNEM---AQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQALnNLTFSTKELAQIDQ 330
Cdd:cd19102 231 LArNLALVDALrpiAERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAA-DLRLTPEELAEIEA 300
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
22-329 |
4.28e-47 |
|
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: 160.09 E-value: 4.28e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 22 GLRLPALSLGLWHNFGHVNALESQR----AILRKAFDLGITHFDLANNYGPppGSAEENFGRLLReDFAayRDELIISTK 97
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGMSKDYSDDkkaiEALRYAIELGINLIDTAEMYGG--GHAEELVGKAIK-GFD--REDLFITTK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 98 AgydmWPgpygSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPERTQK 177
Cdd:cd19072 76 V----SP----DHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 178 MVELLRewKIPLLIHQPSYNLLNRWVDKsGLLDTLQNNGVGCIAFTPLAQGLLTGKYLngipqdsrmhregnkvrgltpk 257
Cdd:cd19072 148 AQSYLK--KGPIVANQVEYNLFDREEES-GLLPYCQKNGIAIIAYSPLEKGKLSNAKG---------------------- 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
4AST_G 258 mlteanlnsLRLLNEMAQQRGQSMAQMALSWLLKDDRVTsVLIGASRAEQLEENVQALnNLTFSTKELAQID 329
Cdd:cd19072 203 ---------SPLLDEIAKKYGKTPAQIALNWLISKPNVI-AIPKASNIEHLEENAGAL-GWELSEEDLQRLD 263
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
15-330 |
5.80e-47 |
|
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: 161.29 E-value: 5.80e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 15 YRYCGKSGLRLPALSLGLW-----HNFGHVNALESQRAIlRKAFDLGITHFDLANNYGPppGSAEENFGRLLREdfaaYR 89
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTWaigggPWWGGSDDNESIRTI-HAALDLGINLIDTAPAYGF--GHSEEIVGKAIKG----RR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 90 DELIISTKAGYdMWPGPYGSGGS-------RKYLLAS-----LDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAV 157
Cdd:cd19149 74 DKVVLATKCGL-RWDREGGSFFFvrdgvtvYKNLSPEsireeVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 158 QSGKALYVGISSYSPERTQKMVELlrewkIPLLIHQPSYNLLNRWVDKSgLLDTLQNNGVGCIAFTPLAQGLLTGKYL-- 235
Cdd:cd19149 153 RQGKIRAIGASNVSVEQIKEYVKA-----GQLDIIQEKYSMLDRGIEKE-LLPYCKKNNIAFQAYSPLEQGLLTGKITpd 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 236 ---------NGIPQDSRMHREgnKVRGLTPKMLteanlnslrllnEMAQQRGQSMAQMALSWLLKDDRVTSVLIGASRAE 306
Cdd:cd19149 227 refdagdarSGIPWFSPENRE--KVLALLEKWK------------PLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPE 292
|
330 340
....*....|....*....|....
4AST_G 307 QLEENVQALnNLTFSTKELAQIDQ 330
Cdd:cd19149 293 QAEENAKAG-DIRLSAEDIATMRS 315
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
13-336 |
1.89e-45 |
|
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: 157.60 E-value: 1.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 13 MQYRYCGKSGLRLPAL---SLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGPppgsAEENFGRLLREDfAAYR 89
Cdd:cd19144 1 IPTRTLGRNGPSVPALgfgAMGLSAFYGPPKPDEERFAVLDAAFELGCTFWDTADIYGD----SEELIGRWFKQN-PGKR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 90 DELIISTKAGYDMWP--GPYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGI 167
Cdd:cd19144 76 EKIFLATKFGIEKNVetGEYSVDGSPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 168 SSYSPErtqkmvELLREWKI-PLLIHQPSYNLLNRWVDKS--GLLDTLQNNGVGCIAFTPLAQGLLTGKYlngipqDSRM 244
Cdd:cd19144 156 SECSAE------TLRRAHAVhPIAAVQIEYSPFSLDIERPeiGVLDTCRELGVAIVAYSPLGRGFLTGAI------RSPD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 245 HREGNKVRGLTPKMLTEANLNSLRLLNEM---AQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQALnNLTFS 321
Cdd:cd19144 224 DFEEGDFRRMAPRFQAENFPKNLELVDKIkaiAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLGAL-KVKLT 302
|
330
....*....|....*
4AST_G 322 TKELAQIDQHIADGE 336
Cdd:cd19144 303 EEEEKEIREIAEEAE 317
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
26-316 |
2.81e-45 |
|
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: 155.79 E-value: 2.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 26 PALSLG---LWHNFGHVnALESQRAILRKAFDLGITHFDLANNYGPppgsAEENFGRLLREdfaAYRDELIISTKAGYDM 102
Cdd:cd19090 1 SALGLGtagLGGVFGGV-DDDEAVATIRAALDLGINYIDTAPAYGD----SEERLGLALAE---LPREPLVLSTKVGRLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 103 -WPGPYgsggSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETA-----SALAHAVQSGKALYVGISSYSPErtq 176
Cdd:cd19090 73 eDTADY----SADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILApggalEALLELKEEGLIKHIGLGGGPPD--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 177 KMVELLREWKIPLLIHQPSYNLLNRwVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKYlngipqdsrMHREGNKVRGLTP 256
Cdd:cd19090 146 LLRRAIETGDFDVVLTANRYTLLDQ-SAADELLPAAARHGVGVINASPLGMGLLAGRP---------PERVRYTYRWLSP 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 257 KMLTEAnlnslRLLNEMAQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQALN 316
Cdd:cd19090 216 ELLDRA-----KRLYELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAAE 270
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
20-316 |
1.90e-44 |
|
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: 153.87 E-value: 1.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 20 KSGLRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGPppGSAEENFGRLLREDfAAYRDELIISTKAG 99
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADWGESAEELLSLIEAALELGITTFDHADIYGG--GKCEELFGEALALN-PGLREKIEIQTKCG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 100 -------YDMWPGPYGSggSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSP 172
Cdd:cd19092 78 irlgddpRPGRIKHYDT--SKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFTP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 173 ERTqkmvELL-REWKIPLLIHQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGkylngiPQDSRMHRegnkV 251
Cdd:cd19092 156 SQI----ELLqSYLDQPLVTNQIELSLLHTEAIDDGTLDYCQLLDITPMAWSPLGGGRLFG------GFDERFQR----L 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
4AST_G 252 RgltpkmlteanlnslRLLNEMAQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQALN 316
Cdd:cd19092 222 R---------------AALEELAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALD 271
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
47-316 |
1.07e-43 |
|
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) and Streptomyces glaucescens aldo-keto reductase (StrT) are founding members of aldo-keto reductase family 10 member A1 (AKR10A1) and A2 (AKR10A2). BlmT is bluensomycin aldo-keto reductase (AKR) and StrT is streptomycin AKR.
Pssm-ID: 381308 [Multi-domain] Cd Length: 291 Bit Score: 152.32 E-value: 1.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 47 AILRKAFDLGITHFDLANNYG--PPPGSAEENFGRLLREDfaAYRDELIISTKAGYDMWPGPYGSGGSRKYLLASLDQSL 124
Cdd:cd19082 21 ALLDAFVELGGNFIDTARVYGdwVERGASERVIGEWLKSR--GNRDKVVIATKGGHPDLEDMSRSRLSPEDIRADLEESL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 125 KRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPERTQKMVELLRE-WKIPLLIHQPSYNL----L 199
Cdd:cd19082 99 ERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNWSTERIAEANAYAKAhGLPGFAASSPQWSLarpnE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 200 NRWVDKSG------LLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSRMHRegnkvrgltpKMLTEANLNSLRLLNEM 273
Cdd:cd19082 179 PPWPGPTLvamdeeMRAWHEENQLPVFAYSSQARGFFSKRAAGGAEDDSELRR----------VYYSEENFERLERAKEL 248
|
250 260 270 280
....*....|....*....|....*....|....*....|...
4AST_G 274 AQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQALN 316
Cdd:cd19082 249 AEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAAAD 291
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
46-315 |
1.65e-42 |
|
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: 148.13 E-value: 1.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 46 RAILRKAFDLGITHFDLANNYGPppGSAEenfgRLLREDFAAYRDELIISTKAGydmW----PGPYGSGGSRKYLLASLD 121
Cdd:cd19088 27 IAVLRRALELGVNFIDTADSYGP--DVNE----RLIAEALHPYPDDVVIATKGG---LvrtgPGWWGPDGSPEYLRQAVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 122 QSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSP---ERTQKMVELLREwkipllihQPSYNL 198
Cdd:cd19088 98 ASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVaqiEEARAIVRIVSV--------QNRYNL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 199 LNRwvDKSGLLDTLQNNGVGCIAFTPLAQGLLTGkylngipqdsrmhregnkvrgltpkmlteanlnSLRLLNEMAQQRG 278
Cdd:cd19088 170 ANR--DDEGVLDYCEAAGIAFIPWFPLGGGDLAQ---------------------------------PGGLLAEVAARLG 214
|
250 260 270
....*....|....*....|....*....|....*..
4AST_G 279 QSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQAL 315
Cdd:cd19088 215 ATPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAAA 251
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-315 |
3.06e-42 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 147.35 E-value: 3.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 13 MQYRYCGKSGLRLPALSLGlwhnfGHVNALESQrAILRKAFDLGITHFDLANNYGPppGSAEENFGRLLREdfaAYRDEL 92
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFG-----GGGLPRESP-ELLRRALDLGINYFDTAEGYGN--GNSEEIIGEALKG---LRRDKV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 93 IISTKAGydmwpgPYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTP---MEETASALAHAVQSGKALYVGISS 169
Cdd:cd19105 70 FLATKAS------PRLDKKDKAELLKSVEESLKRLQTDYIDIYQLHGVDTPEErllNEELLEALEKLKKEGKVRFIGFST 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 170 YSPertqkMVELLREwkiplLIH-------QPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLtgkylngIPQDS 242
Cdd:cd19105 144 HDN-----MAEVLQA-----AIEsgwfdviMVAYNFLNQPAELEEALAAAAEKGIGVVAMKTLAGGYL-------QPALL 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
4AST_G 243 RMHREGnkvrgltpkmlteanlnslrllnemaqqrGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQAL 315
Cdd:cd19105 207 SVLKAK-----------------------------GFSLPQAALKWVLSNPRVDTVVPGMRNFAELEENLAAA 250
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
26-314 |
8.13e-42 |
|
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381321 [Multi-domain] Cd Length: 253 Bit Score: 146.23 E-value: 8.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 26 PALSLGLWHNFGHVNALESQRA--ILRKAFDLGITHFDLANNYGpppgSAEENFGRLLREDFaayRDELIISTKAGYdmw 103
Cdd:cd19095 1 SVLGLGTSGIGRVWGVPSEAEAarLLNTALDLGINLIDTAPAYG----RSEERLGRALAGLR---RDDLFIATKVGT--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 104 PGPYGSGG---SRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPErtqkMVE 180
Cdd:cd19095 71 HGEGGRDRkdfSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVSGDGEE----LEA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 181 LLREWKIPLLihQPSYNLLNRWVDKsgLLDTLQNNGVGCIAFTPLAQGLLTgkylngipqdsrmhregNKVRGLTPKMLT 260
Cdd:cd19095 147 AIASGVFDVV--QLPYNVLDREEEE--LLPLAAEAGLGVIVNRPLANGRLR-----------------RRVRRRPLYADY 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
4AST_G 261 EanlnslRLLNEMAQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQA 314
Cdd:cd19095 206 A------RRPEFAAEIGGATWAQAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
47-329 |
3.85e-41 |
|
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: 145.84 E-value: 3.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 47 AILRKAFDLGITHFDLANNYGPPPGSAEEnfgRLLREDFAAY---RDELIISTKAGYDmwPGPYGSGGSRKYLLASLDQS 123
Cdd:cd19077 29 ETMKAALDAGSNLWNGGEFYGPPDPHANL---KLLARFFRKYpeyADKVVLSVKGGLD--PDTLRPDGSPEAVRKSIENI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 124 LKRMG-LEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPErtqkmvELLREWKI-PLLIHQPSYNLLNR 201
Cdd:cd19077 104 LRALGgTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAE------TIRRAHAVhPIAAVEVEYSLFSR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 202 WVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKY--LNGIPqDSRMHREGNKvrgLTPKMLtEANLNSLRLLNEMAQQRGQ 279
Cdd:cd19077 178 EIEENGVLETCAELGIPIIAYSPLGRGLLTGRIksLADIP-EGDFRRHLDR---FNGENF-EKNLKLVDALQELAEKKGC 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
4AST_G 280 SMAQMALSWLLKDDRVTSVLI-GASRAEQLEENVQALnNLTFSTKELAQID 329
Cdd:cd19077 253 TPAQLALAWILAQSGPKIIPIpGSTTLERVEENLKAA-NVELTDEELKEIN 302
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-329 |
2.12e-40 |
|
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: 144.33 E-value: 2.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 14 QYRYCGKSGLRLPALSLG------LWhnfGHVNAlESQRAILRKAFDLGITHFDLANNYGppPGSAEENFGRLLREDfaa 87
Cdd:cd19104 1 KYRRFGRTGLKVSELTFGgggiggLM---GRTTR-EEQIAAVRRALDLGINFFDTAPSYG--DGKSEENLGRALKGL--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 88 yRDELIISTKAGYDmwPGPYGSGGSRkyLLASLDQSLKRMGLEYVDIFYSH---RVDENTPMEETAS------------A 152
Cdd:cd19104 72 -PAGPYITTKVRLD--PDDLGDIGGQ--IERSVEKSLKRLKRDSVDLLQLHnriGDERDKPVGGTLSttdvlglggvadA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 153 LAHAVQSGKALYVGISSYSPERTqkMVELLREWKIPLLihQPSYNLLN---------RWV--DKSGLLDTLQNNGVGCIA 221
Cdd:cd19104 147 FERLRSEGKIRFIGITGLGNPPA--IRELLDSGKFDAV--QVYYNLLNpsaaearprGWSaqDYGGIIDAAAEHGVGVMG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 222 FTPLAQGLLTGkylngipqDSRMHREGNkvrgLTPKMLTEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDDRVTSVLIG 301
Cdd:cd19104 223 IRVLAAGALTT--------SLDRGREAP----PTSDSDVAIDFRRAAAFRALAREWGETLAQLAHRFALSNPGVSTVLVG 290
|
330 340
....*....|....*....|....*...
4AST_G 302 ASRAEQLEENVQALNNLTFSTKELAQID 329
Cdd:cd19104 291 VKNREELEEAVAAEAAGPLPAENLARLE 318
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
46-310 |
3.61e-40 |
|
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381374 [Multi-domain] Cd Length: 302 Bit Score: 143.22 E-value: 3.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 46 RAILRKAFDLGITHFDLANNYGPppGSAEENFGRLLREdfAAYRDELIISTKAGYDmWP--GPYGSGGSRKYLLASLDQS 123
Cdd:cd19148 28 IETIHKALDLGINLIDTAPVYGF--GLSEEIVGKALKE--YGKRDRVVIATKVGLE-WDegGEVVRNSSPARIRKEVEDS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 124 LKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPERtqkmVELLREwKIPLLIHQPSYNLLNRWV 203
Cdd:cd19148 103 LRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSPEQ----METFRK-VAPLHTVQPPYNLFEREI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 204 DKSgLLDTLQNNGVGCIAFTPLAQGLLTGKylngIPQDSRMhrEGNKVRGLTPKmLTEAN----LNSLRLLNEMAQQR-G 278
Cdd:cd19148 178 EKD-VLPYARKHNIVTLAYGALCRGLLSGK----MTKDTKF--EGDDLRRTDPK-FQEPRfsqyLAAVEELDKLAQERyG 249
|
250 260 270
....*....|....*....|....*....|..
4AST_G 279 QSMAQMALSWLLKDDRVTSVLIGASRAEQLEE 310
Cdd:cd19148 250 KSVIHLAVRWLLDQPGVSIALWGARKPEQLDA 281
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
13-330 |
3.07e-38 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 139.57 E-value: 3.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 13 MQYRYCGKSGLRLPALSLGLWHnFGHVNALESQRaILRKAFDLGITHFDLANNYGpppGSaEENFGRLLREdfaaYRDEL 92
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGMR-LPRKDEEEAEA-LIRRAIDNGINYIDTARGYG---DS-EEFLGKALKG----PRDKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 93 IISTKAGydmwpgPYGSggSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETAS------ALAHAVQSGKALYVG 166
Cdd:COG1453 71 ILATKLP------PWVR--DPEDMRKDLEESLKRLQTDYIDLYLIHGLNTEEDLEKVLKpggaleALEKAKAEGKIRHIG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 167 ISSYSPerTQKMVELLREWKIP-LLIHqpsYNLLNrWVDKSG--LLDTLQNNGVGCIAFTPLAQGLLtgkylngipqdsr 243
Cdd:COG1453 143 FSTHGS--LEVIKEAIDTGDFDfVQLQ---YNYLD-QDNQAGeeALEAAAEKGIGVIIMKPLKGGRL------------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 244 mhregnkvrgltpkmlteANLNSlRLLNEMAQQRgqSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQALNNL-TFST 322
Cdd:COG1453 204 ------------------ANPPE-KLVELLCPPL--SPAEWALRFLLSHPEVTTVLSGMSTPEQLDENLKTADNLePLTE 262
|
....*...
4AST_G 323 KELAQIDQ 330
Cdd:COG1453 263 EELAILER 270
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
22-329 |
4.59e-38 |
|
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: 136.55 E-value: 4.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 22 GLRLPALSLGLWHNFGHVNALESQR----AILRKAFDLGITHFDLANNYGPppGSAEENFGRLLReDFAayRDELIISTK 97
Cdd:cd19137 1 GEKIPALGLGTWGIGGFLTPDYSRDeemvELLKTAIELGYTHIDTAEMYGG--GHTEELVGKAIK-DFP--REDLFIVTK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 98 agydMWPgpygSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPERTQK 177
Cdd:cd19137 76 ----VWP----TNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 178 MVELLREwkiPLLIHQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKylngipqdsrmhregnkvrgltpk 257
Cdd:cd19137 148 AISKSQT---PIVCNQVKYNLEDRDPERDGLLEYCQKNGITVVAYSPLRRGLEKTN------------------------ 200
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
4AST_G 258 mlteanlnslRLLNEMAQQRGQSMAQMALSWLLKDDRVTSVLIgASRAEQLEENVQALnNLTFSTKELAQID 329
Cdd:cd19137 201 ----------RTLEEIAKNYGKTIAQIALAWLIQKPNVVAIPK-AGRVEHLKENLKAT-EIKLSEEEMKLLD 260
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
21-329 |
5.41e-38 |
|
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this family. It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381364 [Multi-domain] Cd Length: 266 Bit Score: 136.61 E-value: 5.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 21 SGLRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGPppGSAEENFGRLLREDfaayRDELIISTKagy 100
Cdd:cd19138 7 DGTKVPALGQGTWYMGEDPAKRAQEIEALRAGIDLGMTLIDTAEMYGD--GGSEELVGEAIRGR----RDKVFLVSK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 101 dMWPgpygSGGSRKYLLASLDQSLKRMGLEYVDIFYSH-RvdENTPMEETASALAHAVQSGKALYVGISSYSperTQKMV 179
Cdd:cd19138 78 -VLP----SNASRQGTVRACERSLRRLGTDYLDLYLLHwR--GGVPLAETVAAMEELKKEGKIRAWGVSNFD---TDDME 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 180 ELlreWKIP----LLIHQPSYNLLNRWVDKSgLLDTLQNNGVGCIAFTPLAQGlltgkylnGIPQDSRMHREGnkvrglt 255
Cdd:cd19138 148 EL---WAVPgggnCAANQVLYNLGSRGIEYD-LLPWCREHGVPVMAYSPLAQG--------GLLRRGLLENPT------- 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
4AST_G 256 pkmlteanlnslrlLNEMAQQRGQSMAQMALSWLLKDDRVTSVlIGASRAEQLEENVQALnNLTFSTKELAQID 329
Cdd:cd19138 209 --------------LKEIAARHGATPAQVALAWVLRDGNVIAI-PKSGSPEHARENAAAA-DLELTEEDLAELD 266
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
13-315 |
1.41e-36 |
|
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: 133.45 E-value: 1.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 13 MQYRYCGKSGLRLPALSLG---LWHNFGHVNALESQRAIlRKAFDLGITHFDLANNYGPppGSAEENFGRLLRedfAAYR 89
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGaspLGGVFGPVDEEEAIRTV-HEALDSGINYIDTAPWYGQ--GRSETVLGKALK---GIPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 90 DELIISTKAGYdmwpgpYGSGG------SRKYLLASLDQSLKRMGLEYVDIFYSHRV----DENTPMEETASALAHAVQS 159
Cdd:cd19163 75 DSYYLATKVGR------YGLDPdkmfdfSAERITKSVEESLKRLGLDYIDIIQVHDIefapSLDQILNETLPALQKLKEE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 160 GKALYVGISSYsPERTQKMVELLREWKIPLLIHQPSYNLLNRWVdkSGLLDTLQNNGVGCIAFTPLAQGLLTgkyLNGIP 239
Cdd:cd19163 149 GKVRFIGITGY-PLDVLKEVLERSPVKIDTVLSYCHYTLNDTSL--LELLPFFKEKGVGVINASPLSMGLLT---ERGPP 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
4AST_G 240 QdsrMHREGNKVRGLTPKMLteanlnslrllnEMAQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQAL 315
Cdd:cd19163 223 D---WHPASPEIKEACAKAA------------AYCKSRGVDISKLALQFALSNPDIATTLVGTASPENLRKNLEAA 283
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
23-330 |
1.41e-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: 381329 [Multi-domain] Cd Length: 299 Bit Score: 133.61 E-value: 1.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 23 LRLPALSLGLW----------HNFGHVNALESQRAILRKAFDLGITHFDLANNYGPppGSAEENFGRLLReDFAayRDEL 92
Cdd:cd19103 2 KKLPKIALGTWswgsggaggdQVFGNHLDEDTLKAVFDKAMAAGLNLWDTAAVYGM--GASEKILGEFLK-RYP--REDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 93 IISTKAGydmwpgPYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHR---VDENTPmeetasALAHAVQSGKALYVGISS 169
Cdd:cd19103 77 IISTKFT------PQIAGQSADPVADMLEGSLARLGTDYIDIYWIHNpadVERWTP------ELIPLLKSGKVKHVGVSN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 170 YSPERTQKMVELLREWKIPLLIHQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKYL--NGIPQDSRMhre 247
Cdd:cd19103 145 HNLAEIKRANEILAKAGVSLSAVQNHYSLLYRSSEEAGILDYCKENGITFFAYMVLEQGALSGKYDtkHPLPEGSGR--- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 248 GNKVRGLTPKMlteANLNSlrLLNEMAQQRGQSMAQMALSWLLKddRVTSVLIGASRAEQLEENVQAlNNLTFSTKELAQ 327
Cdd:cd19103 222 AETYNPLLPQL---EELTA--VMAEIGAKHGASIAQVAIAWAIA--KGTTPIIGVTKPHHVEDAARA-ASITLTDDEIKE 293
|
...
4AST_G 328 IDQ 330
Cdd:cd19103 294 LEQ 296
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
26-316 |
1.79e-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: 381391 [Multi-domain] Cd Length: 291 Bit Score: 133.23 E-value: 1.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 26 PALSLGLWhNFGHVNALESQRAILRKAFDLGITHFDLANNY-----GPPPGSAEENFGRLLREDFAayRDELIISTKAGY 100
Cdd:cd19752 1 SELCLGTM-YFGTRTDEETSFAILDRYVAAGGNFLDTANNYafwteGGVGGESERLIGRWLKDRGN--RDDVVIATKVGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 101 dMWPGPYGS-----GGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPERT 175
Cdd:cd19752 78 -GPRDPDGGpespeGLSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 176 QKMVELLRE--WKIPLLIHQP-SYNLLNRWVDKSG-------LLDTLQNNG-VGCIAFTPLAQGLLTgkylngipqdsrm 244
Cdd:cd19752 157 ERARQIARQqgWAEFSAIQQRhSYLRPRPGADFGVqrivtdeLLDYASSRPdLTLLAYSPLLSGAYT------------- 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
4AST_G 245 hREGNKVRgltPKMLTEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQALN 316
Cdd:cd19752 224 -RPDRPLP---EQYDGPDSDARLAVLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAALD 291
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
21-330 |
6.95e-35 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 127.86 E-value: 6.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 21 SGLRLPALSLGLWHnfghVNALESQRAIlRKAFDLGITHFDLANNYGpppgsAEENFGRLLRE-DFAayRDELIISTKag 99
Cdd:COG0656 1 NGVEIPALGLGTWQ----LPGEEAAAAV-RTALEAGYRHIDTAAMYG-----NEEGVGEAIAAsGVP--REELFVTTK-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 100 ydMWPGPYGSGGsrkyLLASLDQSLKRMGLEYVDIFYSH-RVDEntPMEETASALAHAVQSGKALYVGISSYSPERtqkM 178
Cdd:COG0656 67 --VWNDNHGYDD----TLAAFEESLERLGLDYLDLYLIHwPGPG--PYVETWRALEELYEEGLIRAIGVSNFDPEH---L 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 179 VELLREWKIPLLIHQPSYNLLNRWVDksgLLDTLQNNGVGCIAFTPLAQGlltgkylngipqdsrmhregnkvrgltpKM 258
Cdd:COG0656 136 EELLAETGVKPAVNQVELHPYLQQRE---LLAFCREHGIVVEAYSPLGRG----------------------------KL 184
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
4AST_G 259 LTEAnlnslrLLNEMAQQRGQSMAQMALSWLLkdDRVTSVLIGASRAEQLEENVQALnNLTFSTKELAQIDQ 330
Cdd:COG0656 185 LDDP------VLAEIAEKHGKTPAQVVLRWHL--QRGVVVIPKSVTPERIRENLDAF-DFELSDEDMAAIDA 247
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
22-329 |
1.48e-34 |
|
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: 126.99 E-value: 1.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 22 GLRLPALSLGLWHNFGhvnalESQRAILRKAFDLGITHFDLANNYGpppgsAEENFGRLLREDFAAyRDELIISTKagyd 101
Cdd:cd19140 5 GVRIPALGLGTYPLTG-----EECTRAVEHALELGYRHIDTAQMYG-----NEAQVGEAIAASGVP-RDELFLTTK---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 102 MWPGPYgsggSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPERTQKMVEL 181
Cdd:cd19140 70 VWPDNY----SPDDFLASVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 182 LrewKIPLLIHQPSYNLLnrwVDKSGLLDTLQNNGVGCIAFTPLAQGlltgkylngipqdsrmhregnkvrgltpKMLTE 261
Cdd:cd19140 146 S---EAPLFTNQVEYHPY---LDQRKLLDAAREHGIALTAYSPLARG----------------------------EVLKD 191
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
4AST_G 262 AnlnslrLLNEMAQQRGQSMAQMALSWLLKDDRVtSVLIGASRAEQLEENVQALnNLTFSTKELAQID 329
Cdd:cd19140 192 P------VLQEIGRKHGKTPAQVALRWLLQQEGV-AAIPKATNPERLEENLDIF-DFTLSDEEMARIA 251
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
19-328 |
4.04e-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: 4.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 19 GKSGLRLPALSLGLWHNFGHVNALESQR---AILRKAFDLGITHFDLANNYGPppGSAEENFGRLLREdfaAYRDELIIS 95
Cdd:cd19145 6 GSQGLEVSAQGLGCMGLSGDYGAPKPEEegiALIHHAFNSGVTFLDTSDIYGP--NTNEVLLGKALKD---GPREKVQLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 96 TKAGYdMWPGPYGSG--GSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPE 173
Cdd:cd19145 81 TKFGI-HEIGGSGVEvrGDPAYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSEASAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 174 --RTQKMVEllrewkiPLLIHQPSYNLLNRWVDKSgLLDTLQNNGVGCIAFTPLAQGLLTGK-YLNGIPqdsrmhrEGNK 250
Cdd:cd19145 160 tiRRAHAVH-------PITAVQLEWSLWTRDIEEE-IIPTCRELGIGIVPYSPLGRGFFAGKaKLEELL-------ENSD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 251 VRGLTPKMLTEaNLNSLRLLNE----MAQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQALnNLTFSTKELA 326
Cdd:cd19145 225 VRKSHPRFQGE-NLEKNKVLYErveaLAKKKGCTPAQLALAWVLHQGEDVVPIPGTTKIKNLNQNIGAL-SVKLTKEDLK 302
|
..
4AST_G 327 QI 328
Cdd:cd19145 303 EI 304
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-312 |
7.79e-33 |
|
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: 122.21 E-value: 7.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 15 YRYCGKSGLRLPALSLGLWHnFGHVNALESQRaILRKAFDLGITHFDLANNYgpppGSAEENFGRLLREdfaaYRDELII 94
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGP-LGRLSQEEAAA-IIRRALDLGINYFDTAPSY----GDSEEKIGKALKG----RRDKVFL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 95 STKAGYDmwpgpygsggSRKYLLASLDQSLKRMGLEYVDIFYSHRVD-ENTPMEETAS-----ALAHAVQSGKALYVGIS 168
Cdd:cd19100 71 ATKTGAR----------DYEGAKRDLERSLKRLGTDYIDLYQLHAVDtEEDLDQVFGPggaleALLEAKEEGKIRFIGIS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 169 SYSPERTQKMVELLrewkiPLLIHQPSYNLLNRWVDKSG--LLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQdsrmhr 246
Cdd:cd19100 141 GHSPEVLLRALETG-----EFDVVLFPINPAGDHIDSFReeLLPLAREKGVGVIAMKVLAGGRLLSGDPLDPEQ------ 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
4AST_G 247 egnkvrgltpkmlteanlnslrllnemaqqrgqsmaqmALSWLLKDDRVTSVLIGASRAEQLEENV 312
Cdd:cd19100 210 --------------------------------------ALRYALSLPPVDVVIVGMDSPEELDENL 237
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
13-329 |
9.66e-33 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 124.58 E-value: 9.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 13 MQYRYCGKSGLRLPALSLGLWhNFGHVNALESQRAILRKAFDLGITHFDLANNYGPPP-----GSAEENFGRLLREdfAA 87
Cdd:PRK10625 1 MQYHRIPHSSLEVSTLGLGTM-TFGEQNSEADAHAQLDYAVAQGINLIDVAEMYPVPPrpetqGLTETYIGNWLAK--RG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 88 YRDELIISTKAGydmwpGPYGSGGS---------RKYLLASLDQSLKRMGLEYVDIFYSH--------------RVDENT 144
Cdd:PRK10625 78 SREKLIIASKVS-----GPSRNNDKgirpnqaldRKNIREALHDSLKRLQTDYLDLYQVHwpqrptncfgklgySWTDSA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 145 P---MEETASALAHAVQSGKALYVGISSYSPERTQKMVELLREWKIPLLIH-QPSYNLLNRWVDkSGLLDTLQNNGVGCI 220
Cdd:PRK10625 153 PavsLLETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEKHDLPRIVTiQNPYSLLNRSFE-VGLAEVSQYEGVELL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 221 AFTPLAQGLLTGKYLNGI-PQDSRmhregNKVRGLTPKMLTEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDDRVTSVL 299
Cdd:PRK10625 232 AYSCLAFGTLTGKYLNGAkPAGAR-----NTLFSRFTRYSGEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTL 306
|
330 340 350
....*....|....*....|....*....|
4AST_G 300 IGASRAEQLEENVQALnNLTFSTKELAQID 329
Cdd:PRK10625 307 LGATTMEQLKTNIESL-HLTLSEEVLAEIE 335
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
15-334 |
1.02e-32 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 123.73 E-value: 1.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 15 YRYCGKSGLRLPALSLG---LWHNFGHVnALESQRAILRKAFDLGITHFDLANNYGPPpgSAEENFGRLLREdFAAYRDE 91
Cdd:PLN02587 1 LRELGSTGLKVSSVGFGaspLGSVFGPV-SEEDAIASVREAFRLGINFFDTSPYYGGT--LSEKVLGKALKA-LGIPREK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 92 LIISTKAGYdmwpgpYGSGG--SRKYLLASLDQSLKRMGLEYVDIFYSHRV---DENTPMEETASALAHAVQSGKALYVG 166
Cdd:PLN02587 77 YVVSTKCGR------YGEGFdfSAERVTKSVDESLARLQLDYVDILHCHDIefgSLDQIVNETIPALQKLKESGKVRFIG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 167 ISSYSPERTQKMVELLREWKIPLLIHQPSYNlLNrwvDKS--GLLDTLQNNGVGCIAFTPLAQGLLTGkylNGIPQdsrM 244
Cdd:PLN02587 151 ITGLPLAIFTYVLDRVPPGTVDVILSYCHYS-LN---DSSleDLLPYLKSKGVGVISASPLAMGLLTE---NGPPE---W 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 245 HRegnkvrglTPKMLTEAnlnsLRLLNEMAQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQALNNLtfstkE 324
Cdd:PLN02587 221 HP--------APPELKSA----CAAAATHCKEKGKNISKLALQYSLSNKDISTTLVGMNSVQQVEENVAAATEL-----E 283
|
330
....*....|
4AST_G 325 LAQIDQHIAD 334
Cdd:PLN02587 284 TSGIDEELLS 293
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
31-315 |
1.31e-31 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 120.39 E-value: 1.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 31 GLWH-NFGHVNALESQRAI--LRKAFDLGITHFDLANNYGPppgsAEENFGRLLRE--DFAAYRDELIISTKagydmW-P 104
Cdd:cd19101 8 GMWQlSGGHGGIRDEDAAVraMAAYVDAGLTTFDCADIYGP----AEELIGEFRKRlrRERDAADDVQIHTK-----WvP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 105 GPYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTP-MEETASALAHAVQSGKALYVGISSYSPERTQKMVELLr 183
Cdd:cd19101 79 DPGELTMTRAYVEAAIDRSLKRLGVDRLDLVQFHWWDYSDPgYLDAAKHLAELQEEGKIRHLGLTNFDTERLREILDAG- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 184 ewkIPLLIHQPSYNLLNRWVDKsGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNgipqdsrmHREGNKVRGLTP------K 257
Cdd:cd19101 158 ---VPIVSNQVQYSLLDRRPEN-GMAALCEDHGIKLLAYGTLAGGLLSEKYLG--------VPEPTGPALETRslqkykL 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
4AST_G 258 MLTEA-------NLnsLRLLNEMAQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQAL 315
Cdd:cd19101 226 MIDEWggwdlfqEL--LRTLKAIADKHGVSIANVAVRWVLDQPGVAGVIVGARNSEHIDDNVRAF 288
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
43-313 |
3.48e-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: 381325 [Multi-domain] Cd Length: 316 Bit Score: 111.64 E-value: 3.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 43 ESQRAILRKAFDLGITHFDLANNYGPppGSAEENFGRLLREDFAAY---RDELIISTKAGY-----------DMWPGPYG 108
Cdd:cd19099 21 EEYREALKAALDSGINVIDTAINYRG--GRSERLIGKALRELIEKGgikRDEVVIVTKAGYipgdgdeplrpLKYLEEKL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 109 SGG--------------SRKYLLASLDQSLKRMGLEYVDIFYSH----------RVDENTPMEETASALAHAVQSGKALY 164
Cdd:cd19099 99 GRGlidvadsaglrhciSPAYLEDQIERSLKRLGLDTIDLYLLHnpeeqllelgEEEFYDRLEEAFEALEEAVAEGKIRY 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 165 VGISSYSPERT----------QKMVELLRE-------WK---IPLLIHQPS-YNLLNRWVDKS-GLLDTLQNNGVGCIAF 222
Cdd:cd19099 179 YGISTWDGFRAppalpghlslEKLVAAAEEvggdnhhFKviqLPLNLLEPEaLTEKNTVKGEAlSLLEAAKELGLGVIAS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 223 TPLAQGLLTGkylngipqdsrmhregnkvrgltpkmlteanlnSLRLLNEMAQQRGQSMAQMALSWLLKDDRVTSVLIGA 302
Cdd:cd19099 259 RPLNQGQLLG---------------------------------ELRLADLLALPGGATLAQRALQFARSTPGVDSALVGM 305
|
330
....*....|.
4AST_G 303 SRAEQLEENVQ 313
Cdd:cd19099 306 RRPEHVDENLA 316
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
46-317 |
2.34e-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: 381323 [Multi-domain] Cd Length: 267 Bit Score: 108.38 E-value: 2.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 46 RAILRKAFDLGITHFDLANNYgpppGSAEENFGRLLREDfaayrDELIISTKAGydmwPGPYGSGGSRKYLLASLDQSLK 125
Cdd:cd19097 29 KKILEYALKAGINTLDTAPAY----GDSEKVLGKFLKRL-----DKFKIITKLP----PLKEDKKEDEAAIEASVEASLK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 126 RMGLEYVDIFYSHRV-DENTPMEETASALAHAVQSGKALYVGISSYSPErtqkMVELLREWKIPLLIhQPSYNLLNRWVD 204
Cdd:cd19097 96 RLKVDSLDGLLLHNPdDLLKHGGKLVEALLELKKEGLIRKIGVSVYSPE----ELEKALESFKIDII-QLPFNILDQRFL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 205 KSGLLDTLQNNGVGCIAFTPLAQGLLTgkylngipqdsrMhrEGNKVrgltPKMLTEANlNSLRLLNEMAQQRGQSMAQM 284
Cdd:cd19097 171 KSGLLAKLKKKGIEIHARSVFLQGLLL------------M--EPDKL----PAKFAPAK-PLLKKLHELAKKLGLSPLEL 231
|
250 260 270
....*....|....*....|....*....|...
4AST_G 285 ALSWLLKDDRVTSVLIGASRAEQLEENVQALNN 317
Cdd:cd19097 232 ALGFVLSLPEIDKIVVGVDSLEQLKEIIAAFKK 264
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
25-329 |
8.45e-27 |
|
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: 106.20 E-value: 8.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 25 LPALSLGLWHNFGhvnalESQRAILRKAFDLGITHFDLANNYGpppgsAEENFGRLLREdFAAYRDELIISTKAGYDMWp 104
Cdd:cd19073 1 IPALGLGTWQLRG-----DDCANAVKEALELGYRHIDTAEIYN-----NEAEVGEAIAE-SGVPREDLFITTKVWRDHL- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 105 gpygsggSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPERTQKMVELLRE 184
Cdd:cd19073 69 -------RPEDLKKSVDRSLEKLGTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 185 wkiPLLIHQPSYN-LLNRWvdksGLLDTLQNNGVGCIAFTPLAQGlltgkylnGIPQDSrmhregnkvrgltpkmltean 263
Cdd:cd19073 142 ---PIAVNQVEFHpFLYQA----ELLEYCRENDIVITAYSPLARG--------EVLRDP--------------------- 185
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
4AST_G 264 lnslrLLNEMAQQRGQSMAQMALSWLLKDDrvTSVLIGASRAEQLEENVQALnNLTFSTKELAQID 329
Cdd:cd19073 186 -----VIQEIAEKYDKTPAQVALRWLVQKG--IVVIPKASSEDHLKENLAIF-DWELTSEDVAKID 243
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
47-319 |
1.45e-26 |
|
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381322 [Multi-domain] Cd Length: 255 Bit Score: 105.72 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 47 AILRKAFDLGITHFDLANNYGppPGSAEENFGRLLREdfaAYRDELIISTKagydmwpGPYGSGGSRKYLLASLDQSLKR 126
Cdd:cd19096 25 EMIRYAIDAGINYFDTAYGYG--GGKSEEILGEALKE---GPREKFYLATK-------LPPWSVKSAEDFRRILEESLKR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 127 MGLEYVDIFYSH-----RVDENTPMEETASALAHAVQSGKALYVGISSY-SPERTQKMVElLREWKIpLLIHqpsYNLLN 200
Cdd:cd19096 93 LGVDYIDFYLLHglnspEWLEKARKGGLLEFLEKAKKEGLIRHIGFSFHdSPELLKEILD-SYDFDF-VQLQ---YNYLD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 201 RWVDKS-GLLDTLQNNGVGCIAFTPLAQGLLtgkyLNGIPQdsrmhregnkvrgltpkmlteanlnSLRLLNemaqQRGQ 279
Cdd:cd19096 168 QENQAGrPGIEYAAKKGMGVIIMEPLKGGGL----ANNPPE-------------------------ALAILC----GAPL 214
|
250 260 270 280
....*....|....*....|....*....|....*....|
4AST_G 280 SMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQALNNLT 319
Cdd:cd19096 215 SPAEWALRFLLSHPEVTTVLSGMSTPEQLDENIAAADEFE 254
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
46-315 |
2.62e-26 |
|
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: 105.90 E-value: 2.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 46 RAILRKAFDLGITHFDLANNYGPppGSAEENFGRLLRedfAAYRDELIISTKAGYDMWPGPYGSGG--------SRKYLL 117
Cdd:cd19162 22 AATLDAAWDAGIRYFDTAPLYGL--GLSERRLGAALA---RHPRAEYVVSTKVGRLLEPGAAGRPAgadrrfdfSADGIR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 118 ASLDQSLKRMGLEYVDIFYSHRVDE--NTPMEETASALAHAVQSGKALYVGISSyspERTQKMVELLREWKIPLLIHQPS 195
Cdd:cd19162 97 RSIEASLERLGLDRLDLVFLHDPDRhlLQALTDAFPALEELRAEGVVGAIGVGV---TDWAALLRAARRADVDVVMVAGR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 196 YNLLNRwVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGkylnGIPQDSRMHRegnkvrgltpKMLTEANLNSLRLLNEMAQ 275
Cdd:cd19162 174 YTLLDR-RAATELLPLCAAKGVAVVAAGVFNSGILAT----DDPAGDRYDY----------RPATPEVLARARRLAAVCR 238
|
250 260 270 280
....*....|....*....|....*....|....*....|
4AST_G 276 QRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQAL 315
Cdd:cd19162 239 RYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLALL 278
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
21-329 |
1.18e-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: 99.42 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 21 SGLRLPALSLG-LWHNFGHVNALESQRAILRKAFDLGITHFDLANNYgpPPGSAEENFGRLL--REDfaayRDELIISTK 97
Cdd:cd19146 12 SPLCLGAMSFGeAWKSMMGECDKETAFKLLDAFYEQGGNFIDTANNY--QGEESERWVGEWMasRGN----RDEMVLATK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 98 --AGYDMW-PGPYGS---GGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYS 171
Cdd:cd19146 86 ytTGYRRGgPIKIKSnyqGNHAKSLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSDTP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 172 PERTQKMVELLREW-KIPLLIHQPSYNLLNRWVDKSgLLDTLQNNGVGCIAFTPLAQGLLtgKYLNGIPQDSRMHREGNK 250
Cdd:cd19146 166 AWVVSKANAYARAHgLTQFVVYQGHWSAAFRDFERD-ILPMCEAEGMALAPWGVLGQGQF--RTEEEFKRRGRSGRKGGP 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
4AST_G 251 vrgltpkmLTEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQALnNLTFSTKELAQID 329
Cdd:cd19146 243 --------QTEKERKVSEKLEKVAEEKGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIEAL-GISLSDEEIQEIE 312
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
25-329 |
1.77e-23 |
|
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: 97.17 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 25 LPALSLGLWHNFGhvnalESQRAILRKAFDLGITHFDLANNYGpppgsAEENFGRLLREDFAAyRDELIISTKagydMWP 104
Cdd:cd19071 1 MPLIGLGTYKLKP-----EETAEAVLAALEAGYRHIDTAAAYG-----NEAEVGEAIRESGVP-REELFITTK----LWP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 105 GPYGSGGSRKyllaSLDQSLKRMGLEYVDIFYSH------RVDENTPMEETASALAHAVQSGKALYVGISSYSPErtqKM 178
Cdd:cd19071 66 TDHGYERVRE----ALEESLKDLGLDYLDLYLIHwpvpgkEGGSKEARLETWRALEELVDEGLVRSIGVSNFNVE---HL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 179 VELLREWKIPLLIHQpsyNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGlltgkylngipqdsrmhregnkvrglTPKM 258
Cdd:cd19071 139 EELLAAARIKPAVNQ---IELHPYLQQKELVEFCKEHGIVVQAYSPLGRG--------------------------RRPL 189
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
4AST_G 259 LTEAnlnslrLLNEMAQQRGQSMAQMALSWLLkdDRVTSVLIGASRAEQLEENVQALnNLTFSTKELAQID 329
Cdd:cd19071 190 LDDP------VLKEIAKKYGKTPAQVLLRWAL--QRGVVVIPKSSNPERIKENLDVF-DFELSEEDMAAID 251
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
43-317 |
6.27e-22 |
|
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: 94.21 E-value: 6.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 43 ESQRAILRKAFDLGITHFDLANNYGPppGSAEENFGRLLREdfaAYRDELIISTKAGYDMWP----GPYGSGGSRKYL-- 116
Cdd:cd19152 20 EEAKATLVAAWDLGIRYFDTAPWYGA--GLSEERLGAALRE---LGREDYVISTKVGRLLVPlqevEPTFEPGFWNPLpf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 117 -----------LASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQ-----------SGKALYVGISSYSPER 174
Cdd:cd19152 95 davfdysydgiLRSIEDSLQRLGLSRIDLLSIHDPDEDLAGAESDEHFAQAIKgafraleelreEGVIKAIGLGVNDWEV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 175 TQKMvelLREWKIPLLIHQPSYNLLnrwvDKSGLLDTL---QNNGVGCIAFTPLAQGLLTGkylngipQDSRMHREGNKV 251
Cdd:cd19152 175 ILRI---LEEADLDWVMLAGRYTLL----DHSAARELLpecEKRGVKVVNAGPFNSGFLAG-------GDNFDYYEYGPA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
4AST_G 252 rgltpkmlTEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQALNN 317
Cdd:cd19152 241 --------PPELIARRDRIEALCEQHGVSLAAAALQFALAPPAVASVAPGASSPERVEENVALLAT 298
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
26-315 |
8.78e-22 |
|
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: 93.93 E-value: 8.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 26 PALSLG---LWHNFGHVNALESQrAILRKAFDLGITHFDLANNYGPppGSAEENFGRLLREDfaaYRDELIISTKAGYDM 102
Cdd:cd19161 1 SELGLGtagLGNLYTAVSNADAD-ATLDAAWDSGIRYFDTAPMYGH--GLAEHRLGDFLREK---PRDEFVLSTKVGRLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 103 WPGPYGSGG-----------------SRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETAS-ALAHAVQSG-KAL 163
Cdd:cd19161 75 KPAREGSVPdpngfvdplpfeivydySYDGIMRSFEDSLQRLGLNRIDILYVHDIGVYTHGDRKERhHFAQLMSGGfKAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 164 -------YVGISSYSPERTQKMVELLREWKIPLLIHQPSYNLLNRWVDKsGLLDTLQNNGVGCIAFTPLAQGLL-TGKyl 235
Cdd:cd19161 155 eelkkagVIKAFGLGVNEVQICLEALDEADLDCFLLAGRYSLLDQSAEE-EFLPRCEQRGTSLVIGGVFNSGILaTGT-- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 236 ngipqDSRMHREGNkvrgltpkmltEANLNSLRLLNEM---AQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENV 312
Cdd:cd19161 232 -----KSGAKFNYG-----------DAPAEIISRVMEIekiCDAYNVPLAAAALQFPLRHPAVASVLTGARNPAQLRQNV 295
|
...
4AST_G 313 QAL 315
Cdd:cd19161 296 EAF 298
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
25-329 |
1.56e-21 |
|
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: 92.03 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 25 LPALSLGLWHNFGHVNalesqRAILRKAFDLGITHFDLANNYGpppgsAEENFGRLLREdFAAYRDELIISTKagydMWP 104
Cdd:cd19139 1 IPAFGLGTFRLKDDVV-----IDSVRTALELGYRHIDTAQIYD-----NEAAVGQAIAE-SGVPRDELFITTK----IWI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 105 GPYGSGGsrkyLLASLDQSLKRMGLEYVDIFYSH--RVDENTPMEETASALAHAVQSGKALYVGISSYSPERTQKMVELL 182
Cdd:cd19139 66 DNLSKDK----LLPSLEESLEKLRTDYVDLTLIHwpSPNDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 183 REWKIPLLIHQPSYNLLNRwvdksGLLDTLQNNGVGCIAFTPLAQGlltgkylngipqdsrmhregnkvrgltpKMLTEA 262
Cdd:cd19139 142 GAGAIATNQIELSPYLQNR-----KLVAHCKQHGIHVTSYMTLAYG----------------------------KVLDDP 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
4AST_G 263 nlnslrLLNEMAQQRGQSMAQMALSWLLKddRVTSVLIGASRAEQLEENVQALnNLTFSTKELAQID 329
Cdd:cd19139 189 ------VLAAIAERHGATPAQIALAWAMA--RGYAVIPSSTKREHLRSNLLAL-DLTLDADDMAAIA 246
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
47-318 |
1.66e-20 |
|
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: 89.90 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 47 AILRKAFDLGITHFDLANNYGPPpgSAEENFGRLLREdFAAYRDELIISTKAGYdmwpgpYGSGG---SRKYLLASLDQS 123
Cdd:cd19153 37 AIVAEAFAAGINHFDTSPYYGAE--SSEAVLGKALAA-LQVPRSSYTVATKVGR------YRDSEfdySAERVRASVATS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 124 LKRMGLEYVDIFYSHRV---DENTPMEETASALAHAVQSGKALYVGISSYSPERTQKMVELLREWKIPLLIHQPSYNLLN 200
Cdd:cd19153 108 LERLHTTYLDVVYLHDIefvDYDTLVDEALPALRTLKDEGVIKRIGIAGYPLDTLTRATRRCSPGSLDAVLSYCHLTLQD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 201 rwvdkSGLLDTL----QNNGVGCIAFTPLAQGLLTGKylnGIPQDSRMHREgnkvrgltpkmLTEANLNSLRllneMAQQ 276
Cdd:cd19153 188 -----ARLESDApglvRGAGPHVINASPLSMGLLTSQ---GPPPWHPASGE-----------LRHYAAAADA----VCAS 244
|
250 260 270 280
....*....|....*....|....*....|....*....|...
4AST_G 277 RGQSMAQMALSWLLKD-DRVTSVLIGASRAEQLEENVQALNNL 318
Cdd:cd19153 245 VEASLPDLALQYSLAAhAGVGTVLLGPSSLAQLRSMLAAVDAV 287
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
25-314 |
2.11e-18 |
|
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: 84.25 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 25 LPALSLGLW-HNFGHVNALESQR--AILRKAFDLGITHFDLANNYGPppgsAEENFGRLLREDFAAY-RDELIISTKAG- 99
Cdd:cd19164 13 LPPLIFGAAtFSYQYTTDPESIPpvDIVRRALELGIRAFDTSPYYGP----SEIILGRALKALRDEFpRDTYFIITKVGr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 100 YDMWPGPYgsggSRKYLLASLDQSLKRMGLEYVDIFYSHRVdENTPMEETASALAHAVQ---SGKALYVGISSYSPERTQ 176
Cdd:cd19164 89 YGPDDFDY----SPEWIRASVERSLRRLHTDYLDLVYLHDV-EFVADEEVLEALKELFKlkdEGKIRNVGISGYPLPVLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 177 KMVEL-LREWKIPL--LIHQPSYNLLNrwvdkSGLLDTLQ----NNGVGCI--AfTPLAQGLLTGKylnGIPQdsrMHRE 247
Cdd:cd19164 164 RLAELaRTTAGRPLdaVLSYCHYTLQN-----TTLLAYIPkflaAAGVKVVlnA-SPLSMGLLRSQ---GPPE---WHPA 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
4AST_G 248 GNKVRGlTPKMLTeanlnslrllnEMAQQRGQSMAQMALSWLLK-DDRVTSVLIGASRAEQLEENVQA 314
Cdd:cd19164 232 SPELRA-AAAKAA-----------EYCQAKGTDLADVALRYALReWGGEGPTVVGCSNVDELEEAVEA 287
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
21-313 |
2.18e-18 |
|
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: 83.53 E-value: 2.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 21 SGLRLPALSLGLWHNFGHvnaleSQRAILRKAFDLGITHFDLANNYGpppgsAEENFGRLLREDfAAYRDELIISTKagy 100
Cdd:cd19135 9 NGVEMPILGLGTSHSGGY-----SHEAVVYALKECGYRHIDTAKRYG-----CEELLGKAIKES-GVPREDLFLTTK--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 101 dMWPGPYGSGGSRKYLLASLdqslKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALY-------VGISSYSPE 173
Cdd:cd19135 75 -LWPSDYGYESTKQAFEASL----KRLGVDYLDLYLLHWPDCPSSGKNVKETRAETWRALEELYdeglcraIGVSNFLIE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 174 rtqKMVELLREWKIPLLIHQPSYNLLNRWVDksgLLDTLQNNGVGCIAFTPLAQGlltgkylngipqdsrmhregnkvrg 253
Cdd:cd19135 150 ---HLEQLLEDCSVVPHVNQVEFHPFQNPVE---LIEYCRDNNIVFEGYCPLAKG------------------------- 198
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
4AST_G 254 ltpKMLTEANlnslrlLNEMAQQRGQSMAQMALSWLLKDDRVTsvlIGAS-RAEQLEENVQ 313
Cdd:cd19135 199 ---KALEEPT------VTELAKKYQKTPAQILIRWSIQNGVVT---IPKStKEERIKENCQ 247
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
43-329 |
2.20e-17 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 81.17 E-value: 2.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 43 ESQRAILRKAFDLGITHFDLANNYGPPPGSaeenfgRLLREDFAAYRDELIISTKAGYDMwpGPYGS---GGSRKYLLAS 119
Cdd:PRK10376 40 DAAIAVLREAVALGVNHIDTSDFYGPHVTN------QLIREALHPYPDDLTIVTKVGARR--GEDGSwlpAFSPAELRRA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 120 LDQSLKRMGLEYVDI------FYSHRVDENtPMEETASALAHAVQSGKALYVGISSYSPER---TQKMVellrewkiPLL 190
Cdd:PRK10376 112 VHDNLRNLGLDVLDVvnlrlmGDGHGPAEG-SIEEPLTVLAELQRQGLVRHIGLSNVTPTQvaeARKIA--------EIV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 191 IHQPSYNLLNRwvDKSGLLDTLQNNGVGCIAFTPLAqglltgkylngipqdsrmhregnkvrGLTPkmlteanLNSlRLL 270
Cdd:PRK10376 183 CVQNHYNLAHR--ADDALIDALARDGIAYVPFFPLG--------------------------GFTP-------LQS-STL 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
4AST_G 271 NEMAQQRGQSMAQMALSWLLKddRVTSVLI--GASRAEQLEENVQAlNNLTFSTKELAQID 329
Cdd:PRK10376 227 SDVAASLGATPMQVALAWLLQ--RSPNILLipGTSSVAHLRENLAA-AELVLSEEVLAELD 284
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
21-329 |
2.89e-17 |
|
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: 81.41 E-value: 2.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 21 SGLRLPALSLG-LWHNF-GHVNALESQRaILRKAFDLGITHFDLANNYGPPpgSAEENFGRLLREdfAAYRDELIISTKA 98
Cdd:cd19147 11 SPLILGAMSIGdAWSGFmGSMDKEQAFE-LLDAFYEAGGNFIDTANNYQDE--QSETWIGEWMKS--RKNRDQIVIATKF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 99 GYDMWPGPYGSGGSRKY-------LLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYS 171
Cdd:cd19147 86 TTDYKAYEVGKGKAVNYcgnhkrsLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDTP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 172 PERTQKMVELLREW-KIPLLIHQPSYNLLNRWVDKSgLLDTLQNNGvgcIAFTPLaQGLLTGKYLNGIPQDSRMHREGNK 250
Cdd:cd19147 166 AWVVSAANYYATAHgKTPFSVYQGRWNVLNRDFERD-IIPMARHFG---MALAPW-DVLGGGKFQSKKAVEERKKNGEGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 251 VRGLTPKMLTEANLNSLRLLNEMAQQRG-QSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQALnNLTFSTKELAQID 329
Cdd:cd19147 241 RSFVGGTEQTPEEVKISEALEKVAEEHGtESVTAIALAYVRSKAPNVFPLVGGRKIEHLKDNIEAL-SIKLTPEEIEYLE 319
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
21-330 |
8.90e-17 |
|
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: 79.25 E-value: 8.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 21 SGLRLPALSLGLWHNFGHvnalESQRAILRKAFDLGITHFDLANNYGpppgsAEENFGRLLREDFAA---YRDELIISTK 97
Cdd:cd19116 7 DGNEIPAIALGTWKLKDD----EGVRQAVKHAIEAGYRHIDTAYLYG-----NEAEVGEAIREKIAEgvvKREDLFITTK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 98 agydMWpgpyGSGGSRKYLLASLDQSLKRMGLEYVDIFYSH-------RVDENTPME---------ETASALAHAVQSGK 161
Cdd:cd19116 78 ----LW----NSYHEREQVEPALRESLKRLGLDYVDLYLIHwpvafkeNNDSESNGDgslsdidylETWRGMEDLVKLGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 162 ALYVGISSYSPERTQKmveLLREWKIPLLIHQ----PSYNLLNrwvdksgLLDTLQNNGVGCIAFTPLaqglltgkylnG 237
Cdd:cd19116 150 TRSIGVSNFNSEQINR---LLSNCNIKPAVNQievhPTLTQEK-------LVAYCQSNGIVVMAYSPF-----------G 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 238 IPQDSRmhregnkVRGLTPKMLTEAnlnslrlLNEMAQQRGQSMAQMALSWLLkdDRVTSVLIGASRAEQLEENVQALN- 316
Cdd:cd19116 209 RLVPRG-------QTNPPPRLDDPT-------LVAIAKKYGKTTAQIVLRYLI--DRGVVPIPKSSNKKRIKENIDIFDf 272
|
330
....*....|....
4AST_G 317 NLTfsTKELAQIDQ 330
Cdd:cd19116 273 QLT--PEEVAALNS 284
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
22-329 |
3.02e-16 |
|
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: 77.23 E-value: 3.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 22 GLRLPALSLGLWHnfghVNALESQRAILRKAFDLGITHFDLANNYGpppgsAEENFGRLLREDFAAyRDELIISTKagyd 101
Cdd:cd19133 6 GVEMPILGFGVFQ----IPDPEECERAVLEAIKAGYRLIDTAAAYG-----NEEAVGRAIKKSGIP-REELFITTK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 102 MWPGPYGSGGSRKyllaSLDQSLKRMGLEYVDIFYSHRvdentPM---EETASALAHAVQSGKALYVGISSYSPERtqkM 178
Cdd:cd19133 72 LWIQDAGYEKAKK----AFERSLKRLGLDYLDLYLIHQ-----PFgdvYGAWRAMEELYKEGKIRAIGVSNFYPDR---L 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 179 VELLREWKIPLLIHQPSYNLLNRwvdKSGLLDTLQNNGVGCIAFTPLAQGlltgkyLNGIPQDSrmhregnkvrgltpkm 258
Cdd:cd19133 140 VDLILHNEVKPAVNQIETHPFNQ---QIEAVEFLKKYGVQIEAWGPFAEG------RNNLFENP---------------- 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
4AST_G 259 lteanlnslrLLNEMAQQRGQSMAQMALSWLLKDDRVtsVLIGASRAEQLEENVqALNNLTFSTKELAQID 329
Cdd:cd19133 195 ----------VLTEIAEKYGKSVAQVILRWLIQRGIV--VIPKSVRPERIAENF-DIFDFELSDEDMEAIA 252
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
20-316 |
6.58e-16 |
|
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: 77.00 E-value: 6.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 20 KSGLRLPALSLGLWHNFGHVNALESQRAIlrkafDLGITHFDLANNYGpppgsAEENFGRLLREDFAA---YRDELIIST 96
Cdd:cd19125 6 NTGAKIPAVGLGTWQADPGVVGNAVKTAI-----KEGYRHIDCAAIYG-----NEKEIGKALKKLFEDgvvKREDLFITS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 97 KagydMWPGPYGSGGSRKyllaSLDQSLKRMGLEYVDIFYSH-----RVDENTP---------MEETASALAHAVQSGKA 162
Cdd:cd19125 76 K----LWCTDHAPEDVPP----ALEKTLKDLQLDYLDLYLIHwpvrlKKGAHMPepeevlppdIPSTWKAMEKLVDSGKV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 163 LYVGISSYSperTQKMVELLREWKIPLLIHQPSYNLLNRwvdKSGLLDTLQNNGVGCIAFTPLaqglltgkylnGIPQDS 242
Cdd:cd19125 148 RAIGVSNFS---VKKLEDLLAVARVPPAVNQVECHPGWQ---QDKLHEFCKSKGIHLSAYSPL-----------GSPGTT 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
4AST_G 243 RMHregnkvrgltPKMLTEAnlnslrLLNEMAQQRGQSMAQMALSWLLKddRVTSVLIGASRAEQLEENVQALN 316
Cdd:cd19125 211 WVK----------KNVLKDP------IVTKVAEKLGKTPAQVALRWGLQ--RGTSVLPKSTNEERIKENIDVFD 266
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
22-330 |
8.08e-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: 8.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 22 GLRLPALSLGL---WHNFGHVNAlesQRAI---LRKAFDLGITHFDLANNYGpppgsAEENFGRLLREdFAAYRDELIIS 95
Cdd:cd19120 1 GSKIPAIAFGTgtaWYKSGDDDI---QRDLvdsVKLALKAGFRHIDTAEMYG-----NEKEVGEALKE-SGVPREDLFIT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 96 TKagydmwpgpYGSGGSRKYllASLDQSLKRMGLEYVDIFYSH---RVDENTP-MEETASALAHAVQSGKALYVGISSYS 171
Cdd:cd19120 72 TK---------VSPGIKDPR--EALRKSLAKLGVDYVDLYLIHspfFAKEGGPtLAEAWAELEALKDAGLVRSIGVSNFR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 172 PERTQkmvELLREWKIPLLIHQPSYNLLNrWVDKSGLLDTLQNNGVGCIAFTPLAqglltgkylngiPQDSRMHREGNKV 251
Cdd:cd19120 141 IEDLE---ELLDTAKIKPAVNQIEFHPYL-YPQQPALLEYCREHGIVVSAYSPLS------------PLTRDAGGPLDPV 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
4AST_G 252 rgltpkmlteanlnslrlLNEMAQQRGQSMAQMALSWLLKDDRVtsVLIGASRAEQLEENVQALnNLTFSTKELAQIDQ 330
Cdd:cd19120 205 ------------------LEKIAEKYGVTPAQVLLRWALQKGIV--VVTTSSKEERMKEYLEAF-DFELTEEEVEEIDK 262
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
23-328 |
3.52e-15 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 74.29 E-value: 3.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 23 LRLPALSLGLWHnfghvnaLESQRAI--LRKAFDLGITHFDLANNYGpppgsAEENFGRLLREDFAAyRDELIISTKagy 100
Cdd:PRK11172 1 MSIPAFGLGTFR-------LKDQVVIdsVKTALELGYRAIDTAQIYD-----NEAAVGQAIAESGVP-RDELFITTK--- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 101 dMWPGPYGSGGsrkyLLASLDQSLKRMGLEYVDIFYSH--RVDENTPMEETASALAHAVQSGKALYVGISSYSPERTQKM 178
Cdd:PRK11172 65 -IWIDNLAKDK----LIPSLKESLQKLRTDYVDLTLIHwpSPNDEVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 179 VELLREWKIPLLIHQPSYNLLNRwvdksGLLDTLQNNGVGCIAFTPLAQGlltgkylngipqdsrmhregnkvrgltpKM 258
Cdd:PRK11172 140 IAAVGAENIATNQIELSPYLQNR-----KVVAFAKEHGIHVTSYMTLAYG----------------------------KV 186
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 259 LTEAnlnslrLLNEMAQQRGQSMAQMALSWLLKDDrvTSVLIGASRAEQLEENVQALnNLTFSTKELAQI 328
Cdd:PRK11172 187 LKDP------VIARIAAKHNATPAQVILAWAMQLG--YSVIPSSTKRENLASNLLAQ-DLQLDAEDMAAI 247
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
22-331 |
5.38e-15 |
|
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: 74.37 E-value: 5.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 22 GLRLPALSLGLWHNfghvNALESQRAIlRKAFDLGITHFDLANNYGpppgsAEENFGRLLREDFAA---YRDELIISTKa 98
Cdd:cd19123 9 GDLIPALGLGTWKS----KPGEVGQAV-KQALEAGYRHIDCAAIYG-----NEAEIGAALAEVFKEgkvKREDLWITSK- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 99 gydMWpgpyGSGGSRKYLLASLDQSLKRMGLEYVDIFYSH------------------RVDENTPMEETASALAHAVQSG 160
Cdd:cd19123 78 ---LW----NNSHAPEDVLPALEKTLADLQLDYLDLYLMHwpvalkkgvgfpesgedlLSLSPIPLEDTWRAMEELVDKG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 161 KALYVGISSYSperTQKMVELLREWKIPLLIHQPSynlLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGlltgkylnGIPQ 240
Cdd:cd19123 151 LCRHIGVSNFS---VKKLEDLLATARIKPAVNQVE---LHPYLQQPELLAFCRDNGIHLTAYSPLGSG--------DRPA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 241 DSRMHREgnkvrgltPKMLTEAnlnslrLLNEMAQQRGQSMAQMALSWLLKddRVTSVLIGASRAEQLEENVQALN-NLT 319
Cdd:cd19123 217 AMKAEGE--------PVLLEDP------VINKIAEKHGASPAQVLIAWAIQ--RGTVVIPKSVNPERIQQNLEAAEvELD 280
|
330
....*....|...
4AST_G 320 FS-TKELAQIDQH 331
Cdd:cd19123 281 ASdMATIAALDRH 293
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
21-312 |
1.29e-14 |
|
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: 73.29 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 21 SGLRLPALSLGLWHNFGHVnalesQRAILRKAFDLGITHFDLANNYGpppgsAEENFGRLLREDFA---AYRDELIISTK 97
Cdd:cd19112 7 SGHKMPVIGLGVWRMEPGE-----IKELILNAIKIGYRHFDCAADYK-----NEKEVGEALAEAFKtglVKREDLFITTK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 98 agydMWPGPYGsggsrkYLLASLDQSLKRMGLEYVDIFYSH-----------------------RVDENTPMEETASALA 154
Cdd:cd19112 77 ----LWNSDHG------HVIEACKDSLKKLQLDYLDLYLVHfpvatkhtgvgttgsalgedgvlDIDVTISLETTWHAME 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 155 HAVQSGKALYVGISSYSPERTQkmvELLREWKIpllihQPSYNLL--NRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTG 232
Cdd:cd19112 147 KLVSAGLVRSIGISNYDIFLTR---DCLAYSKI-----KPAVNQIetHPYFQRDSLVKFCQKHGISVTAHTPLGGAAANA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 233 KYLNGIP--QDSrmhregnkvrgltpkmlteanlnslrLLNEMAQQRGQSMAQMALSWLLKddRVTSVLIGASRAEQLEE 310
Cdd:cd19112 219 EWFGSVSplDDP--------------------------VLKDLAKKYGKSAAQIVLRWGIQ--RNTAVIPKSSKPERLKE 270
|
..
4AST_G 311 NV 312
Cdd:cd19112 271 NI 272
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
20-331 |
3.16e-14 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381380 [Multi-domain] Cd Length: 303 Bit Score: 72.06 E-value: 3.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 20 KSGLRLPALSLGLWHNFGhvnalESQRAILRKAFDLGITHFDLANNYgpppgSAEENFGRLLREDFAA---YRDELIIST 96
Cdd:cd19154 7 SNGVKMPLIGLGTWQSKG-----AEGITAVRTALKAGYRLIDTAFLY-----QNEEAIGEALAELLEEgvvKREDLFITT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 97 KAgydmWPGPYgsggSRKYLLASLDQSLKRMGLEYVDIFYSH------------RVDEN-------TPMEETASALAHAV 157
Cdd:cd19154 77 KL----WTHEH----APEDVEEALRESLKKLQLEYVDLYLIHapaafkddegesGTMENgmsihdaVDVEDVWRGMEKVY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 158 QSGKALYVGISSYSperTQKMVELLREWKIPLLIHQPSYNLlnrWVDKSGLLDTLQNNGVGCIAFTPLaqglltgkylnG 237
Cdd:cd19154 149 DEGLTKAIGVSNFN---NDQIQRILDNARVKPHNNQVECHL---YFPQKELVEFCKKHNISVTSYATL-----------G 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 238 IPqdSRM-HREGNKVRGLtPKMLTEANlnslrlLNEMAQQRGQSMAQMALSWLLkdDRVTSVLIGASRAEQLEENVQaLN 316
Cdd:cd19154 212 SP--GRAnFTKSTGVSPA-PNLLQDPI------VKAIAEKHGKTPAQVLLRYLL--QRGIAVIPKSATPSRIKENFN-IF 279
|
330
....*....|....*
4AST_G 317 NLTFSTKELAQIDQH 331
Cdd:cd19154 280 DFSLSEEDMATLEEI 294
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
22-333 |
3.74e-14 |
|
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: 71.76 E-value: 3.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 22 GLRLPALSLGLWHNFGhvnalESQRAILRKAFDLGITHFDLANNYGpppgsAEENFGRLLREDFAA---YRDELIISTKA 98
Cdd:cd19111 1 GFPMPVIGLGTYQSPP-----EEVRAAVDYALFVGYRHIDTALSYQ-----NEKAIGEALKWWLKNgklKREEVFITTKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 99 gydmWPgpygSGGSRKYLLASLDQSLKRMGLEYVDIFYSH-------------RVDENTPMEETASALAHAVQSGKALYV 165
Cdd:cd19111 71 ----PP----VYLEFKDTEKSLEKSLENLKLPYVDLYLIHhpcgfvnkkdkgeRELASSDVTSVWRAMEALVSEGKVKSI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 166 GISSYSPERTQKMvellreWKIPLLihqPSYNL---LNRWVDKSGLLDTLQNNGVGCIAFTPLaqglltgkylnGIPQDS 242
Cdd:cd19111 143 GLSNFNPRQINKI------LAYAKV---KPSNLqleCHAYLQQRELRKFCNKKNIVVTAYAPL-----------GSPGRA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 243 RMHREGNKvrgltPKMLTEANLNSLrllnemAQQRGQSMAQMALSWLLkdDRVTSVLIGASRAEQLEENVQALN-NLTFS 321
Cdd:cd19111 203 NQSLWPDQ-----PDLLEDPTVLAI------AKELDKTPAQVLLRFVL--QRGTGVLPKSTNKERIEENFEVFDfELTEE 269
|
330
....*....|...
4AST_G 322 -TKELAQIDQHIA 333
Cdd:cd19111 270 hFKKLKTLDRNMK 282
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
21-330 |
9.68e-14 |
|
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: 70.37 E-value: 9.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 21 SGLRLPALSLGLWHNFghVNALESQRAILRkAFDLGITHFDLANNYGpppgsAEENFGRLLREDFA----AYRDELIIST 96
Cdd:cd19124 1 SGQTMPVIGMGTASDP--PSPEDIKAAVLE-AIEVGYRHFDTAAAYG-----TEEALGEALAEALRlglvKSRDELFVTS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 97 KagydMWPgpygSGGSRKYLLASLDQSLKRMGLEYVDIF------------YSHRVDENTP----MEETASALAHAVQSG 160
Cdd:cd19124 73 K----LWC----SDAHPDLVLPALKKSLRNLQLEYVDLYlihwpvslkpgkFSFPIEEEDFlpfdIKGVWEAMEECQRLG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 161 KALYVGISSYSperTQKMVELLREWKIPLLIHQPSYNLLnrWVDKSgLLDTLQNNGVGCIAFTPLaqglltGKYLNGIPQ 240
Cdd:cd19124 145 LTKAIGVSNFS---CKKLQELLSFATIPPAVNQVEMNPA--WQQKK-LREFCKANGIHVTAYSPL------GAPGTKWGS 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 241 DSRMhreGNKVrgltpkmlteanlnslrlLNEMAQQRGQSMAQMALSWLLkdDRVTSVLIGASRAEQLEENVQALnNLTF 320
Cdd:cd19124 213 NAVM---ESDV------------------LKEIAAAKGKTVAQVSLRWVY--EQGVSLVVKSFNKERMKQNLDIF-DWEL 268
|
330
....*....|
4AST_G 321 STKELAQIDQ 330
Cdd:cd19124 269 TEEDLEKISE 278
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
25-330 |
1.41e-13 |
|
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: 69.58 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 25 LPALSLGLWHnfghVNALESQRAILRKAFDLGITHFDLANNYGpppgsAEENFGRLLREDFAAY---RDELIISTKAGyd 101
Cdd:cd19136 1 MPILGLGTFR----LRGEEEVRQAVDAALKAGYRLIDTASVYR-----NEADIGKALRDLLPKYglsREDIFITSKLA-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 102 mwpgPYGSGGSRKYllASLDQSLKRMGLEYVDIFYSH-----RVDENTPME-----ETASALAHAVQSGKALYVGISSYS 171
Cdd:cd19136 70 ----PKDQGYEKAR--AACLGSLERLGTDYLDLYLIHwpgvqGLKPSDPRNaelrrESWRALEDLYKEGKLRAIGVSNYT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 172 PertQKMVELLREWKIPLLIHQPSYNllNRWVDKSgLLDTLQNNGVGCIAFTPLAQGlltgkylngipqdsrmhregnkv 251
Cdd:cd19136 144 V---RHLEELLKYCEVPPAVNQVEFH--PHLVQKE-LLKFCKDHGIHLQAYSSLGSG----------------------- 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
4AST_G 252 rglTPKMLTEAnlnslrLLNEMAQQRGQSMAQMALSWLLKDDrvTSVLIGASRAEQLEENVQaLNNLTFSTKELAQIDQ 330
Cdd:cd19136 195 ---DLRLLEDP------TVLAIAKKYGRTPAQVLLRWALQQG--IGVIPKSTNPERIAENIK-VFDFELSEEDMAELNA 261
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
22-311 |
3.64e-13 |
|
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family.
Pssm-ID: 381355 [Multi-domain] Cd Length: 295 Bit Score: 69.02 E-value: 3.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 22 GLRLPALSLG-LWHNfghvnALESQRAIlRKAFDLGITHFDLANNYgpppgSAEENFGRLLREDFAA---YRDELIISTK 97
Cdd:cd19129 3 SGAIPALGFGtLIPD-----PSATRNAV-KAALEAGFRHFDCAERY-----RNEAEVGEAMQEVFKAgkiRREDLFVTTK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 98 agydMWpgpyGSGGSRKYLLASLDQSLKRMGLEYVDIFYSH------------------RV--DENTPMEETASALAHAV 157
Cdd:cd19129 72 ----LW----NTNHRPERVKPAFEASLKRLQLDYLDLYLIHtpfafqpgdeqdprdangNViyDDGVTLLDTWRAMERLV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 158 QSGKALYVGISSYSPERTQKMVELLRewkI-PLLIHQPSYNLLNRWvdksGLLDTLQNNGVGCIAFTPLAQglltgkyln 236
Cdd:cd19129 144 DEGRCKAIGLSDVSLEKLREIFEAAR---IkPAVVQVESHPYLPEW----ELLDFCKNHGIVLQAFAPLGH--------- 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
4AST_G 237 gipqdsrmhregnkvrGLTPKMLTEAnlnslrLLNEMAQQRGQSMAQMALSWLLKddRVTSVLIGASRAEQLEEN 311
Cdd:cd19129 208 ----------------GMEPKLLEDP------VITAIARRVNKTPAQVLLAWAIQ--RGTALLTTSKTPSRIREN 258
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
22-179 |
5.03e-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: 68.17 E-value: 5.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 22 GLRLPALSLGLWHNFGhvnalESQRAILRKAFDLGITHFDLANNYGpppgsAEENFGRLLReDFAAYRDELIISTKagyd 101
Cdd:cd19131 7 GNTIPQLGLGVWQVSN-----DEAASAVREALEVGYRSIDTAAIYG-----NEEGVGKAIR-ASGVPREELFITTK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 102 MWPGPYGSGGSRKyllaSLDQSLKRMGLEYVDIFYSHRVdenTPME----ETASALAHAVQSGKALYVGISSYSPERTQK 177
Cdd:cd19131 72 LWNSDQGYDSTLR----AFDESLRKLGLDYVDLYLIHWP---VPAQdkyvETWKALIELKKEGRVKSIGVSNFTIEHLQR 144
|
..
4AST_G 178 MV 179
Cdd:cd19131 145 LI 146
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
26-325 |
3.09e-12 |
|
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), also called aldehyde reductase, is the prototype of this family. It catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
Pssm-ID: 381354 [Multi-domain] Cd Length: 277 Bit Score: 66.01 E-value: 3.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 26 PALSLGLWHnfghVNALESQRAIlRKAFDLGITHFDLANNYGpppgsAEENFGRLLREDF---AAYRDELIISTKagydM 102
Cdd:cd19128 2 PRLGFGTYK----ITESESKEAV-KNAIKAGYRHIDCAYYYG-----NEAFIGIAFSEIFkdgGVKREDLFITSK----L 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 103 WPGPYGSGGSRKYLLasldQSLKRMGLEYVDIFYSH-------------------RVDENTPMEETASALAHAVQSGKAL 163
Cdd:cd19128 68 WPTMHQPENVKEQLL----ITLQDLQLEYLDLFLIHwplafdmdtdgdprddnqiQSLSKKPLEDTWRAMEQCVDEKLTK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 164 YVGISSYSperTQKMVELLREWKIPLLIHQPSYNLlnrWVDKSGLLDTLQNNGVGCIAFTPLAqglltGKYlngipqdsr 243
Cdd:cd19128 144 NIGVSNYS---TKLLTDLLNYCKIKPFMNQIECHP---YFQNDKLIKFCIENNIHVTAYRPLG-----GSY--------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 244 mhREGNkvrgLTPKMLTEanlnslrlLNEMAQQRGQSMAQMALSW-LLKDDRVTSVLIGASRAEQLEENVQAlNNLTFST 322
Cdd:cd19128 204 --GDGN----LTFLNDSE--------LKALATKYNTTPPQVIIAWhLQKWPKNYSVIPKSANKSRCQQNFDI-NDLALTK 268
|
...
4AST_G 323 KEL 325
Cdd:cd19128 269 EDM 271
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
21-315 |
4.38e-12 |
|
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis.
Pssm-ID: 381348 [Multi-domain] Cd Length: 291 Bit Score: 65.72 E-value: 4.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 21 SGLRLPALSLGLWHNFGHVNalESQRAILrKAFDLGITHFDLANNY--GPPPGSAEENFgrlLREDFAAYRDELIISTKa 98
Cdd:cd19122 5 NGVKIPAVGFGTFANEGAKG--ETYAAVT-KALDVGYRHLDCAWFYlnEDEVGDAVRDF---LKENPSVKREDLFICTK- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 99 gydMWPGPYgsggSRKYLLASLDQSLKRMGLEYVDIFYSH------RVDENTPM-----------------EETASALAH 155
Cdd:cd19122 78 ---VWNHLH----EPEDVKWSIDNSLKNLKLDYIDLFLVHwpiaaeKNDQRSPKlgpdgkyvilkdltenpEPTWRAMEE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 156 AVQSGKALYVGISSYSPERTQKMVELLrewKIPLLIHQPSynlLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGlltgkyl 235
Cdd:cd19122 151 IYESGKAKAIGVSNWTIPGLKKLLSFA---KVKPHVNQIE---IHPFLPNEELVDYCFSNDILPEAYSPLGSQ------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 236 NGIPQdsrmhrEGNKVrgltpkmlteanlNSLRLLNEMAQQRGQSMAQMALSWLLKDDRVtsVLIGASRAEQLEENVQAL 315
Cdd:cd19122 218 NQVPS------TGERV-------------SENPTLNEVAEKGGYSLAQVLIAWGLRRGYV--VLPKSSTPSRIESNFKSI 276
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
22-330 |
1.05e-11 |
|
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from Leishmania major and Trypanosoma brucei are founding members of aldo-keto reductase family 5 member A1 (AKR5A1) and A2 (AKR5A2), respectively. PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity toward the synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde.
Pssm-ID: 381382 [Multi-domain] Cd Length: 266 Bit Score: 64.46 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 22 GLRLPALSLGLWHnfghVNALESQRAILRKAFDLGITHFDLANNYgpppgSAEENFGRLLREDfAAYRDELIISTKagyd 101
Cdd:cd19156 6 GVEMPRLGLGVWR----VQDGAEAENAVKWAIEAGYRHIDTAAIY-----KNEEGVGQGIRES-GVPREEVFVTTK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 102 MWPGPYGSGGSrkylLASLDQSLKRMGLEYVDIFYSHRVDENTpMEETASALAHAVQSGKALYVGISSYSPERTQkmvEL 181
Cdd:cd19156 72 LWNSDQGYEST----LAAFEESLEKLGLDYVDLYLIHWPVKGK-FKDTWKAFEKLYKEKKVRAIGVSNFHEHHLE---EL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 182 LREWKIPLLIHQPSYNLLNrwvDKSGLLDTLQNNGVGCIAFTPLAQGlltgkylngipqdsrmhregnkvrgltpKMLTE 261
Cdd:cd19156 144 LKSCKVAPMVNQIELHPLL---TQEPLRKFCKEKNIAVEAWSPLGQG----------------------------KLLSN 192
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
4AST_G 262 AnlnslrLLNEMAQQRGQSMAQMALSWLLKDDRVTsvLIGASRAEQLEENVqALNNLTFSTKELAQIDQ 330
Cdd:cd19156 193 P------VLKAIGKKYGKSAAQVIIRWDIQHGIIT--IPKSVHEERIQENF-DVFDFELTAEEIRQIDG 252
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
22-329 |
1.46e-11 |
|
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: 63.78 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 22 GLRLPALSLGLWHnfghVNALESQRAIlRKAFDLGITHFDLANNYGpppgsAEENFGRLLREDFAAyRDELIISTKAGYD 101
Cdd:cd19130 7 GNSIPQLGYGVFK----VPPADTQRAV-ATALEVGYRHIDTAAIYG-----NEEGVGAAIAASGIP-RDELFVTTKLWND 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 102 mwpgpyGSGGSRkyLLASLDQSLKRMGLEYVDIFYSHRvdeNTPME----ETASALAHAVQSGKALYVGISSYSPERTQK 177
Cdd:cd19130 76 ------RHDGDE--PAAAFAESLAKLGLDQVDLYLVHW---PTPAAgnyvHTWEAMIELRAAGRTRSIGVSNFLPPHLER 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 178 MVELLREwkipllihQPSYNL--LNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKylngipqdsrmhregnkvrglt 255
Cdd:cd19130 145 IVAATGV--------VPAVNQieLHPAYQQRTIRDWAQAHDVKIEAWSPLGQGKLLGD---------------------- 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
4AST_G 256 pkmlteanlnslRLLNEMAQQRGQSMAQMALSWLLKDDRVtsVLIGASRAEQLEENVqALNNLTFSTKELAQID 329
Cdd:cd19130 195 ------------PPVGAIAAAHGKTPAQIVLRWHLQKGHV--VFPKSVRRERMEDNL-DVFDFDLTDTEIAAID 253
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
22-330 |
1.95e-11 |
|
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: 63.56 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 22 GLRLPALSLGLWHnfghVNALESQRAILRKAFDLGITHFDLANNYGpppgsAEENFGRLLREDFAAyRDELIISTKA--- 98
Cdd:cd19157 7 GVKMPWLGLGVFK----VEEGSEVVNAVKTALKNGYRSIDTAAIYG-----NEEGVGKGIKESGIP-REELFITSKVwna 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 99 --GYDMwpgpygsggsrkyLLASLDQSLKRMGLEYVDIFYSHRVDENTpMEETASALAHAVQSGKALYVGISSYspeRTQ 176
Cdd:cd19157 77 dqGYDS-------------TLKAFEASLERLGLDYLDLYLIHWPVKGK-YKETWKALEKLYKDGRVRAIGVSNF---QVH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 177 KMVELLREWKIPLLIHQPSYNllNRWVDKSgLLDTLQNNGVGCIAFTPLAQGlltgkylngipqdsrmhregnkvrgltp 256
Cdd:cd19157 140 HLEDLLADAEIVPMVNQVEFH--PRLTQKE-LRDYCKKQGIQLEAWSPLMQG---------------------------- 188
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
4AST_G 257 kmlteaNLNSLRLLNEMAQQRGQSMAQMALSWLLKDDRVTsvLIGASRAEQLEENVqALNNLTFSTKELAQIDQ 330
Cdd:cd19157 189 ------QLLDNPVLKEIAEKYNKSVAQVILRWDLQNGVVT--IPKSIKEHRIIENA-DVFDFELSQEDMDKIDA 253
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
22-329 |
2.51e-11 |
|
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: 63.19 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 22 GLRLPALSLGLWHnfghVNALESQRAIlRKAFDLGITHFDLANNYGpppgsAEENFGRLLREDfAAYRDELIISTKagyd 101
Cdd:cd19127 6 GVEMPALGLGVFQ----TPPEETADAV-ATALADGYRLIDTAAAYG-----NEREVGEGIRRS-GVDRSDIFVTTK---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 102 MWPGPYGSGGSRKyllaSLDQSLKRMGLEYVDIFYSHRVdenTPME-----ETASALAHAVQSGKALYVGISSYSPERTQ 176
Cdd:cd19127 71 LWISDYGYDKALR----GFDASLRRLGLDYVDLYLLHWP---VPNDfdrtiQAYKALEKLLAEGRVRAIGVSNFTPEHLE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 177 KMVEllREWKIPlLIHQPSynlLNRWVDKSGLLDTLQNNGVGCIAFTPLAqglltgkylnGIPQDSRMHREGNKvRGLTP 256
Cdd:cd19127 144 RLID--ATTVVP-AVNQVE---LHPYFSQKDLRAFHRRLGIVTQAWSPIG----------GVMRYGASGPTGPG-DVLQD 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
4AST_G 257 KMLTeanlnslrllnEMAQQRGQSMAQMALSWLLKDDRVTsvlIGAS-RAEQLEENVQALnNLTFSTKELAQID 329
Cdd:cd19127 207 PTIT-----------GLAEKYGKTPAQIVLRWHLQNGVSA---IPKSvHPERIAENIDIF-DFALSAEDMAAID 265
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
21-329 |
3.93e-11 |
|
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: 62.90 E-value: 3.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 21 SGLRLPALSLGLWHNFGHvnalESQRAILrKAFDLGITHFDLANNYGpppgsAEENFGRLLReDFAAYRDELIISTKagy 100
Cdd:cd19117 10 TGAEIPAVGLGTWQSKPN----EVAKAVE-AALKAGYRHIDTAAIYG-----NEEEVGQGIK-DSGVPREEIFITTK--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 101 dMWpgpygsGGSRKYLLASLDQSLKRMGLEYVDIFYSH-------RVDENTPMEETASA--------------LAHAVQS 159
Cdd:cd19117 76 -LW------CTWHRRVEEALDQSLKKLGLDYVDLYLMHwpvpldpDGNDFLFKKDDGTKdhepdwdfiktwelMQKLPAT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 160 GKALYVGISSYSperTQKMVELLREWKIPLLihqPSYNL--LNRWVDKSGLLDTLQNNGVGCIAFTPLAQglltgkylng 237
Cdd:cd19117 149 GKVKAIGVSNFS---IKNLEKLLASPSAKIV---PAVNQieLHPLLPQPKLVDFCKSKGIHATAYSPLGS---------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 238 ipqdsrmhregnkvrgltpkmlTEANLNSLRLLNEMAQQRGQSMAQMALSWLLKddRVTSVLIGASRAEQLEENVQAlnn 317
Cdd:cd19117 213 ----------------------TNAPLLKEPVIIKIAKKHGKTPAQVIISWGLQ--RGYSVLPKSVTPSRIESNFKL--- 265
|
330
....*....|..
4AST_G 318 LTFSTKELAQID 329
Cdd:cd19117 266 FTLSDEEFKEID 277
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
21-329 |
3.71e-10 |
|
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: 60.12 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 21 SGLRLPALSLGLWHNF-GHVnalesqRAILRKAFDLGITHFDLANNYGPPP--GSAEENfgrLLREDFAAYRDELIISTK 97
Cdd:cd19118 3 TGNKIPAIGLGTWQAEpGEV------GAAVKIALKAGYRHLDLAKVYQNQHevGQALKE---LLKEEPGVKREDLFITSK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 98 AgydmWpgpyGSGGSRKYLLASLDQSLKRMGLEYVDIFYSH------------------------RVDENTPMEETASAL 153
Cdd:cd19118 74 L----W----NNSHRPEYVEPALDDTLKELGLDYLDLYLIHwpvafkptgdlnpltavptnggevDLDLSVSLVDTWKAM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 154 AHAVQSGKALYVGISSYSPERTQKMVELLREWKI-------PLLIHQPsynllnrwvdksgLLDTLQNNGVGCIAFTPLa 226
Cdd:cd19118 146 VELKKTGKVKSIGVSNFSIDHLQAIIEETGVVPAvnqieahPLLLQDE-------------LVDYCKSKNIHITAYSPL- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 227 qglltgkylngipqdsrmhreGNKVRGLTPkmlteanLNSLRLLNEMAQQRGQSMAQMALSWLLKddRVTSVLIGASRAE 306
Cdd:cd19118 212 ---------------------GNNLAGLPL-------LVQHPEVKAIAAKLGKTPAQVLIAWGIQ--RGHSVIPKSVTPS 261
|
330 340
....*....|....*....|...
4AST_G 307 QLEENVQalnNLTFSTKELAQID 329
Cdd:cd19118 262 RIRSNFE---QVELSDDEFNAVT 281
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
22-333 |
5.04e-10 |
|
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: 59.85 E-value: 5.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 22 GLRLPALSLGLWHNfghvNALESQRAIlRKAFDLGITHFDLANNYGpppgsAEENFGRLLREDFAA---YRDELIISTKa 98
Cdd:cd19155 9 GEKMPVVGLGTWQS----SPEEIETAV-DTALEAGYRHIDTAYVYR-----NEAAIGNVLKKWIDSgkvKREELFIVTK- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 99 gydMWPGPYGSGGSRKYLLASLdqslKRMGLEYVDIFY---------------------SHRVDENTPMEETASALAHAV 157
Cdd:cd19155 78 ---LPPGGNRREKVEKFLLKSL----EKLQLDYVDLYLihfpvgslskeddsgkldptgEHKQDYTTDLLDIWKAMEAQV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 158 QSGKALYVGISSYSPErtqKMVELLREWKIpllihQPSyNL---LNRWVDKSGLLDTLQNNGVGCIAFTPLaqglltgky 234
Cdd:cd19155 151 DQGLTRSIGLSNFNRE---QMARILKNARI-----KPA-NLqveLHVYLQQKDLVDFCSTHSITVTAYAPL--------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 235 lnGIPQDSRMHREGNKVRGLTPKMLTEAnlnslrLLNEMAQQRGQSMAQMALSWLLkdDRVTSVLIGASRAEQLEENVQA 314
Cdd:cd19155 213 --GSPGAAHFSPGTGSPSGSSPDLLQDP------VVKAIAERHGKSPAQVLLRWLM--QRGVVVIPKSTNAARIKENFQV 282
|
330 340
....*....|....*....|.
4AST_G 315 LN-NLT-FSTKELAQIDQHIA 333
Cdd:cd19155 283 FDfELTeADMAKLSSLDKNIR 303
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
21-228 |
1.92e-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: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 21 SGLRLPALSLGLWHNfghVNALESQRAILRKAFDLGITHFDLANNYGpppgsAEENFGRLLREDFA---AYRDELIISTK 97
Cdd:cd19119 8 TGASIPALGLGTASP---HEDRAEVKEAVEAAIKEGYRHIDTAYAYE-----TEDFVGEAIKRAIDdgsIKREELFITTK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 98 agydMWPGPYgsggsrKYLLASLDQSLKRMGLEYVDIFYSH------RVDENTPME-------------------ETASA 152
Cdd:cd19119 80 ----VWPTFY------DEVERSLDESLKALGLDYVDLLLVHwpvcfeKDSDDSGKPftpvnddgktryaasgdhiTTYKQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
4AST_G 153 LAHAVQSGKALYVGISSYSPErtqKMVELLREWKIPLLIHQPSynlLNRWVDKSGLLDTLQNNGVGCIAFTPLAQG 228
Cdd:cd19119 150 LEKIYLDGRAKAIGVSNYSIV---YLERLIKECKVVPAVNQVE---LHPHLPQMDLRDFCFKHGILVTAYSPLGSH 219
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
22-329 |
2.01e-09 |
|
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes prostaglandin F2-alpha synthase (PGFS) from Leishmania major (AKR5A1) and Trypanosoma brucei (AKR5A2). PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity for synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde. The AKR5G family of AKR includes Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase, which corresponds to aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381352 [Multi-domain] Cd Length: 254 Bit Score: 57.45 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 22 GLRLPALSLGLWHNfghVNALESQRAIlRKAFDLGITHFDLANNYgpppgSAEENFGRLLREDfAAYRDELIISTKagyd 101
Cdd:cd19126 6 GTRMPWLGLGVFQT---PDGDETERAV-QTALENGYRSIDTAAIY-----KNEEGVGEAIRES-GVPREELFVTTK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 102 MWPGPYGSggsrKYLLASLDQSLKRMGLEYVDIFYSHRVDENTpMEETASALAHAVQSGKALYVGISSYSPERTQkmvEL 181
Cdd:cd19126 72 LWNDDQRA----RRTEDAFQESLDRLGLDYVDLYLIHWPGKDK-FIDTWKALEKLYASGKVKAIGVSNFQEHHLE---EL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 182 LREWKIPLLIHQPSYN-LLNRwvdkSGLLDTLQNNGVGCIAFTPLAQG-LLTGKYLNGIpqdsrmhregnkvrgltpkml 259
Cdd:cd19126 144 LAHADVVPAVNQVEFHpYLTQ----KELRGYCKSKGIVVEAWSPLGQGgLLSNPVLAAI--------------------- 198
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 260 teanlnslrllnemAQQRGQSMAQMALSWLLKDDRVTsvLIGASRAEQLEENVQALnNLTFSTKELAQID 329
Cdd:cd19126 199 --------------GEKYGKSAAQVVLRWDIQHGVVT--IPKSVHASRIKENADIF-DFELSEDDMTAID 251
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
21-332 |
7.63e-08 |
|
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent D-xylose reductase (XR) from Pichia stipites, Kluyveromyces lactis, Pachysolen tannophilus, Candida tropicalis, and Candida tenuis, Gre3p from Saccharomyces cerevisiae, XR from Candida tropicalis, Pichia guilliermondii, Debaryomyces hansenli, and Debaryomyces nepalensis, which correspond to aldo-keto reductase family 2 member B1-B10 (AKR2B1-10), respectively. XR (EC1.1.1.307) catalyzes the NAD(P)H dependent reduction of xylose to xylitol.
Pssm-ID: 381339 [Multi-domain] Cd Length: 310 Bit Score: 53.22 E-value: 7.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 21 SGLRLPALSLGLWHNFGHVNALESQRAIlrkafDLGITHFDLANNYGPPPgSAEENFGRLLREDFAAyRDELIISTKagy 100
Cdd:cd19113 7 SGYKMPSVGFGCWKLDNATAADQIYQAI-----KAGYRLFDGAEDYGNEK-EVGEGVNRAIDEGLVK-REELFLTSK--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 101 dMWpgpyGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHR-------------------------VDENTPMEETASALAH 155
Cdd:cd19113 77 -LW----NNFHDPKNVETALNKTLSDLKLDYVDLFLIHFpiafkfvpieekyppgfycgdgdnfVYEDVPILDTWKALEK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 156 AVQSGKALYVGISSYSPERTQkmvELLREWKI-PLLI---HQPsynllnrWVDKSGLLDTLQNNGVGCIAFTPLAqgllt 231
Cdd:cd19113 152 LVDAGKIKSIGVSNFPGALIL---DLLRGATIkPAVLqieHHP-------YLQQPKLIEYAQKAGITITAYSSFG----- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 232 gkylngiPQDsrmHREGNKVRGLTPKMLTEANlnslrLLNEMAQQRGQSMAQMALSWllKDDRVTSVLIGASRAEQLEEN 311
Cdd:cd19113 217 -------PQS---FVELNQGRALNTPTLFEHD-----TIKSIAAKHNKTPAQVLLRW--ATQRGIAVIPKSNLPERLLQN 279
|
330 340
....*....|....*....|....
4AST_G 312 VQaLNNLTFSTKELAQI---DQHI 332
Cdd:cd19113 280 LS-VNDFDLTKEDFEEIaklDIGL 302
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
21-225 |
7.80e-08 |
|
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: 52.92 E-value: 7.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 21 SGLRLPALSLGLWHNfghvNALESQRAILRkAFDLGITHFDLANNYGpppgsAEENFGRLLREDFAA--YRDELIISTKa 98
Cdd:cd19121 8 TGASIPAVGLGTWQA----KAGEVKAAVAH-ALKIGYRHIDGALCYQ-----NEDEVGEGIKEAIAGgvKREDLFVTTK- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 99 gydMWpgpygSGGSRKYLLAsLDQSLKRMGLEYVDIFYSH----------------------RVDENTPMEETASALAHA 156
Cdd:cd19121 77 ---LW-----STYHRRVELC-LDRSLKSLGLDYVDLYLVHwpvllnpngnhdlfptlpdgsrDLDWDWNHVDTWKQMEKV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
4AST_G 157 VQSGKALYVGISSYSPERTQkmvELLREWKIPLLIHQPSynlLNRWVDKSGLLDTLQNNGVGCIAFTPL 225
Cdd:cd19121 148 LKTGKTKAIGVSNYSIPYLE---ELLKHATVVPAVNQVE---NHPYLPQQELVDFCKEKGILIEAYSPL 210
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
22-316 |
1.36e-07 |
|
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: 52.17 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 22 GLRLPALSLGLWHnfghVNALESQRAILrKAFDLGITHFDLANNYGpppgsAEENFGRLLR---EDFAAYRDELIISTKa 98
Cdd:cd19114 1 GDKMPLVGFGTAK----IKANETEEVIY-NAIKVGYRLIDGALLYG-----NEAEVGRGIRkaiQEGLVKREDLFIVTK- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 99 gydMWPGPYGsggsRKYLLASLDQSLKRMGLEYVDIFYSH------RVD-------------------ENTPMEETASAL 153
Cdd:cd19114 70 ---LWNNFHG----KDHVREAFDRQLKDYGLDYIDLYLIHfpipaaYVDpaenypflwkdkelkkfplEQSPMQECWREM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 154 AHAVQSGKALYVGISSYSperTQKMVELLREWKI-PLLI---HQPsynllnrWVDKSGLLDTLQNNGVGCIAFTPLaqgl 229
Cdd:cd19114 143 EKLVDAGLVRNIGIANFN---VQLILDLLTYAKIkPAVLqieHHP-------YLQQKRLIDWAKKQGIQITAYSSF---- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 230 ltgkylngipqdsrmhreGNKVRGLTPKML-TEANLNSLRLLNEMAQQRGQSMAQMALSWLLkdDRVTSVLIGASRAEQL 308
Cdd:cd19114 209 ------------------GNAVYTKVTKHLkHFTNLLEHPVVKKLADKHKRDTGQVLLRWAV--QRNITVIPKSVNVERM 268
|
....*...
4AST_G 309 EENVQALN 316
Cdd:cd19114 269 KTNLDITS 276
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
22-180 |
1.85e-07 |
|
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: 51.50 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 22 GLRLPALSLGLWHnfghVNALESQRAILrKAFDLGITHFDLANNYGpppgsAEENFGRLLREDFAAyRDELIISTKAgyd 101
Cdd:cd19132 4 GTQIPAIGFGTYP----LKGDEGVEAVV-AALQAGYRLLDTAFNYE-----NEGAVGEAVRRSGVP-REELFVTTKL--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 102 mwPGPYGSggsRKYLLASLDQSLKRMGLEYVDIFYSH----RVDENTpmeETASALAHAVQSGKALYVGISSYSPERTQK 177
Cdd:cd19132 70 --PGRHHG---YEEALRTIEESLYRLGLDYVDLYLIHwpnpSRDLYV---EAWQALIEAREEGLVRSIGVSNFLPEHLDR 141
|
...
4AST_G 178 MVE 180
Cdd:cd19132 142 LID 144
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
21-329 |
3.44e-07 |
|
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: 51.23 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 21 SGLRLPALSLGLWHNF-GHV-NALESqrailrkAFDLGITHFDLANNYGpppgsAEENFGRLLREDFAAY----RDELII 94
Cdd:cd19106 3 TGQKMPLIGLGTWKSKpGQVkAAVKY-------ALDAGYRHIDCAAVYG-----NEQEVGEALKEKVGPGkavpREDLFV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 95 STKagydMWpgpygsggSRKY----LLASLDQSLKRMGLEYVDIFYSH------RVDE-------------NTPMEETAS 151
Cdd:cd19106 71 TSK----LW--------NTKHhpedVEPALRKTLKDLQLDYLDLYLIHwpyafeRGDNpfpknpdgtirydSTHYKETWK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 152 ALAHAVQSGKALYVGISSYSPERTQKMVELLRewkiplliHQPSYNLL--NRWVDKSGLLDTLQNNGVGCIAFTPLaqgl 229
Cdd:cd19106 139 AMEKLVDKGLVKAIGLSNFNSRQIDDILSVAR--------IKPAVLQVecHPYLAQNELIAHCKARGLVVTAYSPL---- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 230 ltgkylnGIPqdSRMHREGNKvrgltPKMLTEANlnslrlLNEMAQQRGQSMAQMALSWLLKddRVTSVLIGASRAEQLE 309
Cdd:cd19106 207 -------GSP--DRPWAKPDE-----PVLLEEPK------VKALAKKYNKSPAQILLRWQVQ--RGVVVIPKSVTPSRIK 264
|
330 340
....*....|....*....|
4AST_G 310 ENVQALnNLTFSTKELAQID 329
Cdd:cd19106 265 QNIQVF-DFTLSPEEMKQLD 283
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
22-344 |
4.03e-06 |
|
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: 47.72 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 22 GLRLPALSLGLWHNFGH---------VNALESQ-RAILRKAFDLGITHFDLANNYGpppgSAEENFGRLLREDFAAyRDE 91
Cdd:cd19098 4 GLGLAALGRPGYINLGHaadlgsgrsVEAMRAHtHAVLDAAWAAGVRYFDAARSYG----RAEEFLGSWLRSRNIA-PDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 92 LIISTKAGYDMWPGPYGSGG-------SRKYLLASLDQSLKRMGlEYVDIFYSHRVDENTPMEETASALAHAVQSGKA-L 163
Cdd:cd19098 79 VFVGSKWGYTYTADWQVDAAvhevkdhSLARLLKQWEETRSLLG-KHLDLYQIHSATLESGVLEDADVLAALAELKAEgV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 164 YVGISSYSPERTQKMVELLrewKIPLLIH------QPSYNLLNRWVdkSGLLDTLQNNGVGCIAFTPLAQGLLTgkylng 237
Cdd:cd19098 158 KIGLSLSGPQQAETLRRAL---EIEIDGArlfdsvQATWNLLEQSA--GEALEEAHEAGMGVIVKEALANGRLT------ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 238 ipqdsrmhregnkVRGLTPKMLTEANLnslrlLNEMAQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQALnN 317
Cdd:cd19098 227 -------------DRNPSPELAPLMAV-----LKAVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRAL-D 287
|
330 340
....*....|....*....|....*..
4AST_G 318 LTFSTKELAQIDQHIADGElNLWQASS 344
Cdd:cd19098 288 VSLDLELLAALADLAEPPE-DYWATRS 313
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
25-313 |
1.24e-05 |
|
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: 46.00 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 25 LPALSLGLWHnfghVNALESQRAILrKAFDLGITHFDLANNYGpppgsAEENFGRLLREDFAAyRDELIISTKagydMWP 104
Cdd:cd19134 11 MPVIGLGVGE----LSDDEAERSVS-AALEAGYRLIDTAAAYG-----NEAAVGRAIAASGIP-RGELFVTTK----LAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 105 GPYGSGGSRKYLLASLDqslkRMGLEYVDIFYSH--RVDENTPMeETASALAHAVQSGKALYVGISSYSPERTQKMVELL 182
Cdd:cd19134 76 PDQGFTASQAACRASLE----RLGLDYVDLYLIHwpAGREGKYV-DSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 183 REwkIPLLIHQPSYNLLNrwvdKSGLLDTLQNNGVGCIAFTPLAQGLLTgkylngipqdsrmhrEGNKVRGLtpkmltea 262
Cdd:cd19134 151 FF--TPAVNQIELHPLLN----QAELRKVNAQHGIVTQAYSPLGVGRLL---------------DNPAVTAI-------- 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
4AST_G 263 nlnslrllnemAQQRGQSMAQMALSWLLKDDRVtsVLIGASRAEQLEENVQ 313
Cdd:cd19134 202 -----------AAAHGRTPAQVLLRWSLQLGNV--VISRSSNPERIASNLD 239
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|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
22-138 |
1.53e-04 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 42.75 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 22 GLRLPALSLGLWHnfghVNALESQRAILrKAFDLGITHFDLANNYGpppgsAEENFGRLLREDFAAyRDELIISTKagyd 101
Cdd:PRK11565 12 GNVMPQLGLGVWQ----ASNEEVITAIH-KALEVGYRSIDTAAIYK-----NEEGVGKALKEASVA-REELFITTK---- 76
|
90 100 110
....*....|....*....|....*....|....*..
4AST_G 102 MWpgpygsGGSRKYLLASLDQSLKRMGLEYVDIFYSH 138
Cdd:PRK11565 77 LW------NDDHKRPREALEESLKKLQLDYVDLYLMH 107
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
22-225 |
1.84e-03 |
|
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase (AR, EC 1.1.1.21) from Homo sapiens (AKR1B1), Oryctolagus cuniculus (kidney, AKR1B2), Mus musculus (AKR1B3), Rattus norvegicus (lens, AKR1B4), Bos taurus (lens/testis, AKR1B5), and Sus scrofa (lens, AKR1B6), aldose reductase-related protein 1 (ALD1, EC1.1.1.21) from Mus musculus (AKR1B7), Rattus norvegicus (AKR1B14), and Homo sapiens (AKR1B15), Mus musculus fibroblast growth factor induced protein (FR-1 or AKR1B8, EC 1.1.1.21), Cricetulus griseus aldose reductase-related protein 2 (ALD2 or AKR1B9, EC 1.1.1.21), aldose reductase-like from Homo sapiens (ARL-1 or AKR1B10) and Rattus norvegicus (AKR1B13), aldo-keto reductase from Gallus domesticus (eye, tongue, esophagus, AKR1B12), and Oryctolagus cuniculus AR-like protein (3beta-HSD, AKR1B19). AR, also called aldehyde reductase, catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. ALD1 reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. It may play a role in the metabolism of xenobiotic aromatic aldehydes. FR-1, also called aldose reductase-related protein 2, or fibroblast growth factor-regulated protein (FGFRP), is induced by fibroblast growth factor-1. It may play a role in the regulation of the cell cycle. FR-1 belongs to the NADPH-dependent aldo-keto reductase family. ALD2 is an inducible aldo-keto reductase with a preference for aliphatic substrates. It can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. ARL-1, also called aldose reductase-like, or aldose reductase-related protein (ARP), or small intestine reductase, or SI reductase, acts as all-trans-retinaldehyde reductase that can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). It may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. AKR1B15, also called estradiol 17-beta-dehydrogenase AKR1B15, is a mitochondrial aldo-keto reductase that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. It has a strong selectivity towards NADP(H). AKR1B19 is aldose reductase-like that may show 3-beta-hydroxysteroid dehydrogenase (3beta-HSD) activity.
Pssm-ID: 381333 [Multi-domain] Cd Length: 307 Bit Score: 39.71 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 22 GLRLPALSLGLWHN-FGHVnalesqRAILRKAFDLGITHFDLANNYgpppgSAEENFGRLLREDF---AAYRDELIISTK 97
Cdd:cd19107 1 GAKMPILGLGTWKSpPGQV------TEAVKVAIDAGYRHIDCAYVY-----QNENEVGEAIQEKIkeqVVKREDLFIVSK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 98 agydMWPGPYgsggSRKYLLASLDQSLKRMGLEYVDIFYSH-------------------RVDENTPMEETASALAHAVQ 158
Cdd:cd19107 70 ----LWCTFH----EKGLVKGACQKTLSDLKLDYLDLYLIHwptgfkpgkelfpldesgnVIPSDTTFLDTWEAMEELVD 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
4AST_G 159 SGKALYVGISSYSPERTQKmveLLREwkiPLLIHQPSYNLL--NRWVDKSGLLDTLQNNGVGCIAFTPL 225
Cdd:cd19107 142 EGLVKAIGVSNFNHLQIER---ILNK---PGLKYKPAVNQIecHPYLTQEKLIQYCQSKGIVVTAYSPL 204
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
22-138 |
2.92e-03 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 39.14 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4AST_G 22 GLRLPALSLGLWHNfGHVNALESQRAIlRKAFDLGITHFDLANNYGpppgsAEENFGRLLREDFAA---YRDELIISTKa 98
Cdd:cd19108 8 GHFIPVLGFGTYAP-EEVPKSKALEAT-KLAIDAGFRHIDSAYLYQ-----NEEEVGQAIRSKIADgtvKREDIFYTSK- 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
4AST_G 99 gydMWPGPYgsggsRKYLL-ASLDQSLKRMGLEYVDIFYSH 138
Cdd:cd19108 80 ---LWCTFH-----RPELVrPALEKSLKKLQLDYVDLYLIH 112
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