|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
14-321 |
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: 587.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 14 YRRLGKSGLKLPAISLGLWHNFGDVDTLDNQRAIVRAAFDHGITHFDLANNYGPPAGSAEINFGRILKEDMFPYRDELII 93
Cdd:cd19151 2 YNRCGRSGLKLPAISLGLWHNFGDVDRYENSRAMLRRAFDLGITHFDLANNYGPPPGSAEENFGRILKEDLKPYRDELII 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 94 SSKAGYYMWPGPYGEWGSRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVSNYSAEQ 173
Cdd:cd19151 82 STKAGYTMWPGPYGDWGSKKYLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGISNYPPEE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 174 TAEISKIFQELRTPFIIHQPRYNMFDRWIEDGLTDVLAEEGIGTITFSPLAQGLLTNRYLHGIPEDSRAHRSDSPFLTED 253
Cdd:cd19151 162 AREAAAILKDLGTPCLIHQPKYSMFNRWVEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYLNGIPEDSRAAKGSSFLKPEQ 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510806721 254 NVQSTIEVVKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALDHLAFSKEELT 321
Cdd:cd19151 242 ITEEKLAKVRRLNEIAQARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALDNREFSEEELA 309
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
14-320 |
0e+00 |
|
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo. Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2). It catalyzes the conversion of 3-hydroxybutanal (3-HB) to 1,3-butanediol (1,3-BDO) by using NADPH as a cofactor.
Pssm-ID: 381315 [Multi-domain] Cd Length: 308 Bit Score: 560.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 14 YRRLGKSGLKLPAISLGLWHNFGDVDTLDNQRAIVRAAFDHGITHFDLANNYGPPAGSAEINFGRILKEDMFPYRDELII 93
Cdd:cd19089 1 YRRCGRSGLHLPAISLGLWHNFGDYTSPEEARELLRTAFDLGITHFDLANNYGPPPGSAEENFGRILKRDLRPYRDELVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 94 SSKAGYYMWPGPYGEWGSRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVSNYSAEQ 173
Cdd:cd19089 81 STKAGYGMWPGPYGDGGSRKYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPGAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 174 TAEISKIFQELRTPFIIHQPRYNMFDRWIEDGLTDVLAEEGIGTITFSPLAQGLLTNRYLHGIPEDSRAHRSDSPFLTED 253
Cdd:cd19089 161 ARRAIALLRELGVPLIIHQPRYSLLDRWAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKYLNGIPPDSRRAAESKFLTEEA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510806721 254 NVQSTIEVVKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALDHLAFSKEEL 320
Cdd:cd19089 241 LTPEKLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAALKNLDFSEEEL 307
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
14-320 |
0e+00 |
|
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
Pssm-ID: 381376 [Multi-domain] Cd Length: 309 Bit Score: 529.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 14 YRRLGKSGLKLPAISLGLWHNFGDVDTLDNQRAIVRAAFDHGITHFDLANNYGPPAGSAEINFGRILKEDMFPYRDELII 93
Cdd:cd19150 2 YRRCGKSGLKLPALSLGLWHNFGDDTPLETQRAILRTAFDLGITHFDLANNYGPPPGSAEENFGRILREDFAGYRDELII 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 94 SSKAGYYMWPGPYGEWGSRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVSNYSAEQ 173
Cdd:cd19150 82 STKAGYDMWPGPYGEWGSRKYLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYSPER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 174 TAEISKIFQELRTPFIIHQPRYNMFDRWIE-DGLTDVLAEEGIGTITFSPLAQGLLTNRYLHGIPEDSRAHRSDSpFLTE 252
Cdd:cd19150 162 TREAAAILRELGTPLLIHQPSYNMLNRWVEeSGLLDTLQELGVGCIAFTPLAQGLLTDKYLNGIPEGSRASKERS-LSPK 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510806721 253 DNVQSTIEVVKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALDHLAFSKEEL 320
Cdd:cd19150 241 MLTEANLNSIRALNEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGALDNLTFSADEL 308
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
2-324 |
1.23e-172 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 482.95 E-value: 1.23e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 2 YLANEQRYEKMDYRRLGKSGLKLPAISLGLWHNFGDVDTLDNQRAIVRAAFDHGITHFDLANNYGPPAGSAEINFGRILK 81
Cdd:PRK09912 3 WLANPERYGQMQYRYCGKSGLRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGPPPGSAEENFGRLLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 82 EDMFPYRDELIISSKAGYYMWPGPYGEWGSRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKT 161
Cdd:PRK09912 83 EDFAAYRDELIISTKAGYDMWPGPYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 162 LYVGVSNYSAEQTAEISKIFQELRTPFIIHQPRYNMFDRWIE-DGLTDVLAEEGIGTITFSPLAQGLLTNRYLHGIPEDS 240
Cdd:PRK09912 163 LYVGISSYSPERTQKMVELLREWKIPLLIHQPSYNLLNRWVDkSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 241 RAHRS-------DSPFLTEDNVQStievVKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALDHL 313
Cdd:PRK09912 243 RMHREgnkvrglTPKMLTEANLNS----LRLLNEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQALNNL 318
|
330
....*....|.
gi 510806721 314 AFSKEELTQID 324
Cdd:PRK09912 319 TFSTEELAQID 329
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
12-331 |
1.24e-144 |
|
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: 410.72 E-value: 1.24e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 12 MDYRRLGKSGLKLPAISLGLW---HNFGDVDtLDNQRAIVRAAFDHGITHFDLANNYGPpaGSAEINFGRILKEDmfpYR 88
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTMtfgGPWGGVD-EAEAIAILDAALDAGINFFDTADVYGP--GRSEELLGEALKGR---PR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 89 DELIISSKAGYYMWPGPYGEWGSRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVSN 168
Cdd:COG0667 75 DDVVIATKVGRRMGPGPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 169 YSAEQTAEISKIFQELrTPFIIHQPRYNMFDRWIEDGLTDVLAEEGIGTITFSPLAQGLLTNRYLHG--IPEDSRAHRSd 246
Cdd:COG0667 155 YSAEQLRRALAIAEGL-PPIVAVQNEYSLLDRSAEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGatFPEGDRAATN- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 247 spFLTEDNVQSTIEVVKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALDhLAFSKEELTQIDAI 326
Cdd:COG0667 233 --FVQGYLTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAAD-LELSAEDLAALDAA 309
|
....*
gi 510806721 327 LAKLT 331
Cdd:COG0667 310 LAAVP 314
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
21-311 |
6.13e-115 |
|
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: 334.56 E-value: 6.13e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 21 GLKLPAISLGLWHNFGDVDTLDNQRAIVRAAFDHGITHFDLANNYGppAGSAEINFGRILKEdmFPyRDELIISSKAGYY 100
Cdd:cd19074 1 GLKVSELSLGTWLTFGGQVDDEDAKACVRKAYDLGINFFDTADVYA--AGQAEEVLGKALKG--WP-RESYVISTKVFWP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 101 MWPGPYgEWG-SRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVSNYSAEQTAEISK 179
Cdd:cd19074 76 TGPGPN-DRGlSRKHIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 180 IFQELR-TPFIIHQPRYNMFDRWIEDGLTDVLAEEGIGTITFSPLAQGLLTNRYLHGIPEDSRAHRSDS---PFLTEDNV 255
Cdd:cd19074 155 LARQFGlIPPVVEQPQYNMLWREIEEEVIPLCEKNGIGLVVWSPLAQGLLTGKYRDGIPPPSRSRATDEdnrDKKRRLLT 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 510806721 256 QSTIEVVKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALD 311
Cdd:cd19074 235 DENLEKVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKASG 290
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
12-326 |
1.88e-103 |
|
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: 306.06 E-value: 1.88e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 12 MDYRRLGKSGLKLPAISLGLWHNFGDVDTLDNQRAIVRAAFDHGITHFDLANNYGppAGSAEINFGRILKEDMFPyRDEL 91
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSWVTFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYA--NGQSEEIMGQAIKELGWP-RSDY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 92 IISSKAgYYMWPGPYG-EWG-SRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVSNY 169
Cdd:cd19143 78 VVSTKI-FWGGGGPPPnDRGlSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGTSEW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 170 SAEQTAEISKIFQELR-TPFIIHQPRYNMFDRW-IEDGLTDVLAEEGIGTITFSPLAQGLLTNRYLHGIPEDSRAHRSDS 247
Cdd:cd19143 157 SAQQIEEAHEIADRLGlIPPVMEQPQYNLFHRErVEVEYAPLYEKYGLGTTTWSPLASGLLTGKYNNGIPEGSRLALPGY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 248 PFLTE---DNVQSTIEVVKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALDHLA-FSKEELTQI 323
Cdd:cd19143 237 EWLKDrkeELGQEKIEKVRKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEENLKALEVLPkLTPEVMEKI 316
|
...
gi 510806721 324 DAI 326
Cdd:cd19143 317 EAI 319
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
27-327 |
1.95e-95 |
|
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: 284.59 E-value: 1.95e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 27 ISLGLWHNFGDVDTLDNQRA--IVRAAFDHGITHFDLANNYGPpaGSAEINFGRILKEDMFPyRDELIISSKagYYMWPG 104
Cdd:pfam00248 1 IGLGTWQLGGGWGPISKEEAleALRAALEAGINFIDTAEVYGD--GKSEELLGEALKDYPVK-RDKVVIATK--VPDGDG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 105 PYGEWGSRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVSNYSAEQtaeISKIFQEL 184
Cdd:pfam00248 76 PWPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQ---IEKALTKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 185 RTPFIIHQPRYNMFDRWIEDGLTDVLAEEGIGTITFSPLAQGLLTNRYLHGIPEDSRAHRSDSPFLTEDNVqstiEVVKQ 264
Cdd:pfam00248 153 KIPIVAVQVEYNLLRRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPGERRRLLKKGTPLNL----EALEA 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 510806721 265 LNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALDhLAFSKEELTQIDAIL 327
Cdd:pfam00248 229 LEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALE-FPLSDEEVARIDELL 290
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
21-324 |
2.79e-95 |
|
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: 284.42 E-value: 2.79e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 21 GLKLPAISLGLW----HNFGDVDTLDNQRAIvRAAFDHGITHFDLANNYGppAGSAEINFGRILKEdmfpYRDELIISSK 96
Cdd:cd19084 1 DLKVSRIGLGTWaiggTWWGEVDDQESIEAI-KAAIDLGINFFDTAPVYG--FGHSEEILGKALKG----RRDDVVIATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 97 AGYYmWPGPYGEW--GSRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVSNYSAEQT 174
Cdd:cd19084 74 CGLR-WDGGKGVTkdLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 175 AEISKIfqelrTPFIIHQPRYNMFDRWIEDGLTDVLAEEGIGTITFSPLAQGLLTNRYLHGIPEDSRAHRSDSPFLTEDN 254
Cdd:cd19084 153 EEARKY-----GPIVSLQPPYSMLEREIEEELLPYCRENGIGVLPYGPLAQGLLTGKYKKEPTFPPDDRRSRFPFFRGEN 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 255 VQSTIEVVKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALDhLAFSKEELTQID 324
Cdd:cd19084 228 FEKNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALD-WELTEEELKEID 296
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
12-326 |
2.05e-91 |
|
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: 275.65 E-value: 2.05e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 12 MDYRRLGKSGLKLPAISLG---------LWHNFGDVDTLDNQRaIVRAAFDHGITHFDLANNYGppAGSAEINFGRILKe 82
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGtmtfgggggFFGAWGGVDQEEADR-LVDIALDAGINFFDTADVYS--EGESEEILGKALK- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 83 dmfPYRDELIISSKAGYYMWPGPYGEWGSRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTL 162
Cdd:cd19091 77 ---GRRDDVLIATKVRGRMGEGPNDVGLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 163 YVGVSNYSAEQTAEISKIfQELR--TPFIIHQPRYNMFDRWIEDGLTDVLAEEGIGTITFSPLAQGLLTNRYLHG--IPE 238
Cdd:cd19091 154 YIGVSNFSAWQIMKALGI-SERRglARFVALQAYYSLLGRDLEHELMPLALDQGVGLLVWSPLAGGLLSGKYRRGqpAPE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 239 DSRAHRSDSPFLTEDNVQStIEVVKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALDhLAFSKE 318
Cdd:cd19091 233 GSRLRRTGFDFPPVDRERG-YDVVDALREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGAAG-LSLTPE 310
|
....*...
gi 510806721 319 ELTQIDAI 326
Cdd:cd19091 311 EIARLDKV 318
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
12-326 |
2.17e-91 |
|
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: 275.22 E-value: 2.17e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 12 MDYRRLGKSGLKLPAISLGLWhNFGDVDTLDNQRAIVRAAFDHGITHFDLANNYGppAGSAEINFGRILKEDmfpyRDEL 91
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGTM-NFGGRTDEETSFAIMDRALDAGINFFDTADVYG--GGRSEEIIGRWIAGR----RDDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 92 IISSKAGYYMWPGPYGEWGSRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVSNYSA 171
Cdd:cd19087 74 VLATKVFGPMGDDPNDRGLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 172 EQTAEISKIFQELR-TPFIIHQPRYNMFDRWIEDGLTDVLAEEGIGTITFSPLAQGLLTNRYLHGIPEDSRAHRSDSPFL 250
Cdd:cd19087 154 WQIAKAQGIAARRGlLRFVSEQPMYNLLKRQAELEILPAARAYGLGVIPYSPLAGGLLTGKYGKGKRPESGRLVERARYQ 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510806721 251 TEDNVQSTIEVVKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALDhLAFSKEELTQIDAI 326
Cdd:cd19087 234 ARYGLEEYRDIAERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALE-ITLTPELLAEIDEL 308
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
13-324 |
1.65e-83 |
|
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: 255.20 E-value: 1.65e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 13 DYRRLGKSGLKLPAISLGLWHnFGDVD----TLDNQ--RAIVRAAFDHGITHFDLANNYGppAGSAEINFGRILKEdmFP 86
Cdd:cd19079 1 EYVRLGNSGLKVSRLCLGCMS-FGDPKwrpwVLDEEesRPIIKRALDLGINFFDTANVYS--GGASEEILGRALKE--FA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 87 YRDELIISSKAGYYMWPGPYGEWGSRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGV 166
Cdd:cd19079 76 PRDEVVIATKVYFPMGDGPNGRGLSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 167 SNYSAEQTAEISKIfQELR--TPFIIHQPRYNMFDRWIEDGLTDVLAEEGIGTITFSPLAQGLLTNRYLHG---IPEDSR 241
Cdd:cd19079 156 SSMYAWQFAKALHL-AEKNgwTKFVSMQNHYNLLYREEEREMIPLCEEEGIGVIPWSPLARGRLARPWGDTterRRSTTD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 242 AHRSDSPFLTEDNVqstiEVVKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALDhLAFSKEELT 321
Cdd:cd19079 235 TAKLKYDYFTEADK----EIVDRVEEVAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAALD-IKLSEEEIK 309
|
...
gi 510806721 322 QID 324
Cdd:cd19079 310 YLE 312
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
24-326 |
2.64e-82 |
|
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: 251.35 E-value: 2.64e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 24 LPAISLGLWhNFGDVDTLDNQ-----RAIVRAAFDHGITHFDLANNYGppAGSAEINFGRILKedmfPYRDELIISSKAg 98
Cdd:cd19085 1 VSRLGLGCW-QFGGGYWWGDQddeesIATIHAALDAGINFFDTAEAYG--DGHSEEVLGKALK----GRRDDVVIATKV- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 99 yymWPGPygewGSRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVSNYSAEQTAEIS 178
Cdd:cd19085 73 ---SPDN----LTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 179 KifqelRTPFIIHQPRYNMFDRWIEDGLTDVLAEEGIGTITFSPLAQGLLTNRYLHGIPEDSRAHRSDSPFLTED-NVQS 257
Cdd:cd19085 146 D-----AGRIDSNQLPYNLLWRAIEYEILPFCREHGIGVLAYSPLAQGLLTGKFSSAEDFPPGDARTRLFRHFEPgAEEE 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 510806721 258 TIEVVKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALDhLAFSKEELTQIDAI 326
Cdd:cd19085 221 TFEALEKLKEIADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVD-LELSPSVLERLDEI 288
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
25-308 |
6.31e-77 |
|
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: 235.49 E-value: 6.31e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 25 PAISLGLWHnFGDVDTLDNQRAIVRAAFDHGITHFDLANNYGppAGSAEINFGRILKEDmfPYRDELIISSKAGYYMWPG 104
Cdd:cd06660 1 SRLGLGTMT-FGGDGDEEEAFALLDAALEAGGNFFDTADVYG--DGRSERLLGRWLKGR--GNRDDVVIATKGGHPPGGD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 105 PYGEWGSRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVSNYSAEQTAEISKIFQEL 184
Cdd:cd06660 76 PSRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKAH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 185 -RTPFIIHQPRYNMFDRW-IEDGLTDVLAEEGIGTITFSPLAQGlltnrylhgipedsrahrsdspfltednvqstievv 262
Cdd:cd06660 156 gLPGFAAVQPQYSLLDRSpMEEELLDWAEENGLPLLAYSPLARG------------------------------------ 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 510806721 263 kqlndiaekrgqtLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLK 308
Cdd:cd06660 200 -------------PAQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
16-324 |
1.02e-76 |
|
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a founding member of aldo-keto reductase family 9 member C1 (AKR9C1).
Pssm-ID: 381307 [Multi-domain] Cd Length: 308 Bit Score: 237.50 E-value: 1.02e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 16 RLGKSGLKLPAISLGLWhNFGDvdTLDNQR--AIVRAAFDHGITHFDLANNY-----GPPAGSAEINFGRILKEDMfpYR 88
Cdd:cd19081 1 PLGRTGLSVSPLCLGTM-VFGW--TADEETsfALLDAFVDAGGNFIDTADVYsawvpGNAGGESETIIGRWLKSRG--KR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 89 DELIISSKAGyyMWPGPYGEWGSRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVSN 168
Cdd:cd19081 76 DRVVIATKVG--FPMGPNGPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 169 YSAEQTAEISKIFQELRTP-FIIHQPRYNMFDR-WIEDGLTDVLAEEGIGTITFSPLAQGLLTNRYLHG--IPEDSRAHR 244
Cdd:cd19081 154 YSAWRLQEALELSRQHGLPrYVSLQPEYNLVDReSFEGELLPLCREEGIGVIPYSPLAGGFLTGKYRSEadLPGSTRRGE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 245 SDSPFLTEDNVQstieVVKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALDhLAFSKEELTQID 324
Cdd:cd19081 234 AAKRYLNERGLR----ILDALDEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAG-LRLTDEEVARLD 308
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
24-327 |
4.94e-71 |
|
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: 222.93 E-value: 4.94e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 24 LPAISLGLW--------HNFGDVDTLDNQRAIvRAAFDHGITHFDLANNYGppAGSAEINFGRILKEdmfpYRDELIISS 95
Cdd:cd19102 1 LTTIGLGTWaiggggwgGGWGPQDDRDSIAAI-RAALDLGINWIDTAAVYG--LGHSEEVVGRALKG----LRDRPIVAT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 96 KAGYyMW--PGPYGEWGSRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVSNYSAEQ 173
Cdd:cd19102 74 KCGL-LWdeEGRIRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 174 TAEISKIfqelrTPFIIHQPRYNMFDRWIEDGLTDVLAEEGIGTITFSPLAQGLLTNR----YLHGIPEDSRAHRsdSPF 249
Cdd:cd19102 153 MKRCQAI-----HPIASLQPPYSLLRRGIEAEILPFCAEHGIGVIVYSPMQSGLLTGKmtpeRVASLPADDWRRR--SPF 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510806721 250 LTEDNVQSTIEVVKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALDhLAFSKEELTQIDAIL 327
Cdd:cd19102 226 FQEPNLARNLALVDALRPIAERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAAD-LRLTPEELAEIEALL 302
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
14-325 |
1.01e-70 |
|
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: 222.53 E-value: 1.01e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 14 YRRLGKSGLKLPAISLGLW-----HNFGDVDTLDNQRAIvRAAFDHGITHFDLANNYGppAGSAEINFGRILKedmfPYR 88
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTWaigggPWWGGSDDNESIRTI-HAALDLGINLIDTAPAYG--FGHSEEIVGKAIK----GRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 89 DELIISSKAGYyMWPGPYGEWG------------SRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLV 156
Cdd:cd19149 74 DKVVLATKCGL-RWDREGGSFFfvrdgvtvyknlSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 157 RQGKTLYVGVSNYSAEQTAEISKIFQelrtPFIIhQPRYNMFDRWIEDGLTDVLAEEGIGTITFSPLAQGLLTNRYLHGI 236
Cdd:cd19149 153 RQGKIRAIGASNVSVEQIKEYVKAGQ----LDII-QEKYSMLDRGIEKELLPYCKKNNIAFQAYSPLEQGLLTGKITPDR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 237 PEDSRAHRSDSPFLTEDNVQSTIEVVKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALDhLAFS 316
Cdd:cd19149 228 EFDAGDARSGIPWFSPENREKVLALLEKWKPLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPEQAEENAKAGD-IRLS 306
|
....*....
gi 510806721 317 KEELTQIDA 325
Cdd:cd19149 307 AEDIATMRS 315
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
14-310 |
5.89e-68 |
|
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: 215.39 E-value: 5.89e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 14 YRRLGKSGLKLPAISLGLWHNFGDVDTLDNQRAIVRAAFDHGITHFDLANNYGppAGSAEINFGRILKEDMFpYRDELII 93
Cdd:cd19141 2 YRNLGKSGLRVSCLGLGTWVTFGSQISDEVAEELVTLAYENGINLFDTAEVYA--AGKAEIVLGKILKKKGW-RRSSYVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 94 SSKAgyyMWPG-PYGEWG-SRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVSNYSA 171
Cdd:cd19141 79 TTKI---FWGGkAETERGlSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 172 eqtAEISKIFQELRT----PFIIHQPRYNMFDR-WIEDGLTDVLAEEGIGTITFSPLAQGLLTNRYLHGIPEDSRAHRSD 246
Cdd:cd19141 156 ---MEIMEAYSVARQfnliPPIVEQAEYHLFQReKVEMQLPELFHKIGVGAMTWSPLACGILSGKYDDGVPEYSRASLKG 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 510806721 247 SPFLtEDNVQS-----TIEVVKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKAL 310
Cdd:cd19141 233 YQWL-KEKILSeegrrQQAKLKELQIIADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQAI 300
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
14-323 |
9.96e-66 |
|
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: 209.38 E-value: 9.96e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 14 YRRLGKSGLKLPAISLG---LWHNFGDVDTLDNQRAIVRAaFDHGITHFDLANNYGPpaGSAEINFGRILKEdmfpYRDE 90
Cdd:cd19076 2 TRKLGTQGLEVSALGLGcmgMSAFYGPADEEESIATLHRA-LELGVTFLDTADMYGP--GTNEELLGKALKD----RRDE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 91 LIISSKAGYYMWPGPY--GEWGSRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVSN 168
Cdd:cd19076 75 VVIATKFGIVRDPGSGfrGVDGRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLSE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 169 YSAEQtaeiskifqeLRTPFIIH-----QPRYNMFDRWIEDGLTDVLAEEGIGTITFSPLAQGLLTNRY--LHGIPEDSR 241
Cdd:cd19076 155 ASADT----------IRRAHAVHpitavQSEYSLWTRDIEDEVLPTCRELGIGFVAYSPLGRGFLTGAIksPEDLPEDDF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 242 ahRSDSPFLTEDNVQSTIEVVKQLNDIAEKRGQTLAEMALAWNLRQ-PTVtsVLI-GASRVSQLEDNLKALDhLAFSKEE 319
Cdd:cd19076 225 --RRNNPRFQGENFDKNLKLVEKLEAIAAEKGCTPAQLALAWVLAQgDDI--VPIpGTKRIKYLEENVGALD-VVLTPEE 299
|
....
gi 510806721 320 LTQI 323
Cdd:cd19076 300 LAEI 303
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
15-324 |
1.05e-63 |
|
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD), are founding members of aldo-keto reductase family 9 member A1-3 (AKR9A1-3), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis. AAD (EC1.1.1.91) is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). The AKR9B family includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381306 [Multi-domain] Cd Length: 307 Bit Score: 203.99 E-value: 1.05e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 15 RRLGKSGLKLPAISLG---LWHNFGDVDTLDNQRAIVRAAFDHGITHFDLANNYgpPAGSAEinfgRILKEDMFPYRDEL 91
Cdd:cd19080 1 RLLGRSGLRVSPLALGtmtFGTEWGWGADREEARAMFDAYVEAGGNFIDTANNY--TNGTSE----RLLGEFIAGNRDRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 92 IISSKAGYYMWPG-PYGEWGSRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVSNYS 170
Cdd:cd19080 75 VLATKYTMNRRPGdPNAGGNHRKNLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 171 AEQTAEISKIfQELR--TPFIIHQPRYNMFDRWIEDGLTDVLAEEGIGTITFSPLAQGLLTNRYlhgiPEDSRAHRSDSP 248
Cdd:cd19080 155 AWVVARANTL-AELRgwSPFVALQIEYSLLERTPERELLPMARALGLGVTPWSPLGGGLLTGKY----QRGEEGRAGEAK 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 510806721 249 FLTEDNVQST---IEVVKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALDhLAFSKEELTQID 324
Cdd:cd19080 230 GVTVGFGKLTernWAIVDVVAAVAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALD-LTLSPEQLARLD 307
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
15-326 |
1.41e-63 |
|
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: 203.80 E-value: 1.41e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 15 RRLGKSGLKLPAISLGL----WHN-FGDVDTLDNqRAIVRAAFDHGITHFDLANNYGPpaGSAEINFGRILKEDMfpyRD 89
Cdd:cd19083 2 VKLGKSDIDVNPIGLGTnavgGHNlYPNLDEEEG-KDLVREALDNGVNLLDTAFIYGL--GRSEELVGEVLKEYN---RN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 90 ELIISSKAGYYMWPGPYGEWGSRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVSNY 169
Cdd:cd19083 76 EVVIATKGAHKFGGDGSVLNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 170 SAEQTAEISKIFQelrtpFIIHQPRYNMFDRWIEDGLTDVLAEEGIGTITFSPLAQGLLTNRYLHGIPEDSRAHRSDSPF 249
Cdd:cd19083 156 SLEQLKEANKDGY-----VDVLQGEYNLLQREAEEDILPYCVENNISFIPYFPLASGLLAGKYTKDTKFPDNDLRNDKPL 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510806721 250 LTEDNVQSTIEVVKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALDhLAFSKEELTQIDAI 326
Cdd:cd19083 231 FKGERFSENLDKVDKLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKALD-VTLTEEEIAFIDAL 306
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
12-327 |
7.91e-63 |
|
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: 202.52 E-value: 7.91e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 12 MDYRRLGKSGLKLPAISLGLWHNFGDVDTLDNQRAIVRAAFDHGITHFDLANNYGppAGSAEINFGRILKEDMFpYRDEL 91
Cdd:cd19160 3 MKYRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDLLTVAYEHGVNLFDTAEVYA--AGKAERTLGNILKSKGW-RRSSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 92 IISSKAgyyMWPG-PYGEWG-SRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVSNY 169
Cdd:cd19160 80 VVTTKI---YWGGqAETERGlSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 170 SAEQTAEISKIFQELR-TPFIIHQPRYNMFDR-WIEDGLTDVLAEEGIGTITFSPLAQGLLTNRYLHGIPEDSRAHRSDS 247
Cdd:cd19160 157 SAMEIMEAYSVARQFNlIPPVCEQAEYHLFQReKVEMQLPELYHKIGVGSVTWSPLACGLITGKYDGRVPDTCRAAVKGY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 248 PFLTE----DNVQSTIEVVKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALDHLA-FSKEELTQ 322
Cdd:cd19160 237 QWLKEkvqsEEGKKQQAKVKELHPIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGSIQVLSqLTPQTVME 316
|
....*
gi 510806721 323 IDAIL 327
Cdd:cd19160 317 IDALL 321
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
21-327 |
7.25e-62 |
|
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: 199.38 E-value: 7.25e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 21 GLKLPAISLG---LWHNFGDVDTLDNQRAIVRAAFDHGITHFDLANNYGPPAGsaEINFGRILKedmfPYRDELIISSKA 97
Cdd:cd19078 1 GLEVSAIGLGcmgMSHGYGPPPDKEEMIELIRKAVELGITFFDTAEVYGPYTN--EELVGEALK----PFRDQVVIATKF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 98 GYYMWPGPYGEWG---SRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVSNYSAEQT 174
Cdd:cd19078 75 GFKIDGGKPGPLGldsRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 175 AEISKIfqelrTPFIIHQPRYNMFDRWIEDGLTDVLAEEGIGTITFSPLAQGLLTNRYLHGIPEDSRAHRSDSPFLTEDN 254
Cdd:cd19078 155 RRAHAV-----CPVTAVQSEYSMMWREPEKEVLPTLEELGIGFVPFSPLGKGFLTGKIDENTKFDEGDDRASLPRFTPEA 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510806721 255 VQSTIEVVKQLNDIAEKRGQTLAEMALAWNLRQ-PTVtsVLI-GASRVSQLEDNLKALDhLAFSKEELTQIDAIL 327
Cdd:cd19078 230 LEANQALVDLLKEFAEEKGATPAQIALAWLLAKkPWI--VPIpGTTKLSRLEENIGAAD-IELTPEELREIEDAL 301
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
12-327 |
4.27e-61 |
|
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: 197.96 E-value: 4.27e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 12 MDYRRLGKSGLKLPAISLGLWHNFGDVDTLDNQRAIVRAAFDHGITHFDLANNYGppAGSAEINFGRILKEDMFpYRDEL 91
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYA--AGKAEVILGSIIKKKGW-RRSSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 92 IISSKagyYMWPGPY-GEWG-SRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVSNY 169
Cdd:cd19159 78 VITTK---LYWGGKAeTERGlSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 170 SAEQTAEISKIFQELR-TPFIIHQPRYNMFDRW-IEDGLTDVLAEEGIGTITFSPLAQGLLTNRYLHGIPEDSRAHRSDS 247
Cdd:cd19159 155 SAMEIMEAYSVARQFNmIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 248 PFLTEDNV----QSTIEVVKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALDHL-AFSKEELTQ 322
Cdd:cd19159 235 QWLKERIVseegRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLpKMTSHVVNE 314
|
....*
gi 510806721 323 IDAIL 327
Cdd:cd19159 315 IDNIL 319
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
23-324 |
2.72e-60 |
|
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: 194.75 E-value: 2.72e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 23 KLPAISLGLWH------NFGDVDTLDNQRAIVRAAFDHGITHFDLANNYGppAGSAEINFGRILKEDmfPYRDELIISSK 96
Cdd:cd19093 1 EVSPLGLGTWQwgdrlwWGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYG--TGRSERLLGRFLKEL--GDRDEVVIATK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 97 agyyMWPGPygeW-GSRKSIIASCEQSLKRMGLDYVDIFYSHRPDP-DTPLEETALALDQLVRQGKTLYVGVSNYSAEQT 174
Cdd:cd19093 77 ----FAPLP---WrLTRRSVVKALKASLERLGLDSIDLYQLHWPGPwYSQIEALMDGLADAVEEGLVRAVGVSNYSADQL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 175 AEISKIFQELRTPFIIHQPRYNMFDRWIE-DGLTDVLAEEGIGTITFSPLAQGLLTNRYlhgiPEDSRAHRSDSPFLTED 253
Cdd:cd19093 150 RRAHKALKERGVPLASNQVEYSLLYRDPEqNGLLPACDELGITLIAYSPLAQGLLTGKY----SPENPPPGGRRRLFGRK 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510806721 254 NVQSTIEVVKQLNDIAEKRGQTLAEMALAWNLRQPTVtsVLIGASRVSQLEDNLKALDhLAFSKEELTQID 324
Cdd:cd19093 226 NLEKVQPLLDALEEIAEKYGKTPAQVALNWLIAKGVV--PIPGAKNAEQAEENAGALG-WRLSEEEVAELD 293
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
12-328 |
8.89e-60 |
|
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.
Pssm-ID: 381384 [Multi-domain] Cd Length: 324 Bit Score: 194.53 E-value: 8.89e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 12 MDYRRLGKSGLKLPAISLGLWHNFGDVDTLDNQRAIVRAAFDHGITHFDLANNYGppAGSAEINFGRILKEDMFpYRDEL 91
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYA--AGKAEVVLGNIIKKKGW-RRSSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 92 IISSKAgyyMWPGPY-GEWG-SRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVSNY 169
Cdd:cd19158 78 VITTKI---FWGGKAeTERGlSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 170 SAEQTAEISKIFQELR-TPFIIHQPRYNMFDRW-IEDGLTDVLAEEGIGTITFSPLAQGLLTNRYLHGIPEDSRAHRS-- 245
Cdd:cd19158 155 SSMEIMEAYSVARQFNlIPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKgy 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 246 ---DSPFLTEDNVQSTIEvVKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALDHL-AFSKEELT 321
Cdd:cd19158 235 qwlKDKILSEEGRRQQAK-LKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVLpKLSSSIVH 313
|
....*..
gi 510806721 322 QIDAILA 328
Cdd:cd19158 314 EIDSILG 320
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
12-327 |
2.24e-57 |
|
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: 188.44 E-value: 2.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 12 MDYRRLGKSGLKLPAISLGLWHNFGDVDTLDNQRAIVRAAFDHGITHFDLANnyGPPAGSAEINFGRILKEDMFPyRDEL 91
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGTWSTFSTAISEEQAEEIVTLAYENGINYFDTSD--AFTSGQAETELGRILKKKGWK-RSSY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 92 IISSKAgyYMWPGPYGEWGSRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVSNYSA 171
Cdd:cd19142 78 IVSTKI--YWSYGSEERGLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRWSP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 172 eqtAEISKIFQELR-----TPfIIHQPRYNMFDR-WIEDGLTDVLAEEGIGTITFSPLA------QGLLTNRYLHGIPED 239
Cdd:cd19142 156 ---VEIMEAFSIARqfncpTP-ICEQSEYHMFCReKMELYMPELYNKVGVGLITWSPLSlgldpgISEETRRLVTKLSFK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 240 SRAHRSDS-PFLTEDNVQSTIEVVKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALDHLA-FSK 317
Cdd:cd19142 232 SSKYKVGSdGNGIHEETRRASHKLRELSLIAERLGCDLTQLLIAWSLKNENVQCVLIGASSLEQLYSQLNSLQLLPkLNS 311
|
330
....*....|
gi 510806721 318 EELTQIDAIL 327
Cdd:cd19142 312 AVMEELERIL 321
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
51-326 |
7.52e-57 |
|
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: 187.00 E-value: 7.52e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 51 AFDHGITHFDLANNYGPPA-----GSAEINFGRILKEDmfPYRDELIISSK-AGY---YMWPGPYGEWGSRKSIIASCEQ 121
Cdd:cd19094 27 AFDEGVNFIDTAEMYPVPPspetqGRTEEIIGSWLKKK--GNRDKVVLATKvAGPgegITWPRGGGTRLDRENIREAVEG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 122 SLKRMGLDYVDIFYSHRPDPDTPL------------------EETALALDQLVRQGKTLYVGVSNYSAEQTAEISKIFQE 183
Cdd:cd19094 105 SLKRLGTDYIDLYQLHWPDRYTPLfgggyytepseeedsvsfEEQLEALGELVKAGKIRHIGLSNETPWGVMKFLELAEQ 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 184 LRTPFIIH-QPRYNMFDRWIEDGLTDVLAEEGIGTITFSPLAQGLLTNRYLHGIPEDSRAHRSDSP-FLTEDNVQSTIEV 261
Cdd:cd19094 185 LGLPRIVSiQNPYSLLNRNFEEGLAEACHRENVGLLAYSPLAGGVLTGKYLDGAARPEGGRLNLFPgYMARYRSPQALEA 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510806721 262 VKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALDhLAFSKEELTQIDAI 326
Cdd:cd19094 265 VAEYVKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLKENIDAFD-VPLSDELLAEIDAV 328
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
21-324 |
1.14e-56 |
|
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: 184.74 E-value: 1.14e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 21 GLKLPAISLGLW----HNFGDVDTLDNQRAIVRAAFDHGITHFDLANNYGppAGSAEINFGRILKEdmFPyRDELIISSK 96
Cdd:cd19072 1 GEEVPVLGLGTWgiggGMSKDYSDDKKAIEALRYAIELGINLIDTAEMYG--GGHAEELVGKAIKG--FD-REDLFITTK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 97 AgyymWPgpygEWGSRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVSNYSAEQTAE 176
Cdd:cd19072 76 V----SP----DHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 177 ISKIFQelRTPFIIHQPRYNMFDRWIEDGLTDVLAEEGIGTITFSPLAQGLLTNRYLHGIpedsrahrsdspfltednvq 256
Cdd:cd19072 148 AQSYLK--KGPIVANQVEYNLFDREEESGLLPYCQKNGIAIIAYSPLEKGKLSNAKGSPL-------------------- 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510806721 257 stievvkqLNDIAEKRGQTLAEMALAWNLRQPTVTsVLIGASRVSQLEDNLKALDhLAFSKEELTQID 324
Cdd:cd19072 206 --------LDEIAKKYGKTPAQIALNWLISKPNVI-AIPKASNIEHLEENAGALG-WELSEEDLQRLD 263
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
25-326 |
2.18e-55 |
|
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: 182.76 E-value: 2.18e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 25 PAISLG--LWHNFGDVDTLDNQRAIVRAAFDHGITHFDLANNYGPpaGSAEINFGRILKEDmfpyrDELIISSKAgyYMW 102
Cdd:cd19075 1 PKIILGtmTFGSQGRFTTAEAAAELLDAFLERGHTEIDTARVYPD--GTSEELLGELGLGE-----RGFKIDTKA--NPG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 103 PGPygeWGSRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVSNYSAEQTAEISKIFQ 182
Cdd:cd19075 72 VGG---GLSPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 183 E----LRTpfiIHQPRYNMFDRWIEDGLTDVLAEEGIGTITFSPLAQGLLTNRYlHGIPEDSRAHRSDSPFLTEDNVQ-- 256
Cdd:cd19075 149 EngwvLPT---VYQGMYNAITRQVETELFPCLRKLGIRFYAYSPLAGGFLTGKY-KYSEDKAGGGRFDPNNALGKLYRdr 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 510806721 257 ----STIEVVKQLNDIAEKRGQTLAEMALAW-----NLRQPTVTSVLIGASRVSQLEDNLKALDHLAFSKEELTQIDAI 326
Cdd:cd19075 225 ywkpSYFEALEKVEEAAEKEGISLAEAALRWlyhhsALDGEKGDGVILGASSLEQLEENLAALEKGPLPEEVVKAIDEA 303
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
19-323 |
7.01e-54 |
|
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: 178.13 E-value: 7.01e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 19 KSGLKLPAISLGLWHNFGDVDTLDNQRAIVRAAFDHGITHFDLANNYGppAGSAEINFGRILKEDmfP-YRDELIISSKA 97
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADWGESAEELLSLIEAALELGITTFDHADIYG--GGKCEELFGEALALN--PgLREKIEIQTKC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 98 GYYMWPGPYGEWG-----SRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVSNYSAE 172
Cdd:cd19092 77 GIRLGDDPRPGRIkhydtSKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFTPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 173 QTAEISKifqELRTPFIIHQPRYNMFDR-WIEDGLTDVLAEEGIGTITFSPLAQGlltnrylhgipedsrahrsdspFLT 251
Cdd:cd19092 157 QIELLQS---YLDQPLVTNQIELSLLHTeAIDDGTLDYCQLLDITPMAWSPLGGG----------------------RLF 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 510806721 252 EDNVQSTIEVVKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALDhLAFSKEELTQI 323
Cdd:cd19092 212 GGFDERFQRLRAALEELAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALD-IELTREEWYEI 282
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
12-319 |
2.46e-53 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 177.27 E-value: 2.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 12 MDYRRLGKSGLKLPAISLGLWHnFGDVDTLDNQ-RAIVRAAFDHGITHFDLANNYGppAGSAEINFGRILKEDMFPyRDE 90
Cdd:COG4989 1 MKRIKLGASGLSVSRIVLGCMR-LGEWDLSPAEaAALIEAALELGITTFDHADIYG--GYTCEALFGEALKLSPSL-REK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 91 LIISSKAGYYMWPGPYGEWG-----SRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVG 165
Cdd:COG4989 77 IELQTKCGIRLPSEARDNRVkhydtSKEHIIASVEGSLRRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELKASGKVRHFG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 166 VSNYSAEQTAEISKifqELRTPFIIHQPRYNMFDR-WIEDGLTDVLAEEGIGTITFSPLAQGLltnrylhgipedsrahr 244
Cdd:COG4989 157 VSNFTPSQFELLQS---ALDQPLVTNQIELSLLHTdAFDDGTLDYCQLNGITPMAWSPLAGGR----------------- 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510806721 245 sdspFLTEDNVQsTIEVVKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALDhLAFSKEE 319
Cdd:COG4989 217 ----LFGGFDEQ-FPRLRAALDELAEKYGVSPEAIALAWLLRHPAGIQPVIGTTNPERIKAAAAALD-IELTREE 285
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
22-309 |
3.48e-52 |
|
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: 172.28 E-value: 3.48e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 22 LKLPAISLGLW----HNFGDVDTlDNQRAIVRAAFDHGITHFDLANNYGppAGSAEINFGRILKEDmfpyRDELIISSKA 97
Cdd:cd19086 1 LEVSEIGFGTWglggDWWGDVDD-AEAIRALRAALDLGINFFDTADVYG--DGHSERLLGKALKGR----RDKVVIATKF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 98 GYYMWPGPYGEWG-SRKSIIASCEQSLKRMGLDYVDIFYSHRPDPD-TPLEETALALDQLVRQGKTLYVGVSNYSAEQTA 175
Cdd:cd19086 74 GNRFDGGPERPQDfSPEYIREAVEASLKRLGTDYIDLYQLHNPPDEvLDNDELFEALEKLKQEGKIRAYGVSVGDPEEAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 176 EIskifqeLRTPFI--IhQPRYNMFDRWIEDGLTDVLAEEGIGTITFSPLAQGLLTNRylhgipedsrahrsdspflted 253
Cdd:cd19086 154 AA------LRRGGIdvV-QVIYNLLDQRPEEELFPLAEEHGVGVIARVPLASGLLTGK---------------------- 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 510806721 254 nvqstievvkqlndiaekrgqtLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKA 309
Cdd:cd19086 205 ----------------------LAQAALRFILSHPAVSTVIPGARSPEQVEENAAA 238
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
21-327 |
4.95e-52 |
|
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: 174.03 E-value: 4.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 21 GLKLPAISLGLWHNFGDV-DTLDNQRAI--VRAAFDHGITHFDLANNYGppAGSAEINFGRILKEdmFPYRDELIISSKA 97
Cdd:cd19148 1 DLPVSRIALGTWAIGGWMwGGTDEKEAIetIHKALDLGINLIDTAPVYG--FGLSEEIVGKALKE--YGKRDRVVIATKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 98 GYyMWP--GPYGEWGSRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVSNYSAEQTA 175
Cdd:cd19148 77 GL-EWDegGEVVRNSSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSPEQME 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 176 EISKIfqelrTPFIIHQPRYNMFDRWIEDgltDVLA---EEGIGTITFSPLAQGLLTNRYLHGIPEDSRAHRSDSPFLTE 252
Cdd:cd19148 156 TFRKV-----APLHTVQPPYNLFEREIEK---DVLPyarKHNIVTLAYGALCRGLLSGKMTKDTKFEGDDLRRTDPKFQE 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510806721 253 DNVQSTIEVVKQLNDIAEKR-GQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDnLKALDHLAFSKEELTQIDAIL 327
Cdd:cd19148 228 PRFSQYLAAVEELDKLAQERyGKSVIHLAVRWLLDQPGVSIALWGARKPEQLDA-VDEVFGWSLNDEDMKEIDAIL 302
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
15-311 |
1.72e-50 |
|
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: 168.55 E-value: 1.72e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 15 RRLGKSGLKLPAisLGLWhnfGDVDTLDNQRAIVRAAFDHGITHFDLANNYGPpaGSAEinfgRILKEDMFPYRDELIIS 94
Cdd:cd19088 2 SRLGYGAMRLTG--PGIW---GPPADREEAIAVLRRALELGVNFIDTADSYGP--DVNE----RLIAEALHPYPDDVVIA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 95 SKAGyymW--PGPyGEW---GSRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVSNY 169
Cdd:cd19088 71 TKGG---LvrTGP-GWWgpdGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 170 SAEQTAEISKIFqelrtPFIIHQPRYNMFDRwIEDGLTDVLAEEGIGTITFSPLAQGLLTnrylhgipEDSRAHRSdspf 249
Cdd:cd19088 147 TVAQIEEARAIV-----RIVSVQNRYNLANR-DDEGVLDYCEAAGIAFIPWFPLGGGDLA--------QPGGLLAE---- 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 510806721 250 ltednvqstievvkqlndIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALD 311
Cdd:cd19088 209 ------------------VAARLGATPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAAAG 252
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
15-329 |
2.11e-49 |
|
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: 167.62 E-value: 2.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 15 RRLGKSGLKLPAI---SLGLWHNFGDVDTlDNQR-AIVRAAFDHGITHFDLANNYGPpagSAEInFGRILKEDMfPYRDE 90
Cdd:cd19144 4 RTLGRNGPSVPALgfgAMGLSAFYGPPKP-DEERfAVLDAAFELGCTFWDTADIYGD---SEEL-IGRWFKQNP-GKREK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 91 LIISSKAGYYMwPGPYGEW---GSRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVS 167
Cdd:cd19144 78 IFLATKFGIEK-NVETGEYsvdGSPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 168 NYSAEQtaeiskifqeLRTPFIIH-----QPRYNMFDRWIED---GLTDVLAEEGIGTITFSPLAQGLLTNRYLHgiPED 239
Cdd:cd19144 157 ECSAET----------LRRAHAVHpiaavQIEYSPFSLDIERpeiGVLDTCRELGVAIVAYSPLGRGFLTGAIRS--PDD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 240 SRAH--RSDSPFLTEDNVQSTIEVVKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALdHLAFSK 317
Cdd:cd19144 225 FEEGdfRRMAPRFQAENFPKNLELVDKIKAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLGAL-KVKLTE 303
|
330
....*....|..
gi 510806721 318 EELTQIDAILAK 329
Cdd:cd19144 304 EEEKEIREIAEE 315
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
34-311 |
2.88e-49 |
|
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: 166.19 E-value: 2.88e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 34 NFGDVDTLDNQRAIVRAAFDHGITHFDLANNYG--PPAGSAEINFGRILKEDmfPYRDELIISSKAGYYMWPGPYGEWGS 111
Cdd:cd19082 9 DFGTRIDEEEAFALLDAFVELGGNFIDTARVYGdwVERGASERVIGEWLKSR--GNRDKVVIATKGGHPDLEDMSRSRLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 112 RKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVSNYSAEQTAEISKIFQEL-RTPFII 190
Cdd:cd19082 87 PEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNWSTERIAEANAYAKAHgLPGFAA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 191 HQPRYNMF----DRWIEDGLTDV-------LAEEGIGTITFSPLAQGLLTNRYLHGIPEDSRAHRsdsPFLTEDNVQsTI 259
Cdd:cd19082 167 SSPQWSLArpnePPWPGPTLVAMdeemrawHEENQLPVFAYSSQARGFFSKRAAGGAEDDSELRR---VYYSEENFE-RL 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 510806721 260 EVVKQLndiAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALD 311
Cdd:cd19082 243 ERAKEL---AEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAAAD 291
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
12-312 |
5.97e-49 |
|
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: 165.42 E-value: 5.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 12 MDYRRLGKSGLKLPAISLG---LWHNFGDVDTlDNQRAIVRAAFDHGITHFDLANNYGppAGSAEINFGRILKEdmFPyR 88
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGaspLGGVFGPVDE-EEAIRTVHEALDSGINYIDTAPWYG--QGRSETVLGKALKG--IP-R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 89 DELIISSKAGYYMwPGPYGEWG-SRKSIIASCEQSLKRMGLDYVDIFYSH----RPDPDTPLEETALALDQLVRQGKTLY 163
Cdd:cd19163 75 DSYYLATKVGRYG-LDPDKMFDfSAERITKSVEESLKRLGLDYIDIIQVHdiefAPSLDQILNETLPALQKLKEEGKVRF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 164 VGVSNYSAeqtaeisKIFQEL--RTP----FIIHQPRYNMFDRWIEDgLTDVLAEEGIGTITFSPLAQGLLTNRylhGIP 237
Cdd:cd19163 154 IGITGYPL-------DVLKEVleRSPvkidTVLSYCHYTLNDTSLLE-LLPFFKEKGVGVINASPLSMGLLTER---GPP 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510806721 238 EDSRAHrsdspfltednvQSTIEVVKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALDH 312
Cdd:cd19163 223 DWHPAS------------PEIKEACAKAAAYCKSRGVDISKLALQFALSNPDIATTLVGTASPENLRKNLEAAEE 285
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
20-324 |
1.18e-48 |
|
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: 163.96 E-value: 1.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 20 SGLKLPAISLGLWHNFGDVDTLDNQRAIVRAAFDHGITHFDLANNYGppAGSAEinfgRILKEDMFPYRDELIISSKagy 99
Cdd:cd19138 7 DGTKVPALGQGTWYMGEDPAKRAQEIEALRAGIDLGMTLIDTAEMYG--DGGSE----ELVGEAIRGRRDKVFLVSK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 100 yMWPGPygewGSRKSIIASCEQSLKRMGLDYVDIFYSHRPDpDTPLEETALALDQLVRQGKTLYVGVSNYSAEQtaeisk 179
Cdd:cd19138 78 -VLPSN----ASRQGTVRACERSLRRLGTDYLDLYLLHWRG-GVPLAETVAAMEELKKEGKIRAWGVSNFDTDD------ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 180 iFQEL-RTPFIIH----QPRYNMFDRWIEDGLTDVLAEEGIGTITFSPLAQGLLTNRYLHGIPEdsrahrsdspfltedn 254
Cdd:cd19138 146 -MEELwAVPGGGNcaanQVLYNLGSRGIEYDLLPWCREHGVPVMAYSPLAQGGLLRRGLLENPT---------------- 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 255 vqstievvkqLNDIAEKRGQTLAEMALAWNLRQPTVTSVlIGASRVSQLEDNLKALDhLAFSKEELTQID 324
Cdd:cd19138 209 ----------LKEIAARHGATPAQVALAWVLRDGNVIAI-PKSGSPEHARENAAAAD-LELTEEDLAELD 266
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
25-309 |
3.09e-46 |
|
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH) and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. The family also includes L-galactose dehydrogenase (L-galDH) and D-arabinose 1-dehydrogenase (ARA2). L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381316 [Multi-domain] Cd Length: 278 Bit Score: 158.10 E-value: 3.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 25 PAISLG---LWHNFGDVDtLDNQRAIVRAAFDHGITHFDLANNYGppaGSAEInFGRILKEdmfPYRDELIISSKAGYYM 101
Cdd:cd19090 1 SALGLGtagLGGVFGGVD-DDEAVATIRAALDLGINYIDTAPAYG---DSEER-LGLALAE---LPREPLVLSTKVGRLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 102 -WPGPYgewgSRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETAL--ALDQLVR---QGKTLYVGVSNYSAEqta 175
Cdd:cd19090 73 eDTADY----SADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILAPggALEALLElkeEGLIKHIGLGGGPPD--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 176 EISKIFQELRTPFIIHQPRYNMFDRWIEDGLTDVLAEEGIGTITFSPLAQGLLTNRYlhgipeDSRAHRSDSPFLTEDNV 255
Cdd:cd19090 146 LLRRAIETGDFDVVLTANRYTLLDQSAADELLPAAARHGVGVINASPLGMGLLAGRP------PERVRYTYRWLSPELLD 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 510806721 256 QstievVKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKA 309
Cdd:cd19090 220 R-----AKRLYELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAA 268
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
20-326 |
2.09e-45 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 155.21 E-value: 2.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 20 SGLKLPAISLGLWHNfGDVDTldnqRAIVRAAFDHGITHFDLANNYGppagsAEINFGRILKEDMFPyRDELIISSKagy 99
Cdd:COG0656 1 NGVEIPALGLGTWQL-PGEEA----AAAVRTALEAGYRHIDTAAMYG-----NEEGVGEAIAASGVP-REELFVTTK--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 100 yMWPGPYGewgsRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDtPLEETALALDQLVRQGKTLYVGVSNYSAEQTAEisk 179
Cdd:COG0656 67 -VWNDNHG----YDDTLAAFEESLERLGLDYLDLYLIHWPGPG-PYVETWRALEELYEEGLIRAIGVSNFDPEHLEE--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 180 IFQELRTPFIIHQPRYNMFDRwiEDGLTDVLAEEGIGTITFSPLAQG-LLTNrylhgipedsrahrsdspfltednvqst 258
Cdd:COG0656 138 LLAETGVKPAVNQVELHPYLQ--QRELLAFCREHGIVVEAYSPLGRGkLLDD---------------------------- 187
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510806721 259 iEVVKqlnDIAEKRGQTLAEMALAWNLRQPTVtsVLIGASRVSQLEDNLKALDhLAFSKEELTQIDAI 326
Cdd:COG0656 188 -PVLA---EIAEKHGKTPAQVVLRWHLQRGVV--VIPKSVTPERIRENLDAFD-FELSDEDMAAIDAL 248
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
25-309 |
2.24e-45 |
|
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: 155.09 E-value: 2.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 25 PAISLGLWHNFGD--VDTLDNQRAIVRAAFDHGITHFDLANNYGppagSAEINFGRILKEDMfpyRDELIISSKAGY-YM 101
Cdd:cd19095 1 SVLGLGTSGIGRVwgVPSEAEAARLLNTALDLGINLIDTAPAYG----RSEERLGRALAGLR---RDDLFIATKVGThGE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 102 WPGPYGEWgSRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVSNYsaeqTAEISKIF 181
Cdd:cd19095 74 GGRDRKDF-SPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVSGD----GEELEAAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 182 QELRTPFIihQPRYNMFDRWIEDGLtDVLAEEGIGTITFSPLAQGLLTNRYLHgipedsrahrsdspfltednVQSTIEV 261
Cdd:cd19095 149 ASGVFDVV--QLPYNVLDREEEELL-PLAAEAGLGVIVNRPLANGRLRRRVRR--------------------RPLYADY 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 510806721 262 VKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKA 309
Cdd:cd19095 206 ARRPEFAAEIGGATWAQAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
46-324 |
7.59e-45 |
|
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: 155.09 E-value: 7.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 46 AIVRAAFDHGITHFDLANNYGPPAGSAEInfgRILKE--DMFP-YRDELIISSKAGyyMWPGPYGEWGSRKSIIASCEQS 122
Cdd:cd19077 29 ETMKAALDAGSNLWNGGEFYGPPDPHANL---KLLARffRKYPeYADKVVLSVKGG--LDPDTLRPDGSPEAVRKSIENI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 123 LKRMG-LDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVSNYSAEQTAEISKIFqelrtPFIIHQPRYNMFDRW 201
Cdd:cd19077 104 LRALGgTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAETIRRAHAVH-----PIAAVEVEYSLFSRE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 202 IED-GLTDVLAEEGIGTITFSPLAQGLLTNRY--LHGIPEDsrAHRSDSPFLTEDNVQSTIEVVKQLNDIAEKRGQTLAE 278
Cdd:cd19077 179 IEEnGVLETCAELGIPIIAYSPLGRGLLTGRIksLADIPEG--DFRRHLDRFNGENFEKNLKLVDALQELAEKKGCTPAQ 256
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 510806721 279 MALAWNLRQPTVTSVLI-GASRVSQLEDNLKALDhLAFSKEELTQID 324
Cdd:cd19077 257 LALAWILAQSGPKIIPIpGSTTLERVEENLKAAN-VELTDEELKEIN 302
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
12-310 |
4.55e-43 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 148.89 E-value: 4.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 12 MDYRRLGKSGLKLPAISLGlwhnfGDVDTLDNQrAIVRAAFDHGITHFDLANNYGppAGSAEINFGRILKEDMfpyRDEL 91
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFG-----GGGLPRESP-ELLRRALDLGINYFDTAEGYG--NGNSEEIIGEALKGLR---RDKV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 92 IISSKAGyymwpgPYGEWGSRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPL---EETALALDQLVRQGKTLYVGVSN 168
Cdd:cd19105 70 FLATKAS------PRLDKKDKAELLKSVEESLKRLQTDYIDIYQLHGVDTPEERllnEELLEALEKLKKEGKVRFIGFST 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 169 YSAEQtaeisKIFQEL-RTPFI-IHQPRYN-MFDRWIEDGLTDVLAEEGIGTITFSPLAQGLLtnrylhgipedsraHRS 245
Cdd:cd19105 144 HDNMA-----EVLQAAiESGWFdVIMVAYNfLNQPAELEEALAAAAEKGIGVVAMKTLAGGYL--------------QPA 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510806721 246 DSPFLtednvqstievvkqlndiaEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKAL 310
Cdd:cd19105 205 LLSVL-------------------KAKGFSLPQAALKWVLSNPRVDTVVPGMRNFAELEENLAAA 250
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
15-323 |
5.43e-43 |
|
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: 150.28 E-value: 5.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 15 RRLGKSGLKLPAISLG---LWHNFGDVDTLDNQRAIVRAAFDHGITHFDLANNYGPPAGsaEINFGRILKEDMfpyRDEL 91
Cdd:cd19145 3 VKLGSQGLEVSAQGLGcmgLSGDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYGPNTN--EVLLGKALKDGP---REKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 92 IISSKAG-YYMWPGPYGEWGSRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVSNYS 170
Cdd:cd19145 78 QLATKFGiHEIGGSGVEVRGDPAYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSEAS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 171 AEqtaeiskifqELRTPFIIH-----QPRYNMFDRWIEDGLTDVLAEEGIGTITFSPLAQGLLTNR-YLHGIPEDSrAHR 244
Cdd:cd19145 158 AD----------TIRRAHAVHpitavQLEWSLWTRDIEEEIIPTCRELGIGIVPYSPLGRGFFAGKaKLEELLENS-DVR 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 510806721 245 SDSPFLTEDNVQSTIEVVKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALDhLAFSKEELTQI 323
Cdd:cd19145 227 KSHPRFQGENLEKNKVLYERVEALAKKKGCTPAQLALAWVLHQGEDVVPIPGTTKIKNLNQNIGALS-VKLTKEDLKEI 304
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
12-333 |
6.95e-43 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 151.51 E-value: 6.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 12 MDYRRLGKSGLKLPAISLGLWHnFGDVDTlDNQRAIVRAAFDHGITHFDLANNYGppaGSaEINFGRILKEdmfpYRDEL 91
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGMR-LPRKDE-EEAEALIRRAIDNGINYIDTARGYG---DS-EEFLGKALKG----PRDKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 92 IISSKAGYYMWpgpygewgSRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETAL------ALDQLVRQGKTLYVG 165
Cdd:COG1453 71 ILATKLPPWVR--------DPEDMRKDLEESLKRLQTDYIDLYLIHGLNTEEDLEKVLKpggaleALEKAKAEGKIRHIG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 166 VSNYSAEQtaeiskIFQE-LRTPFI----IHqprYNMFDRWIEDG--LTDVLAEEGIGTITFSPLAQGLLTNrylhgIPE 238
Cdd:COG1453 143 FSTHGSLE------VIKEaIDTGDFdfvqLQ---YNYLDQDNQAGeeALEAAAEKGIGVIIMKPLKGGRLAN-----PPE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 239 DsrahrsdspfltednvqstievvkqLNDIAEKrGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALDHL-AFSK 317
Cdd:COG1453 209 K-------------------------LVELLCP-PLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENLKTADNLePLTE 262
|
330
....*....|....*.
gi 510806721 318 EELTQIDAILAKLTKK 333
Cdd:COG1453 263 EELAILERLAEELGEL 278
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-326 |
7.30e-43 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 150.49 E-value: 7.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 13 DYRRLGKSGLKLPAISLG------LWHNfgdvDTLDNQRAIVRAAFDHGITHFDLANNYGppAGSAEINFGRILKEDmfp 86
Cdd:cd19104 1 KYRRFGRTGLKVSELTFGgggiggLMGR----TTREEQIAAVRRALDLGINFFDTAPSYG--DGKSEENLGRALKGL--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 87 yRDELIISSKAGyyMWPGPYGEWGSRksIIASCEQSLKRMGLDYVDIFYSH-RPDPDTP--------------LEETALA 151
Cdd:cd19104 72 -PAGPYITTKVR--LDPDDLGDIGGQ--IERSVEKSLKRLKRDSVDLLQLHnRIGDERDkpvggtlsttdvlgLGGVADA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 152 LDQLVRQGKTLYVG---VSNYSAEQTAEISKIFQELR--------TPFIIHQPRYNMFDrwiEDGLTDVLAEEGIGTITF 220
Cdd:cd19104 147 FERLRSEGKIRFIGitgLGNPPAIRELLDSGKFDAVQvyynllnpSAAEARPRGWSAQD---YGGIIDAAAEHGVGVMGI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 221 SPLAQGLLTNRYLHGIPEDsraHRSDSPFLTEdnvqstIEVVKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRV 300
Cdd:cd19104 224 RVLAAGALTTSLDRGREAP---PTSDSDVAID------FRRAAAFRALAREWGETLAQLAHRFALSNPGVSTVLVGVKNR 294
|
330 340
....*....|....*....|....*.
gi 510806721 301 SQLEDNLKALDHLAFSKEELTQIDAI 326
Cdd:cd19104 295 EELEEAVAAEAAGPLPAENLARLEAL 320
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
25-311 |
5.57e-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: 381391 [Multi-domain] Cd Length: 291 Bit Score: 147.48 E-value: 5.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 25 PAISLGLWhNFGDVDTLDNQRAIVRAAFDHGITHFDLANNY-----GPPAGSAEINFGRILKEDmfPYRDELIISSKAGY 99
Cdd:cd19752 1 SELCLGTM-YFGTRTDEETSFAILDRYVAAGGNFLDTANNYafwteGGVGGESERLIGRWLKDR--GNRDDVVIATKVGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 100 yMWPGPYG-----EWGSRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVSNYSAEQT 174
Cdd:cd19752 78 -GPRDPDGgpespEGLSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 175 AEISKIF-QELRTPFIIHQPRYNMF----------DRWIEDGLTDVLAEEGIGTI-TFSPLAQGLLTNrylhgipeDSRA 242
Cdd:cd19752 157 ERARQIArQQGWAEFSAIQQRHSYLrprpgadfgvQRIVTDELLDYASSRPDLTLlAYSPLLSGAYTR--------PDRP 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 510806721 243 HRsdSPFLTEDNvQSTIEVvkqLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALD 311
Cdd:cd19752 229 LP--EQYDGPDS-DARLAV---LEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAALD 291
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
21-324 |
7.13e-42 |
|
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: 146.18 E-value: 7.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 21 GLKLPAISLGLWhNFGDVDTLDNQR-----AIVRAAFDHGITHFDLANNYGppAGSAEINFGRILKEdmFPyRDELIISS 95
Cdd:cd19137 1 GEKIPALGLGTW-GIGGFLTPDYSRdeemvELLKTAIELGYTHIDTAEMYG--GGHTEELVGKAIKD--FP-REDLFIVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 96 KagyyMWPgpygEWGSRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVSNYSAEQTA 175
Cdd:cd19137 75 K----VWP----TNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 176 EISKIfqeLRTPFIIHQPRYNMFDR-WIEDGLTDVLAEEGIGTITFSPLAQGLLtnrylhgipedsrahrsdspfLTEDN 254
Cdd:cd19137 147 EAISK---SQTPIVCNQVKYNLEDRdPERDGLLEYCQKNGITVVAYSPLRRGLE---------------------KTNRT 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 255 VQstievvkqlnDIAEKRGQTLAEMALAWNLRQPTVTSVLIgASRVSQLEDNLKALDhLAFSKEELTQID 324
Cdd:cd19137 203 LE----------EIAKNYGKTIAQIALAWLIQKPNVVAIPK-AGRVEHLKENLKATE-IKLSEEEMKLLD 260
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-308 |
3.61e-39 |
|
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: 138.38 E-value: 3.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 14 YRRLGKSGLKLPAISLGLWHNFGDvdTLDNQRAIVRAAFDHGITHFDLANNYgppaGSAEINFGRILKedmfPYRDELII 93
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPLGRL--SQEEAAAIIRRALDLGINYFDTAPSY----GDSEEKIGKALK----GRRDKVFL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 94 SSKAGYYMWPgpygewGSRKSIiascEQSLKRMGLDYVDIFYSH----RPDPDTPLEET-AL-ALDQLVRQGKTLYVGVS 167
Cdd:cd19100 71 ATKTGARDYE------GAKRDL----ERSLKRLGTDYIDLYQLHavdtEEDLDQVFGPGgALeALLEAKEEGKIRFIGIS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 168 NYSAEQTAEISKIFqelrtPFIIHQPRYNMFDRWIEDGLTDVL---AEEGIGTITFSPLAQGLLTNrylhgipedsrahr 244
Cdd:cd19100 141 GHSPEVLLRALETG-----EFDVVLFPINPAGDHIDSFREELLplaREKGVGVIAMKVLAGGRLLS-------------- 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510806721 245 sdspfltednvqstievvkqlndiaekRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLK 308
Cdd:cd19100 202 ---------------------------GDPLDPEQALRYALSLPPVDVVIVGMDSPEELDENLA 238
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
14-328 |
3.98e-39 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 140.68 E-value: 3.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 14 YRRLGKSGLKLPAISLG---LWHNFGDVDTlDNQRAIVRAAFDHGITHFDLANNYGppAGSAEINFGRILKEDMFPyRDE 90
Cdd:PLN02587 1 LRELGSTGLKVSSVGFGaspLGSVFGPVSE-EDAIASVREAFRLGINFFDTSPYYG--GTLSEKVLGKALKALGIP-REK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 91 LIISSKAGYYMwpgpYGEWGSRKSIIASCEQSLKRMGLDYVDIFYSHR---PDPDTPLEETALALDQLVRQGKTLYVGVS 167
Cdd:PLN02587 77 YVVSTKCGRYG----EGFDFSAERVTKSVDESLARLQLDYVDILHCHDiefGSLDQIVNETIPALQKLKESGKVRFIGIT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 168 NYSAEqtaeiskIFQEL--RTP-----FIIHQPRYNMFDRWIEDgLTDVLAEEGIGTITFSPLAQGLLTNRylhGIPEDS 240
Cdd:PLN02587 153 GLPLA-------IFTYVldRVPpgtvdVILSYCHYSLNDSSLED-LLPYLKSKGVGVISASPLAMGLLTEN---GPPEWH 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 241 RAhrsdSPFLTEdnvqstieVVKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALDHLAFS---K 317
Cdd:PLN02587 222 PA----PPELKS--------ACAAAATHCKEKGKNISKLALQYSLSNKDISTTLVGMNSVQQVEENVAAATELETSgidE 289
|
330
....*....|.
gi 510806721 318 EELTQIDAILA 328
Cdd:PLN02587 290 ELLSEVEAILA 300
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
22-311 |
3.98e-38 |
|
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: 137.11 E-value: 3.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 22 LKLPAISLGLWHNFGDvdtlDNQRAIVRAAFDHGITHFDLANNYGppAGSAEINFGRILKEDMfpyRDELIISSKAGYYM 101
Cdd:cd19162 3 LGLGAASLGNLARAGE----DEAAATLDAAWDAGIRYFDTAPLYG--LGLSERRLGAALARHP---RAEYVVSTKVGRLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 102 WPGPYG-------EWG-SRKSIIASCEQSLKRMGLDYVDIFYSHRPDP--DTPLEETALALDQLVRQGKTLYVGVSNYSA 171
Cdd:cd19162 74 EPGAAGrpagadrRFDfSADGIRRSIEASLERLGLDRLDLVFLHDPDRhlLQALTDAFPALEELRAEGVVGAIGVGVTDW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 172 EQTAEISKIFqelRTPFIIHQPRYNMFDRWIEDGLTDVLAEEGIGTITFSPLAQGLL------TNRYLHG-IPEDSRAHr 244
Cdd:cd19162 154 AALLRAARRA---DVDVVMVAGRYTLLDRRAATELLPLCAAKGVAVVAAGVFNSGILatddpaGDRYDYRpATPEVLAR- 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510806721 245 sdspfltednvqstievVKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALD 311
Cdd:cd19162 230 -----------------ARRLAAVCRRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLALLR 279
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
46-327 |
4.48e-38 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 137.34 E-value: 4.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 46 AIVRAAFDH---GITHFDLANNYGPpagsAEINFGRILKE--DMFPYRDELIISSKagyymW-PGPYGEWGSRKSIIASC 119
Cdd:cd19101 24 AAVRAMAAYvdaGLTTFDCADIYGP----AEELIGEFRKRlrRERDAADDVQIHTK-----WvPDPGELTMTRAYVEAAI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 120 EQSLKRMGLDYVDIFYSHRPDPDTP-LEETALALDQLVRQGKTLYVGVSNYSAEQTAEISkifqELRTPFIIHQPRYNMF 198
Cdd:cd19101 95 DRSLKRLGVDRLDLVQFHWWDYSDPgYLDAAKHLAELQEEGKIRHLGLTNFDTERLREIL----DAGVPIVSNQVQYSLL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 199 DRWIEDGLTDVLAEEGIGTITFSPLAQGLLTNRYLhGIPE------DSRAHRSDSPFLTE----DNVQstiEVVKQLNDI 268
Cdd:cd19101 171 DRRPENGMAALCEDHGIKLLAYGTLAGGLLSEKYL-GVPEptgpalETRSLQKYKLMIDEwggwDLFQ---ELLRTLKAI 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 510806721 269 AEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALDhLAFSKEELTQIDAIL 327
Cdd:cd19101 247 ADKHGVSIANVAVRWVLDQPGVAGVIVGARNSEHIDDNVRAFS-FRLDDEDRAAIDAVL 304
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
21-326 |
1.91e-36 |
|
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381366 [Multi-domain] Cd Length: 253 Bit Score: 131.61 E-value: 1.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 21 GLKLPAISLGLWHNFGDvdtldNQRAIVRAAFDHGITHFDLANNYGppagsAEINFGRILKEDMFPyRDELIISSKagyy 100
Cdd:cd19140 5 GVRIPALGLGTYPLTGE-----ECTRAVEHALELGYRHIDTAQMYG-----NEAQVGEAIAASGVP-RDELFLTTK---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 101 MWPGPYgewgSRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVSNYSAEQTAEISKI 180
Cdd:cd19140 70 VWPDNY----SPDDFLASVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 181 fqeLRTPFIIHQPRYNMFDRwiEDGLTDVLAEEGIGTITFSPLAQGLLTNRYLhgipedsrahrsdspfltednvqstie 260
Cdd:cd19140 146 ---SEAPLFTNQVEYHPYLD--QRKLLDAAREHGIALTAYSPLARGEVLKDPV--------------------------- 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510806721 261 vvkqLNDIAEKRGQTLAEMALAWNLRQPTVtSVLIGASRVSQLEDNLKALDhLAFSKEELTQIDAI 326
Cdd:cd19140 194 ----LQEIGRKHGKTPAQVALRWLLQQEGV-AAIPKATNPERLEENLDIFD-FTLSDEEMARIAAL 253
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
12-331 |
8.17e-36 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 132.67 E-value: 8.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 12 MDYRRLGKSGLKLPAISLGLWhNFGDVDTLDNQRAIVRAAFDHGITHFDLANNYG-PP----AGSAEINFGRILKEDmfP 86
Cdd:PRK10625 1 MQYHRIPHSSLEVSTLGLGTM-TFGEQNSEADAHAQLDYAVAQGINLIDVAEMYPvPPrpetQGLTETYIGNWLAKR--G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 87 YRDELIISSKAGyymwpGPYGEWGS---------RKSIIASCEQSLKRMGLDYVDIFYSHRPD----------------- 140
Cdd:PRK10625 78 SREKLIIASKVS-----GPSRNNDKgirpnqaldRKNIREALHDSLKRLQTDYLDLYQVHWPQrptncfgklgyswtdsa 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 141 PDTPLEETALALDQLVRQGKTLYVGVSNYSAEQTAEISKIFQELRTPFIIH-QPRYNMFDRWIEDGLTDVLAEEGIGTIT 219
Cdd:PRK10625 153 PAVSLLETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEKHDLPRIVTiQNPYSLLNRSFEVGLAEVSQYEGVELLA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 220 FSPLAQGLLTNRYLHGI-PEDSRahrsDSPF--LTEDNVQSTIEVVKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIG 296
Cdd:PRK10625 233 YSCLAFGTLTGKYLNGAkPAGAR----NTLFsrFTRYSGEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLLG 308
|
330 340 350
....*....|....*....|....*....|....*
gi 510806721 297 ASRVSQLEDNLKALdHLAFSKEELTQIDAILAKLT 331
Cdd:PRK10625 309 ATTMEQLKTNIESL-HLTLSEEVLAEIEAVHQVYT 342
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
24-324 |
1.77e-34 |
|
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: 126.23 E-value: 1.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 24 LPAISLGLWHNFGDvdtldNQRAIVRAAFDHGITHFDLANNYGppagsAEINFGRILKEDMFPyRDELIISSKagyyMWP 103
Cdd:cd19073 1 IPALGLGTWQLRGD-----DCANAVKEALELGYRHIDTAEIYN-----NEAEVGEAIAESGVP-REDLFITTK----VWR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 104 GPYgewgSRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVSNYSAEQTAEISKIfqe 183
Cdd:cd19073 66 DHL----RPEDLKKSVDRSLEKLGTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDI--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 184 LRTPFIIHQPRYNMFDRWIEdgLTDVLAEEGIGTITFSPLAQGlltnrylhgipedsrahrsdspfltednvqsTIEVVK 263
Cdd:cd19073 139 SPLPIAVNQVEFHPFLYQAE--LLEYCRENDIVITAYSPLARG-------------------------------EVLRDP 185
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510806721 264 QLNDIAEKRGQTLAEMALAWNLRQPTVtsVLIGASRVSQLEDNLKALDhLAFSKEELTQID 324
Cdd:cd19073 186 VIQEIAEKYDKTPAQVALRWLVQKGIV--VIPKASSEDHLKENLAIFD-WELTSEDVAKID 243
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
22-325 |
5.58e-32 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 121.29 E-value: 5.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 22 LKLPAISLGLW----------HNFGDVDTLDNQRAIVRAAFDHGITHFDLANNYGppAGSAEINFGRILKedMFPyRDEL 91
Cdd:cd19103 2 KKLPKIALGTWswgsggaggdQVFGNHLDEDTLKAVFDKAMAAGLNLWDTAAVYG--MGASEKILGEFLK--RYP-REDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 92 IISSKAGyymwpgPYGEWGSRKSIIASCEQSLKRMGLDYVDIFYSHRPdpdTPLEETALALDQLVRQGKTLYVGVSNYSA 171
Cdd:cd19103 77 IISTKFT------PQIAGQSADPVADMLEGSLARLGTDYIDIYWIHNP---ADVERWTPELIPLLKSGKVKHVGVSNHNL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 172 EQTAEISKIFQELRTPFIIHQPRYNMFDR-WIEDGLTDVLAEEGIGTITFSPLAQGLLTNRYL--HGIPEDSRAHRSDSP 248
Cdd:cd19103 148 AEIKRANEILAKAGVSLSAVQNHYSLLYRsSEEAGILDYCKENGITFFAYMVLEQGALSGKYDtkHPLPEGSGRAETYNP 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510806721 249 FLtednvQSTIEVVKQLNDIAEKRGQTLAEMALAWNLRQPTVTsvLIGASRVSQLEDNLKALDhLAFSKEELTQIDA 325
Cdd:cd19103 228 LL-----PQLEELTAVMAEIGAKHGASIAQVAIAWAIAKGTTP--IIGVTKPHHVEDAARAAS-ITLTDDEIKELEQ 296
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
45-311 |
1.67e-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: 381323 [Multi-domain] Cd Length: 267 Bit Score: 119.17 E-value: 1.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 45 RAIVRAAFDHGITHFDLANNYGppagSAEINFGRILKEDmfpyrDELIISSKAGyymwPGPYGEWGSRKSIIASCEQSLK 124
Cdd:cd19097 29 KKILEYALKAGINTLDTAPAYG----DSEKVLGKFLKRL-----DKFKIITKLP----PLKEDKKEDEAAIEASVEASLK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 125 RMGLDYVDIFYSHRP-DPDTPLEETALALDQLVRQGKTLYVGVSNYSAEQTAEISKIFQelrtPFIIHQPrYNMFD-RWI 202
Cdd:cd19097 96 RLKVDSLDGLLLHNPdDLLKHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKALESFK----IDIIQLP-FNILDqRFL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 203 EDGLTDVLAEEGIGTITFSPLAQGLLTNRYLHgIPEDSRAHRsdspfltednvqstiEVVKQLNDIAEKRGQTLAEMALA 282
Cdd:cd19097 171 KSGLLAKLKKKGIEIHARSVFLQGLLLMEPDK-LPAKFAPAK---------------PLLKKLHELAKKLGLSPLELALG 234
|
250 260
....*....|....*....|....*....
gi 510806721 283 WNLRQPTVTSVLIGASRVSQLEDNLKALD 311
Cdd:cd19097 235 FVLSLPEIDKIVVGVDSLEQLKEIIAAFK 263
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
24-324 |
2.98e-31 |
|
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: 117.97 E-value: 2.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 24 LPAISLGLWHNFGDvdtldNQRAIVRAAFDHGITHFDLANNYGppaGSAEInfGRILKEDMFPyRDELIISSKagyyMWP 103
Cdd:cd19071 1 MPLIGLGTYKLKPE-----ETAEAVLAALEAGYRHIDTAAAYG---NEAEV--GEAIRESGVP-REELFITTK----LWP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 104 GPYGewgsRKSIIASCEQSLKRMGLDYVDIFYSHRP------DPDTPLEETALALDQLVRQGKTLYVGVSNYSAEQTAEI 177
Cdd:cd19071 66 TDHG----YERVREALEESLKDLGLDYLDLYLIHWPvpgkegGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEEL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 178 SKIFQElrTPFiIHQPRYNMFDRWIEdgLTDVLAEEGIGTITFSPLAQGlltnrylhgipedsrahrsDSPFLTEDNVQS 257
Cdd:cd19071 142 LAAARI--KPA-VNQIELHPYLQQKE--LVEFCKEHGIVVQAYSPLGRG-------------------RRPLLDDPVLKE 197
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510806721 258 tievvkqlndIAEKRGQTLAEMALAWNLRQPTVtsVLIGASRVSQLEDNLKALDhLAFSKEELTQID 324
Cdd:cd19071 198 ----------IAKKYGKTPAQVLLRWALQRGVV--VIPKSSNPERIKENLDVFD-FELSEEDMAAID 251
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
15-326 |
1.19e-28 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 111.98 E-value: 1.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 15 RRLGKSGLKLPAIslglwHNFGDVDTLDNQRAIVRAAFDHGITHFDLANNYGPPAGSaeinfgRILKEDMFPYRDELIIS 94
Cdd:PRK10376 18 NRLGYGAMQLAGP-----GVFGPPKDRDAAIAVLREAVALGVNHIDTSDFYGPHVTN------QLIREALHPYPDDLTIV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 95 SKAGYYMwpGPYGEWG---SRKSIIASCEQSLKRMGLDYVDI------FYSHRPDPDtPLEETALALDQLVRQGKTLYVG 165
Cdd:PRK10376 87 TKVGARR--GEDGSWLpafSPAELRRAVHDNLRNLGLDVLDVvnlrlmGDGHGPAEG-SIEEPLTVLAELQRQGLVRHIG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 166 VSNYSAEQTAEISKIfqelrTPFIIHQPRYNMFDRwIEDGLTDVLAEEGIGTITFSPLAqGLltnrylhgipedsrahrs 245
Cdd:PRK10376 164 LSNVTPTQVAEARKI-----AEIVCVQNHYNLAHR-ADDALIDALARDGIAYVPFFPLG-GF------------------ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 246 dSPfltednVQSTievvkQLNDIAEKRGQTLAEMALAWNL-RQPTVtsVLI-GASRVSQLEDNLKALDhLAFSKEELTQI 323
Cdd:PRK10376 219 -TP------LQSS-----TLSDVAASLGATPMQVALAWLLqRSPNI--LLIpGTSSVAHLRENLAAAE-LVLSEEVLAEL 283
|
...
gi 510806721 324 DAI 326
Cdd:PRK10376 284 DGI 286
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
20-327 |
1.86e-28 |
|
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: 112.13 E-value: 1.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 20 SGLKLPAISLG-LWHN-FGDVDTlDNQRAIVRAAFDHGITHFDLANNYgpPAGSAEINFGRILKEDmfPYRDELIISSK- 96
Cdd:cd19146 12 SPLCLGAMSFGeAWKSmMGECDK-ETAFKLLDAFYEQGGNFIDTANNY--QGEESERWVGEWMASR--GNRDEMVLATKy 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 97 -AGYYM---------WPGpygewGSRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGV 166
Cdd:cd19146 87 tTGYRRggpikiksnYQG-----NHAKSLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 167 SNYSAeqtAEISKIFQELR----TPFIIHQPRYNMFDRWIEDGLTDVLAEEGIGTITFSPLAQGLLTNRylhgiPEDSRA 242
Cdd:cd19146 162 SDTPA---WVVSKANAYARahglTQFVVYQGHWSAAFRDFERDILPMCEAEGMALAPWGVLGQGQFRTE-----EEFKRR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 243 HRSDSPFLTEDnvQSTIEVVKQLNDIAEKRGQTLAEMALAWNLRQ-PTVTSVlIGASRVSQLEDNLKALdHLAFSKEELT 321
Cdd:cd19146 234 GRSGRKGGPQT--EKERKVSEKLEKVAEEKGTAITSVALAYVMHKaPYVFPI-VGGRKVEHLKGNIEAL-GISLSDEEIQ 309
|
....*.
gi 510806721 322 QIDAIL 327
Cdd:cd19146 310 EIEDAY 315
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
25-314 |
2.79e-28 |
|
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: 109.96 E-value: 2.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 25 PAISLG---LWHNFGDVDTLDNQRAIVRAAFDHGITHFDLANNYGPpaGSAEINFGRILKEDmfpYRDELIISSKagyym 101
Cdd:cd19096 1 SVLGFGtmrLPESDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGG--GKSEEILGEALKEG---PREKFYLATK----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 102 wpGPYGEWGSRKSIIASCEQSLKRMGLDYVDIFYSH---RPDpdtpLEETAL------ALDQLVRQGKTLYVGVSnySAE 172
Cdd:cd19096 71 --LPPWSVKSAEDFRRILEESLKRLGVDYIDFYLLHglnSPE----WLEKARkgglleFLEKAKKEGLIRHIGFS--FHD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 173 QTAEISKIFQELRTPFIIHQprYNMFDRWIEDGLT--DVLAEEGIGTITFSPLAQGLLTNRylhgipedsrahrsdspfl 250
Cdd:cd19096 143 SPELLKEILDSYDFDFVQLQ--YNYLDQENQAGRPgiEYAAKKGMGVIIMEPLKGGGLANN------------------- 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510806721 251 tednvqstievVKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALDHLA 314
Cdd:cd19096 202 -----------PPEALAILCGAPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENIAAADEFE 254
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
21-326 |
4.75e-28 |
|
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: 110.01 E-value: 4.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 21 GLKLPAISLGL--WHNFGDVDTLdnQRAI---VRAAFDHGITHFDLANNYGppagsAEINFGRILKEDMFPyRDELIISS 95
Cdd:cd19120 1 GSKIPAIAFGTgtAWYKSGDDDI--QRDLvdsVKLALKAGFRHIDTAEMYG-----NEKEVGEALKESGVP-REDLFITT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 96 KAGyymwpgpygewGSRKSIIASCEQSLKRMGLDYVDIFYSHRP----DPDTPLEETALALDQLVRQGKTLYVGVSNYSA 171
Cdd:cd19120 73 KVS-----------PGIKDPREALRKSLAKLGVDYVDLYLIHSPffakEGGPTLAEAWAELEALKDAGLVRSIGVSNFRI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 172 EQtaeISKIFQELRTPFIIHQPRYNMFDRWIEDGLTDVLAEEGIGTITFSPLAqglltnrylhgipedSRAHRSDSPFLt 251
Cdd:cd19120 142 ED---LEELLDTAKIKPAVNQIEFHPYLYPQQPALLEYCREHGIVVSAYSPLS---------------PLTRDAGGPLD- 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510806721 252 ednvqstievvKQLNDIAEKRGQTLAEMALAWNLRQ---PTVTSvligaSRVSQLEDNLKALDhLAFSKEELTQIDAI 326
Cdd:cd19120 203 -----------PVLEKIAEKYGVTPAQVLLRWALQKgivVVTTS-----SKEERMKEYLEAFD-FELTEEEVEEIDKA 263
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
42-310 |
1.52e-27 |
|
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: 109.24 E-value: 1.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 42 DNQRAIVRAAFDHGITHFDLANNYGppAGSAEINFGRILKEDMfpyRDELIISSKAGYYMWP----GPYGEWG------- 110
Cdd:cd19152 20 EEAKATLVAAWDLGIRYFDTAPWYG--AGLSEERLGAALRELG---REDYVISTKVGRLLVPlqevEPTFEPGfwnplpf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 111 ------SRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEET-----------ALALDQLVRQGKTLYVGV-SNysae 172
Cdd:cd19152 95 davfdySYDGILRSIEDSLQRLGLSRIDLLSIHDPDEDLAGAESdehfaqaikgaFRALEELREEGVIKAIGLgVN---- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 173 QTAEISKIFQELRTPFIIHQPRYNMFDRWIEDGLTDVLAEEGIGTITFSPLAQGLLTNRYLHGIPEDSRAHrsdspflte 252
Cdd:cd19152 171 DWEVILRILEEADLDWVMLAGRYTLLDHSAARELLPECEKRGVKVVNAGPFNSGFLAGGDNFDYYEYGPAP--------- 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 510806721 253 dnvQSTIEVVKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKAL 310
Cdd:cd19152 242 ---PELIARRDRIEALCEQHGVSLAAAALQFALAPPAVASVAPGASSPERVEENVALL 296
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
15-314 |
5.43e-27 |
|
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: 107.62 E-value: 5.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 15 RRLGKSGLKLPAISLG---LWHNFGDVDTLDNQRAIVRAAFDHGITHFDLANNYGPPagSAEINFGRILKEDMFPyRDEL 91
Cdd:cd19153 3 ETLEIALGNVSPVGLGtaaLGGVYGDGLEQDEAVAIVAEAFAAGINHFDTSPYYGAE--SSEAVLGKALAALQVP-RSSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 92 IISSKAGYYmwpGPYGEWGSRKSIIASCEQSLKRMGLDYVDIFYSHR---PDPDTPLEETALALDQLVRQGKTLYVGVSN 168
Cdd:cd19153 80 TVATKVGRY---RDSEFDYSAERVRASVATSLERLHTTYLDVVYLHDiefVDYDTLVDEALPALRTLKDEGVIKRIGIAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 169 YSAEQTAEISKiFQELRTPFIIHQ-PRYNMFDRWIEDGLTDVLAEEGIGTITFSPLAQGLLTnrylhgiPEDSRAHRSDS 247
Cdd:cd19153 157 YPLDTLTRATR-RCSPGSLDAVLSyCHLTLQDARLESDAPGLVRGAGPHVINASPLSMGLLT-------SQGPPPWHPAS 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510806721 248 PFLTednvqstiEVVKQLNDIAEKRGQTLAEMALAWNL-RQPTVTSVLIGASRVSQLEDNLKALDHLA 314
Cdd:cd19153 229 GELR--------HYAAAADAVCASVEASLPDLALQYSLaAHAGVGTVLLGPSSLAQLRSMLAAVDAVA 288
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
24-326 |
5.45e-26 |
|
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: 103.97 E-value: 5.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 24 LPAISLGLWHNFGDVDTldnqrAIVRAAFDHGITHFDLANNYGppagsAEINFGRILKEDMFPyRDELIISSKagyyMWP 103
Cdd:cd19139 1 IPAFGLGTFRLKDDVVI-----DSVRTALELGYRHIDTAQIYD-----NEAAVGQAIAESGVP-RDELFITTK----IWI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 104 GPYgewgSRKSIIASCEQSLKRMGLDYVDIFYSHRPDPD--TPLEETALALDQLVRQGKTLYVGVSNYSAEQTAEISKIF 181
Cdd:cd19139 66 DNL----SKDKLLPSLEESLEKLRTDYVDLTLIHWPSPNdeVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 182 QELR--------TPFIihQPRynmfdrwiedGLTDVLAEEGIGTITFSPLAQGLLTnrylhgipedsrahrsDSPflted 253
Cdd:cd19139 142 GAGAiatnqielSPYL--QNR----------KLVAHCKQHGIHVTSYMTLAYGKVL----------------DDP----- 188
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 510806721 254 nvqstievvkQLNDIAEKRGQTLAEMALAWNLRQPtvTSVLIGASRVSQLEDNLKALDhLAFSKEELTQIDAI 326
Cdd:cd19139 189 ----------VLAAIAERHGATPAQIALAWAMARG--YAVIPSSTKREHLRSNLLALD-LTLDADDMAAIAAL 248
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
22-308 |
2.08e-25 |
|
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: 103.55 E-value: 2.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 22 LKLPAISLGLWHNFGDVDTLDNQRAIVRAAFDHGITHFDLANNYGppAGSAEINFGRILKEDMFPY---RDELIISSKAG 98
Cdd:cd19099 1 LTLSSLGLGTYRGDSDDETDEEYREALKAALDSGINVIDTAINYR--GGRSERLIGKALRELIEKGgikRDEVVIVTKAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 99 YY-----------MWPGPYGEWG--------------SRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTP--------- 144
Cdd:cd19099 79 YIpgdgdeplrplKYLEEKLGRGlidvadsaglrhciSPAYLEDQIERSLKRLGLDTIDLYLLHNPEEQLLelgeeefyd 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 145 -LEETALALDQLVRQGKTLYVGVS-------------NYSAEQTAEISKI-------FQELRTPFIIHQPRYNMfDRWIE 203
Cdd:cd19099 159 rLEEAFEALEEAVAEGKIRYYGIStwdgfrappalpgHLSLEKLVAAAEEvggdnhhFKVIQLPLNLLEPEALT-EKNTV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 204 DG----LTDVLAEEGIGTITFSPLAQGLLtnrylhgipedsrahrsdspfltednvqstIEVVKQLNDIAEKRGQTLAEM 279
Cdd:cd19099 238 KGealsLLEAAKELGLGVIASRPLNQGQL------------------------------LGELRLADLLALPGGATLAQR 287
|
330 340
....*....|....*....|....*....
gi 510806721 280 ALAWNLRQPTVTSVLIGASRVSQLEDNLK 308
Cdd:cd19099 288 ALQFARSTPGVDSALVGMRRPEHVDENLA 316
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
20-326 |
9.13e-25 |
|
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: 100.86 E-value: 9.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 20 SGLKLPAISLGLWHNFGDvdtldNQRAIVRAAFDHGITHFDLANNYGppagsAEINFGRILKEDMFPyRDELIISSKagy 99
Cdd:cd19135 9 NGVEMPILGLGTSHSGGY-----SHEAVVYALKECGYRHIDTAKRYG-----CEELLGKAIKESGVP-REDLFLTTK--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 100 yMWPGPYGEwgsrKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTP-------LEETALALDQLVRQGKTLYVGVSNYSAE 172
Cdd:cd19135 75 -LWPSDYGY----ESTKQAFEASLKRLGVDYLDLYLLHWPDCPSSgknvketRAETWRALEELYDEGLCRAIGVSNFLIE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 173 qtaEISKIFQELRTPFIIHQPRYNMFDRWIEdgLTDVLAEEGIGTITFSPLAQGlltnrylhgipedsrahrsdsPFLTE 252
Cdd:cd19135 150 ---HLEQLLEDCSVVPHVNQVEFHPFQNPVE--LIEYCRDNNIVFEGYCPLAKG---------------------KALEE 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510806721 253 DNVQstievvkqlnDIAEKRGQTLAEMALAWNLRQPTVTsvlIGAS-RVSQLEDNLKALDhLAFSKEELTQIDAI 326
Cdd:cd19135 204 PTVT----------ELAKKYQKTPAQILIRWSIQNGVVT---IPKStKEERIKENCQVFD-FSLSEEDMATLDSL 264
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
45-311 |
2.32e-24 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 100.86 E-value: 2.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 45 RAIVRAAFDHGITHFDLANNYGppAGSAEINFGRILKEDMfpyRDELIISSKAGYYMWPG------PYGEWG-------- 110
Cdd:cd19161 23 DATLDAAWDSGIRYFDTAPMYG--HGLAEHRLGDFLREKP---RDEFVLSTKVGRLLKPAregsvpDPNGFVdplpfeiv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 111 ---SRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETAL------------ALDQLVRQGKTLYVGVSNYSAEQTA 175
Cdd:cd19161 98 ydySYDGIMRSFEDSLQRLGLNRIDILYVHDIGVYTHGDRKERhhfaqlmsggfkALEELKKAGVIKAFGLGVNEVQICL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 176 EISKIFQelrTPFIIHQPRYNMFDRWIEDGLTDVLAEEGIGTITFSPLAQGLLTNrylhgiPEDSRAHrsdspFLTEDNV 255
Cdd:cd19161 178 EALDEAD---LDCFLLAGRYSLLDQSAEEEFLPRCEQRGTSLVIGGVFNSGILAT------GTKSGAK-----FNYGDAP 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 510806721 256 QSTIEVVKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALD 311
Cdd:cd19161 244 AEIISRVMEIEKICDAYNVPLAAAALQFPLRHPAVASVLTGARNPAQLRQNVEAFQ 299
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
20-324 |
1.78e-23 |
|
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: 98.36 E-value: 1.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 20 SGLKLPAISLG-LWHNFgdVDTLDNQRA--IVRAAFDHGITHFDLANNYgpPAGSAEINFGRILKEDMFpyRDELIISSK 96
Cdd:cd19147 11 SPLILGAMSIGdAWSGF--MGSMDKEQAfeLLDAFYEAGGNFIDTANNY--QDEQSETWIGEWMKSRKN--RDQIVIATK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 97 AGYYMWPGPYGE------WG-SRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETALALDQLVRQGKTLYVGVSNY 169
Cdd:cd19147 85 FTTDYKAYEVGKgkavnyCGnHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 170 SAEQTAEISKIFQEL-RTPFIIHQPRYNMFDRWIEDGLTDVLAEEGIGTITFSPLAQGLLTNRylhgipeDSRAHRSDS- 247
Cdd:cd19147 165 PAWVVSAANYYATAHgKTPFSVYQGRWNVLNRDFERDIIPMARHFGMALAPWDVLGGGKFQSK-------KAVEERKKNg 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 248 ----PFLTEDNvQSTIEVV--KQLNDIAEKRG-QTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALDhLAFSKEEL 320
Cdd:cd19147 238 eglrSFVGGTE-QTPEEVKisEALEKVAEEHGtESVTAIALAYVRSKAPNVFPLVGGRKIEHLKDNIEALS-IKLTPEEI 315
|
....
gi 510806721 321 TQID 324
Cdd:cd19147 316 EYLE 319
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
20-330 |
1.73e-21 |
|
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: 92.93 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 20 SGLKLPAISLGLWHNFGDVdtldnQRAIVRAAFDHGITHFDLANNYGPPAGSAEInFGRILKEDMFPyRDELIISSKagy 99
Cdd:cd19112 7 SGHKMPVIGLGVWRMEPGE-----IKELILNAIKIGYRHFDCAADYKNEKEVGEA-LAEAFKTGLVK-REDLFITTK--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 100 yMWPGPYGEwgsrksIIASCEQSLKRMGLDYVDIFYSHRP-----------------------DPDTPLEETALALDQLV 156
Cdd:cd19112 77 -LWNSDHGH------VIEACKDSLKKLQLDYLDLYLVHFPvatkhtgvgttgsalgedgvldiDVTISLETTWHAMEKLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 157 RQGKTLYVGVSNYSAEQTAEI---SKIfqelrTPFIIHQPRYNMFDRwieDGLTDVLAEEGIGTITFSPLAQGLltnryl 233
Cdd:cd19112 150 SAGLVRSIGISNYDIFLTRDClaySKI-----KPAVNQIETHPYFQR---DSLVKFCQKHGISVTAHTPLGGAA------ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 234 hgipedSRAHRSDSPFLTEDNVqstievvkqLNDIAEKRGQTLAEMALAWNLRQPTVtsVLIGASRVSQLEDNLKALDhL 313
Cdd:cd19112 216 ------ANAEWFGSVSPLDDPV---------LKDLAKKYGKSAAQIVLRWGIQRNTA--VIPKSSKPERLKENIDVFD-F 277
|
330
....*....|....*..
gi 510806721 314 AFSKEELTQIDAILAKL 330
Cdd:cd19112 278 QLSKEDMKLIKSLDRKY 294
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
20-326 |
8.55e-20 |
|
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: 87.83 E-value: 8.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 20 SGLKLPAISLGLWHNF-GDVdtldnqRAIVRAAFDHGITHFDLANNYGppaGSAEInfGRILKEDMFPY----RDELIIS 94
Cdd:cd19106 3 TGQKMPLIGLGTWKSKpGQV------KAAVKYALDAGYRHIDCAAVYG---NEQEV--GEALKEKVGPGkavpREDLFVT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 95 SKAgyymwpgpygeWGSR---KSIIASCEQSLKRMGLDYVDIFYSHRP------------DPD-------TPLEETALAL 152
Cdd:cd19106 72 SKL-----------WNTKhhpEDVEPALRKTLKDLQLDYLDLYLIHWPyafergdnpfpkNPDgtirydsTHYKETWKAM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 153 DQLVRQGKTLYVGVSNYSAEQTAEISKIFQelrtpfiiHQPRYNMFD---RWIEDGLTDVLAEEGIGTITFSPLaqgllt 229
Cdd:cd19106 141 EKLVDKGLVKAIGLSNFNSRQIDDILSVAR--------IKPAVLQVEchpYLAQNELIAHCKARGLVVTAYSPL------ 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 230 nrylhGIPEDSRAHrSDSPFLTEDNVqstievvkqLNDIAEKRGQTLAEMALAWNLRQPTVT---SVliGASRVSQledN 306
Cdd:cd19106 207 -----GSPDRPWAK-PDEPVLLEEPK---------VKALAKKYNKSPAQILLRWQVQRGVVVipkSV--TPSRIKQ---N 266
|
330 340
....*....|....*....|
gi 510806721 307 LKALDhLAFSKEELTQIDAI 326
Cdd:cd19106 267 IQVFD-FTLSPEEMKQLDAL 285
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
21-326 |
8.87e-20 |
|
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: 87.06 E-value: 8.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 21 GLKLPAISLGLWHNFGDVDTLDNqraiVRAAFDHGITHFDLANNYGPPAGsaeinFGRILKEDMFPyRDELIISSKagyy 100
Cdd:cd19157 7 GVKMPWLGLGVFKVEEGSEVVNA----VKTALKNGYRSIDTAAIYGNEEG-----VGKGIKESGIP-REELFITSK---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 101 MWPGPYGewgsRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTpLEETALALDQLVRQGKTLYVGVSNYsaeQTAEISKI 180
Cdd:cd19157 73 VWNADQG----YDSTLKAFEASLERLGLDYLDLYLIHWPVKGK-YKETWKALEKLYKDGRVRAIGVSNF---QVHHLEDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 181 FQELRTPFIIHQPRYNmfDRWIEDGLTDVLAEEGIGTITFSPLAQGLLTnrylhgipedsrahrsDSPFLTEdnvqstie 260
Cdd:cd19157 145 LADAEIVPMVNQVEFH--PRLTQKELRDYCKKQGIQLEAWSPLMQGQLL----------------DNPVLKE-------- 198
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510806721 261 vvkqlndIAEKRGQTLAEMALAWNLRQPTVTsvLIGASRVSQLEDNLKALDhLAFSKEELTQIDAI 326
Cdd:cd19157 199 -------IAEKYNKSVAQVILRWDLQNGVVT--IPKSIKEHRIIENADVFD-FELSQEDMDKIDAL 254
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
19-326 |
9.32e-20 |
|
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: 87.40 E-value: 9.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 19 KSGLKLPAISLGLWH-NFGDVDTldnqraIVRAAFDHGITHFDLANNYGppagsAEINFGRILKEDM---FPYRDELIIS 94
Cdd:cd19125 6 NTGAKIPAVGLGTWQaDPGVVGN------AVKTAIKEGYRHIDCAAIYG-----NEKEIGKALKKLFedgVVKREDLFIT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 95 SKagyyMWpgpyGEWGSRKSIIASCEQSLKRMGLDYVDIFYSHRP--------------DPDTPLEETALALDQLVRQGK 160
Cdd:cd19125 75 SK----LW----CTDHAPEDVPPALEKTLKDLQLDYLDLYLIHWPvrlkkgahmpepeeVLPPDIPSTWKAMEKLVDSGK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 161 TLYVGVSNYSAEQtaeISKIFQELRTPFIIHQprYNMFDRWIEDGLTDVLAEEGIGTITFSPLAqglltnrylhgipeds 240
Cdd:cd19125 147 VRAIGVSNFSVKK---LEDLLAVARVPPAVNQ--VECHPGWQQDKLHEFCKSKGIHLSAYSPLG---------------- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 241 rahRSDSPFLTEDNVQSTIevvkqLNDIAEKRGQTLAEMALAWNLRQPtvTSVLIGASRVSQLEDNLKALDhLAFSKEEL 320
Cdd:cd19125 206 ---SPGTTWVKKNVLKDPI-----VTKVAEKLGKTPAQVALRWGLQRG--TSVLPKSTNEERIKENIDVFD-WSIPEEDF 274
|
....*.
gi 510806721 321 TQIDAI 326
Cdd:cd19125 275 AKFSSI 280
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
20-326 |
1.18e-19 |
|
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: 87.34 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 20 SGLKLPAISLGLWHNFGDvdtlDNQRAIVRAAFDHGITHFDLANNYGPPA--GSA---EINFGRILKEDMFpyrdeliIS 94
Cdd:cd19116 7 DGNEIPAIALGTWKLKDD----EGVRQAVKHAIEAGYRHIDTAYLYGNEAevGEAireKIAEGVVKREDLF-------IT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 95 SKagyyMWpgpyGEWGSRKSIIASCEQSLKRMGLDYVDIFYSHRP------------DPDTPLE----ETALALDQLVRQ 158
Cdd:cd19116 76 TK----LW----NSYHEREQVEPALRESLKRLGLDYVDLYLIHWPvafkenndsesnGDGSLSDidylETWRGMEDLVKL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 159 GKTLYVGVSNYSAEQtaeISKIFQELRTPFIIHQ----PRYNMFDrwiedgLTDVLAEEGIGTITFSPLaqglltnrylh 234
Cdd:cd19116 148 GLTRSIGVSNFNSEQ---INRLLSNCNIKPAVNQievhPTLTQEK------LVAYCQSNGIVVMAYSPF----------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 235 GIPeDSRAHRSDSPFLTEDNVQStievvkqlndIAEKRGQTLAEMALAWNLRQPTVtsVLIGASRVSQLEDNLKALD-HL 313
Cdd:cd19116 208 GRL-VPRGQTNPPPRLDDPTLVA----------IAKKYGKTTAQIVLRYLIDRGVV--PIPKSSNKKRIKENIDIFDfQL 274
|
330
....*....|...
gi 510806721 314 afSKEELTQIDAI 326
Cdd:cd19116 275 --TPEEVAALNSF 285
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
22-326 |
1.59e-19 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 86.62 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 22 LKLPAISLGLWHnfgdvdtLDNQRAI--VRAAFDHGITHFDLANNYGppaGSAEInfGRILKEDMFPyRDELIISSKagy 99
Cdd:PRK11172 1 MSIPAFGLGTFR-------LKDQVVIdsVKTALELGYRAIDTAQIYD---NEAAV--GQAIAESGVP-RDELFITTK--- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 100 yMWPGPYgewgSRKSIIASCEQSLKRMGLDYVDIFYSHRPDPD--TPLEETALALDQLVRQGKTLYVGVSNYSAEQTAEI 177
Cdd:PRK11172 65 -IWIDNL----AKDKLIPSLKESLQKLRTDYVDLTLIHWPSPNdeVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 178 skifqelrtpfiihqprynmfdrwiedglTDVLAEEGIGT--ITFSPLAQglltNRYLhgipedsrahrsdSPFLTEDNV 255
Cdd:PRK11172 140 -----------------------------IAAVGAENIATnqIELSPYLQ----NRKV-------------VAFAKEHGI 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 256 QSTI-------EVVKQ--LNDIAEKRGQTLAEMALAWNLRQPtvTSVLIGASRVSQLEDNLKALDhLAFSKEELTQIDAI 326
Cdd:PRK11172 174 HVTSymtlaygKVLKDpvIARIAAKHNATPAQVILAWAMQLG--YSVIPSSTKRENLASNLLAQD-LQLDAEDMAAIAAL 250
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
21-326 |
2.22e-19 |
|
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: 85.70 E-value: 2.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 21 GLKLPAISLGLWHnfgdVDTLDNQRAIVRAAFDHGITHFDLANNYGppagsAEINFGRILKEDMFPyRDELIISSKagyy 100
Cdd:cd19133 6 GVEMPILGFGVFQ----IPDPEECERAVLEAIKAGYRLIDTAAAYG-----NEEAVGRAIKKSGIP-REELFITTK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 101 MWPGPYGEWGSRKSIiascEQSLKRMGLDYVDIFYSHRPDPDtpLEETALALDQLVRQGKTLYVGVSNYSAEQTAEISKI 180
Cdd:cd19133 72 LWIQDAGYEKAKKAF----ERSLKRLGLDYLDLYLIHQPFGD--VYGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLILH 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 181 FqelRTPFIIHQPRYNMFDRWIEDglTDVLAEEGIGTITFSPLAQG---LLTNrylhgipedsrahrsdsPFLTEdnvqs 257
Cdd:cd19133 146 N---EVKPAVNQIETHPFNQQIEA--VEFLKKYGVQIEAWGPFAEGrnnLFEN-----------------PVLTE----- 198
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 510806721 258 tievvkqlndIAEKRGQTLAEMALAWNLRQPTVtsVLIGASRVSQLEDNLKALDhLAFSKEELTQIDAI 326
Cdd:cd19133 199 ----------IAEKYGKSVAQVILRWLIQRGIV--VIPKSVRPERIAENFDIFD-FELSDEDMEAIAAL 254
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
25-326 |
3.04e-19 |
|
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: 86.04 E-value: 3.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 25 PAISLGLWHNfgdVDTLDNQRaiVRAAFDHGITHFDLANNYGPPAGSAEInFGRILKEDMFPyRDELIISSKagyyMWPG 104
Cdd:cd19128 2 PRLGFGTYKI---TESESKEA--VKNAIKAGYRHIDCAYYYGNEAFIGIA-FSEIFKDGGVK-REDLFITSK----LWPT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 105 PYgewgSRKSIIASCEQSLKRMGLDYVDIFYSHRP---DPDT----------------PLEETALALDQLVRQGKTLYVG 165
Cdd:cd19128 71 MH----QPENVKEQLLITLQDLQLEYLDLFLIHWPlafDMDTdgdprddnqiqslskkPLEDTWRAMEQCVDEKLTKNIG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 166 VSNYSAEQTAEI---SKIfqelrtpfiihQPRYNMFDRWIE---DGLTDVLAEEGIGTITFSPLAQglltnrylhgiped 239
Cdd:cd19128 147 VSNYSTKLLTDLlnyCKI-----------KPFMNQIECHPYfqnDKLIKFCIENNIHVTAYRPLGG-------------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 240 srahRSDSPFLTEDNvqstievVKQLNDIAEKRGQTLAEMALAWNL-RQPTVTSVLIGASRVSQLEDNLKALDhLAFSKE 318
Cdd:cd19128 202 ----SYGDGNLTFLN-------DSELKALATKYNTTPPQVIIAWHLqKWPKNYSVIPKSANKSRCQQNFDIND-LALTKE 269
|
....*...
gi 510806721 319 ELTQIDAI 326
Cdd:cd19128 270 DMDAINTL 277
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
19-326 |
3.09e-19 |
|
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: 86.31 E-value: 3.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 19 KSGLKLPAISLGLWHNFGDvdtldNQRAIVRAAFDHGITHFDLANNYgppagSAEINFGRILKEDM---FPYRDELIISS 95
Cdd:cd19154 7 SNGVKMPLIGLGTWQSKGA-----EGITAVRTALKAGYRLIDTAFLY-----QNEEAIGEALAELLeegVVKREDLFITT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 96 KAgyymWPGPYgewgSRKSIIASCEQSLKRMGLDYVDIFYSHRP-------------------DPDTPLEETALALDQLV 156
Cdd:cd19154 77 KL----WTHEH----APEDVEEALRESLKKLQLEYVDLYLIHAPaafkddegesgtmengmsiHDAVDVEDVWRGMEKVY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 157 RQGKTLYVGVSNYSAEQtaeISKIFQELRTPFIIHQPRYNMFdrWIEDGLTDVLAEEGIGTITFSPLaqglltnrylhGI 236
Cdd:cd19154 149 DEGLTKAIGVSNFNNDQ---IQRILDNARVKPHNNQVECHLY--FPQKELVEFCKKHNISVTSYATL-----------GS 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 237 PEDSRAHRSDSPFLTEDNVQSTIevVKQlndIAEKRGQTLAEMALAWNLRQPTVtsVLIGASRVSQLEDNLKALDhLAFS 316
Cdd:cd19154 213 PGRANFTKSTGVSPAPNLLQDPI--VKA---IAEKHGKTPAQVLLRYLLQRGIA--VIPKSATPSRIKENFNIFD-FSLS 284
|
330
....*....|
gi 510806721 317 KEELTQIDAI 326
Cdd:cd19154 285 EEDMATLEEI 294
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
21-323 |
5.40e-19 |
|
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: 84.73 E-value: 5.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 21 GLKLPAISLGLWHNFGDVdtldnQRAIVRAAFDHGITHFDLANNYGPPAGsaeinFGRILKEDMFPyRDELIISSKagyy 100
Cdd:cd19131 7 GNTIPQLGLGVWQVSNDE-----AASAVREALEVGYRSIDTAAIYGNEEG-----VGKAIRASGVP-REELFITTK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 101 MWPGPYGewgsRKSIIASCEQSLKRMGLDYVDIFYSHRPDP--DTPLeETALALDQLVRQGKTLYVGVSNYSAEQtaeIS 178
Cdd:cd19131 72 LWNSDQG----YDSTLRAFDESLRKLGLDYVDLYLIHWPVPaqDKYV-ETWKALIELKKEGRVKSIGVSNFTIEH---LQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 179 KIFQELRTPFIIHQ----PRYNmfdrwiEDGLTDVLAEEGIGTITFSPLAQGlltnrylhGIPEDSRahrsdspfltedn 254
Cdd:cd19131 144 RLIDETGVVPVVNQielhPRFQ------QRELRAFHAKHGIQTESWSPLGQG--------GLLSDPV------------- 196
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 510806721 255 vqstievvkqLNDIAEKRGQTLAEMALAWNLRQPTVtsVLIGASRVSQLEDNLKALDhLAFSKEELTQI 323
Cdd:cd19131 197 ----------IGEIAEKHGKTPAQVVIRWHLQNGLV--VIPKSVTPSRIAENFDVFD-FELDADDMQAI 252
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
24-326 |
9.77e-19 |
|
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: 84.22 E-value: 9.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 24 LPAISLGLWHnfgdVDTLDNQRAIVRAAFDHGITHFDLANNYGppagsAEINFGRILKEDMFPY---RDELIISSKAGyy 100
Cdd:cd19136 1 MPILGLGTFR----LRGEEEVRQAVDAALKAGYRLIDTASVYR-----NEADIGKALRDLLPKYglsREDIFITSKLA-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 101 mwpgPYgEWGSRKSIiASCEQSLKRMGLDYVDIFYSHRP-----DPDTPLE-----ETALALDQLVRQGKTLYVGVSNYS 170
Cdd:cd19136 70 ----PK-DQGYEKAR-AACLGSLERLGTDYLDLYLIHWPgvqglKPSDPRNaelrrESWRALEDLYKEGKLRAIGVSNYT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 171 AEQTAEISK-------IFQelrtpfIIHQPRYnmfdrwIEDGLTDVLAEEGIGTITFSPLAQGLLTnrylhgipedsrah 243
Cdd:cd19136 144 VRHLEELLKycevppaVNQ------VEFHPHL------VQKELLKFCKDHGIHLQAYSSLGSGDLR-------------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 244 rsdspFLTEDNVQstievvkqlnDIAEKRGQTLAEMALAWNLRQPtvTSVLIGASRVSQLEDNLKaLDHLAFSKEELTQI 323
Cdd:cd19136 198 -----LLEDPTVL----------AIAKKYGRTPAQVLLRWALQQG--IGVIPKSTNPERIAENIK-VFDFELSEEDMAEL 259
|
...
gi 510806721 324 DAI 326
Cdd:cd19136 260 NAL 262
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
21-326 |
1.66e-18 |
|
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: 84.38 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 21 GLKLPAISLGLWHNF-GDVdtldnQRAiVRAAFDHGITHFDLANNYGppaGSAEInfGRILKEDMFP---YRDELIISSK 96
Cdd:cd19123 9 GDLIPALGLGTWKSKpGEV-----GQA-VKQALEAGYRHIDCAAIYG---NEAEI--GAALAEVFKEgkvKREDLWITSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 97 agyyMWPGPYgewgSRKSIIASCEQSLKRMGLDYVDIFYSHRP------------------DPDTPLEETALALDQLVRQ 158
Cdd:cd19123 78 ----LWNNSH----APEDVLPALEKTLADLQLDYLDLYLMHWPvalkkgvgfpesgedllsLSPIPLEDTWRAMEELVDK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 159 GKTLYVGVSNYSAEQTAEI---SKIFQELRT----PFiIHQPRynmfdrwiedgLTDVLAEEGIGTITFSPLaqglltnr 231
Cdd:cd19123 150 GLCRHIGVSNFSVKKLEDLlatARIKPAVNQvelhPY-LQQPE-----------LLAFCRDNGIHLTAYSPL-------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 232 ylhGIPEDSRAHRS-DSPFLTEDNVqstievvkqLNDIAEKRGQTLAEMALAWNLRQPTVtsVLIGASRVSQLEDNLKAl 310
Cdd:cd19123 210 ---GSGDRPAAMKAeGEPVLLEDPV---------INKIAEKHGASPAQVLIAWAIQRGTV--VIPKSVNPERIQQNLEA- 274
|
330
....*....|....*.
gi 510806721 311 DHLAFSKEELTQIDAI 326
Cdd:cd19123 275 AEVELDASDMATIAAL 290
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
20-326 |
2.05e-18 |
|
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: 83.70 E-value: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 20 SGLKLPAISLGLWHNfgdvdTLDNQRAIVRAAFDHGITHFDLANNYGppagsAEINFGRILKEDMFPyRDELIISSKAgy 99
Cdd:cd19117 10 TGAEIPAVGLGTWQS-----KPNEVAKAVEAALKAGYRHIDTAAIYG-----NEEEVGQGIKDSGVP-REEIFITTKL-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 100 ymwpgpygeWGSRKSIIASC-EQSLKRMGLDYVDIFYSHRPDP-------DTPLEETALALD--------------QLVR 157
Cdd:cd19117 77 ---------WCTWHRRVEEAlDQSLKKLGLDYVDLYLMHWPVPldpdgndFLFKKDDGTKDHepdwdfiktwelmqKLPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 158 QGKTLYVGVSNYSaeqTAEISKIFQELRTPFIihqPRYNMfdrwIE-------DGLTDVLAEEGIGTITFSPLAQglltn 230
Cdd:cd19117 148 TGKVKAIGVSNFS---IKNLEKLLASPSAKIV---PAVNQ----IElhpllpqPKLVDFCKSKGIHATAYSPLGS----- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 231 rylhgipedsrahrSDSPFLTEDNVQstievvkqlnDIAEKRGQTLAEMALAWNLRQPtvTSVLIGASRVSQLEDNLKAl 310
Cdd:cd19117 213 --------------TNAPLLKEPVII----------KIAKKHGKTPAQVIISWGLQRG--YSVLPKSVTPSRIESNFKL- 265
|
330
....*....|....*.
gi 510806721 311 dhLAFSKEELTQIDAI 326
Cdd:cd19117 266 --FTLSDEEFKEIDEL 279
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
24-326 |
3.67e-18 |
|
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: 82.60 E-value: 3.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 24 LPAISLGLWHNFGDVdtldNQRAiVRAAFDHGITHFDLANNYGPPAGsaeinFGRILKEDMFPyRDELIISSKagyyMWP 103
Cdd:cd19134 11 MPVIGLGVGELSDDE----AERS-VSAALEAGYRLIDTAAAYGNEAA-----VGRAIAASGIP-RGELFVTTK----LAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 104 GPYGEWGSRksiiASCEQSLKRMGLDYVDIFYSHRPDPDT-PLEETALALDQLVRQGKTLYVGVSNYSAEQTAEIskIFQ 182
Cdd:cd19134 76 PDQGFTASQ----AACRASLERLGLDYVDLYLIHWPAGREgKYVDSWGGLMKLREEGLARSIGVSNFTAEHLENL--IDL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 183 ELRTPFI----IHqPRYNmfdrwiEDGLTDVLAEEGIGTITFSPLAQGLLTnrylhgipedsrahrsDSPFLTEdnvqst 258
Cdd:cd19134 150 TFFTPAVnqieLH-PLLN------QAELRKVNAQHGIVTQAYSPLGVGRLL----------------DNPAVTA------ 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510806721 259 ievvkqlndIAEKRGQTLAEMALAWNLRQPTVtsVLIGASRVSQLEDNLKALDhLAFSKEELTQIDAI 326
Cdd:cd19134 201 ---------IAAAHGRTPAQVLLRWSLQLGNV--VISRSSNPERIASNLDVFD-FELTADHMDALDGL 256
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
45-309 |
1.91e-17 |
|
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: 81.17 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 45 RAIVRAAFDHGITHFDLANNYGPpagsAEINFGRILK--EDMFPyRDELIISSKAGYYmwpGP----YgewgSRKSIIAS 118
Cdd:cd19164 37 VDIVRRALELGIRAFDTSPYYGP----SEIILGRALKalRDEFP-RDTYFIITKVGRY---GPddfdY----SPEWIRAS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 119 CEQSLKRMGLDYVDIFYSHrpdpD---TPLEETALALDQLVR---QGKTLYVGVSNYSAEQTAEISkifQELRTPF---- 188
Cdd:cd19164 105 VERSLRRLHTDYLDLVYLH----DvefVADEEVLEALKELFKlkdEGKIRNVGISGYPLPVLLRLA---ELARTTAgrpl 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 189 --IIHQPRYNMFDRWIEDGLTDVLAEEGIGTI-TFSPLAQGLLTNRylhGIPEdsrAHRSdSPFLtEDNVQSTIEVVKQl 265
Cdd:cd19164 178 daVLSYCHYTLQNTTLLAYIPKFLAAAGVKVVlNASPLSMGLLRSQ---GPPE---WHPA-SPEL-RAAAAKAAEYCQA- 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 510806721 266 ndiaekRGQTLAEMALAWNLRQ-PTVTSVLIGASRVSQLEDNLKA 309
Cdd:cd19164 249 ------KGTDLADVALRYALREwGGEGPTVVGCSNVDELEEAVEA 287
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
20-326 |
3.45e-17 |
|
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: 80.15 E-value: 3.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 20 SGLKLPAISLGLWHNF-GDVdtldnqRAIVRAAFDHGITHFDLANNYG--PPAGSAeinFGRILKEDMFPYRDELIISSK 96
Cdd:cd19118 3 TGNKIPAIGLGTWQAEpGEV------GAAVKIALKAGYRHLDLAKVYQnqHEVGQA---LKELLKEEPGVKREDLFITSK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 97 AgyymwpgpygeWGSR---KSIIASCEQSLKRMGLDYVDIFYSHRP---------DPDTP---------------LEETA 149
Cdd:cd19118 74 L-----------WNNShrpEYVEPALDDTLKELGLDYLDLYLIHWPvafkptgdlNPLTAvptnggevdldlsvsLVDTW 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 150 LALDQLVRQGKTLYVGVSNYSA-------EQTAEISKIFQELRTPFIIHQPrynmfdrwiedgLTDVLAEEGIGTITFSP 222
Cdd:cd19118 143 KAMVELKKTGKVKSIGVSNFSIdhlqaiiEETGVVPAVNQIEAHPLLLQDE------------LVDYCKSKNIHITAYSP 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 223 L---AQGLltnrylhgipedsrahrsdsPFLTEDnvqstiEVVKqlnDIAEKRGQTLAEMALAWNLRQPtvTSVLIGASR 299
Cdd:cd19118 211 LgnnLAGL--------------------PLLVQH------PEVK---AIAAKLGKTPAQVLIAWGIQRG--HSVIPKSVT 259
|
330 340
....*....|....*....|....*..
gi 510806721 300 VSQLEDNLKALDhlaFSKEELTQIDAI 326
Cdd:cd19118 260 PSRIRSNFEQVE---LSDDEFNAVTAL 283
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
21-326 |
4.14e-17 |
|
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: 79.40 E-value: 4.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 21 GLKLPAISLGLWHNFGDvdtlDNQRAIVRAAFDHGITHFDLANNYgppagSAEINFGRILKEDMFPyRDELIISSKagyy 100
Cdd:cd19126 6 GTRMPWLGLGVFQTPDG----DETERAVQTALENGYRSIDTAAIY-----KNEEGVGEAIRESGVP-REELFVTTK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 101 MWPGPYGEwgsrKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTpLEETALALDQLVRQGKTLYVGVSNYsaeQTAEISKI 180
Cdd:cd19126 72 LWNDDQRA----RRTEDAFQESLDRLGLDYVDLYLIHWPGKDK-FIDTWKALEKLYASGKVKAIGVSNF---QEHHLEEL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 181 FQELRTPFIIHQPRYNMFdrWIEDGLTDVLAEEGIGTITFSPLAQG-LLTNRYLHGipedsrahrsdspfltednvqsti 259
Cdd:cd19126 144 LAHADVVPAVNQVEFHPY--LTQKELRGYCKSKGIVVEAWSPLGQGgLLSNPVLAA------------------------ 197
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510806721 260 evvkqlndIAEKRGQTLAEMALAWNLRQPTVTsvLIGASRVSQLEDNLKALDhLAFSKEELTQIDAI 326
Cdd:cd19126 198 --------IGEKYGKSAAQVVLRWDIQHGVVT--IPKSVHASRIKENADIFD-FELSEDDMTAIDAL 253
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
21-326 |
4.45e-17 |
|
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: 79.57 E-value: 4.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 21 GLKLPAISLGLWhnfgDVDTLDNQRAiVRAAFDHGITHFDLANNYGPPAGsaeinFGRILKEDMFPyRDELIISSKagyy 100
Cdd:cd19130 7 GNSIPQLGYGVF----KVPPADTQRA-VATALEVGYRHIDTAAIYGNEEG-----VGAAIAASGIP-RDELFVTTK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 101 MWPGPYGEwgsrKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLE-ETALALDQLVRQGKTLYVGVSNYsaeQTAEISK 179
Cdd:cd19130 72 LWNDRHDG----DEPAAAFAESLAKLGLDQVDLYLVHWPTPAAGNYvHTWEAMIELRAAGRTRSIGVSNF---LPPHLER 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 180 IFQELRTPFIIHQ----PRYNmfdrwiEDGLTDVLAEEGIGTITFSPLAQGLLTnrylhgipedsrahrsDSPFLTEdnv 255
Cdd:cd19130 145 IVAATGVVPAVNQielhPAYQ------QRTIRDWAQAHDVKIEAWSPLGQGKLL----------------GDPPVGA--- 199
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510806721 256 qstievvkqlndIAEKRGQTLAEMALAWNLRQPTVtsVLIGASRVSQLEDNLKALDhLAFSKEELTQIDAI 326
Cdd:cd19130 200 ------------IAAAHGKTPAQIVLRWHLQKGHV--VFPKSVRRERMEDNLDVFD-FDLTDTEIAAIDAL 255
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
21-324 |
1.18e-16 |
|
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: 78.69 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 21 GLKLPAISLGLWHNFGDvdtldnqraIVRAAFDHGIT----HFDLANNYGPPAGSAE-----INFGRILKEDMFpyrdel 91
Cdd:cd19111 1 GFPMPVIGLGTYQSPPE---------EVRAAVDYALFvgyrHIDTALSYQNEKAIGEalkwwLKNGKLKREEVF------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 92 iISSKAgyymWPgpYGEwgSRKSIIASCEQSLKRMGLDYVDIFYSH-------------RPDPDTPLEETALALDQLVRQ 158
Cdd:cd19111 66 -ITTKL----PP--VYL--EFKDTEKSLEKSLENLKLPYVDLYLIHhpcgfvnkkdkgeRELASSDVTSVWRAMEALVSE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 159 GKTLYVGVSNYSAEQtaeISKIFQELRTPFIIHQPRYNMFdrWIEDGLTDVLAEEGIGTITFSPLAQGLLTNRYLHGipe 238
Cdd:cd19111 137 GKVKSIGLSNFNPRQ---INKILAYAKVKPSNLQLECHAY--LQQRELRKFCNKKNIVVTAYAPLGSPGRANQSLWP--- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 239 dsrahrsDSPFLTEDNVqstievvkqLNDIAEKRGQTLAEMALAWNLRQPTVtsVLIGASRVSQLEDNLKALDhLAFSKE 318
Cdd:cd19111 209 -------DQPDLLEDPT---------VLAIAKELDKTPAQVLLRFVLQRGTG--VLPKSTNKERIEENFEVFD-FELTEE 269
|
....*.
gi 510806721 319 ELTQID 324
Cdd:cd19111 270 HFKKLK 275
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
21-325 |
2.68e-16 |
|
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: 77.31 E-value: 2.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 21 GLKLPAISLGLWHNFGDvdtlDNQRAIVrAAFDHGITHFDLANNYGppagsAEINFGRILKEDMFPyRDELIISSKAgyy 100
Cdd:cd19132 4 GTQIPAIGFGTYPLKGD----EGVEAVV-AALQAGYRLLDTAFNYE-----NEGAVGEAVRRSGVP-REELFVTTKL--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 101 mwPGPYGewgSRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTPLE-ETALALDQLVRQGKTLYVGVSNYSAEQtaeISK 179
Cdd:cd19132 70 --PGRHH---GYEEALRTIEESLYRLGLDYVDLYLIHWPNPSRDLYvEAWQALIEAREEGLVRSIGVSNFLPEH---LDR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 180 IFQELRTPFIIHQprYNMFDRWIEDGLTDVLAEEGIGTITFSPLAQGlltnrylhgipedsrahrsdSPFLTEDNVQsti 259
Cdd:cd19132 142 LIDETGVTPAVNQ--IELHPYFPQAEQRAYHREHGIVTQSWSPLGRG--------------------SGLLDEPVIK--- 196
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510806721 260 evvkqlnDIAEKRGQTLAEMALAWNLrQPTVTSVLIGASRVSQLEdNLKALDhLAFSKEELTQIDA 325
Cdd:cd19132 197 -------AIAEKHGKTPAQVVLRWHV-QLGVVPIPKSANPERQRE-NLAIFD-FELSDEDMAAIAA 252
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
20-326 |
6.88e-16 |
|
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: 76.54 E-value: 6.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 20 SGLKLPAISLGLWHNFGDVDTLdnqRAIVRAAFDHGITHFDLANNYGppagsAEINFGRILKEDM----FPYRDELIISS 95
Cdd:cd19124 1 SGQTMPVIGMGTASDPPSPEDI---KAAVLEAIEVGYRHFDTAAAYG-----TEEALGEALAEALrlglVKSRDELFVTS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 96 KagyyMWPgpygEWGSRKSIIASCEQSLKRMGLDYVDIF------------YSHRPDPDTPL----EETALALDQLVRQG 159
Cdd:cd19124 73 K----LWC----SDAHPDLVLPALKKSLRNLQLEYVDLYlihwpvslkpgkFSFPIEEEDFLpfdiKGVWEAMEECQRLG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 160 KTLYVGVSNYSAEqtaeisKIFQELRTPFIihQPRYN---MFDRWIEDGLTDVLAEEGIGTITFSPL---AQGLLTNRYL 233
Cdd:cd19124 145 LTKAIGVSNFSCK------KLQELLSFATI--PPAVNqveMNPAWQQKKLREFCKANGIHVTAYSPLgapGTKWGSNAVM 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 234 hgipedsrahrsDSPFltednvqstievvkqLNDIAEKRGQTLAEMALAWNLRQptvtsvliGASRV------SQLEDNL 307
Cdd:cd19124 217 ------------ESDV---------------LKEIAAAKGKTVAQVSLRWVYEQ--------GVSLVvksfnkERMKQNL 261
|
330
....*....|....*....
gi 510806721 308 KALDhLAFSKEELTQIDAI 326
Cdd:cd19124 262 DIFD-WELTEEDLEKISEI 279
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
20-326 |
8.39e-15 |
|
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: 73.43 E-value: 8.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 20 SGLKLPAISLGLWHNFGdvdTLDNQRAIVRAAFDHGITHFDLANNY--GPPAGSAEINFgriLKEDMFPYRDELIISSKA 97
Cdd:cd19122 5 NGVKIPAVGFGTFANEG---AKGETYAAVTKALDVGYRHLDCAWFYlnEDEVGDAVRDF---LKENPSVKREDLFICTKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 98 GYYMWPGPYGEWgsrksiiaSCEQSLKRMGLDYVDIFYSHRP------DPDTPL-----------------EETALALDQ 154
Cdd:cd19122 79 WNHLHEPEDVKW--------SIDNSLKNLKLDYIDLFLVHWPiaaeknDQRSPKlgpdgkyvilkdltenpEPTWRAMEE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 155 LVRQGKTLYVGVSNYSA---EQTAEISKIFQELRT----PFIIHQPrynmfdrwiedgLTDVLAEEGIGTITFSPLAqgl 227
Cdd:cd19122 151 IYESGKAKAIGVSNWTIpglKKLLSFAKVKPHVNQieihPFLPNEE------------LVDYCFSNDILPEAYSPLG--- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 228 ltnrylhgipedsrahrsdspflTEDNVQSTIEVV---KQLNDIAEKRGQTLAEMALAWNLRQPTVtsVLIGASRVSQLE 304
Cdd:cd19122 216 -----------------------SQNQVPSTGERVsenPTLNEVAEKGGYSLAQVLIAWGLRRGYV--VLPKSSTPSRIE 270
|
330 340
....*....|....*....|..
gi 510806721 305 DNLKALDhlaFSKEELTQIDAI 326
Cdd:cd19122 271 SNFKSIE---LSDEDFEAINQV 289
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
21-326 |
1.37e-14 |
|
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: 72.44 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 21 GLKLPAISLGLWHNFGDvDTLDnqraIVRAAFDHGITHFDLANNYGppagsAEINFGRILKEDMFPyRDELIISSKagyy 100
Cdd:cd19127 6 GVEMPALGLGVFQTPPE-ETAD----AVATALADGYRLIDTAAAYG-----NEREVGEGIRRSGVD-RSDIFVTTK---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 101 MWPGPYGEWGSRKSIiascEQSLKRMGLDYVDIFYSHRPDPdTPLEETAL---ALDQLVRQGKTLYVGVSNYSAEQTAEI 177
Cdd:cd19127 71 LWISDYGYDKALRGF----DASLRRLGLDYVDLYLLHWPVP-NDFDRTIQaykALEKLLAEGRVRAIGVSNFTPEHLERL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 178 SKifqelRTPFIIHQPRYNMFDRWIEDGLTDVLAEEGIGTITFSPLAqGLLTNRYLHGipeDSRAHRSDSPFLTEdnvqs 257
Cdd:cd19127 146 ID-----ATTVVPAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIG-GVMRYGASGP---TGPGDVLQDPTITG----- 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 510806721 258 tievvkqlndIAEKRGQTLAEMALAWNLRQPTVT---SVliGASRVSQledNLKALDhLAFSKEELTQIDAI 326
Cdd:cd19127 212 ----------LAEKYGKTPAQIVLRWHLQNGVSAipkSV--HPERIAE---NIDIFD-FALSAEDMAAIDAL 267
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
21-326 |
7.19e-14 |
|
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: 70.62 E-value: 7.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 21 GLKLPAISLGLWHnFGDVDTLDNQraiVRAAFDHGITHFDLANNYgppagSAEINFGRILKEDMFPyRDELIISSKagyy 100
Cdd:cd19156 6 GVEMPRLGLGVWR-VQDGAEAENA---VKWAIEAGYRHIDTAAIY-----KNEEGVGQGIRESGVP-REEVFVTTK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 101 MWPGPYGewgsRKSIIASCEQSLKRMGLDYVDIFYSHRPDPDTpLEETALALDQLVRQGKTLYVGVSNYSAEQtaeISKI 180
Cdd:cd19156 72 LWNSDQG----YESTLAAFEESLEKLGLDYVDLYLIHWPVKGK-FKDTWKAFEKLYKEKKVRAIGVSNFHEHH---LEEL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 181 FQELRTPFIIHQ----PRYNmfdrwiEDGLTDVLAEEGIGTITFSPLAQG-LLTNrylhgipedsrahrsdsPFLTEdnv 255
Cdd:cd19156 144 LKSCKVAPMVNQielhPLLT------QEPLRKFCKEKNIAVEAWSPLGQGkLLSN-----------------PVLKA--- 197
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510806721 256 qstievvkqlndIAEKRGQTLAEMALAWNLRQPTVTsvLIGASRVSQLEDNLKALDhLAFSKEELTQIDAI 326
Cdd:cd19156 198 ------------IGKKYGKSAAQVIIRWDIQHGIIT--IPKSVHEERIQENFDVFD-FELTAEEIRQIDGL 253
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
20-326 |
1.91e-13 |
|
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: 69.48 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 20 SGLKLPAISLGLWH-NFGDVdtldnqRAIVRAAFDHGITHFDLANNYGppagsAEINFGRILKE--DMFPYRDELIISSK 96
Cdd:cd19121 8 TGASIPAVGLGTWQaKAGEV------KAAVAHALKIGYRHIDGALCYQ-----NEDEVGEGIKEaiAGGVKREDLFVTTK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 97 AgyymwpgpygeWGSRKSIIASC-EQSLKRMGLDYVDIFYSHRP----------------------DPDTPLEETALALD 153
Cdd:cd19121 77 L-----------WSTYHRRVELClDRSLKSLGLDYVDLYLVHWPvllnpngnhdlfptlpdgsrdlDWDWNHVDTWKQME 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 154 QLVRQGKTLYVGVSNYSaeqtaeISKIFQELRTPFIIhqPRYNMFD---RWIEDGLTDVLAEEGIGTITFSPLAQglltn 230
Cdd:cd19121 146 KVLKTGKTKAIGVSNYS------IPYLEELLKHATVV--PAVNQVEnhpYLPQQELVDFCKEKGILIEAYSPLGS----- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 231 rylhgipedsrahrSDSPFLTEDNVqstievvkqlNDIAEKRGQTLAEMALAWNLRQPTVtsVLIGASRVSQLEDNLKAL 310
Cdd:cd19121 213 --------------TGSPLISDEPV----------VEIAKKHNVGPGTVLISYQVARGAV--VLPKSVTPDRIKSNLEII 266
|
330
....*....|....*.
gi 510806721 311 DhlaFSKEELTQIDAI 326
Cdd:cd19121 267 D---LDDEDMNKLNDI 279
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
20-326 |
1.04e-12 |
|
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: 67.86 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 20 SGLKLPAISLGLWHNfgDVDTLDNQraiVRAAFDHGITHFDLANNYGppaGSAEINFG--RILKEDMFPyRDELIISSKa 97
Cdd:cd19113 7 SGYKMPSVGFGCWKL--DNATAADQ---IYQAIKAGYRLFDGAEDYG---NEKEVGEGvnRAIDEGLVK-REELFLTSK- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 98 gyyMWpgpyGEWGSRKSIIASCEQSLKRMGLDYVDIFYSHRP-------------------------DPDTPLEETALAL 152
Cdd:cd19113 77 ---LW----NNFHDPKNVETALNKTLSDLKLDYVDLFLIHFPiafkfvpieekyppgfycgdgdnfvYEDVPILDTWKAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 153 DQLVRQGKTLYVGVSNYSAE------QTAEISKIFQElrtpfIIHQPrYNMFDRWIE----DGLTdVLAEEGIGTITFSP 222
Cdd:cd19113 150 EKLVDAGKIKSIGVSNFPGAlildllRGATIKPAVLQ-----IEHHP-YLQQPKLIEyaqkAGIT-ITAYSSFGPQSFVE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 223 LAQGlltnrylhgipedsRAhrSDSPFLTEDnvqstiEVVKQlndIAEKRGQTLAEMALAWNLRQPtvTSVLIGASRVSQ 302
Cdd:cd19113 223 LNQG--------------RA--LNTPTLFEH------DTIKS---IAAKHNKTPAQVLLRWATQRG--IAVIPKSNLPER 275
|
330 340
....*....|....*....|....
gi 510806721 303 LEDNLKaLDHLAFSKEELTQIDAI 326
Cdd:cd19113 276 LLQNLS-VNDFDLTKEDFEEIAKL 298
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-331 |
4.44e-12 |
|
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: 65.83 E-value: 4.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 17 LGKSGLKLPA-ISLGLWHNFGDVDTLDNQRA----IVRAAFDHGITHFDLANNYGppagSAEINFGRILKEDMFPyRDEL 91
Cdd:cd19098 5 LGLAALGRPGyINLGHAADLGSGRSVEAMRAhthaVLDAAWAAGVRYFDAARSYG----RAEEFLGSWLRSRNIA-PDAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 92 IISSKAGYYmwpgpY-GEWG-----------SRKSIIASCEQSLKRMGlDYVDIFYSHRPDPDTP-LEETAL--ALDQLV 156
Cdd:cd19098 80 FVGSKWGYT-----YtADWQvdaavhevkdhSLARLLKQWEETRSLLG-KHLDLYQIHSATLESGvLEDADVlaALAELK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 157 RQGktLYVGVSNYSAEQTAEISK---IFQELRTPFIIHQPRYNMFDRWIEDGLTDVlAEEGIGTITFSPLAQGLLTNRyl 233
Cdd:cd19098 154 AEG--VKIGLSLSGPQQAETLRRaleIEIDGARLFDSVQATWNLLEQSAGEALEEA-HEAGMGVIVKEALANGRLTDR-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 234 hgipedsrahrSDSPfltednvqSTIEVVKQLNDIAEKRGQTLAEMALAWNLRQPTVTSVLIGASRVSQLEDNLKALDhl 313
Cdd:cd19098 229 -----------NPSP--------ELAPLMAVLKAVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRALD-- 287
|
330
....*....|....*...
gi 510806721 314 afsKEELTQIDAILAKLT 331
Cdd:cd19098 288 ---VSLDLELLAALADLA 302
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
21-323 |
7.94e-12 |
|
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: 65.13 E-value: 7.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 21 GLKLPAISLGLWHN-FGDVdtldnqRAIVRAAFDHGITHFDLANNYGPP-----AGSAEINFGRILKEDMFpyrdeliIS 94
Cdd:cd19107 1 GAKMPILGLGTWKSpPGQV------TEAVKVAIDAGYRHIDCAYVYQNEnevgeAIQEKIKEQVVKREDLF-------IV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 95 SKagyyMWPGPYgewgSRKSIIASCEQSLKRMGLDYVDIFYSHRPD-------------------PDTPLEETALALDQL 155
Cdd:cd19107 68 SK----LWCTFH----EKGLVKGACQKTLSDLKLDYLDLYLIHWPTgfkpgkelfpldesgnvipSDTTFLDTWEAMEEL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 156 VRQGKTLYVGVSNYSAEQtaeISKIfqeLRTPFIIHQPRYNMFD---RWIEDGLTDVLAEEGIGTITFSPLaqglltnry 232
Cdd:cd19107 140 VDEGLVKAIGVSNFNHLQ---IERI---LNKPGLKYKPAVNQIEchpYLTQEKLIQYCQSKGIVVTAYSPL--------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 233 lhGIPEDSRAHRSDsPFLTEDnvqstievvKQLNDIAEKRGQTLAEMALAWNLRQPTVtsVLIGASRVSQLEDNLKALDh 312
Cdd:cd19107 205 --GSPDRPWAKPED-PSLLED---------PKIKEIAAKHNKTTAQVLIRFPIQRNLV--VIPKSVTPERIAENFKVFD- 269
|
330
....*....|.
gi 510806721 313 LAFSKEELTQI 323
Cdd:cd19107 270 FELSSEDMATI 280
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
20-326 |
1.87e-11 |
|
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: 63.67 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 20 SGLKLPAISLGLWHnfgDVDTLDNQRAIVRAAFDHGITHFDLANNYGppagsAEINFGRILK---EDMFPYRDELIISSK 96
Cdd:cd19119 8 TGASIPALGLGTAS---PHEDRAEVKEAVEAAIKEGYRHIDTAYAYE-----TEDFVGEAIKraiDDGSIKREELFITTK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 97 agyyMWPGPYgewgsrKSIIASCEQSLKRMGLDYVDIFYSHRPDP------DTPLEETALALDQLVR------------- 157
Cdd:cd19119 80 ----VWPTFY------DEVERSLDESLKALGLDYVDLLLVHWPVCfekdsdDSGKPFTPVNDDGKTRyaasgdhittykq 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 158 ------QGKTLYVGVSNYSAEQtaeISKIFQELRTPFIIHQ----PRYNMFDrwiedgLTDVLAEEGIGTITFSPLAQgl 227
Cdd:cd19119 150 lekiylDGRAKAIGVSNYSIVY---LERLIKECKVVPAVNQvelhPHLPQMD------LRDFCFKHGILVTAYSPLGS-- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 228 ltnrylHGIPedsrAHRsdspfltednvqstIEVVKQlndIAEKRGQTLAEMALAWNLRQPTVtsVLIGASRVSQLEDNL 307
Cdd:cd19119 219 ------HGAP----NLK--------------NPLVKK---IAEKYNVSTGDILISYHVRQGVI--VLPKSLKPVRIVSNG 269
|
330
....*....|....*....
gi 510806721 308 KAldhLAFSKEELTQIDAI 326
Cdd:cd19119 270 KI---VSLTKEDLQKLDDI 285
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
21-326 |
8.97e-11 |
|
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: 61.77 E-value: 8.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 21 GLKLPAISLGLWHNFGDVDTldnqrAIVRAAFDHGITHFDLANNYGPPAGSAE-----INFGRILKEDMFpyrdeliISS 95
Cdd:cd19155 9 GEKMPVVGLGTWQSSPEEIE-----TAVDTALEAGYRHIDTAYVYRNEAAIGNvlkkwIDSGKVKREELF-------IVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 96 KAgyymwpgPYGewGSRKSIIASC-EQSLKRMGLDYVDIFYSHRP---------------------DPDTPLEETALALD 153
Cdd:cd19155 77 KL-------PPG--GNRREKVEKFlLKSLEKLQLDYVDLYLIHFPvgslskeddsgkldptgehkqDYTTDLLDIWKAME 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 154 QLVRQGKTLYVGVSNYSAEQTAEISKIFQ--------ELRTPFiihQPRynmfdrwiedGLTDVLAEEGIGTITFSPLAQ 225
Cdd:cd19155 148 AQVDQGLTRSIGLSNFNREQMARILKNARikpanlqvELHVYL---QQK----------DLVDFCSTHSITVTAYAPLGS 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 226 GLLTNRYlhgipedsrAHRSDSPFLTEDNVQstIEVVKQlndIAEKRGQTLAEMALAWNLRqpTVTSVLIGASRVSQLED 305
Cdd:cd19155 215 PGAAHFS---------PGTGSPSGSSPDLLQ--DPVVKA---IAERHGKSPAQVLLRWLMQ--RGVVVIPKSTNAARIKE 278
|
330 340
....*....|....*....|.
gi 510806721 306 NLKALDhLAFSKEELTQIDAI 326
Cdd:cd19155 279 NFQVFD-FELTEADMAKLSSL 298
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
21-306 |
9.88e-11 |
|
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: 61.70 E-value: 9.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 21 GLKLPAISLG-LWHnfgdvDTLDNQRAiVRAAFDHGITHFDLANNYGPPAGSAEInFGRILKEDMFPyRDELIISSKAgy 99
Cdd:cd19129 3 SGAIPALGFGtLIP-----DPSATRNA-VKAALEAGFRHFDCAERYRNEAEVGEA-MQEVFKAGKIR-REDLFVTTKL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 100 ymwpgpygeWGSR---KSIIASCEQSLKRMGLDYVDIFYSHRP--------------------DPDTPLEETALALDQLV 156
Cdd:cd19129 73 ---------WNTNhrpERVKPAFEASLKRLQLDYLDLYLIHTPfafqpgdeqdprdangnviyDDGVTLLDTWRAMERLV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 157 RQGKTLYVGVSNYSAEQTAEiskIFQELR-TPFIIHQPRYNMFDRWiedGLTDVLAEEGIGTITFSPLAQGLltnrylhg 235
Cdd:cd19129 144 DEGRCKAIGLSDVSLEKLRE---IFEAARiKPAVVQVESHPYLPEW---ELLDFCKNHGIVLQAFAPLGHGM-------- 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510806721 236 ipedsrahrsdSPFLTEDNVQSTievvkqlndIAEKRGQTLAEMALAWNLRQPtvTSVLIGASRVSQLEDN 306
Cdd:cd19129 210 -----------EPKLLEDPVITA---------IARRVNKTPAQVLLAWAIQRG--TALLTTSKTPSRIREN 258
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
23-173 |
1.98e-10 |
|
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) from Mus musculus (liver, AKR1E1) and Homo sapiens (AKR1E2). 1,5-anhydro-D-fructose reductase), also called AF reductase, or aldo-keto reductase family 1 member C-like protein 2 (AKR1CL2), catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. AKR1E2 is a testis aldo-keto reductase (tAKR), which is also known as testis-specific protein (TSP), or LoopADR.
Pssm-ID: 381336 [Multi-domain] Cd Length: 301 Bit Score: 60.74 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 23 KLPAISLGLWH-NFGDVDTldnqraIVRAAFDHGITHFDLA----NNYGPPAG-SAEINFGRILKEDMFpyrdeliISSK 96
Cdd:cd19110 3 DIPAVGLGTWKaSPGEVTE------AVKVAIDAGYRHFDCAylyhNESEVGAGiREKIKEGVVRREDLF-------IVSK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 97 agyyMWPGPYgewgsRKSIIAS-CEQSLKRMGLDYVDIFYSHRP------DPDTPLEETAL-------------ALDQLV 156
Cdd:cd19110 70 ----LWCTCH-----KKSLVKTaCTRSLKALKLNYLDLYLIHWPmgfkpgEPDLPLDRSGMvipsdtdfldtweAMEDLV 140
|
170
....*....|....*..
gi 510806721 157 RQGKTLYVGVSNYSAEQ 173
Cdd:cd19110 141 IEGLVKNIGVSNFNHEQ 157
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
20-326 |
2.56e-10 |
|
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose reductase xyl1 (XR, EC 1.1.1.307) is a founding member of aldo-keto reductase family 2 member D1 (AKR2D1). It catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol in a NAD(P)H dependent manner.
Pssm-ID: 381341 [Multi-domain] Cd Length: 311 Bit Score: 60.51 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 20 SGLKLPAISLGLWHNfgDVDTLDNQraiVRAAFDHGITHFDLANNYGppaGSAEINFG--RILKEDMFPyRDELIISSKA 97
Cdd:cd19115 9 SGYDMPLVGFGLWKV--NNDTCADQ---VYNAIKAGYRLFDGACDYG---NEVEAGQGvaRAIKEGIVK-REDLFIVSKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 98 gyymwpgpygeWGS---RKSIIASCEQSLKRMGLDYVDIFYSHRP------DP------------------DTPLEETAL 150
Cdd:cd19115 80 -----------WNTfhdGERVEPICRKQLADWGIDYFDLFLIHFPialkyvDPavryppgwfydgkkvefsNAPIQETWT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 151 ALDQLVRQGKTLYVGVSNYSAE------QTAEIS-KIFQELRTPFIIhQPRynmfdrwiedgLTDVLAEEGIGTITFSPL 223
Cdd:cd19115 149 AMEKLVDKGLARSIGVSNFSAQllmdllRYARIRpATLQIEHHPYLT-QPR-----------LVKYAQKEGIAVTAYSSF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 224 A-QGLLtnrylhgipEDSRAHRSDSPFLTEDNVqstievvkqLNDIAEKRGQTLAEMALAWNLRQPtvTSVLIGASRVSQ 302
Cdd:cd19115 217 GpQSFL---------ELDLPGAKDTPPLFEHDV---------IKSIAEKHGKTPAQVLLRWATQRG--IAVIPKSNNPKR 276
|
330 340
....*....|....*....|....
gi 510806721 303 LEDNLKALDhLAFSKEELTQIDAI 326
Cdd:cd19115 277 LAQNLDVTG-FDLEAEEIKAISAL 299
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
21-330 |
1.19e-09 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 58.16 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 21 GLKLPAISLGLWHnfgdvdtLDNQRAI--VRAAFDHGITHFDLANNYGppagsAEINFGRILKEDMFPyRDELIISSKAg 98
Cdd:PRK11565 12 GNVMPQLGLGVWQ-------ASNEEVItaIHKALEVGYRSIDTAAIYK-----NEEGVGKALKEASVA-REELFITTKL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 99 yymwpgpygeWGSR-KSIIASCEQSLKRMGLDYVDIFYSHRPDP--DTPLEetalALDQLV---RQGKTLYVGVSNYsae 172
Cdd:PRK11565 78 ----------WNDDhKRPREALEESLKKLQLDYVDLYLMHWPVPaiDHYVE----AWKGMIelqKEGLIKSIGVCNF--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 173 QTAEISKIFQELR-TPFI----IH---QPRynMFDRWIedgltdvlAEEGIGTITFSPLAQGlltnrylhgipedsrahr 244
Cdd:PRK11565 141 QIHHLQRLIDETGvTPVInqieLHplmQQR--QLHAWN--------ATHKIQTESWSPLAQG------------------ 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 245 SDSPFlteDNvqstiEVVKQLndiAEKRGQTLAEMALAWNLRQPTVtsVLIGASRVSQLEDNLKALDhLAFSKEELTQId 324
Cdd:PRK11565 193 GKGVF---DQ-----KVIRDL---ADKYGKTPAQIVIRWHLDSGLV--VIPKSVTPSRIAENFDVFD-FRLDKDELGEI- 257
|
....*.
gi 510806721 325 ailAKL 330
Cdd:PRK11565 258 ---AKL 260
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
21-311 |
2.90e-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: 51.40 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 21 GLKLPAISLGLWHnfgdVDTLDNQRAIVRAaFDHGITHFDLANNYGPPAGSAE-----INFGRILKEDMFpyrdeliISS 95
Cdd:cd19114 1 GDKMPLVGFGTAK----IKANETEEVIYNA-IKVGYRLIDGALLYGNEAEVGRgirkaIQEGLVKREDLF-------IVT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 96 KagyyMWpgpyGEWGSRKSIIASCEQSLKRMGLDYVDIFYSHRP-----------------DPDT--------PLEETAL 150
Cdd:cd19114 69 K----LW----NNFHGKDHVREAFDRQLKDYGLDYIDLYLIHFPipaayvdpaenypflwkDKELkkfpleqsPMQECWR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 151 ALDQLVRQGKTLYVGVSNYSAEQTAEI---SKIfqelrTPFII---HQPrYNMFDRWIedgltDVLAEEGIGTITFSPLA 224
Cdd:cd19114 141 EMEKLVDAGLVRNIGIANFNVQLILDLltyAKI-----KPAVLqieHHP-YLQQKRLI-----DWAKKQGIQITAYSSFG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 225 QGLLTNRYLHGipedsrahRSDSPFLTEDNVQStievvkqlndIAEKRGQTLAEMALAWNLRQPTVtsVLIGASRVSQLE 304
Cdd:cd19114 210 NAVYTKVTKHL--------KHFTNLLEHPVVKK----------LADKHKRDTGQVLLRWAVQRNIT--VIPKSVNVERMK 269
|
....*..
gi 510806721 305 DNLKALD 311
Cdd:cd19114 270 TNLDITS 276
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
21-326 |
2.49e-05 |
|
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes 3-oxo-5-beta-steroid 4-dehydrogenase (EC 1.3.1.3) from Homo sapiens (AKR1D1), Rattus norvegicus (liver, AKR1D2), and Oryctolagus cuniculus (AKR1D3). 3-oxo-5-beta-steroid 4-dehydrogenase, also called delta(4)-3-ketosteroid 5-beta-reductase (EC 1.3.99.6), or delta(4)-3-oxosteroid 5-beta-reductase, or 5-beta-reductase, efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites.
Pssm-ID: 381335 [Multi-domain] Cd Length: 308 Bit Score: 45.18 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 21 GLKLPAISLGlwhNFGDVDT--LDNQRAIVRAAFDHGITHFDLANNYGPPAGSAE-----INFGRILKEDMFpYRDELII 93
Cdd:cd19109 1 GNSIPIIGLG---TYSEPKTtpKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQairekIAEGKVKREDIF-YCGKLWN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 94 SSKAGYYMWPgpygewgsrksiiaSCEQSLKRMGLDYVDIFYSHRP------DPDTPLEE-------------TALALDQ 154
Cdd:cd19109 77 TCHPPELVRP--------------TLERTLKVLQLDYVDLYIIEMPmafkpgDEIYPRDEngkwlyhktnlcaTWEALEA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 155 LVRQGKTLYVGVSNYSAEQTAEIskifqeLRTPFIIHQPRYNMFD---RWIEDGLTDVLAEEGIGTITFSPLaqglltnr 231
Cdd:cd19109 143 CKDAGLVKSIGVSNFNRRQLELI------LNKPGLKHKPVSNQVEchpYFTQPKLLEFCQQHDIVIVAYSPL-------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 232 ylhGIPEDSRAHRSDSPFLTEDNVqstievvkqLNDIAEKRGQTLAEMALAWNLRQPTVtsVLIGASRVSQLEDNLKALD 311
Cdd:cd19109 209 ---GTCRDPIWVNVSSPPLLEDPL---------LNSIGKKYNKTAAQVVLRFNIQRGVV--VIPKSFNPERIKENFQIFD 274
|
330
....*....|....*
gi 510806721 312 hLAFSKEELTQIDAI 326
Cdd:cd19109 275 -FSLTEEEMKDIEAL 288
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
51-311 |
1.02e-04 |
|
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: 43.37 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 51 AFDHGITHFDLANNYG--PPAGSA---EINFGRILKEDMFpyrdeliISSKagyyMWPGPYgewgsRKSIIASC-EQSLK 124
Cdd:cd19108 36 AIDAGFRHIDSAYLYQneEEVGQAirsKIADGTVKREDIF-------YTSK----LWCTFH-----RPELVRPAlEKSLK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 125 RMGLDYVDIFYSHRPDPDTPLEETaLALDQlvrQGKTLY-----------------------VGVSNYSAEQTAEIskif 181
Cdd:cd19108 100 KLQLDYVDLYLIHFPVALKPGEEL-FPKDE---NGKLIFdtvdlcatweamekckdaglaksIGVSNFNRRQLEMI---- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 182 qeLRTPFIIHQPRYNMFDRWI---EDGLTDVLAEEGIGTITFSPLAqgllTNRYLHGIPEdsrahrsDSPFLTEDNVqst 258
Cdd:cd19108 172 --LNKPGLKYKPVCNQVECHPylnQSKLLDFCKSKDIVLVAYSALG----SQRDKEWVDQ-------NSPVLLEDPV--- 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 510806721 259 ievvkqLNDIAEKRGQTLAEMALAWNLRQPTVtsVLIGASRVSQLEDNLKALD 311
Cdd:cd19108 236 ------LCALAKKHKRTPALIALRYQLQRGVV--VLAKSFNEKRIKENLQVFE 280
|
|
| PRK14863 |
PRK14863 |
bifunctional regulator KidO; Provisional |
117-303 |
1.74e-03 |
|
bifunctional regulator KidO; Provisional
Pssm-ID: 184865 [Multi-domain] Cd Length: 292 Bit Score: 39.51 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 117 ASCEQSLKRMGLDYVDIFYSHRPDPDTPLEETAL--ALDQLVRQGKTLYVGVSNYSAEQTAEISKIFQelrtPFIIHQPR 194
Cdd:PRK14863 90 AEARASLRRMGVERADAILVHSPTELFGPHGAALweRLQALKDQGLFAKIGVSAHASDDPVGVARRFK----PDILQAPA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806721 195 YNMFDRWIEDGLTDVLAEEGIGTITFSPLAQGLLtnrYLHgiPEDSRAHRSDSpfltednvQSTIEVVKQLndIAEKRGQ 274
Cdd:PRK14863 166 SLLDQRLLADGSLQRIAGMGVEVHLRSIFLNGLL---FLP--PDRVPAQLKGA--------SGRLSRVRRM--IAEGRSD 230
|
170 180
....*....|....*....|....*....
gi 510806721 275 TLaEMALAWNLRQPTVTSVLIGASRVSQL 303
Cdd:PRK14863 231 PL-QAALGFALSRPEGSAVLVGVNSAAEL 258
|
|
| |
