|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
41-356 |
6.54e-111 |
|
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: 325.72 E-value: 6.54e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 41 VPLAIGTWQAGNKLLYDYSPERDEALLAAWSLARDRGVRYFDTGDSYGTGdiegNAELLLGRFAGG---GADAYVHTKLA 117
Cdd:cd19093 3 SPLGLGTWQWGDRLWWGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYGTG----RSERLLGRFLKElgdRDEVVIATKFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 118 VYPWRLRPDDFVRACEQSLKRLGAERVALVGQHWSAETYGlggiQDPAVYGGLAKCCELGYASGVGLSNLGPRALGRGVD 197
Cdd:cd19093 79 PLPWRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYS----QIEALMDGLADAVEEGLVRAVGVSNYSADQLRRAHK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 198 AVNGLGARVATHQTQFSLLCRAPLEDGSFDVADAAGVTTVGYSPLALGLLSGRYSADAARSFGDrgadasalpklprgvR 277
Cdd:cd19093 155 ALKERGVPLASNQVEYSLLYRDPEQNGLLPACDELGITLIAYSPLAQGLLTGKYSPENPPPGGR---------------R 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 323456385 278 GFLFRTQLPKLAPLLDALEQVAADRKATVGQVALAWCLNArgpgkpPPLPLVGARTPAMVRDVLGALDVKLDAGDVAGL 356
Cdd:cd19093 220 RLFGRKNLEKVQPLLDALEEIAEKYGKTPAQVALNWLIAK------GVVPIPGAKNAEQAEENAGALGWRLSEEEVAEL 292
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
42-365 |
7.67e-52 |
|
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: 174.98 E-value: 7.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 42 PLAIGTWQAGNkllyDYSPERDEALLAAWSLARDRGVRYFDTGDSYGTGDiegnAELLLGRFAGGGA--DAYVHTKLA-- 117
Cdd:COG0667 15 RLGLGTMTFGG----PWGGVDEAEAIAILDAALDAGINFFDTADVYGPGR----SEELLGEALKGRPrdDVVIATKVGrr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 118 ----VYPWRLRPDDFVRACEQSLKRLGAERVALVGQHWSaetyglggiqDPAV-----YGGLAKCCELGYASGVGLSNLG 188
Cdd:COG0667 87 mgpgPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRP----------DPDTpieetLGALDELVREGKIRYIGVSNYS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 189 PRALGRGVDAVNGLgARVATHQTQFSLLCRAPlEDGSFDVADAAGVTTVGYSPLALGLLSGRYSADAARSFGDRGAdasa 268
Cdd:COG0667 157 AEQLRRALAIAEGL-PPIVAVQNEYSLLDRSA-EEELLPAARELGVGVLAYSPLAGGLLTGKYRRGATFPEGDRAA---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 269 lpklprgvRGFLFRTQLPKLAPLLDALEQVAADRKATVGQVALAWCLnARgpgKPPPLPLVGARTPAMVRDVLGALDVKL 348
Cdd:COG0667 231 --------TNFVQGYLTERNLALVDALRAIAAEHGVTPAQLALAWLL-AQ---PGVTSVIPGARSPEQLEENLAAADLEL 298
|
330
....*....|....*..
gi 323456385 349 DAGDVAGLADVARRAPQ 365
Cdd:COG0667 299 SAEDLAALDAALAAVPA 315
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
42-362 |
2.49e-45 |
|
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: 157.36 E-value: 2.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 42 PLAIGTWQAGNKllYDYSPERDEALLAAWSLARDRGVRYFDTGDSYGtgdiEGNAELLLGRFAGG-GADAYVHTKlaVYP 120
Cdd:cd19085 3 RLGLGCWQFGGG--YWWGDQDDEESIATIHAALDAGINFFDTAEAYG----DGHSEEVLGKALKGrRDDVVIATK--VSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 121 WRLRPDDFVRACEQSLKRLGAERVALVGQHWSAETYglggiqDPAVY-GGLAKCCELGYASGVGLSNLGPRALGRGVDAv 199
Cdd:cd19085 75 DNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDV------PLEETmEALEKLKEEGKIRAIGVSNFGPAQLEEALDA- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 200 nglgARVATHQTQFSLLCRAPlEDGSFDVADAAGVTTVGYSPLALGLLSGRYSADAARSFGDRgadasalpklprgvRGF 279
Cdd:cd19085 148 ----GRIDSNQLPYNLLWRAI-EYEILPFCREHGIGVLAYSPLAQGLLTGKFSSAEDFPPGDA--------------RTR 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 280 LFRTQLP----KLAPLLDALEQVAADRKATVGQVALAWCLNargpGKPPPLPLVGARTPAMVRDVLGALDVKLDAGDVAG 355
Cdd:cd19085 209 LFRHFEPgaeeETFEALEKLKEIADELGVTMAQLALAWVLQ----QPGVTSVIVGARNPEQLEENAAAVDLELSPSVLER 284
|
....*..
gi 323456385 356 LADVARR 362
Cdd:cd19085 285 LDEISDP 291
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
43-354 |
2.02e-42 |
|
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: 149.77 E-value: 2.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 43 LAIGTWQAGNKLLYdysPERDEALlAAWSLARDRGVRYFDTGDSYGtgdiEGNAELLLGRFAGGGADAY----VHTKL-- 116
Cdd:pfam00248 1 IGLGTWQLGGGWGP---ISKEEAL-EALRAALEAGINFIDTAEVYG----DGKSEELLGEALKDYPVKRdkvvIATKVpd 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 117 --AVYPWRLRPDDFVRACEQSLKRLGAERVALVGQHWSAETYGLggiqdPAVYGGLAKCCELGYASGVGLSNLGPRALgr 194
Cdd:pfam00248 73 gdGPWPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPI-----EETWDALEELKKEGKIRAIGVSNFDAEQI-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 195 gVDAVNGLGARVATHQTQFSLLCRAPlEDGSFDVADAAGVTTVGYSPLALGLLSGRYsadaarsfgDRGADAsalpklPR 274
Cdd:pfam00248 146 -EKALTKGKIPIVAVQVEYNLLRRRQ-EEELLEYCKKNGIPLIAYSPLGGGLLTGKY---------TRDPDK------GP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 275 GVRGFLFRTQLPKLAPLLDALEQVAADRKATVGQVALAWCLNARgpgkPPPLPLVGARTPAMVRDVLGALDVKLDAGDVA 354
Cdd:pfam00248 209 GERRRLLKKGTPLNLEALEALEEIAKEHGVSPAQVALRWALSKP----GVTIPIPGASNPEQLEDNLGALEFPLSDEEVA 284
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
42-356 |
8.28e-37 |
|
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: 134.96 E-value: 8.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 42 PLAIGTWQAGNkllYDYSPERDEALLAAWSLARDRGVRYFDTGDSYGtgdiEGNAELLLGRFAGGGAD-AYVHTKLAVYp 120
Cdd:cd19084 6 RIGLGTWAIGG---TWWGEVDDQESIEAIKAAIDLGINFFDTAPVYG----FGHSEEILGKALKGRRDdVVIATKCGLR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 121 WR--------LRPDDFVRACEQSLKRLGAERVALVGQHWsaetyglggiQDPAV-----YGGLAKCCELGYASGVGLSNL 187
Cdd:cd19084 78 WDggkgvtkdLSPESIRKEVEQSLRRLQTDYIDLYQIHW----------PDPNTpieetAEALEKLKKEGKIRYIGVSNF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 188 GPRALGRGVDAVNglgarVATHQTQFSLLCRAPLEDgSFDVADAAGVTTVGYSPLALGLLSGRYSADAARSFGDRgadas 267
Cdd:cd19084 148 SVEQLEEARKYGP-----IVSLQPPYSMLEREIEEE-LLPYCRENGIGVLPYGPLAQGLLTGKYKKEPTFPPDDR----- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 268 alpklpRGVRGFLFRTQLPKLAPLLDALEQVAADRKATVGQVALAWCLNargpGKPPPLPLVGARTPAMVRDVLGALDVK 347
Cdd:cd19084 217 ------RSRFPFFRGENFEKNLEIVDKLKEIAEKYGKSLAQLAIAWTLA----QPGVTSAIVGAKNPEQLEENAGALDWE 286
|
....*....
gi 323456385 348 LDAGDVAGL 356
Cdd:cd19084 287 LTEEELKEI 295
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
42-356 |
3.88e-32 |
|
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: 122.71 E-value: 3.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 42 PLAIGTWQAGnkllYDYSPERDEALLAAWslaRDRGVRYFDTGDSYGT---GDIEGNAELLLGRF--AGGGADAYV-HTK 115
Cdd:cd19081 11 PLCLGTMVFG----WTADEETSFALLDAF---VDAGGNFIDTADVYSAwvpGNAGGESETIIGRWlkSRGKRDRVViATK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 116 LAVYPWR----LRPDDFVRACEQSLKRLGAERVALVGQHWSaetyglggiqDPAV--------YGGLAKCcelGYASGVG 183
Cdd:cd19081 84 VGFPMGPngpgLSRKHIRRAVEASLRRLQTDYIDLYQAHWD----------DPATpleetlgaLNDLIRQ---GKVRYIG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 184 LSNLGPRALGRGVDAVNGLG-ARVATHQTQFSLLCRAPLEDGSFDVADAAGVTTVGYSPLALGLLSGRYSADAARSFGDR 262
Cdd:cd19081 151 ASNYSAWRLQEALELSRQHGlPRYVSLQPEYNLVDRESFEGELLPLCREEGIGVIPYSPLAGGFLTGKYRSEADLPGSTR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 263 GADASALPKLPRGVRgflfrtqlpklapLLDALEQVAADRKATVGQVALAWCLNargpGKPPPLPLVGARTPAMVRDVLG 342
Cdd:cd19081 231 RGEAAKRYLNERGLR-------------ILDALDEVAAEHGATPAQVALAWLLA----RPGVTAPIAGARTVEQLEDLLA 293
|
330
....*....|....
gi 323456385 343 ALDVKLDAGDVAGL 356
Cdd:cd19081 294 AAGLRLTDEEVARL 307
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
42-357 |
4.30e-30 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 117.00 E-value: 4.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 42 PLAIGTWQA-GNKLLYDYSPERDEALLAAWSLARDRGVRYFDTGDSYGTGdiegNAELLLGR-FAGGGADAYVHTKLAVY 119
Cdd:cd19102 3 TIGLGTWAIgGGGWGGGWGPQDDRDSIAAIRAALDLGINWIDTAAVYGLG----HSEEVVGRaLKGLRDRPIVATKCGLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 120 P-------WRLRPDDFVRACEQSLKRLGAERVALVGQHWSAETYGLggiqdPAVYGGLAKCCELGYASGVGLSNLgPRAL 192
Cdd:cd19102 79 WdeegrirRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEPI-----EEAWGALAELKEEGKVRAIGVSNF-SVDQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 193 GRGVDAVnglgARVATHQTQFSLLCRaPLEDGSFDVADAAGVTTVGYSPLALGLLSGRYSADAARSFGDRGAdasalpkl 272
Cdd:cd19102 153 MKRCQAI----HPIASLQPPYSLLRR-GIEAEILPFCAEHGIGVIVYSPMQSGLLTGKMTPERVASLPADDW-------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 273 PRGVRGFlfrtQLPKLAP---LLDALEQVAADRKATVGQVALAWCLnargPGKPPPLPLVGARTPAMVRDVLGALDVKLD 349
Cdd:cd19102 220 RRRSPFF----QEPNLARnlaLVDALRPIAERHGRTVAQLAIAWVL----RRPEVTSAIVGARRPDQIDETVGAADLRLT 291
|
....*...
gi 323456385 350 AGDVAGLA 357
Cdd:cd19102 292 PEELAEIE 299
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
58-356 |
2.01e-29 |
|
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: 115.39 E-value: 2.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 58 YSPERDEALLAAWSLARDRGVRYFDTGDSYGtgdiEGNAELLLGR-FAGGGADAYVHTKlavYPWRLRPD---------- 126
Cdd:cd19076 26 YGPADEEESIATLHRALELGVTFLDTADMYG----PGTNEELLGKaLKDRRDEVVIATK---FGIVRDPGsgfrgvdgrp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 127 DFVR-ACEQSLKRLGAERVALVGQHwsaetyglggIQDPAV-----YGGLAKCCELGYASGVGLSNLGPRALGRG----- 195
Cdd:cd19076 99 EYVRaACEASLKRLGTDVIDLYYQH----------RVDPNVpieetVGAMAELVEEGKVRYIGLSEASADTIRRAhavhp 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 196 VDAVnglgarvathQTQFSLLCRAPlEDGSFDVADAAGVTTVGYSPLALGLLSGRYsadaaRSFGDRGADasalpklprg 275
Cdd:cd19076 169 ITAV----------QSEYSLWTRDI-EDEVLPTCRELGIGFVAYSPLGRGFLTGAI-----KSPEDLPED---------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 276 vrgfLFRTQLPKL--------APLLDALEQVAADRKATVGQVALAWCLnARgpgkpppLPLV----GARTPAMVRDVLGA 343
Cdd:cd19076 223 ----DFRRNNPRFqgenfdknLKLVEKLEAIAAEKGCTPAQLALAWVL-AQ-------GDDIvpipGTKRIKYLEENVGA 290
|
330
....*....|...
gi 323456385 344 LDVKLDAGDVAGL 356
Cdd:cd19076 291 LDVVLTPEELAEI 303
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
72-359 |
9.40e-26 |
|
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: 105.39 E-value: 9.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 72 LARDRGVRYFDTGDSYGtgdiEGNAELLLGR-FAGGGADAYVHTKLavypwRLRPDD-----------FVRACEQSLKRL 139
Cdd:cd19091 47 IALDAGINFFDTADVYS----EGESEEILGKaLKGRRDDVLIATKV-----RGRMGEgpndvglsrhhIIRAVEASLKRL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 140 GAERVALVGQH-WSAET---YGLGGIQDpavyggLAKCCELGYasgVGLSNLGPRALGR--GVDAVNGLgARVATHQTQF 213
Cdd:cd19091 118 GTDYIDLYQLHgFDALTpleETLRALDD------LVRQGKVRY---IGVSNFSAWQIMKalGISERRGL-ARFVALQAYY 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 214 SLLCRApLEDGSFDVADAAGVTTVGYSPLALGLLSGRYSADAarsfgdrgadasalpKLPRGVRGFLFRTQLP-----KL 288
Cdd:cd19091 188 SLLGRD-LEHELMPLALDQGVGLLVWSPLAGGLLSGKYRRGQ---------------PAPEGSRLRRTGFDFPpvdreRG 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 323456385 289 APLLDALEQVAADRKATVGQVALAWCLnargPGKPPPLPLVGARTPAMVRDVLGALDVKLDAGDVAGLADV 359
Cdd:cd19091 252 YDVVDALREIAKETGATPAQVALAWLL----SRPTVSSVIIGARNEEQLEDNLGAAGLSLTPEEIARLDKV 318
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
73-345 |
6.86e-25 |
|
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: 103.11 E-value: 6.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 73 ARDRGVRYFDTGDSYGTgdIEGNAELLLGRFAGGGADAY-----VHTKLAVYPWRLRPDDF------VRACEQSLKRLGA 141
Cdd:cd19089 38 AFDLGITHFDLANNYGP--PPGSAEENFGRILKRDLRPYrdelvISTKAGYGMWPGPYGDGgsrkylLASLDQSLKRMGL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 142 ERVALVGQHwsaeTYglggiqDPAV-----YGGLAKCCELGYASGVGLSNLGPRALGRGVDAVNGLGARVATHQTQFSLL 216
Cdd:cd19089 116 DYVDIFYHH----RY------DPDTpleetMTALADAVRSGKALYVGISNYPGAKARRAIALLRELGVPLIIHQPRYSLL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 217 CRAPlEDGSFDVADAAGVTTVGYSPLALGLLSGRYsadaarsFGDRGADASALpklpRGVRGFLFRTQLPKLAPLLDALE 296
Cdd:cd19089 186 DRWA-EDGLLEVLEEAGIGFIAFSPLAQGLLTDKY-------LNGIPPDSRRA----AESKFLTEEALTPEKLEQLRKLN 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 323456385 297 QVAADRKATVGQVALAWCLNARgpgkPPPLPLVGARTPAMVRDVLGALD 345
Cdd:cd19089 254 KIAAKRGQSLAQLALSWVLRDP----RVTSVLIGASSPSQLEDNVAALK 298
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
42-246 |
1.48e-24 |
|
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: 100.29 E-value: 1.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 42 PLAIGTWQAGNkllyDYSPERDEALLAAwslARDRGVRYFDTGDSYGTGDiegnAELLLGR-FAGGGA--DAYVHTKLAV 118
Cdd:cd06660 2 RLGLGTMTFGG----DGDEEEAFALLDA---ALEAGGNFFDTADVYGDGR----SERLLGRwLKGRGNrdDVVIATKGGH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 119 YPW------RLRPDDFVRACEQSLKRLGAERVALVGQHWsaetyglggiQDPAVY-----GGLAKCCELGYASGVGLSNL 187
Cdd:cd06660 71 PPGgdpsrsRLSPEHIRRDLEESLRRLGTDYIDLYYLHR----------DDPSTPveetlEALNELVREGKIRYIGVSNW 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 188 GPRALGRGVDAVNGLG-ARVATHQTQFSLLCRAPLEDGSFDVADAAGVTTVGYSPLALGL 246
Cdd:cd06660 141 SAERLAEALAYAKAHGlPGFAAVQPQYSLLDRSPMEEELLDWAEENGLPLLAYSPLARGP 200
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
43-250 |
2.35e-24 |
|
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: 99.86 E-value: 2.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 43 LAIGTWQAGNKLLYDYSPER-DEALLAAWslarDRGVRYFDTGDSYGTgdieGNAELLLGR-FAGGGADAYVHTKL--AV 118
Cdd:cd19086 6 IGFGTWGLGGDWWGDVDDAEaIRALRAAL----DLGINFFDTADVYGD----GHSERLLGKaLKGRRDKVVIATKFgnRF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 119 YPWRLRPDDF-----VRACEQSLKRLGAERVALVGQH-WSAETyglggIQDPAVYGGLAKCCELGYASGVGLSnLGPRAL 192
Cdd:cd19086 78 DGGPERPQDFspeyiREAVEASLKRLGTDYIDLYQLHnPPDEV-----LDNDELFEALEKLKQEGKIRAYGVS-VGDPEE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 323456385 193 GR------GVDAVnglgarvathQTQFSLLCRAPlEDGSFDVADAAGVTTVGYSPLALGLLSGR 250
Cdd:cd19086 152 ALaalrrgGIDVV----------QVIYNLLDQRP-EEELFPLAEEHGVGVIARVPLASGLLTGK 204
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
42-354 |
5.30e-23 |
|
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: 97.73 E-value: 5.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 42 PLAIGTWQAGNKLLYDYSPERDeaLLAAWSLARDRGVRYFDTGDSYGTGdiegNAELLLGRFAGGGADAYV--------- 112
Cdd:cd19149 13 VIGLGTWAIGGGPWWGGSDDNE--SIRTIHAALDLGINLIDTAPAYGFG----HSEEIVGKAIKGRRDKVVlatkcglrw 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 113 HTKLAVYPWR---------LRPDDFVRACEQSLKRLGAERVALVGQHWsaetyglggiQDPAV-----YGGLAKCCELGY 178
Cdd:cd19149 87 DREGGSFFFVrdgvtvyknLSPESIREEVEQSLKRLGTDYIDLYQTHW----------QDVETpieetMEALEELKRQGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 179 ASGVGLSNLGPRALGRGVDAVNglgarVATHQTQFSLLCRApLEDGSFDVADAAGVTTVGYSPLALGLLSGRYSADaaRS 258
Cdd:cd19149 157 IRAIGASNVSVEQIKEYVKAGQ-----LDIIQEKYSMLDRG-IEKELLPYCKKNNIAFQAYSPLEQGLLTGKITPD--RE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 259 FGDRGADAsalpKLPRgvrgFLfRTQLPKLAPLLDALEQVAADRKATVGQVALAWCLnargPGKPPPLPLVGARTPAMVR 338
Cdd:cd19149 229 FDAGDARS----GIPW----FS-PENREKVLALLEKWKPLCEKYGCTLAQLVIAWTL----AQPGITSALCGARKPEQAE 295
|
330
....*....|....*.
gi 323456385 339 DVLGALDVKLDAGDVA 354
Cdd:cd19149 296 ENAKAGDIRLSAEDIA 311
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
46-360 |
1.01e-22 |
|
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: 96.89 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 46 GTWQ-AGNkllYDYSPERDEALLAAWSLArDRGVRYFDTGDSYGtgdiegNAELLLGRF-------AGGGADAYVHTKLA 117
Cdd:cd19101 8 GMWQlSGG---HGGIRDEDAAVRAMAAYV-DAGLTTFDCADIYG------PAEELIGEFrkrlrreRDAADDVQIHTKWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 118 VYPWRLRPD--DFVRACEQSLKRLGAERVALVGQHWSaeTYGLGGIQDPAVYggLAKCCELGYASGVGLSNLGPRALGRG 195
Cdd:cd19101 78 PDPGELTMTraYVEAAIDRSLKRLGVDRLDLVQFHWW--DYSDPGYLDAAKH--LAELQEEGKIRHLGLTNFDTERLREI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 196 VDAvnglGARVATHQTQFSLLCRAPlEDGSFDVADAAGVTTVGYSPLALGLLSGRYsADAARSFGDRGADASaLPKLPRG 275
Cdd:cd19101 154 LDA----GVPIVSNQVQYSLLDRRP-ENGMAALCEDHGIKLLAYGTLAGGLLSEKY-LGVPEPTGPALETRS-LQKYKLM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 276 VRGF----LFRTqlpklapLLDALEQVAADRKATVGQVALAWCLNArgpgKPPPLPLVGARTPAMVRDVLGALDVKLDAG 351
Cdd:cd19101 227 IDEWggwdLFQE-------LLRTLKAIADKHGVSIANVAVRWVLDQ----PGVAGVIVGARNSEHIDDNVRAFSFRLDDE 295
|
....*....
gi 323456385 352 DVAGLADVA 360
Cdd:cd19101 296 DRAAIDAVL 304
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
56-358 |
1.39e-22 |
|
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: 96.53 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 56 YDYSPERDEA--LLAAwslARDRGVRYFDTGDSYGTgdiEGNAELLLGRFAGGGADAYVHTKLAVYP---------WRLR 124
Cdd:cd19078 18 YGPPPDKEEMieLIRK---AVELGITFFDTAEVYGP---YTNEELVGEALKPFRDQVVIATKFGFKIdggkpgplgLDSR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 125 PDDFVRACEQSLKRLGAERVALVGQHWSaetyglggiqDP-----AVYGGLAKCCELGYASGVGLSNLGPRALGRG---- 195
Cdd:cd19078 92 PEHIRKAVEGSLKRLQTDYIDLYYQHRV----------DPnvpieEVAGTMKELIKEGKIRHWGLSEAGVETIRRAhavc 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 196 -VDAVnglgarvathQTQFSLLCRAPlEDGSFDVADAAGVTTVGYSPLALGLLSGRYSADAarSFgDRGADASALPKL-P 273
Cdd:cd19078 162 pVTAV----------QSEYSMMWREP-EKEVLPTLEELGIGFVPFSPLGKGFLTGKIDENT--KF-DEGDDRASLPRFtP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 274 RGVRgflfrtqlpKLAPLLDALEQVAADRKATVGQVALAWCLNARgpgkpppLPLV---GARTPAMVRDVLGALDVKLDA 350
Cdd:cd19078 228 EALE---------ANQALVDLLKEFAEEKGATPAQIALAWLLAKK-------PWIVpipGTTKLSRLEENIGAADIELTP 291
|
....*...
gi 323456385 351 GDVAGLAD 358
Cdd:cd19078 292 EELREIED 299
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
58-354 |
6.28e-22 |
|
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: 94.61 E-value: 6.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 58 YSPERDEALLAAWSLARDRGVRYFDTGDSYGTGDIEGNaELLLGRF---AGGGADAYVHT-KLAVYPWRLRPD---DFVR 130
Cdd:cd19077 19 PNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHAN-LKLLARFfrkYPEYADKVVLSvKGGLDPDTLRPDgspEAVR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 131 A-CEQSLKRLGAERVALVgqhwsaetYGLGGIqDPAVY-----GGLAKCCELGYASGVGLSNLGPRALGRGVDAvnglgA 204
Cdd:cd19077 98 KsIENILRALGGTKKIDI--------FEPARV-DPNVPieetiKALKELVKEGKIRGIGLSEVSAETIRRAHAV-----H 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 205 RVATHQTQFSLLCRAPLEDGSFDVADAAGVTTVGYSPLALGLLSGRYSADAARSFGDrgadasalpklprgVRGFLFRTQ 284
Cdd:cd19077 164 PIAAVEVEYSLFSREIEENGVLETCAELGIPIIAYSPLGRGLLTGRIKSLADIPEGD--------------FRRHLDRFN 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 323456385 285 ---LPKLAPLLDALEQVAADRKATVGQVALAWclnARGPGKPPPLPLVGARTPAMVRDVLGALDVKLDAGDVA 354
Cdd:cd19077 230 genFEKNLKLVDALQELAEKKGCTPAQLALAW---ILAQSGPKIIPIPGSTTLERVEENLKAANVELTDEELK 299
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
42-356 |
1.65e-21 |
|
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: 92.68 E-value: 1.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 42 PLAIGTWQAGNKLLYDYSpeRDEALLAAWSLARDRGVRYFDTGDSYGtgdiEGNAELLLGR-FAGGG-ADAYVHTKlaVY 119
Cdd:cd19072 6 VLGLGTWGIGGGMSKDYS--DDKKAIEALRYAIELGINLIDTAEMYG----GGHAEELVGKaIKGFDrEDLFITTK--VS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 120 PWRLRPDDFVRACEQSLKRLGAERVALVGQHWSaetyglggiqDPAV-----YGGLAKCCELGYASGVGLSNLGPRALGR 194
Cdd:cd19072 78 PDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWP----------NPSIpieetLRAMEELVEEGKIRYIGVSNFSLEELEE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 195 GVDAVNglGARVATHQTQFSLLCRAPlEDGSFDVADAAGVTTVGYSPLALGLLSGrysadaarsfgdrgadasalpklpr 274
Cdd:cd19072 148 AQSYLK--KGPIVANQVEYNLFDREE-ESGLLPYCQKNGIAIIAYSPLEKGKLSN------------------------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 275 gvrgflfrtqlpklAPLLDALEQVAADRKATVGQVALAWCLNARgpgkpPPLPLVGARTPAMVRDVLGALDVKLDAGDVA 354
Cdd:cd19072 200 --------------AKGSPLLDEIAKKYGKTPAQIALNWLISKP-----NVIAIPKASNIEHLEENAGALGWELSEEDLQ 260
|
..
gi 323456385 355 GL 356
Cdd:cd19072 261 RL 262
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
42-356 |
3.19e-21 |
|
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: 92.65 E-value: 3.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 42 PLAIGTWQAGNKLLYDYSPERDEALLAaWSLARDRGVRYFDTGDSYGTGDiegnAELLLGRFAGGGA---DAYVHTKlaV 118
Cdd:cd19079 14 RLCLGCMSFGDPKWRPWVLDEEESRPI-IKRALDLGINFFDTANVYSGGA----SEEILGRALKEFAprdEVVIATK--V 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 119 Y-PWRLRPDD-------FVRACEQSLKRLGAERVALVGQH-WSAET---YGLGGIQDpAVYGGLAKccelgYasgVGLSN 186
Cdd:cd19079 87 YfPMGDGPNGrglsrkhIMAEVDASLKRLGTDYIDLYQIHrWDYETpieETLEALHD-VVKSGKVR-----Y---IGASS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 187 LGP----RALGrgVDAVNGLgARVATHQTQFSLLCR------APLedgsfdvADAAGVTTVGYSPLALGLLSGRYSADAA 256
Cdd:cd19079 158 MYAwqfaKALH--LAEKNGW-TKFVSMQNHYNLLYReeeremIPL-------CEEEGIGVIPWSPLARGRLARPWGDTTE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 257 RSFGDRgaDASALPKLPRGVRGFlfrtqlpklaPLLDALEQVAADRKATVGQVALAWCLNargpGKPPPLPLVGARTPAM 336
Cdd:cd19079 228 RRRSTT--DTAKLKYDYFTEADK----------EIVDRVEEVAKERGVSMAQVALAWLLS----KPGVTAPIVGATKLEH 291
|
330 340
....*....|....*....|
gi 323456385 337 VRDVLGALDVKLDAGDVAGL 356
Cdd:cd19079 292 LEDAVAALDIKLSEEEIKYL 311
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
73-350 |
1.46e-20 |
|
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: 90.71 E-value: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 73 ARDRGVRYFDTGDSYGtgdiEGNAELLLGRFAGGGADAYVHTKLAVYPWRLRPDD-------FVRACEQSLKRLGAERVA 145
Cdd:cd19087 39 ALDAGINFFDTADVYG----GGRSEEIIGRWIAGRRDDIVLATKVFGPMGDDPNDrglsrrhIRRAVEASLRRLQTDYID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 146 LVgQ--HWSAET---YGLGGIQDpavygglakcceLgYASG----VGLSNLG----PRALGrgVDAVNGLgARVATHQTQ 212
Cdd:cd19087 115 LY-QmhHFDRDTpleETLRALDD------------L-VRQGkiryIGVSNFAawqiAKAQG--IAARRGL-LRFVSEQPM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 213 FSLLCRAPlEDGSFDVADAAGVTTVGYSPLALGLLSGRYSADAARSFGDRGADAsalpklpRGVRgflfRTQLPKLAPLL 292
Cdd:cd19087 178 YNLLKRQA-ELEILPAARAYGLGVIPYSPLAGGLLTGKYGKGKRPESGRLVERA-------RYQA----RYGLEEYRDIA 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 323456385 293 DALEQVAADRKATVGQVALAWCLNargpGKPPPLPLVGARTPAMVRDVLGALDVKLDA 350
Cdd:cd19087 246 ERFEALAAEAGLTPASLALAWVLS----HPAVTSPIIGPRTLEQLEDSLAALEITLTP 299
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
42-360 |
2.41e-20 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 90.09 E-value: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 42 PLAIGTWQ-----AGNKLLYDYSPERDEaLLAAWSLARDRGVRYFDTGDSYGtgdiEGNAELLLGRFAGGGA--DAYVHT 114
Cdd:cd19103 6 KIALGTWSwgsggAGGDQVFGNHLDEDT-LKAVFDKAMAAGLNLWDTAAVYG----MGASEKILGEFLKRYPreDYIIST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 115 KLAVYPWRLRPDDFVRACEQSLKRLGAERVALvgqHWsaetyglggIQDPA-VYGGLAKCCELgYASG----VGLSNLGP 189
Cdd:cd19103 81 KFTPQIAGQSADPVADMLEGSLARLGTDYIDI---YW---------IHNPAdVERWTPELIPL-LKSGkvkhVGVSNHNL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 190 RALGRGVDAVNGLGARVATHQTQFSLLCRAPLEDGSFDVADAAGVTTVGYSPLALGLLSGRYSadaarsfgdrgadaSAL 269
Cdd:cd19103 148 AEIKRANEILAKAGVSLSAVQNHYSLLYRSSEEAGILDYCKENGITFFAYMVLEQGALSGKYD--------------TKH 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 270 PkLPRGV-RGFLFRTQLPKLAPLLDALEQVAADRKATVGQVALAWCLnargpgKPPPLPLVGARTPAMVRDVLGALDVKL 348
Cdd:cd19103 214 P-LPEGSgRAETYNPLLPQLEELTAVMAEIGAKHGASIAQVAIAWAI------AKGTTPIIGVTKPHHVEDAARAASITL 286
|
330
....*....|..
gi 323456385 349 DAGDVAGLADVA 360
Cdd:cd19103 287 TDDEIKELEQLA 298
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
59-364 |
4.05e-20 |
|
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: 89.81 E-value: 4.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 59 SPERDEALLAAWSLARDRGVRYFDTGDSYGtgdiegNAELLLGRF----AGGGADAYVHTKLAVY-------PWRLRPDD 127
Cdd:cd19144 29 PPKPDEERFAVLDAAFELGCTFWDTADIYG------DSEELIGRWfkqnPGKREKIFLATKFGIEknvetgeYSVDGSPE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 128 FVR-ACEQSLKRLGAERVALVGQHWSAetyglGGIQDPAVYGGLAKCCELGYASGVGLSNLGPRALGRGVdAVNGLGArV 206
Cdd:cd19144 103 YVKkACETSLKRLGVDYIDLYYQHRVD-----GKTPIEKTVAAMAELVQEGKIKHIGLSECSAETLRRAH-AVHPIAA-V 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 207 ATHQTQFSLLCRAPlEDGSFDVADAAGVTTVGYSPLALGLLSGRYSADAARSFGDrgadasalpklprgvrgflFRTQLP 286
Cdd:cd19144 176 QIEYSPFSLDIERP-EIGVLDTCRELGVAIVAYSPLGRGFLTGAIRSPDDFEEGD-------------------FRRMAP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 287 KLAP--------LLDALEQVAADRKATVGQVALAWCLnARGPGKPPPLplvGARTPAMVRDVLGALDVKLDAGDVAGLAD 358
Cdd:cd19144 236 RFQAenfpknleLVDKIKAIAKKKNVTAGQLTLAWLL-AQGDDIIPIP---GTTKLKRLEENLGALKVKLTEEEEKEIRE 311
|
....*.
gi 323456385 359 VARRAP 364
Cdd:cd19144 312 IAEEAE 317
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
43-352 |
8.23e-20 |
|
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: 88.01 E-value: 8.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 43 LAIGTWQAGNKLLYDYSpeRDEALLAAWSLARDRGVRYFDTGDSYGTGDIE---GNAELLLGRfagggADAYVHTKlaVY 119
Cdd:cd19137 7 LGLGTWGIGGFLTPDYS--RDEEMVELLKTAIELGYTHIDTAEMYGGGHTEelvGKAIKDFPR-----EDLFIVTK--VW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 120 PWRLRPDDFVRACEQSLKRLGAERVALVGQHWSAETYGLggiqdPAVYGGLAKCCELGYASGVGLSNLGPRALGRgvdAV 199
Cdd:cd19137 78 PTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPL-----EETLSAMAEGVRQGLIRYIGVSNFNRRLLEE---AI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 200 NGLGARVATHQTQFSLLCRAPLEDGSFDVADAAGVTTVGYSPLALGLLsgrysadaarsfgdrgadasalpklprgvrgf 279
Cdd:cd19137 150 SKSQTPIVCNQVKYNLEDRDPERDGLLEYCQKNGITVVAYSPLRRGLE-------------------------------- 197
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 323456385 280 lfrtqlpklaPLLDALEQVAADRKATVGQVALAWCLNARGPGKPPPlplvgARTPAMVRDVLGALDVKLDAGD 352
Cdd:cd19137 198 ----------KTNRTLEEIAKNYGKTIAQIALAWLIQKPNVVAIPK-----AGRVEHLKENLKATEIKLSEEE 255
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
73-345 |
1.58e-19 |
|
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: 87.84 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 73 ARDRGVRYFDTGDSYGTgdIEGNAELLLGRFAGGGADAY-----VHTKLAVYPWRLRPDDF------VRACEQSLKRLGA 141
Cdd:cd19151 39 AFDLGITHFDLANNYGP--PPGSAEENFGRILKEDLKPYrdeliISTKAGYTMWPGPYGDWgskkylIASLDQSLKRMGL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 142 ERVALVGQHWSaetyglggiqDP-----AVYGGLAKCCELGYASGVGLSNLGPRALGRGVDAVNGLGARVATHQTQFSLL 216
Cdd:cd19151 117 DYVDIFYHHRP----------DPetpleETMGALDQIVRQGKALYVGISNYPPEEAREAAAILKDLGTPCLIHQPKYSMF 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 217 CRAPlEDGSFDVADAAGVTTVGYSPLALGLLSGRYsadaarsfgdrgadASALPKLPRGVRG--FLFRTQL-PKLAPLLD 293
Cdd:cd19151 187 NRWV-EEGLLDVLEEEGIGCIAFSPLAQGLLTDRY--------------LNGIPEDSRAAKGssFLKPEQItEEKLAKVR 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 323456385 294 ALEQVAADRKATVGQVALAWCLNARgpgkPPPLPLVGARTPAMVRDVLGALD 345
Cdd:cd19151 252 RLNEIAQARGQKLAQMALAWVLRNK----RVTSVLIGASKPSQIEDAVGALD 299
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
43-349 |
2.03e-19 |
|
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: 87.26 E-value: 2.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 43 LAIGTWQA-GNKLLYDYSperdEALLAAwslARDRGVRYFDTGDSYGTGDiegnAELLLGRF-AGGGADAYV-HTKlaVY 119
Cdd:cd19074 7 LSLGTWLTfGGQVDDEDA----KACVRK---AYDLGINFFDTADVYAAGQ----AEEVLGKAlKGWPRESYViSTK--VF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 120 pWRLRPDD---------FVRACEQSLKRLGAERVALVGQH-WSAETyglggiqdpAVYGGLAKCCEL---GYASGVGLSN 186
Cdd:cd19074 74 -WPTGPGPndrglsrkhIFESIHASLKRLQLDYVDIYYCHrYDPET---------PLEETVRAMDDLirqGKILYWGTSE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 187 LGPRALGRGVD-AVNGLGARVATHQTQFSLLCRaPLEDGSFDVADAAGVTTVGYSPLALGLLSGRYsaDAARSFGDRGAD 265
Cdd:cd19074 144 WSAEQIAEAHDlARQFGLIPPVVEQPQYNMLWR-EIEEEVIPLCEKNGIGLVVWSPLAQGLLTGKY--RDGIPPPSRSRA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 266 ASalPKLPRGVRGFLFRTQLPKlaplLDALEQVAADRKATVGQVALAWCLNARgpgkPPPLPLVGARTPAMVRDVLGALD 345
Cdd:cd19074 221 TD--EDNRDKKRRLLTDENLEK----VKKLKPIADELGLTLAQLALAWCLRNP----AVSSAIIGASRPEQLEENVKASG 290
|
....
gi 323456385 346 VKLD 349
Cdd:cd19074 291 VKLS 294
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
71-349 |
1.21e-17 |
|
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: 82.61 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 71 SLARDRGVRYFDTGDSY---GTGDIEGNAELLLGR-FAGGGA--DAYVHTKLAVY----PW------RLRPDDFVRACEQ 134
Cdd:cd19094 25 DYAFDEGVNFIDTAEMYpvpPSPETQGRTEEIIGSwLKKKGNrdKVVLATKVAGPgegiTWprgggtRLDRENIREAVEG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 135 SLKRLGAERVALVGQHWSAETYGLGGIQDPAVYG-------------GLAKCCELGYASGVGLSNLGPRALGRGVDAVNG 201
Cdd:cd19094 105 SLKRLGTDYIDLYQLHWPDRYTPLFGGGYYTEPSeeedsvsfeeqleALGELVKAGKIRHIGLSNETPWGVMKFLELAEQ 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 202 LGA-RVATHQTQFSLLCRAPLEDgsfdVADAA---GVTTVGYSPLALGLLSGRYSADAARSFGDRGADasalpklprgVR 277
Cdd:cd19094 185 LGLpRIVSIQNPYSLLNRNFEEG----LAEAChreNVGLLAYSPLAGGVLTGKYLDGAARPEGGRLNL----------FP 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 323456385 278 GFLFRTQLPKLAPLLDALEQVAADRKATVGQVALAWCLNargpGKPPPLPLVGARTPAMVRDVLGALDVKLD 349
Cdd:cd19094 251 GYMARYRSPQALEAVAEYVKLARKHGLSPAQLALAWVRS----RPFVTSTIIGATTLEQLKENIDAFDVPLS 318
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
73-345 |
5.79e-17 |
|
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: 80.58 E-value: 5.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 73 ARDRGVRYFDTGDSYGTGdiEGNAELLLGR-----FAGGGADAYVHTKLAvypWRLRPDDF---------VRACEQSLKR 138
Cdd:cd19150 39 AFDLGITHFDLANNYGPP--PGSAEENFGRilredFAGYRDELIISTKAG---YDMWPGPYgewgsrkylLASLDQSLKR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 139 LGAERVALVGQH-WSAETyglgGIQDPAvyGGLAKCCELGYASGVGLSNLGPRALGRGVDAVNGLGARVATHQTQFSLLC 217
Cdd:cd19150 114 MGLDYVDIFYSHrFDPDT----PLEETM--GALDHAVRSGKALYVGISSYSPERTREAAAILRELGTPLLIHQPSYNMLN 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 218 RAPLEDGSFDVADAAGVTTVGYSPLALGLLSGRYsadaarsfgdrgadasaLPKLPRGVR-----GFLFRTQLPKLAPLL 292
Cdd:cd19150 188 RWVEESGLLDTLQELGVGCIAFTPLAQGLLTDKY-----------------LNGIPEGSRaskerSLSPKMLTEANLNSI 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 323456385 293 DALEQVAADRKATVGQVALAWCLNargpGKPPPLPLVGARTPAMVRDVLGALD 345
Cdd:cd19150 251 RALNEIAQKRGQSLAQMALAWVLR----DGRVTSALIGASRPEQLEENVGALD 299
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
42-354 |
4.34e-16 |
|
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: 77.84 E-value: 4.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 42 PLAIGTWQAGNKLLYdysPERDEA----LLAAwslARDRGVRYFDTGDSYGTGdiegNAELLLGRFAGGG--ADAYVHTK 115
Cdd:cd19083 13 PIGLGTNAVGGHNLY---PNLDEEegkdLVRE---ALDNGVNLLDTAFIYGLG----RSEELVGEVLKEYnrNEVVIATK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 116 LAVY----PWRL--RPDDFVRACEQSLKRLGAERVALVGQHW-SAETyglggIQDPAVyGGLAKCCELGYASGVGLSNLG 188
Cdd:cd19083 83 GAHKfggdGSVLnnSPEFLRSAVEKSLKRLNTDYIDLYYIHFpDGET-----PKAEAV-GALQELKDEGKIRAIGVSNFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 189 PRALgrgvDAVNGLGArVATHQTQFSLLCRAPLEDgSFDVADAAGVTTVGYSPLALGLLSGRYSADAARSFGDRGADaSA 268
Cdd:cd19083 157 LEQL----KEANKDGY-VDVLQGEYNLLQREAEED-ILPYCVENNISFIPYFPLASGLLAGKYTKDTKFPDNDLRND-KP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 269 LPKLPRgvrgflFRTQLPKlaplLDALEQVAADRKATVGQVALAWCLNargpGKPPPLPLVGARTPAMVRDVLGALDVKL 348
Cdd:cd19083 230 LFKGER------FSENLDK----VDKLKSIADEKGVTVAHLALAWYLT----RPAIDVVIPGAKRAEQVIDNLKALDVTL 295
|
....*.
gi 323456385 349 DAGDVA 354
Cdd:cd19083 296 TEEEIA 301
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
41-356 |
4.99e-16 |
|
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: 77.29 E-value: 4.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 41 VP-LAIGTWQAGNkllydySPERDEALLAAWSLARDRGVRYFDTGDSYGtgdiEGNAELLLGR-FAGGGADAYVHTKlaV 118
Cdd:cd19138 11 VPaLGQGTWYMGE------DPAKRAQEIEALRAGIDLGMTLIDTAEMYG----DGGSEELVGEaIRGRRDKVFLVSK--V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 119 YPWRLRPDDFVRACEQSLKRLGAERVALVGQHWSaetyglGGIQDPAVYGGLAKCCELGYASGVGLSNLGPRALgRGVDA 198
Cdd:cd19138 79 LPSNASRQGTVRACERSLRRLGTDYLDLYLLHWR------GGVPLAETVAAMEELKKEGKIRAWGVSNFDTDDM-EELWA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 199 VNGlGARVATHQTQFSLLCRAPledgSFDV---ADAAGVTTVGYSPLALGllsgrysadaarsfgdrgadasalpklprg 275
Cdd:cd19138 152 VPG-GGNCAANQVLYNLGSRGI----EYDLlpwCREHGVPVMAYSPLAQG------------------------------ 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 276 vrGFLFRTQLPKlapllDALEQVAADRKATVGQVALAWCLNARGPGKPPPlplvgARTPAMVRDVLGALDVKLDAGDVAG 355
Cdd:cd19138 197 --GLLRRGLLEN-----PTLKEIAARHGATPAQVALAWVLRDGNVIAIPK-----SGSPEHARENAAAADLELTEEDLAE 264
|
.
gi 323456385 356 L 356
Cdd:cd19138 265 L 265
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
43-349 |
8.33e-16 |
|
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: 76.49 E-value: 8.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 43 LAIGTWQAGNKLLYDYSPERDEA---LLAAWslarDRGVRYFDTGDSYGTGDiegnAELLLGR-FAGGGADAYVHTKL-A 117
Cdd:cd19088 4 LGYGAMRLTGPGIWGPPADREEAiavLRRAL----ELGVNFIDTADSYGPDV----NERLIAEaLHPYPDDVVIATKGgL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 118 VYP----WRL--RPDDFVRACEQSLKRLGAERVALVGQHWSaetyglggiqDPAV-----YGGLAKCCELGYASGVGLSN 186
Cdd:cd19088 76 VRTgpgwWGPdgSPEYLRQAVEASLRRLGLDRIDLYQLHRI----------DPKVpfeeqLGALAELQDEGLIRHIGLSN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 187 LGPRALGRGVDAVnglgaRVATHQTQFSLLCRAPleDGSFDVADAAGVTTVGYSPLALGllsgrysadaarsfgdrgada 266
Cdd:cd19088 146 VTVAQIEEARAIV-----RIVSVQNRYNLANRDD--EGVLDYCEAAGIAFIPWFPLGGG--------------------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 267 salpklprgvrgflfrtqlpKLAPLLDALEQVAADRKATVGQVALAWCLNArgpgKPPPLPLVGARTPAMVRDVLGALDV 346
Cdd:cd19088 198 --------------------DLAQPGGLLAEVAARLGATPAQVALAWLLAR----SPVMLPIPGTSSVEHLEENLAAAGL 253
|
...
gi 323456385 347 KLD 349
Cdd:cd19088 254 RLS 256
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
42-348 |
1.02e-15 |
|
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: 76.87 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 42 PLAIGTWQAGNKLLYDYSPERDEALLAAWslaRDRGVRYFDTGDSYgtgdIEGNAELLLGRFAGGGADAYV-HTKlavYP 120
Cdd:cd19080 12 PLALGTMTFGTEWGWGADREEARAMFDAY---VEAGGNFIDTANNY----TNGTSERLLGEFIAGNRDRIVlATK---YT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 121 WRLRPDD----------FVRACEQSLKRLGAERVALVGQHWSAETYGLggiqdPAVYGGLAKCCELGYASGVGLSNLgPR 190
Cdd:cd19080 82 MNRRPGDpnaggnhrknLRRSVEASLRRLQTDYIDLLYVHAWDFTTPV-----EEVMRALDDLVRAGKVLYVGISDT-PA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 191 ALGRGVDAV---NGLgARVATHQTQFSLLCRAPLEDgSFDVADAAGVTTVGYSPLALGLLSGRYSADAARSFGDRGADAS 267
Cdd:cd19080 156 WVVARANTLaelRGW-SPFVALQIEYSLLERTPERE-LLPMARALGLGVTPWSPLGGGLLTGKYQRGEEGRAGEAKGVTV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 268 ALPKLPrgvrgflfrtqlPKLAPLLDALEQVAADRKATVGQVALAWCLNargpGKPPPLPLVGARTPAMVRDVLGALDVK 347
Cdd:cd19080 234 GFGKLT------------ERNWAIVDVVAAVAEELGRSAAQVALAWVRQ----KPGVVIPIIGARTLEQLKDNLGALDLT 297
|
.
gi 323456385 348 L 348
Cdd:cd19080 298 L 298
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
42-349 |
3.02e-15 |
|
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: 75.29 E-value: 3.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 42 PLAIGTWQAGNKllyDYSPERDEALLAAwslARDRGVRYFDTGDSYGTGDiegnAELLLGRF---AGGGADAYV-HTKLA 117
Cdd:cd19092 8 RLVLGCMRLADW---GESAEELLSLIEA---ALELGITTFDHADIYGGGK----CEELFGEAlalNPGLREKIEiQTKCG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 118 VY------PWRLRPDDF-----VRACEQSLKRLGAERVALVGQHWSaetyglggiqDP-----AVYGGLAKCCELGYASG 181
Cdd:cd19092 78 IRlgddprPGRIKHYDTskehiLASVEGSLKRLGTDYLDLLLLHRP----------DPlmdpeEVAEAFDELVKSGKVRY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 182 VGLSNLGP---RALGRGVDAvnglgaRVATHQTQFSLLCRAPLEDGSFDVADAAGVTTVGYSPLAlgllsgrysadaars 258
Cdd:cd19092 148 FGVSNFTPsqiELLQSYLDQ------PLVTNQIELSLLHTEAIDDGTLDYCQLLDITPMAWSPLG--------------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 259 fgdrgadasalpklprgvRGFLFRTQLPKLAPLLDALEQVAADRKATVGQVALAWCLN--ARgpgkppPLPLVGARTPAM 336
Cdd:cd19092 207 ------------------GGRLFGGFDERFQRLRAALEELAEEYGVTIEAIALAWLLRhpAR------IQPILGTTNPER 262
|
330
....*....|...
gi 323456385 337 VRDVLGALDVKLD 349
Cdd:cd19092 263 IRSAVKALDIELT 275
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
43-362 |
4.10e-15 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 74.32 E-value: 4.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 43 LAIGTWQAGnkllydysperDEALLAAWSLARDRGVRYFDTGDSYGtgdiegnAELLLGR-FAGGG---ADAYVHTKlaV 118
Cdd:COG0656 8 LGLGTWQLP-----------GEEAAAAVRTALEAGYRHIDTAAMYG-------NEEGVGEaIAASGvprEELFVTTK--V 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 119 YPWRLRPDDFVRACEQSLKRLGAERVALVGQHW-SAETYglggiqdPAVYGGLAKCCELGYASGVGLSNLGPRALgrgVD 197
Cdd:COG0656 68 WNDNHGYDDTLAAFEESLERLGLDYLDLYLIHWpGPGPY-------VETWRALEELYEEGLIRAIGVSNFDPEHL---EE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 198 AVNGLGARVATHQTQFSLLCRaplEDGSFDVADAAGVTTVGYSPLALGllsgrysadaaRSFGDrgadasalpklprgvr 277
Cdd:COG0656 138 LLAETGVKPAVNQVELHPYLQ---QRELLAFCREHGIVVEAYSPLGRG-----------KLLDD---------------- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 278 gflfrtqlpklapllDALEQVAADRKATVGQVALAWCLnARgpgkppplplvG------ARTPAMVRDVLGALDVKLDAG 351
Cdd:COG0656 188 ---------------PVLAEIAEKHGKTPAQVVLRWHL-QR-----------GvvvipkSVTPERIRENLDAFDFELSDE 240
|
330
....*....|.
gi 323456385 352 DVAGLADVARR 362
Cdd:COG0656 241 DMAAIDALDRG 251
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
59-315 |
2.91e-14 |
|
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: 72.47 E-value: 2.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 59 SPERDEALLAAWSLARDRGVRYFDTGDSYGTgdiEGNaELLLGRFAGGGADAYVH--TKLAV-----YPWRLRPD-DFVR 130
Cdd:cd19145 28 APKPEEEGIALIHHAFNSGVTFLDTSDIYGP---NTN-EVLLGKALKDGPREKVQlaTKFGIheiggSGVEVRGDpAYVR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 131 -ACEQSLKRLGAERVALVGQHWSAETyglggIQDPAVYGGLAKCCELGYASGVGLSNLGPRALGRGvDAVNGLGARvath 209
Cdd:cd19145 104 aACEASLKRLDVDYIDLYYQHRIDTT-----VPIEITMGELKKLVEEGKIKYIGLSEASADTIRRA-HAVHPITAV---- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 210 QTQFSLLCRaPLEDGSFDVADAAGVTTVGYSPLALGLLSGRysadaarsfgdrgadasalPKLPRGVRGFLFRTQLPKL- 288
Cdd:cd19145 174 QLEWSLWTR-DIEEEIIPTCRELGIGIVPYSPLGRGFFAGK-------------------AKLEELLENSDVRKSHPRFq 233
|
250 260 270
....*....|....*....|....*....|....
gi 323456385 289 -------APLLDALEQVAADRKATVGQVALAWCL 315
Cdd:cd19145 234 genleknKVLYERVEALAKKKGCTPAQLALAWVL 267
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
43-315 |
6.56e-14 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 71.94 E-value: 6.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 43 LAIGTWQAgnkLLYDYSPERDEALLAAwslARDRGVRYFDTGDSYG--TGDIEGN-AELLLGRFAGGGADAYVHTKLAVY 119
Cdd:PRK09912 28 LSLGLWHN---FGHVNALESQRAILRK---AFDLGITHFDLANNYGppPGSAEENfGRLLREDFAAYRDELIISTKAGYD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 120 PWrlrPDDF---------VRACEQSLKRLGAERVALVGQHWSAETYGLggiQDPAvyGGLAKCCELGYASGVGLSNLGPR 190
Cdd:PRK09912 102 MW---PGPYgsggsrkylLASLDQSLKRMGLEYVDIFYSHRVDENTPM---EETA--SALAHAVQSGKALYVGISSYSPE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 191 ALGRGVDAVNGLGARVATHQTQFSLLCRAPLEDGSFDVADAAGVTTVGYSPLALGLLSGRYSADAarsfgdrgADASALP 270
Cdd:PRK09912 174 RTQKMVELLREWKIPLLIHQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGI--------PQDSRMH 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 323456385 271 KLPRGVRGfLFRTQLPKlAPL--LDALEQVAADRKATVGQVALAWCL 315
Cdd:PRK09912 246 REGNKVRG-LTPKMLTE-ANLnsLRLLNEMAQQRGQSMAQMALSWLL 290
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
43-354 |
1.67e-13 |
|
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: 69.61 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 43 LAIGTWQAgnkllydyspeRDEALLAAWSLARDRGVRYFDTGDSYGTGDIEGNAelllgrFAGGG---ADAYVHTKlaVY 119
Cdd:cd19073 4 LGLGTWQL-----------RGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEA------IAESGvprEDLFITTK--VW 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 120 PWRLRPDDFVRACEQSLKRLGAERVALVGQHWSAETYGLggiqdPAVYGGLAKCCELGYASGVGLSNLGPRALGrgvDAV 199
Cdd:cd19073 65 RDHLRPEDLKKSVDRSLEKLGTDYVDLLLIHWPNPTVPL-----EETLGALKELKEAGKVKSIGVSNFTIELLE---EAL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 200 NGLGARVATHQTQFS-LLCRAPLedgsFDVADAAGVTTVGYSPLAlgllsgrysadaarsfgdrgadasalpklprgvRG 278
Cdd:cd19073 137 DISPLPIAVNQVEFHpFLYQAEL----LEYCRENDIVITAYSPLA---------------------------------RG 179
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 323456385 279 FLFRtqlpklaplLDALEQVAADRKATVGQVALAWCLnargpgKPPPLPLVGARTPAMVRDVLGALDVKLDAGDVA 354
Cdd:cd19073 180 EVLR---------DPVIQEIAEKYDKTPAQVALRWLV------QKGIVVIPKASSEDHLKENLAIFDWELTSEDVA 240
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
64-351 |
5.07e-13 |
|
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: 68.73 E-value: 5.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 64 EALLAAWSLardrGVRYFDTGDSYGtgdiegNAELLLGRF--AGGGADAYVHTKLAVYP---WRLRPDDFVRACEQSLKR 138
Cdd:cd19090 24 ATIRAALDL----GINYIDTAPAYG------DSEERLGLAlaELPREPLVLSTKVGRLPedtADYSADRVRRSVEESLER 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 139 LGAERVALVGQHwSAETYGLGGIQDP-AVYGGLAKCCELGYASGVGLSNLGPRALGRGVDAvnGLGARVATHQtQFSLLC 217
Cdd:cd19090 94 LGRDRIDLLMIH-DPERVPWVDILAPgGALEALLELKEEGLIKHIGLGGGPPDLLRRAIET--GDFDVVLTAN-RYTLLD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 218 RAPLEDgSFDVADAAGVTTVGYSPLALGLLSGRYsaDAARSFGDRGADASALPKlprgvrgflfrtqlpklaplLDALEQ 297
Cdd:cd19090 170 QSAADE-LLPAAARHGVGVINASPLGMGLLAGRP--PERVRYTYRWLSPELLDR--------------------AKRLYE 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 323456385 298 VAADRKATVGQVALAWCLNArgpgKPPPLPLVGARTPAMVRDVLGALDVKLDAG 351
Cdd:cd19090 227 LCDEHGVPLPALALRFLLRD----PRISTVLVGASSPEELEQNVAAAEGPLPEE 276
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
43-316 |
1.19e-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: 381323 [Multi-domain] Cd Length: 267 Bit Score: 67.17 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 43 LAIGTWQAGNkllyDYS-------PERDEA--LLAAwslARDRGVRYFDTGDSYGtgdiegNAELLLGRFAGGGADAYVH 113
Cdd:cd19097 3 LALGTAQFGL----DYGianksgkPSEKEAkkILEY---ALKAGINTLDTAPAYG------DSEKVLGKFLKRLDKFKII 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 114 TKL-AVYPWRLRPDDFVRAC-EQSLKRLGAERVALVGQHWSAETYGlggiQDPAVYGGLAKCCELGYASGVGLSNLGP-- 189
Cdd:cd19097 70 TKLpPLKEDKKEDEAAIEASvEASLKRLKVDSLDGLLLHNPDDLLK----HGGKLVEALLELKKEGLIRKIGVSVYSPee 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 190 --RALGRG-VDAVnglgarvathQTQFSLLCRAPLEDGSFDVADAAGVTTVGYSPLALGLLSgrysadaarsfgdrgADA 266
Cdd:cd19097 146 leKALESFkIDII----------QLPFNILDQRFLKSGLLAKLKKKGIEIHARSVFLQGLLL---------------MEP 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 323456385 267 SALPKLprgvrgflfrtqLPKLAPLLDALEQVAADRKATVGQVALAWCLN 316
Cdd:cd19097 201 DKLPAK------------FAPAKPLLKKLHELAKKLGLSPLELALGFVLS 238
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
40-245 |
4.81e-12 |
|
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: 65.36 E-value: 4.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 40 DVP-LAIGTWqagnkllydysPERDEALLAAWSLARDRGVRYFDTGDSYGTGDIEGNAellLGRFAGGGADAYVHTKlaV 118
Cdd:cd19140 7 RIPaLGLGTY-----------PLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEA---IAASGVPRDELFLTTK--V 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 119 YPWRLRPDDFVRACEQSLKRLGAERVALVGQHWSAETYGLGgiqdpAVYGGLAKCCELGYASGVGLSNLGPRALGrgvDA 198
Cdd:cd19140 71 WPDNYSPDDFLASVEESLRKLRTDYVDLLLLHWPNKDVPLA-----ETLGALNEAQEAGLARHIGVSNFTVALLR---EA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 323456385 199 VNGLGARVATHQTQFS-LLCRAPLEdgsfDVADAAGVTTVGYSPLALG 245
Cdd:cd19140 143 VELSEAPLFTNQVEYHpYLDQRKLL----DAAREHGIALTAYSPLARG 186
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
44-352 |
1.97e-11 |
|
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: 64.25 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 44 AIGTWQAGNkllYDYSPERDEALLAAWSLARDRGVRYFDTGDSYGTGdiegNAELLLGRF---AGGGADAYVHTKLA--- 117
Cdd:cd19148 8 ALGTWAIGG---WMWGGTDEKEAIETIHKALDLGINLIDTAPVYGFG----LSEEIVGKAlkeYGKRDRVVIATKVGlew 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 118 ----VYPWRLRPDDFVRACEQSLKRLGAERVALVGQHWSAEtygLGGIQDPAVYggLAKCCELGYASGVGLSNLGPRALG 193
Cdd:cd19148 81 deggEVVRNSSPARIRKEVEDSLRRLQTDYIDLYQVHWPDP---LVPIEETAEA--LKELLDEGKIRAIGVSNFSPEQME 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 194 RgvdavNGLGARVATHQTQFSLLCRApLEDGSFDVADAAGVTTVGYSPLALGLLSGRYSADAARSFGD-RGADasalPKL 272
Cdd:cd19148 156 T-----FRKVAPLHTVQPPYNLFERE-IEKDVLPYARKHNIVTLAYGALCRGLLSGKMTKDTKFEGDDlRRTD----PKF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 273 prgvrgflfrtQLPKLAPLLDA---LEQVAADR-KATVGQVALAWCLNArgpgKPPPLPLVGARTPAMVRDVLGALDVKL 348
Cdd:cd19148 226 -----------QEPRFSQYLAAveeLDKLAQERyGKSVIHLAVRWLLDQ----PGVSIALWGARKPEQLDAVDEVFGWSL 290
|
....
gi 323456385 349 DAGD 352
Cdd:cd19148 291 NDED 294
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
59-313 |
3.45e-11 |
|
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: 63.34 E-value: 3.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 59 SPERDEALLAAWslaRDRGVRYFDTGDSYGtgdiEGNAELLLGRFAGGGADAYVHTKlaVYPW---RLRPDDFVRACEQS 135
Cdd:cd19075 18 TAEAAAELLDAF---LERGHTEIDTARVYP----DGTSEELLGELGLGERGFKIDTK--ANPGvggGLSPENVRKQLETS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 136 LKRLGAERVALVGQHWS------AETyglggiqdpavyggLAKCCEL---GYASGVGLSNLGPRALGRGVD--AVNGLgA 204
Cdd:cd19075 89 LKRLKVDKVDVFYLHAPdrstplEET--------------LAAIDELykeGKFKEFGLSNYSAWEVAEIVEicKENGW-V 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 205 RVATHQTQFSLLCRAPlEDGSFDVADAAGVTTVGYSPLALGLLSGRYSADAARSFGDRGADASALPKLprgvrgFLFRTQ 284
Cdd:cd19075 154 LPTVYQGMYNAITRQV-ETELFPCLRKLGIRFYAYSPLAGGFLTGKYKYSEDKAGGGRFDPNNALGKL------YRDRYW 226
|
250 260
....*....|....*....|....*....
gi 323456385 285 LPKLAPLLDALEQVAADRKATVGQVALAW 313
Cdd:cd19075 227 KPSYFEALEKVEEAAEKEGISLAEAALRW 255
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
42-242 |
1.14e-10 |
|
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a founding member of aldo-keto reductase family 2 member E4 (AKR2E4). It is a NADP-dependent oxidoreductase with high 3-dehydroecdysone reductase activity. It may play a role in the regulation of molting and has lower activity with phenylglyoxal and isatin (in vitro). This family also includes 3-dehydroecdysone 3b-reductase from Spodoptera littoralis and Trichoplusia ni, DL-glyceraldehyde reductase from Drosophila melanogaster, aldo-keto reductase from Bombyx mori, which correspond to aldo-keto reductase family 2 member E1, E2, E3 and E5 (AKR2E1/2/3/5), respectively.
Pssm-ID: 381342 [Multi-domain] Cd Length: 292 Bit Score: 61.91 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 42 PLAIGTWQAGnkllydyspeRDEALLAAWSLARDRGVRYFDTGDSYGTGDIEGNAelLLGRFAGGG---ADAYVHTKLav 118
Cdd:cd19116 13 AIALGTWKLK----------DDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEA--IREKIAEGVvkrEDLFITTKL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 119 ypWRL--RPDDFVRACEQSLKRLGAERVALVGQHW--------SAETYGLGGIQDPA---VYGGLAKCCELGYASGVGLS 185
Cdd:cd19116 79 --WNSyhEREQVEPALRESLKRLGLDYVDLYLIHWpvafkennDSESNGDGSLSDIDyleTWRGMEDLVKLGLTRSIGVS 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 323456385 186 NLGPRALGRGVDAVNglgARVATHQTQFSL-LCRAPLedgsFDVADAAGVTTVGYSPL 242
Cdd:cd19116 157 NFNSEQINRLLSNCN---IKPAVNQIEVHPtLTQEKL----VAYCQSNGIVVMAYSPF 207
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
75-345 |
2.37e-10 |
|
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: 60.81 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 75 DRGVRYFDTGDSYGT---GDIEGNAELLLGRF---AGGGADAYVHTKLAVYPWR----------LRPDDFVRACEQSLKR 138
Cdd:cd19752 28 AAGGNFLDTANNYAFwteGGVGGESERLIGRWlkdRGNRDDVVIATKVGAGPRDpdggpespegLSAETIEQEIDKSLRR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 139 LGAERVALVGQHwsaetyglggIQDPA-----VYGGLAKCCELGYASGVGLSNLGPRALGRGVDAV--NGLGARVATHQt 211
Cdd:cd19752 108 LGTDYIDLYYAH----------VDDRDtpleeTLEAFNELVKAGKVRAIGASNFAAWRLERARQIArqQGWAEFSAIQQ- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 212 QFSLLCRAP---------LEDGSFDVADAAG-VTTVGYSPLalglLSGRYS-ADAARSFGDRGADASAlpklprgvrgfl 280
Cdd:cd19752 177 RHSYLRPRPgadfgvqriVTDELLDYASSRPdLTLLAYSPL----LSGAYTrPDRPLPEQYDGPDSDA------------ 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 323456385 281 frtqlpKLAplldALEQVAADRKATVGQVALAWCLNARgpgkPPPLPLVGARTPAMVRDVLGALD 345
Cdd:cd19752 241 ------RLA----VLEEVAGELGATPNQVVLAWLLHRT----PAIIPLLGASTVEQLEENLAALD 291
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
61-249 |
4.33e-10 |
|
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: 60.36 E-value: 4.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 61 ERDEALlAAWSLARDRGVRYFDTGDSYGtgdiEGNAELLLGR-FAGGGADAYVHTKLavypwRLRPDD-------FVRAC 132
Cdd:cd19104 30 TREEQI-AAVRRALDLGINFFDTAPSYG----DGKSEENLGRaLKGLPAGPYITTKV-----RLDPDDlgdiggqIERSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 133 EQSLKRLGAERVAL------VGQHWSAETYGLGGIQDPAVYGG----LAKCCELGYASGVGLSNLG-PRALGRGVDAvng 201
Cdd:cd19104 100 EKSLKRLKRDSVDLlqlhnrIGDERDKPVGGTLSTTDVLGLGGvadaFERLRSEGKIRFIGITGLGnPPAIRELLDS--- 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 323456385 202 lgARVATHQTQFSLL-----------CRAPLEDGSFDVADAAGVTTVGYSPLALGLLSG 249
Cdd:cd19104 177 --GKFDAVQVYYNLLnpsaaearprgWSAQDYGGIIDAAAEHGVGVMGIRVLAAGALTT 233
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
62-357 |
5.96e-10 |
|
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: 59.29 E-value: 5.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 62 RDEALLAAWSLARDRGVRYFDTGDSYGTgdiEGNAELLLGRFAGGGADAYVHTKlaVYPWRLRPDDFVRACEQSLKRLGA 141
Cdd:cd19139 12 KDDVVIDSVRTALELGYRHIDTAQIYDN---EAAVGQAIAESGVPRDELFITTK--IWIDNLSKDKLLPSLEESLEKLRT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 142 ERVALVGQHWSAETyglGGIQDPAVYGGLAKCCELGYASGVGLSNLGPRALGRGVDAVNglGARVATHQTQFSllcraPL 221
Cdd:cd19139 87 DYVDLTLIHWPSPN---DEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVG--AGAIATNQIELS-----PY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 222 EDGSFDVADA--AGVTTVGYSPLALGLLsgrysadaarsfgdrGADasalpklprgvrgflfrtqlpklapllDALEQVA 299
Cdd:cd19139 157 LQNRKLVAHCkqHGIHVTSYMTLAYGKV---------------LDD---------------------------PVLAAIA 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 323456385 300 ADRKATVGQVALAWCLNargpgkPPPLPLVGARTPAMVRDVLGALDVKLDAGDVAGLA 357
Cdd:cd19139 195 ERHGATPAQIALAWAMA------RGYAVIPSSTKREHLRSNLLALDLTLDADDMAAIA 246
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
42-345 |
2.12e-09 |
|
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: 57.95 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 42 PLAIGTWQAGNKLlydySPERDEALLAAWslaRDRGVRYFDTGDSYGTGDIEGNAELLLGRFA---GGGADAYVHTKLAV 118
Cdd:cd19082 2 RIVLGTADFGTRI----DEEEAFALLDAF---VELGGNFIDTARVYGDWVERGASERVIGEWLksrGNRDKVVIATKGGH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 119 YP------WRLRPDDFVRACEQSLKRLGAERVALVGQHWSAETYGLGGIQDPavyggLAKCCELGYASGVGLSNLgprAL 192
Cdd:cd19082 75 PDledmsrSRLSPEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDT-----LNELVRAGKIRAFGASNW---ST 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 193 GRGVDAV-----NGLGARVAtHQTQFSLLC--RAPLEDGSFDVADAA--------GVTTVGYSPLALGLLSGRYSADAar 257
Cdd:cd19082 147 ERIAEANayakaHGLPGFAA-SSPQWSLARpnEPPWPGPTLVAMDEEmrawheenQLPVFAYSSQARGFFSKRAAGGA-- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 258 sfgdrgadasalPKLPRGVRGFLFRTQLPKLapllDALEQVAADRKATVGQVALAWCLNARGPGKPPplplVGARTPAMV 337
Cdd:cd19082 224 ------------EDDSELRRVYYSEENFERL----ERAKELAEEKGVSPTQIALAYVLNQPFPTVPI----IGPRTPEQL 283
|
....*...
gi 323456385 338 RDVLGALD 345
Cdd:cd19082 284 RDSLAAAD 291
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
43-315 |
2.23e-09 |
|
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: 57.49 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 43 LAIGTWQAGNKLLYdysperdEALLAAWSLardrGVRYFDTGDSYGTGDIEGNA--ELLLGRfagggADAYVHTKLAvyP 120
Cdd:cd19071 4 IGLGTYKLKPEETA-------EAVLAALEA----GYRHIDTAAAYGNEAEVGEAirESGVPR-----EELFITTKLW--P 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 121 WRLRPDDFVRACEQSLKRLGAERVALVGQHW-SAETYGLGGIQDPAVYGGLAKCCELGYASGVGLSNLGPRALGRGVDAv 199
Cdd:cd19071 66 TDHGYERVREALEESLKDLGLDYLDLYLIHWpVPGKEGGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAA- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 200 nglgARV--ATHQTQFSLLC-RAPLedgsFDVADAAGVTTVGYSPLAlgllsgrysadaarsfgdrgadasalpklpRGV 276
Cdd:cd19071 145 ----ARIkpAVNQIELHPYLqQKEL----VEFCKEHGIVVQAYSPLG------------------------------RGR 186
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 323456385 277 RgflfrtqlpklaPLLD--ALEQVAADRKATVGQVALAWCL 315
Cdd:cd19071 187 R------------PLLDdpVLKEIAKKYGKTPAQVLLRWAL 215
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
58-144 |
2.23e-09 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 57.59 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 58 YSPERDEALLAAWslarDRGVRYFDTGDSYGtgdiEGNAELLLGRFAGGG--ADAYVHTKLAVYPWRLRPDDFVRACEQS 135
Cdd:cd19105 23 LPRESPELLRRAL----DLGINYFDTAEGYG----NGNSEEIIGEALKGLrrDKVFLATKASPRLDKKDKAELLKSVEES 94
|
....*....
gi 323456385 136 LKRLGAERV 144
Cdd:cd19105 95 LKRLQTDYI 103
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
42-258 |
7.77e-09 |
|
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: 55.70 E-value: 7.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 42 PLAIGTWQAGNKLLyDYSPERDEALLAAwslARDRGVRYFDTGDSYgtgdieGNAELLLGRFAGGG--ADAYVHTKL-AV 118
Cdd:cd19095 2 VLGLGTSGIGRVWG-VPSEAEAARLLNT---ALDLGINLIDTAPAY------GRSEERLGRALAGLrrDDLFIATKVgTH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 119 YPWRLRPDDFVRAC-----EQSLKRLGAERVALVGQHWSAETYglggiQDPAVYGGLAKCCELGYASGVGLSNLGP---R 190
Cdd:cd19095 72 GEGGRDRKDFSPAAirasiERSLRRLGTDYIDLLQLHGPSDDE-----LTGEVLETLEDLKAAGKVRYIGVSGDGEeleA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 323456385 191 ALGRGV-DAVnglgarvathQTQFSLLCRAplEDGSFDVADAAGVTTVGYSPLALGLLSGRYSADAARS 258
Cdd:cd19095 147 AIASGVfDVV----------QLPYNVLDRE--EEELLPLAAEAGLGVIVNRPLANGRLRRRVRRRPLYA 203
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
43-365 |
4.16e-07 |
|
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: 50.69 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 43 LAIGTwqaGNKLLYDYSPERDEALLAAWSLARDRGVRYFDTGDSYGTGDIEGNA--ELLLGRfagggADAYVHTKLAVyp 120
Cdd:cd19120 7 IAFGT---GTAWYKSGDDDIQRDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEAlkESGVPR-----EDLFITTKVSP-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 121 wrlRPDDFVRACEQSLKRLGAERVALVGQHwSAETYGLGGIQDPAVYGGLAKCCELGYASGVGLSNLGPRALGRGVD--- 197
Cdd:cd19120 77 ---GIKDPREALRKSLAKLGVDYVDLYLIH-SPFFAKEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDtak 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 198 ---AVNglgarvathQTQFSLLCRAPLEDgSFDVADAAGVTTVGYSPLalgllsgrysadaarsfgdrgadaSALPKLPR 274
Cdd:cd19120 153 ikpAVN---------QIEFHPYLYPQQPA-LLEYCREHGIVVSAYSPL------------------------SPLTRDAG 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 275 GvrgflfrtqlpklaPLLDALEQVAADRKATVGQVALAWCLnargpgkppplplvgARTPAMV---------RDVLGALD 345
Cdd:cd19120 199 G--------------PLDPVLEKIAEKYGVTPAQVLLRWAL---------------QKGIVVVttsskeermKEYLEAFD 249
|
330 340
....*....|....*....|
gi 323456385 346 VKLDAGDVAGLADVARRAPQ 365
Cdd:cd19120 250 FELTEEEVEEIDKAGKQKHF 269
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
71-347 |
4.48e-07 |
|
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: 51.06 E-value: 4.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 71 SLARDRGVRYFDTGDSYGtgdiEGNAELLLGR-FAGGG---ADAYVHTKlaVYpWRLR---PDD-------FVRACEQSL 136
Cdd:cd19143 38 KAAYDAGVNFFDNAEVYA----NGQSEEIMGQaIKELGwprSDYVVSTK--IF-WGGGgppPNDrglsrkhIVEGTKASL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 137 KRLGAERVALVGQHWSaetyglggiqDPA-----VYGGLAKCCELGYASGVGLSNLGPRALGRGVDAVNGLG-ARVATHQ 210
Cdd:cd19143 111 KRLQLDYVDLVFCHRP----------DPAtpieeTVRAMNDLIDQGKAFYWGTSEWSAQQIEEAHEIADRLGlIPPVMEQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 211 TQFSLLCR-------APL-EDGSFdvadaaGVTTvgYSPLALGLLSGRYSADAARsfGDRGADASALPKLPRgvrgflFR 282
Cdd:cd19143 181 PQYNLFHRerveveyAPLyEKYGL------GTTT--WSPLASGLLTGKYNNGIPE--GSRLALPGYEWLKDR------KE 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 323456385 283 TQLPKLAPLLDALEQVAADRKATVGQVALAWCL-NARgpgkppplplV-----GARTPAMVRDVLGALDVK 347
Cdd:cd19143 245 ELGQEKIEKVRKLKPIAEELGCSLAQLAIAWCLkNPN----------VstvitGATKVEQLEENLKALEVL 305
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
73-177 |
6.43e-07 |
|
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: 50.25 E-value: 6.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 73 ARDRGVRYFDTGDSYGtgdiEGNAELLLGR-FAGGG-ADAYVHTKLAvyPWRL-RPDDFVRACEQSLKRLGAERVALvgq 149
Cdd:cd19096 30 AIDAGINYFDTAYGYG----GGKSEEILGEaLKEGPrEKFYLATKLP--PWSVkSAEDFRRILEESLKRLGVDYIDF--- 100
|
90 100
....*....|....*....|....*...
gi 323456385 150 hwsaetYGLGGIQDPavyGGLAKCCELG 177
Cdd:cd19096 101 ------YLLHGLNSP---EWLEKARKGG 119
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
59-313 |
1.01e-06 |
|
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: 49.57 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 59 SPERDEALLAAWSLARDRGVRYFDTGDSYGT-GDI-EGNAELLLGRFAGGGADAYVHTKLAVYpwRLRPDDFVRACEQSL 136
Cdd:cd19124 15 DPPSPEDIKAAVLEAIEVGYRHFDTAAAYGTeEALgEALAEALRLGLVKSRDELFVTSKLWCS--DAHPDLVLPALKKSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 137 KRLGAERVALVGQHWSAeTYGLGGIQDP------------AVYGGLAKCCELGYASGVGLSNLGPRALGRGVD------A 198
Cdd:cd19124 93 RNLQLEYVDLYLIHWPV-SLKPGKFSFPieeedflpfdikGVWEAMEECQRLGLTKAIGVSNFSCKKLQELLSfatippA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 199 VNGLGARVATHQTQFSLLCRapledgsfdvadAAGVTTVGYSPLalgllsgrysadaaRSFGDRGADASALPKlprgvrg 278
Cdd:cd19124 172 VNQVEMNPAWQQKKLREFCK------------ANGIHVTAYSPL--------------GAPGTKWGSNAVMES------- 218
|
250 260 270
....*....|....*....|....*....|....*
gi 323456385 279 flfrtqlpklapllDALEQVAADRKATVGQVALAW 313
Cdd:cd19124 219 --------------DVLKEIAAAKGKTVAQVSLRW 239
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
43-345 |
3.52e-06 |
|
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: 48.12 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 43 LAIGTWQAGNKLLYDYSpERDEALLAAWslarDRGVRYFDTGDSYGtgdiEGNAELLLGRFAGG--GADAYVHTKL---- 116
Cdd:cd19162 3 LGLGAASLGNLARAGED-EAAATLDAAW----DAGIRYFDTAPLYG----LGLSERRLGAALARhpRAEYVVSTKVgrll 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 117 ----AVYPWRLRPD-----DFVRAC-EQSLKRLGAERVALVGQHwsaetyGLGGIQDPAVYGGLAKCCELGYASGVGlsn 186
Cdd:cd19162 74 epgaAGRPAGADRRfdfsaDGIRRSiEASLERLGLDRLDLVFLH------DPDRHLLQALTDAFPALEELRAEGVVG--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 187 lgprALGRGVDAVNGLGARVATHQT-------QFSLLCRAPLeDGSFDVADAAGVTTVGYSPLALGLLSGRYSADAArsf 259
Cdd:cd19162 145 ----AIGVGVTDWAALLRAARRADVdvvmvagRYTLLDRRAA-TELLPLCAAKGVAVVAAGVFNSGILATDDPAGDR--- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 260 gdrgadasalpklprgvrgFLFRTQLPKLAPLLDALEQVAADRKATVGQVALAWCLnargPGKPPPLPLVGARTPAMVRD 339
Cdd:cd19162 217 -------------------YDYRPATPEVLARARRLAAVCRRYGVPLPAAALQFPL----RHPAVASVVVGAASPAELRD 273
|
....*.
gi 323456385 340 VLGALD 345
Cdd:cd19162 274 NLALLR 279
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
43-247 |
3.88e-06 |
|
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding member of aldo-keto reductase family 5 member H1 (AKR5H1). It is a NADPH-dependent aldo-keto reductase that reduces methylglyoxal and phenylglyoxal.
Pssm-ID: 381360 [Multi-domain] Cd Length: 263 Bit Score: 47.93 E-value: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 43 LAIGTWQagnklLYDYSPERdeallaAWSLARDRGVRYFDTGDSYGTgdiegnaELLLGR-FAGGG---ADAYVHTKLAV 118
Cdd:cd19134 14 IGLGVGE-----LSDDEAER------SVSAALEAGYRLIDTAAAYGN-------EAAVGRaIAASGiprGELFVTTKLAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 119 ypwrlrPDD-FVR---ACEQSLKRLGAERVALVGQHWSAETYGlggiQDPAVYGGLAKCCELGYASGVGLSNLGPRALGr 194
Cdd:cd19134 76 ------PDQgFTAsqaACRASLERLGLDYVDLYLIHWPAGREG----KYVDSWGGLMKLREEGLARSIGVSNFTAEHLE- 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 323456385 195 gvDAVNGLGARVATHQTQF-SLLCRAPLEdgsfDVADAAGVTTVGYSPLALGLL 247
Cdd:cd19134 145 --NLIDLTFFTPAVNQIELhPLLNQAELR----KVNAQHGIVTQAYSPLGVGRL 192
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
43-346 |
5.70e-06 |
|
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: 47.44 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 43 LAIGTWQA-GNKLlydySPERDEALLaawSLARDRGVRYFDTGDSYGTGdiegNAELLLGRF---AGGGADAYV-HTKLA 117
Cdd:cd19141 15 LGLGTWVTfGSQI----SDEVAEELV---TLAYENGINLFDTAEVYAAG----KAEIVLGKIlkkKGWRRSSYViTTKIF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 118 vypWRLRPDD--------FVRACEQSLKRLGAERVALVGQHWS-----------AETYGLGgiQDPAVYGGLAK--CCEL 176
Cdd:cd19141 84 ---WGGKAETerglsrkhIIEGLKASLERLQLEYVDIVFANRPdpntpmeeivrAFTHVIN--QGMAMYWGTSRwsAMEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 177 GYASGVGLS-NLGPRALgrgvdavnglgarvatHQTQFSLLCRAPLEDGSFDVADAAGVTTVGYSPLALGLLSGRYSada 255
Cdd:cd19141 159 MEAYSVARQfNLIPPIV----------------EQAEYHLFQREKVEMQLPELFHKIGVGAMTWSPLACGILSGKYD--- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 256 arsfgdrgadaSALPKLPRG-VRGFLF----------RTQLPKLAPLldaleQVAADR-KATVGQVALAWCLNargpGKP 323
Cdd:cd19141 220 -----------DGVPEYSRAsLKGYQWlkekilseegRRQQAKLKEL-----QIIADRlGCTLPQLAIAWCLK----NEG 279
|
330 340
....*....|....*....|...
gi 323456385 324 PPLPLVGARTPAMVRDVLGALDV 346
Cdd:cd19141 280 VSSVLLGASSTEQLYENLQAIQV 302
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
43-361 |
7.40e-06 |
|
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: 47.02 E-value: 7.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 43 LAIGTWQAGNKLLYdysperdEALLAAWSLardrGVRYFDTGDSYGTGDIEGNAelLLGRFAGGG---ADAYVHTKLavy 119
Cdd:cd19123 15 LGLGTWKSKPGEVG-------QAVKQALEA----GYRHIDCAAIYGNEAEIGAA--LAEVFKEGKvkrEDLWITSKL--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 120 pW--RLRPDDFVRACEQSLKRLGAERVALVGQHWS-AETYGLGGIQDPAVYGGLA------------KCCELGYASGVGL 184
Cdd:cd19123 79 -WnnSHAPEDVLPALEKTLADLQLDYLDLYLMHWPvALKKGVGFPESGEDLLSLSpipledtwrameELVDKGLCRHIGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 185 SNLGPRAL------GRGVDAVNglgaRVATH----QTQFSLLCRApledgsfdvadaAGVTTVGYSPLAlgllsgrySAD 254
Cdd:cd19123 158 SNFSVKKLedllatARIKPAVN----QVELHpylqQPELLAFCRD------------NGIHLTAYSPLG--------SGD 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 255 AARSFgdrgaDASALPKLprgvrgflfrtqlpklapLLD-ALEQVAADRKATVGQVALAWCLNARGPGKPPPLplvgarT 333
Cdd:cd19123 214 RPAAM-----KAEGEPVL------------------LEDpVINKIAEKHGASPAQVLIAWAIQRGTVVIPKSV------N 264
|
330 340
....*....|....*....|....*...
gi 323456385 334 PAMVRDVLGALDVKLDAGDVAGLADVAR 361
Cdd:cd19123 265 PERIQQNLEAAEVELDASDMATIAALDR 292
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
43-317 |
1.55e-05 |
|
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: 46.52 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 43 LAIGTWQA-GNKLlydySPERDEALLaawSLARDRGVRYFDTGDSYGTGdiegNAELLLGRF---AGGGADAYVHTKlAV 118
Cdd:cd19160 18 LGLGTWVTfGSQI----SDETAEDLL---TVAYEHGVNLFDTAEVYAAG----KAERTLGNIlksKGWRRSSYVVTT-KI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 119 YpWR--------LRPDDFVRACEQSLKRLGAERVALVGQHWS-----------AETYGLGgiQDPAVYGGLAK--CCELG 177
Cdd:cd19160 86 Y-WGgqaetergLSRKHIIEGLRGSLDRLQLEYVDIVFANRSdpnspmeeivrAMTYVIN--QGMAMYWGTSRwsAMEIM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 178 YASGVGLS-NLGPRAlgrgvdavnglgarvaTHQTQFSLLCRAPLEDGSFDVADAAGVTTVGYSPLALGLLSGRYSA--- 253
Cdd:cd19160 163 EAYSVARQfNLIPPV----------------CEQAEYHLFQREKVEMQLPELYHKIGVGSVTWSPLACGLITGKYDGrvp 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 323456385 254 DAARsfgdrgADASALPKLPRGVRGFLFRTQLPKLAPLLDALEQVAadrkATVGQVALAWCLNA 317
Cdd:cd19160 227 DTCR------AAVKGYQWLKEKVQSEEGKKQQAKVKELHPIADRLG----CTVAQLAIAWCLRS 280
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
43-270 |
2.44e-05 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 45.17 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 43 LAIGTWQAGNKllydySPERDEALLAAwslARDRGVRYFDTGDSYgtgdieGNAELLLGRF-AGGGADAYVHTKLAVYpw 121
Cdd:cd19100 14 LGFGGGPLGRL-----SQEEAAAIIRR---ALDLGINYFDTAPSY------GDSEEKIGKAlKGRRDKVFLATKTGAR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 122 rlRPDDFVRACEQSLKRLGAERV------ALVGQHWSAETYGLGGiqdpaVYGGLAKCCELGYASGVGLSNLGPRALGRG 195
Cdd:cd19100 78 --DYEGAKRDLERSLKRLGTDYIdlyqlhAVDTEEDLDQVFGPGG-----ALEALLEAKEEGKIRFIGISGHSPEVLLRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 196 VDAvnglgARVATHQTQFSLLCRAPLEDGS--FDVADAAGVTTVGYSPLALGLLSGRYSADAARSFG---DRGADASALP 270
Cdd:cd19100 151 LET-----GEFDVVLFPINPAGDHIDSFREelLPLAREKGVGVIAMKVLAGGRLLSGDPLDPEQALRyalSLPPVDVVIV 225
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
45-315 |
2.57e-05 |
|
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: 45.48 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 45 IGTWQAgnkllydyspeRDEALLAAWSLARDRGVRYFDTGDSYGTGDIEGNAelLLGRFAGGGA---DAYVHTKLAvyPW 121
Cdd:cd19154 17 LGTWQS-----------KGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEA--LAELLEEGVVkreDLFITTKLW--TH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 122 RLRPDDFVRACEQSLKRLGAERVALVGQH--WSAE--------TYGLGGIQDPA----VYGGLAKCCELGYASGVGLSNL 187
Cdd:cd19154 82 EHAPEDVEEALRESLKKLQLEYVDLYLIHapAAFKddegesgtMENGMSIHDAVdvedVWRGMEKVYDEGLTKAIGVSNF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 188 GPRALGRGVDAvnglgARVATHQTQFSLLCRAPLEDgSFDVADAAGVTTVGYSPLalgllsgrysadaarsfgdrGADAS 267
Cdd:cd19154 162 NNDQIQRILDN-----ARVKPHNNQVECHLYFPQKE-LVEFCKKHNISVTSYATL--------------------GSPGR 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 323456385 268 ALPKLPRGVRgflfrtqlPKLAPLLDAL-EQVAADRKATVGQVALAWCL 315
Cdd:cd19154 216 ANFTKSTGVS--------PAPNLLQDPIvKAIAEKHGKTPAQVLLRYLL 256
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
42-150 |
7.77e-05 |
|
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: 44.14 E-value: 7.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 42 PLAIGTWQAGNklLYDYSPERD--EALLAAWSLardrGVRYFDTGDSYGTgdieGNAELLLGRF-AGGGADAYV-HTKLA 117
Cdd:cd19152 2 KLGFGTAPLGN--LYEAVSDEEakATLVAAWDL----GIRYFDTAPWYGA----GLSEERLGAAlRELGREDYViSTKVG 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 323456385 118 vypWRLRPD-------------------------DFVRAC-EQSLKRLGAERVALVGQH 150
Cdd:cd19152 72 ---RLLVPLqeveptfepgfwnplpfdavfdysyDGILRSiEDSLQRLGLSRIDLLSIH 127
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
43-364 |
1.26e-04 |
|
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: 43.49 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 43 LAIGTWQA-GNKLlydySPERDEALLaawSLARDRGVRYFDTGDSYGTGdiegNAELLLGRF----AGGGADAYVHTKL- 116
Cdd:cd19159 16 LGLGTWVTfGGQI----SDEVAERLM---TIAYESGVNLFDTAEVYAAG----KAEVILGSIikkkGWRRSSLVITTKLy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 117 ----AVYPWRLRPDDFVRACEQSLKRLGAERVALVGQHW-----------SAETYGLGgiQDPAVYGGLAK--CCELGYA 179
Cdd:cd19159 85 wggkAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRpdsntpmeeivRAMTHVIN--QGMAMYWGTSRwsAMEIMEA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 180 SGVGLS-NLGPRAlgrgvdavnglgarvaTHQTQFSLLCRAPLEDGSFDVADAAGVTTVGYSPLALGLLSGRYS---ADA 255
Cdd:cd19159 163 YSVARQfNMIPPV----------------CEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGngvPES 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 256 ARsfgdrgADASALPKLPRGVRGFLFRTQLPKLAPLLDALEQVAadrkATVGQVALAWCLNARgpgkPPPLPLVGARTPA 335
Cdd:cd19159 227 SR------ASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLG----CTLPQLAVAWCLRNE----GVSSVLLGSSTPE 292
|
330 340 350
....*....|....*....|....*....|.
gi 323456385 336 MVRDVLGALDV--KLDAGDVAGLADVARRAP 364
Cdd:cd19159 293 QLIENLGAIQVlpKMTSHVVNEIDNILRNKP 323
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
131-362 |
1.77e-04 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 42.92 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 131 ACEQSLKRLGAERVALVGQHW-SAETYGLGGI------QDPAV-----YGGLAKCCELGYASGVGLSNLGPRALGRGVD- 197
Cdd:PRK10625 113 ALHDSLKRLQTDYLDLYQVHWpQRPTNCFGKLgyswtdSAPAVslletLDALAEQQRAGKIRYIGVSNETAFGVMRYLHl 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 198 AVNGLGARVATHQTQFSLLCRApLEDGSFDVADAAGVTTVGYSPLALGLLSGRYSADAArsfgdrgadasalpklPRGVR 277
Cdd:PRK10625 193 AEKHDLPRIVTIQNPYSLLNRS-FEVGLAEVSQYEGVELLAYSCLAFGTLTGKYLNGAK----------------PAGAR 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 278 GFLF----RTQLPKLAPLLDALEQVAADRKATVGQVALAWClnarGPGKPPPLPLVGARTPAMVRDVLGALDVKLDAGDV 353
Cdd:PRK10625 256 NTLFsrftRYSGEQTQKAVAAYVDIAKRHGLDPAQMALAFV----RRQPFVASTLLGATTMEQLKTNIESLHLTLSEEVL 331
|
....*....
gi 323456385 354 AGLADVARR 362
Cdd:PRK10625 332 AEIEAVHQV 340
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
43-247 |
3.36e-04 |
|
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: 41.93 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 43 LAIGTWQAGNkllydYSperDEALLAAwslARDRGVRYFDTGDSYGTgdiegnaELLLGR-FAGGG---ADAYVHTKLav 118
Cdd:cd19135 16 LGLGTSHSGG-----YS---HEAVVYA---LKECGYRHIDTAKRYGC-------EELLGKaIKESGvprEDLFLTTKL-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 119 ypWrlrPDDF-----VRACEQSLKRLGAERVALVGQHWSAEtyGLGGIQDPAVYGGLAKCCELGYASG----VGLSNLGP 189
Cdd:cd19135 76 --W---PSDYgyestKQAFEASLKRLGVDYLDLYLLHWPDC--PSSGKNVKETRAETWRALEELYDEGlcraIGVSNFLI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 323456385 190 RAL------GRGVDAVNGLGARVATHQTQFSLLCRapledgsfdvadAAGVTTVGYSPLALGLL 247
Cdd:cd19135 149 EHLeqlledCSVVPHVNQVEFHPFQNPVELIEYCR------------DNNIVFEGYCPLAKGKA 200
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
45-242 |
4.90e-04 |
|
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase (ALR) from Hordeum vulgare (AKR4C1), Bromus inermis (AKR4C2), Avena fatua (AKR4C3), and Xerophyta viscosa (AKR4C4), two aldose reductases, DpAR1 (AKR4C5) and DpAR2(AKR4C6), from Digitalis purpurea, aldehyde reductase from Zea mays (AKR4C7), four aldo-keto reductases from Arabidopsis thaliana (AKR4C8-11), and another three aldo-keto reductases from Aloe arborescens (AKR4C12) and Oryza sativa (AKR4C14/15). ALR (EC 1.1.1.21), also called AR, aldehyde reductase, or polyol dehydrogenase (NADP(+)), is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. Both DpAR1 and DpAR2 reduce the ketone group of steroid structures. They may be involved in plant steroid metabolism in general and in cardenolide biosynthesis in particular. Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops.
Pssm-ID: 381351 [Multi-domain] Cd Length: 287 Bit Score: 41.56 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 45 IGTWQAGNKLLYDysperdeALLAAWSLardrGVRYFDTGDSYGTGDIEGNAellLGRFAGGGA----DAYVHTKLavyp 120
Cdd:cd19125 16 LGTWQADPGVVGN-------AVKTAIKE----GYRHIDCAAIYGNEKEIGKA---LKKLFEDGVvkreDLFITSKL---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 121 WR--LRPDDFVRACEQSLKRLGAERVALVGQHW------SAETYGLGGIQD---PAVYGGLAKCCELGYASGVGLSNLGP 189
Cdd:cd19125 78 WCtdHAPEDVPPALEKTLKDLQLDYLDLYLIHWpvrlkkGAHMPEPEEVLPpdiPSTWKAMEKLVDSGKVRAIGVSNFSV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 323456385 190 RALGRGVDAvnglgARV--ATHQTQFSLLCRaplEDGSFDVADAAGVTTVGYSPL 242
Cdd:cd19125 158 KKLEDLLAV-----ARVppAVNQVECHPGWQ---QDKLHEFCKSKGIHLSAYSPL 204
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
43-198 |
7.90e-04 |
|
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: 40.82 E-value: 7.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 43 LAIGTWQAGNkllydysperDEALLAAwSLARDRGVRYFDTGDSYGTGDIEGNAelllgrFAGGG---ADAYVHTKLavy 119
Cdd:cd19131 13 LGLGVWQVSN----------DEAASAV-REALEVGYRSIDTAAIYGNEEGVGKA------IRASGvprEELFITTKL--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 120 pWR--LRPDDFVRACEQSLKRLGAERVALVGQHWSAETYGlggiQDPAVYGGLAKCCELGYASGVGLSNLGPRALGRGVD 197
Cdd:cd19131 73 -WNsdQGYDSTLRAFDESLRKLGLDYVDLYLIHWPVPAQD----KYVETWKALIELKKEGRVKSIGVSNFTIEHLQRLID 147
|
.
gi 323456385 198 A 198
Cdd:cd19131 148 E 148
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
43-139 |
7.93e-04 |
|
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: 40.91 E-value: 7.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 43 LAIGTWQAgnkllydYSPERDEALLAA-WSLARDRGVRYFDTGDSYgtgdIEGNAELLLGRF---AGGGADAY-VHTKLA 117
Cdd:cd19142 16 VGLGTWST-------FSTAISEEQAEEiVTLAYENGINYFDTSDAF----TSGQAETELGRIlkkKGWKRSSYiVSTKIY 84
|
90 100
....*....|....*....|....*....
gi 323456385 118 vypWRLRPDD-------FVRACEQSLKRL 139
Cdd:cd19142 85 ---WSYGSEErglsrkhIIESVRASLRRL 110
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
45-151 |
2.01e-03 |
|
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: 39.44 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 45 IGTWQAGnkllydySPERDEALLAAWSLardrGVRYFDTGDSYGTGDIEGnaELLLGRFAGG--GADAYVHTKLavypWR 122
Cdd:cd19121 17 LGTWQAK-------AGEVKAAVAHALKI----GYRHIDGALCYQNEDEVG--EGIKEAIAGGvkREDLFVTTKL----WS 79
|
90 100
....*....|....*....|....*....
gi 323456385 123 LRPDDFVRACEQSLKRLGAERVALVGQHW 151
Cdd:cd19121 80 TYHRRVELCLDRSLKSLGLDYVDLYLVHW 108
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
73-249 |
2.80e-03 |
|
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: 39.12 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 73 ARDRGVRYFDTGDSYGTGDIEGNAelllgrFAGGG---ADAYVHTKLavypW--RLRPDDFVRACEQSLKRLGAERVALV 147
Cdd:cd19130 32 ALEVGYRHIDTAAIYGNEEGVGAA------IAASGiprDELFVTTKL----WndRHDGDEPAAAFAESLAKLGLDQVDLY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 148 GQHWSAETYGLGgiqdPAVYGGLAKCCELGYASGVGLSNLGPRALGRGVDAVnglGARVATHQTQfslLCRAPLEDGSFD 227
Cdd:cd19130 102 LVHWPTPAAGNY----VHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVAAT---GVVPAVNQIE---LHPAYQQRTIRD 171
|
170 180
....*....|....*....|..
gi 323456385 228 VADAAGVTTVGYSPLALGLLSG 249
Cdd:cd19130 172 WAQAHDVKIEAWSPLGQGKLLG 193
|
|
| PRK13981 |
PRK13981 |
NAD synthetase; Provisional |
90-155 |
2.97e-03 |
|
NAD synthetase; Provisional
Pssm-ID: 237577 [Multi-domain] Cd Length: 540 Bit Score: 39.37 E-value: 2.97e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 323456385 90 GDIEGNAELLL---GRFAGGGADAYVHTKLAV--YPWR---LRPDdFVRACEQSLKRLGAER----VALVGQHWSAET 155
Cdd:PRK13981 13 GDIAGNAAKILaaaAEAADAGADLLLFPELFLsgYPPEdllLRPA-FLAACEAALERLAAATaggpAVLVGHPWREGG 89
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
57-360 |
3.13e-03 |
|
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: 39.25 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 57 DYSPERDEA-----LLAAWslarDRGVRYFDTGDSYGtgdiegNAELLLGRFAGGGA----DAYVHTKLA---VYPWRLR 124
Cdd:cd19098 27 GRSVEAMRAhthavLDAAW----AAGVRYFDAARSYG------RAEEFLGSWLRSRNiapdAVFVGSKWGytyTADWQVD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 125 PDDFVRAcEQSLKRLG---AERVALVGQHW------SAeTYGLGGIQDPAVYGGLAKCCELGYAsgVGLSNLGPR---AL 192
Cdd:cd19098 97 AAVHEVK-DHSLARLLkqwEETRSLLGKHLdlyqihSA-TLESGVLEDADVLAALAELKAEGVK--IGLSLSGPQqaeTL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 193 GRGVdAVNGLGARVATH-QTQFSLLCRAPLEdgSFDVADAAGVTTVGYSPLALGLLSGRYSAdaarsfgdrgadasalpk 271
Cdd:cd19098 173 RRAL-EIEIDGARLFDSvQATWNLLEQSAGE--ALEEAHEAGMGVIVKEALANGRLTDRNPS------------------ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 272 lprgvrgflfrtqlPKLAPLLDALEQVAADRKATVGQVALAWCLnargPGKPPPLPLVGARTPAMVRDVLGALDVKLDAG 351
Cdd:cd19098 232 --------------PELAPLMAVLKAVADRLGVTPDALALAAVL----AQPFVDVVLSGAATPEQLRSNLRALDVSLDLE 293
|
....*....
gi 323456385 352 DVAGLADVA 360
Cdd:cd19098 294 LLAALADLA 302
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
43-346 |
6.39e-03 |
|
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: 38.14 E-value: 6.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 43 LAIGTWQAGNKLLYDyspERDEALLaawSLARDRGVRYFDTGDSYGTGdiegNAELLLGRF---AGGGADAYVHTKLAVY 119
Cdd:cd19158 16 LGLGTWVTFGGQITD---EMAEHLM---TLAYDNGINLFDTAEVYAAG----KAEVVLGNIikkKGWRRSSLVITTKIFW 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 120 PWR------LRPDDFVRACEQSLKRLGAERVALV-----------GQHWSAETYGLGgiQDPAVYGGLAKCCELGYASGV 182
Cdd:cd19158 86 GGKaetergLSRKHIIEGLKASLERLQLEYVDVVfanrpdpntpmEETVRAMTHVIN--QGMAMYWGTSRWSSMEIMEAY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 183 GLS---NLGPRAlgrgvdavnglgarvaTHQTQFSLLCRAPLEDGSFDVADAAGVTTVGYSPLALGLLSGRYsadaarsf 259
Cdd:cd19158 164 SVArqfNLIPPI----------------CEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKY-------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 260 gdrgaDASALPKLPRGVRGFLF----------RTQLPKlaplLDALEQVAADRKATVGQVALAWCLNARgpgkPPPLPLV 329
Cdd:cd19158 220 -----DSGIPPYSRASLKGYQWlkdkilseegRRQQAK----LKELQAIAERLGCTLPQLAIAWCLRNE----GVSSVLL 286
|
330
....*....|....*..
gi 323456385 330 GARTPAMVRDVLGALDV 346
Cdd:cd19158 287 GASNAEQLMENIGAIQV 303
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
73-150 |
8.69e-03 |
|
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: 37.53 E-value: 8.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323456385 73 ARDRGVRYFDTGDSYGtgdiEGNAELLLGRF-AGGGADAYV-HTKLAVYPWRLRPD-DF-----VRACEQSLKRLGAERV 144
Cdd:cd19163 42 ALDSGINYIDTAPWYG----QGRSETVLGKAlKGIPRDSYYlATKVGRYGLDPDKMfDFsaeriTKSVEESLKRLGLDYI 117
|
....*.
gi 323456385 145 ALVGQH 150
Cdd:cd19163 118 DIIQVH 123
|
|
| |
