|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
14-296 |
1.87e-121 |
|
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: 349.55 E-value: 1.87e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 14 SEISLGGLFVG----KESSDTGIQTIRRALELGVNLFDTAPSYfgGKAQEILGEALNGVK-QPHYVSTKVGPCPIfPEPK 88
Cdd:cd19090 1 SALGLGTAGLGgvfgGVDDDEAVATIRAALDLGINYIDTAPAY--GDSEERLGLALAELPrEPLVLSTKVGRLPE-DTAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 89 YDHDSIMQQVEYNLKALKRDKIDLLHIHDPDRYGDKgnpgnyhAVFGKNMALATLQKLKAQGVIRSIGIGSLWLDFQAHC 168
Cdd:cd19090 78 YSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWV-------DILAPGGALEALLELKEEGLIKHIGLGGGPPDLLRRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 169 IDTGEFDVILTFNRYGLIWRDAQFQSFPFCRRHNVGVMQGTPLHQGVLAVPRPEWVTTPPDWMTVTEHDRYRRLLDIQKS 248
Cdd:cd19090 151 IETGDFDVVLTANRYTLLDQSAADELLPAAARHGVGVINASPLGMGLLAGRPPERVRYTYRWLSPELLDRAKRLYELCDE 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1085403013 249 CGIPLPELALRFILQNPTISATIPGAGNLTELAANVACSeKGPLPPDV 296
Cdd:cd19090 231 HGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAA-EGPLPEEL 277
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-303 |
6.50e-69 |
|
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: 216.97 E-value: 6.50e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 1 MKYRSLGRTGWQVSEISLG----GLFVGKESSDTGIQTIRRALELGVNLFDTAPSYFGGKAQEILGEALNGVKQPHYV-S 75
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGtmtfGGPWGGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALKGRPRDDVViA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 76 TKVGPcPIFPEPKYDH---DSIMQQVEYNLKALKRDKIDLLHIHDPDR---YGDkgnpgnyhavfgknmALATLQKLKAQ 149
Cdd:COG0667 81 TKVGR-RMGPGPNGRGlsrEHIRRAVEASLRRLGTDYIDLYQLHRPDPdtpIEE---------------TLGALDELVRE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 150 GVIRSIGIG--SLWLDFQAHCIDTGEFDVILTFNRYGLIWRDAQFQSFPFCRRHNVGVMQGTPLHQGVLA------VPRP 221
Cdd:COG0667 145 GKIRYIGVSnySAEQLRRALAIAEGLPPIVAVQNEYSLLDRSAEEELLPAARELGVGVLAYSPLAGGLLTgkyrrgATFP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 222 EWVTTPPDWMTVTEHDRYRRLLD----IQKSCGIPLPELALRFILQNPTISATIPGAGNLTELAANVACSEkGPLPPDVA 297
Cdd:COG0667 225 EGDRAATNFVQGYLTERNLALVDalraIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAAD-LELSAEDL 303
|
....*.
gi 1085403013 298 TQIESL 303
Cdd:COG0667 304 AALDAA 309
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
1-293 |
5.67e-66 |
|
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: 208.94 E-value: 5.67e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 1 MKYRSLGRTGWQVSEISLGGLFVGKESSDT----GIQTIRRALELGVNLFDTAPSYFGGKAQEILGEALNGVKQPHYV-S 75
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGASPLGGVFGPVdeeeAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKALKGIPRDSYYlA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 76 TKVG-----PCPIFpepKYDHDSIMQQVEYNLKALKRDKIDLLHIHDPDrYGDKGNPgnyhaVFgkNMALATLQKLKAQG 150
Cdd:cd19163 81 TKVGrygldPDKMF---DFSAERITKSVEESLKRLGLDYIDIIQVHDIE-FAPSLDQ-----IL--NETLPALQKLKEEG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 151 VIRSIGIGSLWLDFQAHCID--TGEFDVILTFNRYGLIWRDAQfQSFPFCRRHNVGVMQGTPLHQGVLAvPRPewvttPP 228
Cdd:cd19163 150 KVRFIGITGYPLDVLKEVLErsPVKIDTVLSYCHYTLNDTSLL-ELLPFFKEKGVGVINASPLSMGLLT-ERG-----PP 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1085403013 229 DWMTVTEHDRY--RRLLDIQKSCGIPLPELALRFILQNPTISATIPGAGNLTELAANVACSEKGPLP 293
Cdd:cd19163 223 DWHPASPEIKEacAKAAAYCKSRGVDISKLALQFALSNPDIATTLVGTASPENLRKNLEAAEEPLDA 289
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
2-304 |
4.83e-65 |
|
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: 207.50 E-value: 4.83e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 2 KYRSLGRTGWQVSEISLGGLFVG----KESSDTGIQTIRRALELGVNLFDTAPSYFGGKAQEILGEALNGVKQPHYVSTK 77
Cdd:cd19104 1 KYRRFGRTGLKVSELTFGGGGIGglmgRTTREEQIAAVRRALDLGINFFDTAPSYGDGKSEENLGRALKGLPAGPYITTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 78 VGPCPIFPEPKYDHdsIMQQVEYNLKALKRDKIDLLHIHD---PDRYGDKGNPGNYHAVFGKNMALATLQKLKAQGVIRS 154
Cdd:cd19104 81 VRLDPDDLGDIGGQ--IERSVEKSLKRLKRDSVDLLQLHNrigDERDKPVGGTLSTTDVLGLGGVADAFERLRSEGKIRF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 155 IGIgSLWLDFQA--HCIDTGEFDVILTFnrYGLI-----------WRDAQFQSF-PFCRRHNVGVMQGTPLHQGVLA--V 218
Cdd:cd19104 159 IGI-TGLGNPPAirELLDSGKFDAVQVY--YNLLnpsaaearprgWSAQDYGGIiDAAAEHGVGVMGIRVLAAGALTtsL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 219 PRPEWVTTPPDWMTVTEHDRYRRLLDIQKSCGIPLPELALRFILQNPTISATIPGAGNLTELAANVACSEKGPLPPDVAT 298
Cdd:cd19104 236 DRGREAPPTSDSDVAIDFRRAAAFRALAREWGETLAQLAHRFALSNPGVSTVLVGVKNREELEEAVAAEAAGPLPAENLA 315
|
....*.
gi 1085403013 299 QIESLG 304
Cdd:cd19104 316 RLEALW 321
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
3-285 |
8.11e-59 |
|
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: 188.46 E-value: 8.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 3 YRSLGRTGWQVSEISLGGLFVGKESSDTGIQTIRRALELGVNLFDTAPSYfgGKAQEILGEALNGVKQPHYVSTKVGpcp 82
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPLGRLSQEEAAAIIRRALDLGINYFDTAPSY--GDSEEKIGKALKGRRDKVFLATKTG--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 83 ifpepKYDHDSIMQQVEYNLKALKRDKIDLLHIHDPDRYGDkgnpgnYHAVFGKNMALATLQKLKAQGVIRSIGIGSLWL 162
Cdd:cd19100 76 -----ARDYEGAKRDLERSLKRLGTDYIDLYQLHAVDTEED------LDQVFGPGGALEALLEAKEEGKIRFIGISGHSP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 163 DFQAHCIDTGEFDVILT-FNRYGLIWRDAQFQSFPFCRRHNVGV--MQgtPLHQGVLAVPRPEwvttppdwmtvtehdry 239
Cdd:cd19100 145 EVLLRALETGEFDVVLFpINPAGDHIDSFREELLPLAREKGVGViaMK--VLAGGRLLSGDPL----------------- 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1085403013 240 rrlldiqkscgipLPELALRFILQNPTISATIPGAGNLTELAANVA 285
Cdd:cd19100 206 -------------DPEQALRYALSLPPVDVVIVGMDSPEELDENLA 238
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-285 |
1.39e-58 |
|
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: 188.56 E-value: 1.39e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 1 MKYRSLGRTGWQVSEISLGGLFVGKESsdtgIQTIRRALELGVNLFDTAPSYFGGKAQEILGEALNGVK-QPHYVSTKVG 79
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFGGGGLPRES----PELLRRALDLGINYFDTAEGYGNGNSEEIIGEALKGLRrDKVFLATKAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 80 PcpifPEPKYDHDSIMQQVEYNLKALKRDKIDLLHIHDPDRYGDKGNPGNYHAVFgknmalatlQKLKAQGVIRSIGIGS 159
Cdd:cd19105 77 P----RLDKKDKAELLKSVEESLKRLQTDYIDIYQLHGVDTPEERLLNEELLEAL---------EKLKKEGKVRFIGFST 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 160 LwlDFQAHC----IDTGEFDVILTfnRYG-LIWRDAQFQSFPFCRRHNVGVMQGTPLHQGVLAVPRPEWVTTPpdwmtvt 234
Cdd:cd19105 144 H--DNMAEVlqaaIESGWFDVIMV--AYNfLNQPAELEEALAAAAEKGIGVVAMKTLAGGYLQPALLSVLKAK------- 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1085403013 235 ehdryrrlldiqkscGIPLPELALRFILQNPTISATIPGAGNLTELAANVA 285
Cdd:cd19105 213 ---------------GFSLPQAALKWVLSNPRVDTVVPGMRNFAELEENLA 248
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
11-285 |
1.37e-53 |
|
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: 174.97 E-value: 1.37e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 11 WQVSEI-----SLGGLFVGKESSDTGIQTIRRALELGVNLFDTAPSYFGGKAQEILGEALNGVKQPHYVSTKVGP---CP 82
Cdd:cd19086 1 LEVSEIgfgtwGLGGDWWGDVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKGRRDKVVIATKFGNrfdGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 83 IFPEPKYDHDSIMQQVEYNLKALKRDKIDLLHIHDPDRygdkgnpgnyhAVFGKNMALATLQKLKAQGVIRSIGIgSLW- 161
Cdd:cd19086 81 PERPQDFSPEYIREAVEASLKRLGTDYIDLYQLHNPPD-----------EVLDNDELFEALEKLKQEGKIRAYGV-SVGd 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 162 LDFQAHCIDTGEFDVI-LTFNrygLIWRDAQFQSFPFCRRHNVGVMQGTPLHQGVLAvprpewvttppdwmtvtehdryr 240
Cdd:cd19086 149 PEEALAALRRGGIDVVqVIYN---LLDQRPEEELFPLAEEHGVGVIARVPLASGLLT----------------------- 202
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1085403013 241 rlldiqkscGIpLPELALRFILQNPTISATIPGAGNLTELAANVA 285
Cdd:cd19086 203 ---------GK-LAQAALRFILSHPAVSTVIPGARSPEQVEENAA 237
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
12-288 |
4.38e-50 |
|
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: 168.09 E-value: 4.38e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 12 QVSEISLG-----GLFVGKESSDTGIQTIRRALELGVNLFDTAPSYFGGKAQEILGEALNGVKQPHYVSTKVGPCPiFPE 86
Cdd:cd19084 3 KVSRIGLGtwaigGTWWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKGRRDDVVIATKCGLRW-DGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 87 PKYDHD----SIMQQVEYNLKALKRDKIDLLHIHDPDRYGDKGNpgnyhavfgknmALATLQKLKAQGVIRSIGIGSLWL 162
Cdd:cd19084 82 KGVTKDlspeSIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEE------------TAEALEKLKKEGKIRYIGVSNFSV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 163 DFQAHCIDTGEFDVILtfNRYGLIWRDAQFQSFPFCRRHNVGVMQGTPLHQGVLA-----VPRPEwvttPPDWMtvTEHD 237
Cdd:cd19084 150 EQLEEARKYGPIVSLQ--PPYSMLEREIEEELLPYCRENGIGVLPYGPLAQGLLTgkykkEPTFP----PDDRR--SRFP 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1085403013 238 RYR------------RLLDIQKSCGIPLPELALRFILQNPTISATIPGAGNLTELAANVACSE 288
Cdd:cd19084 222 FFRgenfeknleivdKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALD 284
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
1-292 |
1.63e-48 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 165.76 E-value: 1.63e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 1 MKYRSLGRTGWQVSEISLGGLFVGKESSDTGIQTIRRALELGVNLFDTAPSYfgGKAQEILGEALNGVKQPHYVSTKvgp 80
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGMRLPRKDEEEAEALIRRAIDNGINYIDTARGY--GDSEEFLGKALKGPRDKVILATK--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 81 cpiFPEPKYDHDSIMQQVEYNLKALKRDKIDLLHIHDPDrygdkgNPGNYHAVFGKNMALATLQKLKAQGVIRSIGI--- 157
Cdd:COG1453 76 ---LPPWVRDPEDMRKDLEESLKRLQTDYIDLYLIHGLN------TEEDLEKVLKPGGALEALEKAKAEGKIRHIGFsth 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 158 GSLWLdFQAhCIDTGEFDVI-LTFNrYgLIWRDAQFQS-FPFCRRHNVGVMQGTPLHQGVLAVPRPEWVttppdwmtvte 235
Cdd:COG1453 147 GSLEV-IKE-AIDTGDFDFVqLQYN-Y-LDQDNQAGEEaLEAAAEKGIGVIIMKPLKGGRLANPPEKLV----------- 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1085403013 236 hdryrRLLDIQKScgipLPELALRFILQNPTISATIPGAGNLTELAANVA-CSEKGPL 292
Cdd:COG1453 212 -----ELLCPPLS----PAEWALRFLLSHPEVTTVLSGMSTPEQLDENLKtADNLEPL 260
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
13-304 |
2.92e-48 |
|
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: 163.14 E-value: 2.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 13 VSEISLG------GLFVGKESSDTGIQTIRRALELGVNLFDTAPSYFGGKAQEILGEALNGVKQPHYVSTKVGPCPIFPE 86
Cdd:cd19085 1 VSRLGLGcwqfggGYWWGDQDDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKGRRDDVVIATKVSPDNLTPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 87 pkydhdSIMQQVEYNLKALKRDKIDLLHIHDPDRygdkgnpgnyhavfGKNMA--LATLQKLKAQGVIRSIGIG--SLWl 162
Cdd:cd19085 81 ------DVRKSCERSLKRLGTDYIDLYQIHWPSS--------------DVPLEetMEALEKLKEEGKIRAIGVSnfGPA- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 163 DFQAhCIDTGEFDVI-LTFNrygLIWRDAQFQSFPFCRRHNVGVMQGTPLHQGVLAVP-RPEWVTTPPDwmTVTEHDRY- 239
Cdd:cd19085 140 QLEE-ALDAGRIDSNqLPYN---LLWRAIEYEILPFCREHGIGVLAYSPLAQGLLTGKfSSAEDFPPGD--ARTRLFRHf 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1085403013 240 ------------RRLLDIQKSCGIPLPELALRFILQNPTISATIPGAGNLTELAANVACSEKgPLPPDVATQIESLG 304
Cdd:cd19085 214 epgaeeetfealEKLKEIADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVDL-ELSPSVLERLDEIS 289
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
17-285 |
9.32e-48 |
|
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: 162.39 E-value: 9.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 17 SLGGLFVgKESSDTGIQTIRRALELGVNLFDTAPSYFGGKAQEILGEALNGVKQPHYV-STKVG------------PCPI 83
Cdd:cd19152 9 PLGNLYE-AVSDEEAKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELGREDYViSTKVGrllvplqeveptFEPG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 84 FP-----EPKYDH--DSIMQQVEYNLKALKRDKIDLLHIHDPDRY--GDKGNPGNYHAVFGknmALATLQKLKAQGVIRS 154
Cdd:cd19152 88 FWnplpfDAVFDYsyDGILRSIEDSLQRLGLSRIDLLSIHDPDEDlaGAESDEHFAQAIKG---AFRALEELREEGVIKA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 155 IGIGSLWLDFQAHCIDTGEFDVILTFNRYGLIWRDAQFQSFPFCRRHNVGVMQGTPLHQGVLAVP----RPEWVTTPPDw 230
Cdd:cd19152 165 IGLGVNDWEVILRILEEADLDWVMLAGRYTLLDHSAARELLPECEKRGVKVVNAGPFNSGFLAGGdnfdYYEYGPAPPE- 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1085403013 231 mtvtEHDRYRRLLDIQKSCGIPLPELALRFILQNPTISATIPGAGNLTELAANVA 285
Cdd:cd19152 244 ----LIARRDRIEALCEQHGVSLAAAALQFALAPPAVASVAPGASSPERVEENVA 294
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
29-303 |
5.38e-46 |
|
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: 157.09 E-value: 5.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 29 DTGIQTIRRALELGVNLFDTAPSYFGGKAQEILGEALNG--VKQPHY-VSTKVGPCPIFPEPKYDHDSIMQQVEYNLKAL 105
Cdd:pfam00248 18 EEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDypVKRDKVvIATKVPDGDGPWPSGGSKENIRKSLEESLKRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 106 KRDKIDLLHIHDPDRYGDKGNpgnyhavfgknmALATLQKLKAQGVIRSIGIGSLWLDFQAHCIDTGEFDVILTFNRYGL 185
Cdd:pfam00248 98 GTDYIDLYYLHWPDPDTPIEE------------TWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGKIPIVAVQVEYNL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 186 IWRDAQFQSFPFCRRHNVGVMQGTPLHQGVL--------AVPRPEWVTTPPDWmTVTEHDRYRRLLDIQKSCGIPLPELA 257
Cdd:pfam00248 166 LRRRQEEELLEYCKKNGIPLIAYSPLGGGLLtgkytrdpDKGPGERRRLLKKG-TPLNLEALEALEEIAKEHGVSPAQVA 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1085403013 258 LRFILQNPTISATIPGAGNLTELAANVAcSEKGPLPPDVATQIESL 303
Cdd:pfam00248 245 LRWALSKPGVTIPIPGASNPEQLEDNLG-ALEFPLSDEEVARIDEL 289
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
17-285 |
5.43e-45 |
|
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: 154.44 E-value: 5.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 17 SLGGLFVGKEssDTGIQTIRRALELGVNLFDTAPSYFGGKAQEILGEALNGVKQPHY-VSTKVGPCPIFPEPKYDHDSIM 95
Cdd:cd19162 9 SLGNLARAGE--DEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALARHPRAEYvVSTKVGRLLEPGAAGRPAGADR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 96 QQ----------VEYNLKALKRDKIDLLHIHDPDRYGDKGNPGnyhavfgknmALATLQKLKAQGVIRSIGIGSLWLDFQ 165
Cdd:cd19162 87 RFdfsadgirrsIEASLERLGLDRLDLVFLHDPDRHLLQALTD----------AFPALEELRAEGVVGAIGVGVTDWAAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 166 AHCIDTGEFDVILTFNRYGLIWRDAQFQSFPFCRRHNVGVMQGTPLHQGVLAVPRPEWVTTPPDWMTVTEHDRYRRLLDI 245
Cdd:cd19162 157 LRAARRADVDVVMVAGRYTLLDRRAATELLPLCAAKGVAVVAAGVFNSGILATDDPAGDRYDYRPATPEVLARARRLAAV 236
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1085403013 246 QKSCGIPLPELALRFILQNPTISATIPGAGNLTELAANVA 285
Cdd:cd19162 237 CRRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLA 276
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
14-286 |
6.18e-44 |
|
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381321 [Multi-domain] Cd Length: 253 Bit Score: 150.85 E-value: 6.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 14 SEISLG--GLF--VGKESSDTGIQTIRRALELGVNLFDTAPSYfgGKAQEILGEALNGVKQPHYV-STKVGPCPIFPEPK 88
Cdd:cd19095 1 SVLGLGtsGIGrvWGVPSEAEAARLLNTALDLGINLIDTAPAY--GRSEERLGRALAGLRRDDLFiATKVGTHGEGGRDR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 89 YDH--DSIMQQVEYNLKALKRDKIDLLHIH---DPDRYGDkgnpgnyhavfgknmALATLQKLKAQGVIRSIGIGSlwlD 163
Cdd:cd19095 79 KDFspAAIRASIERSLRRLGTDYIDLLQLHgpsDDELTGE---------------VLETLEDLKAAGKVRYIGVSG---D 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 164 FQA--HCIDTGEFDVILTfnRYGLIWRDAQfQSFPFCRRHNVGVMQGTPLHQGVLaVPRPEWVTTPPDWMtvtehDRYRR 241
Cdd:cd19095 141 GEEleAAIASGVFDVVQL--PYNVLDREEE-ELLPLAAEAGLGVIVNRPLANGRL-RRRVRRRPLYADYA-----RRPEF 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1085403013 242 LLDIQkscGIPLPELALRFILQNPTISATIPGAGNLTELAANVAC 286
Cdd:cd19095 212 AAEIG---GATWAQAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
10-296 |
1.28e-42 |
|
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: 148.51 E-value: 1.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 10 GWQVSEISLGG--LFVGKESSDTGIQTIRRALELGVNLFDTAPSYFGGKAQEILGEALNGVKQPHYV-STKVgpcpIFPE 86
Cdd:cd19074 1 GLKVSELSLGTwlTFGGQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALKGWPRESYViSTKV----FWPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 87 PKYDHDS------IMQQVEYNLKALKRDKIDLLHIHdpdRYgDKGNPgnyhavfgknM--ALATLQKLKAQGVIRSIGIg 158
Cdd:cd19074 77 GPGPNDRglsrkhIFESIHASLKRLQLDYVDIYYCH---RY-DPETP----------LeeTVRAMDDLIRQGKILYWGT- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 159 SLWL-----DFQAHCIDTGEFDVILTFNRYGLIWRDAQFQSFPFCRRHNVGVMQGTPLHQGVLA------VPRPE----W 223
Cdd:cd19074 142 SEWSaeqiaEAHDLARQFGLIPPVVEQPQYNMLWREIEEEVIPLCEKNGIGLVVWSPLAQGLLTgkyrdgIPPPSrsraT 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1085403013 224 VTTPPDWMTVTEHDRY----RRLLDIQKSCGIPLPELALRFILQNPTISATIPGAGNLTELAANVACSEKgPLPPDV 296
Cdd:cd19074 222 DEDNRDKKRRLLTDENlekvKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKASGV-KLSPEV 297
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
14-284 |
4.48e-40 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 142.46 E-value: 4.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 14 SEISLGGLFVG----KESSDTGIQTIRRALELGVNLFDTAPSYFGGKAQEILGEALNGVKQPHYV-STKVG--------- 79
Cdd:cd19161 1 SELGLGTAGLGnlytAVSNADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKPRDEFVlSTKVGrllkpareg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 80 ----------PCPIFPEPKYDHDSIMQQVEYNLKALKRDKIDLLHIHDPDRY--GDKgnpgNYHAVFGKNM--ALATLQK 145
Cdd:cd19161 81 svpdpngfvdPLPFEIVYDYSYDGIMRSFEDSLQRLGLNRIDILYVHDIGVYthGDR----KERHHFAQLMsgGFKALEE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 146 LKAQGVIRSIGIGSLWLDFQAHCIDTGEFDVILTFNRYGLIWRDAQFQSFPFCRRHNVGVMQGTPLHQGVLAVPRP---- 221
Cdd:cd19161 157 LKKAGVIKAFGLGVNEVQICLEALDEADLDCFLLAGRYSLLDQSAEEEFLPRCEQRGTSLVIGGVFNSGILATGTKsgak 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1085403013 222 -EWVTTPPDWMTvtehdryrRLLDIQKSC---GIPLPELALRFILQNPTISATIPGAGNLTELAANV 284
Cdd:cd19161 237 fNYGDAPAEIIS--------RVMEIEKICdayNVPLAAAALQFPLRHPAVASVLTGARNPAQLRQNV 295
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
24-303 |
4.73e-38 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 136.65 E-value: 4.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 24 GKESSDTGIQTIRRALELGVNLFDTAPSYFGGKAQEILGEALNGVKQPHYVSTKVGPCPIFPEPKYDH---DSIMQQVEY 100
Cdd:cd19102 21 GPQDDRDSIAAIRAALDLGINWIDTAAVYGLGHSEEVVGRALKGLRDRPIVATKCGLLWDEEGRIRRSlkpASIRAECEA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 101 NLKALKRDKIDLLHIHDPDRygdkgnPGNYHAVFGknmalaTLQKLKAQGVIRSIGIGSLWLDFQAHCIDTGEFDVILtf 180
Cdd:cd19102 101 SLRRLGVDVIDLYQIHWPDP------DEPIEEAWG------ALAELKEEGKVRAIGVSNFSVDQMKRCQAIHPIASLQ-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 181 NRYGLIWRDAQFQSFPFCRRHNVGVMQGTPLHQGVL--AVPrPEWVTTPP--DWMTVT------EHDRYRRLLD----IQ 246
Cdd:cd19102 167 PPYSLLRRGIEAEILPFCAEHGIGVIVYSPMQSGLLtgKMT-PERVASLPadDWRRRSpffqepNLARNLALVDalrpIA 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1085403013 247 KSCGIPLPELALRFILQNPTISATIPGAGNLTELAANV-ACSEKgpLPPDVATQIESL 303
Cdd:cd19102 246 ERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVgAADLR--LTPEELAEIEAL 301
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
4-284 |
6.10e-37 |
|
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: 134.08 E-value: 6.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 4 RSLGRTGWQVSEISLGGLFVGKES------SDTGIQTIRRALELGVNLFDTAPSYFGGKAQEILGEALNGVKQPHYV-ST 76
Cdd:cd19083 2 VKLGKSDIDVNPIGLGTNAVGGHNlypnldEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLKEYNRNEVViAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 77 K------VGPCPIFPEPKYdhdsIMQQVEYNLKALKRDKIDLLHIHDPdrygDKGNPgnyhavfgKNMALATLQKLKAQG 150
Cdd:cd19083 82 KgahkfgGDGSVLNNSPEF----LRSAVEKSLKRLNTDYIDLYYIHFP----DGETP--------KAEAVGALQELKDEG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 151 VIRSIGIGSLWLDFQAHCIDTGEFDVILtfNRYGLIWRDAQFQSFPFCRRHNVGVMQGTPLHQGVLAVPRPEWVTTPP-D 229
Cdd:cd19083 146 KIRAIGVSNFSLEQLKEANKDGYVDVLQ--GEYNLLQREAEEDILPYCVENNISFIPYFPLASGLLAGKYTKDTKFPDnD 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1085403013 230 WMTVTEH----------DRYRRLLDIQKSCGIPLPELALRFILQNPTISATIPGAGNLTELAANV 284
Cdd:cd19083 224 LRNDKPLfkgerfsenlDKVDKLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNL 288
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
1-303 |
3.33e-36 |
|
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: 131.93 E-value: 3.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 1 MKYRSLGRTGWQVSEISLGGLFVGKESS-DTGIQTIRRALELGVNLFDTAPSYFGGKAQEILGEALNGVKQPHYVSTKVG 79
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGTMNFGGRTDeETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAGRRDDIVLATKVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 80 PcPIFPEPKYDHDS---IMQQVEYNLKALKRDKIDLLHIHDPDRY--GDKGnpgnyhavfgknmaLATLQKLKAQGVIRS 154
Cdd:cd19087 81 G-PMGDDPNDRGLSrrhIRRAVEASLRRLQTDYIDLYQMHHFDRDtpLEET--------------LRALDDLVRQGKIRY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 155 IG---------IGSLWLDFQAHcidTGEFDVILTfnRYGLIWRDAQFQSFPFCRRHNVGVMQGTPLHQGVLA-VPRPewv 224
Cdd:cd19087 146 IGvsnfaawqiAKAQGIAARRG---LLRFVSEQP--MYNLLKRQAELEILPAARAYGLGVIPYSPLAGGLLTgKYGK--- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 225 TTPPDWMTVTEHDRYR-------------RLLDIQKSCGIPLPELALRFILQNPTISATIPGAGNLTELAANVACSEKgP 291
Cdd:cd19087 218 GKRPESGRLVERARYQarygleeyrdiaeRFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEI-T 296
|
330
....*....|..
gi 1085403013 292 LPPDVATQIESL 303
Cdd:cd19087 297 LTPELLAEIDEL 308
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
14-285 |
4.49e-36 |
|
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: 129.56 E-value: 4.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 14 SEISLGGLFVG-KESSDTGIQTIRRALELGVNLFDTAPSYFGGKAQEILGEALNGVKQPH--YVSTKVGPcPIFPEPK-- 88
Cdd:cd06660 1 SRLGLGTMTFGgDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRGNRDdvVIATKGGH-PPGGDPSrs 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 89 -YDHDSIMQQVEYNLKALKRDKIDLLHIH--DPDRYGDKgnpgnyhavfgknmALATLQKLKAQGVIRSIGIG--SLW-- 161
Cdd:cd06660 80 rLSPEHIRRDLEESLRRLGTDYIDLYYLHrdDPSTPVEE--------------TLEALNELVREGKIRYIGVSnwSAErl 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 162 LDFQAHCIDTGEFDVILTFNRYGLIWRDAQFQS-FPFCRRHNVGVMQGTPLHQGvlavprpewvttppdwmtvtehdryr 240
Cdd:cd06660 146 AEALAYAKAHGLPGFAAVQPQYSLLDRSPMEEElLDWAEENGLPLLAYSPLARG-------------------------- 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1085403013 241 rlldiqkscgipLPELALRFILQNPTISATIPGAGNLTELAANVA 285
Cdd:cd06660 200 ------------PAQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
1-288 |
7.07e-36 |
|
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: 131.58 E-value: 7.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 1 MKYRSLGRTGWQVSEISLG--------GLF-----VGKESSDtgiQTIRRALELGVNLFDTAPSYFGGKAQEILGEALNG 67
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGtmtfggggGFFgawggVDQEEAD---RLVDIALDAGINFFDTADVYSEGESEEILGKALKG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 68 VKQPHYVSTKVGpcpiFPEPKYDHDS------IMQQVEYNLKALKRDKIDLLHIHDPDRYGdkgnPgnyhavfgKNMALA 141
Cdd:cd19091 78 RRDDVLIATKVR----GRMGEGPNDVglsrhhIIRAVEASLKRLGTDYIDLYQLHGFDALT----P--------LEETLR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 142 TLQKLKAQGVIRSIGIG--SLWLDFQAHCIDT----GEFdVILTFNrYGLIWRDAQFQSFPFCRRHNVGVMQGTPLHQGV 215
Cdd:cd19091 142 ALDDLVRQGKVRYIGVSnfSAWQIMKALGISErrglARF-VALQAY-YSLLGRDLEHELMPLALDQGVGLLVWSPLAGGL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 216 L------AVPRPEWVTTPPDWMTVTEHDRYR------RLLDIQKSCGIPLPELALRFILQNPTISATIPGAGNLTELAAN 283
Cdd:cd19091 220 LsgkyrrGQPAPEGSRLRRTGFDFPPVDRERgydvvdALREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDN 299
|
....*
gi 1085403013 284 VACSE 288
Cdd:cd19091 300 LGAAG 304
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
3-286 |
1.08e-35 |
|
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: 130.86 E-value: 1.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 3 YRSLGRTGWQVSEISLGGLFVGKESSDTG------IQTIRRALELGVNLFDTAPSYFGGKAQEILGEALNGVKQPHYVST 76
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTWAIGGGPWWGGsddnesIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKGRRDKVVLAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 77 KvgpCPI--------FPEPKYDHD--------SIMQQVEYNLKALKRDKIDLLHIHdpdrYGDKGNPgnyhavFGKNMal 140
Cdd:cd19149 81 K---CGLrwdreggsFFFVRDGVTvyknlspeSIREEVEQSLKRLGTDYIDLYQTH----WQDVETP------IEETM-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 141 ATLQKLKAQGVIRSIGIGSLWLDFQAHCIDTGEFDVILTfnRYGLIWRDAQFQSFPFCRRHNVGVMQGTPLHQGVL---A 217
Cdd:cd19149 146 EALEELKRQGKIRAIGASNVSVEQIKEYVKAGQLDIIQE--KYSMLDRGIEKELLPYCKKNNIAFQAYSPLEQGLLtgkI 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1085403013 218 VPRPEWVTTPP----DWMTVTEHDRYRRLLDI------QKSCGIplPELALRFILQNPTISATIPGAGNLTELAANVAC 286
Cdd:cd19149 224 TPDREFDAGDArsgiPWFSPENREKVLALLEKwkplceKYGCTL--AQLVIAWTLAQPGITSALCGARKPEQAEENAKA 300
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
2-274 |
4.00e-35 |
|
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: 129.24 E-value: 4.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 2 KYRSLGRTGWQVSEISLGGLFVGKESS-------DTGIQTIRRALELGVNLFDTAPSYFGGKAQEILGEAL--NGVKQPH 72
Cdd:cd19079 1 EYVRLGNSGLKVSRLCLGCMSFGDPKWrpwvldeEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALkeFAPRDEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 73 YVSTKVGPcPIFPEPKYDHDS---IMQQVEYNLKALKRDKIDLLHIHDPDrygdkgnpgnYHAVFGKNMalATLQKLKAQ 149
Cdd:cd19079 81 VIATKVYF-PMGDGPNGRGLSrkhIMAEVDASLKRLGTDYIDLYQIHRWD----------YETPIEETL--EALHDVVKS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 150 GVIRSIGIGSLW----LDFQAHCIDTGEFDVILTFNRYGLIWRDAQFQSFPFCRRHNVGVMQGTPLHQGVLAVPR---PE 222
Cdd:cd19079 148 GKVRYIGASSMYawqfAKALHLAEKNGWTKFVSMQNHYNLLYREEEREMIPLCEEEGIGVIPWSPLARGRLARPWgdtTE 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1085403013 223 WVTTPPD-----WMTVTEHDR--YRRLLDIQKSCGIPLPELALRFILQNPTISATIPGA 274
Cdd:cd19079 228 RRRSTTDtaklkYDYFTEADKeiVDRVEEVAKERGVSMAQVALAWLLSKPGVTAPIVGA 286
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
3-308 |
1.77e-34 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 127.59 E-value: 1.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 3 YRSLGRTGWQVSEISLG----GLFVGKESSDTGIQTIRRALELGVNLFDTAPSYFGGKAQEILGEALNGVKQP---HYVS 75
Cdd:PLN02587 1 LRELGSTGLKVSSVGFGasplGSVFGPVSEEDAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKALGIPrekYVVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 76 TKvgpCPIFPEP-KYDHDSIMQQVEYNLKALKRDKIDLLHIHDPDrygdkgnpgnyhavFGK-----NMALATLQKLKAQ 149
Cdd:PLN02587 81 TK---CGRYGEGfDFSAERVTKSVDESLARLQLDYVDILHCHDIE--------------FGSldqivNETIPALQKLKES 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 150 GVIRSIGIGSLWLDFQAHCID---TGEFDVILTFNRYGLiwRDAQFQSF-PFCRRHNVGVMQGTPLHQGVLA-VPRPEWV 224
Cdd:PLN02587 144 GKVRFIGITGLPLAIFTYVLDrvpPGTVDVILSYCHYSL--NDSSLEDLlPYLKSKGVGVISASPLAMGLLTeNGPPEWH 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 225 TTPPDWMTVTehdryRRLLDIQKSCGIPLPELALRFILQNPTISATIPGAGNLTELAANVAcsekgplppdVATQIESLG 304
Cdd:PLN02587 222 PAPPELKSAC-----AAAATHCKEKGKNISKLALQYSLSNKDISTTLVGMNSVQQVEENVA----------AATELETSG 286
|
....
gi 1085403013 305 ILHE 308
Cdd:PLN02587 287 IDEE 290
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
14-290 |
3.01e-33 |
|
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: 122.67 E-value: 3.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 14 SEISLGG-----LFVGKESSDTGIQTIRRALELGVNLFDTAPSYFGGKAQEILGEALNGVKQPH-YVSTKvgpCPIFPEP 87
Cdd:cd19096 1 SVLGFGTmrlpeSDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKEGPREKfYLATK---LPPWSVK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 88 KYDHdsIMQQVEYNLKALKRDKIDLLHIHDPDRYgdkgnpgNYHAVFGKNMALATLQKLKAQGVIRSIGI---GSLWLdF 164
Cdd:cd19096 78 SAED--FRRILEESLKRLGVDYIDFYLLHGLNSP-------EWLEKARKGGLLEFLEKAKKEGLIRHIGFsfhDSPEL-L 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 165 QAhCIDTGEFD-VILTFNrYgLIWRDaqFQSFP---FCRRHNVGVMQGTPLHQGVLAVPRPEwvttppdwmtvtehdryr 240
Cdd:cd19096 148 KE-ILDSYDFDfVQLQYN-Y-LDQEN--QAGRPgieYAAKKGMGVIIMEPLKGGGLANNPPE------------------ 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1085403013 241 rLLDIQKSCGIPLPELALRFILQNPTISATIPGAGNLTELAANVACSEKG 290
Cdd:cd19096 205 -ALAILCGAPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENIAAADEF 253
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
24-292 |
2.01e-32 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 121.09 E-value: 2.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 24 GKESSDTGIQTIRRALELGVNLFDTAPSYfgGKAQEILGEALNGVKQPHYVsTKVGPCPifPEPKYDHDSIMQQVEYNLK 103
Cdd:cd19097 21 GKPSEKEAKKILEYALKAGINTLDTAPAY--GDSEKVLGKFLKRLDKFKII-TKLPPLK--EDKKEDEAAIEASVEASLK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 104 ALKRDKIDLLHIHDPDRYgdkgnPGNYHAVFgknmalATLQKLKAQGVIRSIGIgSL--WLDFQAhCIDTGEFDVI-LTF 180
Cdd:cd19097 96 RLKVDSLDGLLLHNPDDL-----LKHGGKLV------EALLELKKEGLIRKIGV-SVysPEELEK-ALESFKIDIIqLPF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 181 NryglIWrDAQFQSFPFCRR---HNVGVmqgtplH------QGVLAVPRPEWVTTPPDWMTVteHDRYRRLLdiqKSCGI 251
Cdd:cd19097 163 N----IL-DQRFLKSGLLAKlkkKGIEI------HarsvflQGLLLMEPDKLPAKFAPAKPL--LKKLHELA---KKLGL 226
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1085403013 252 PLPELALRFILQNPTISATIPGAGNLTELAANVACSEKGPL 292
Cdd:cd19097 227 SPLELALGFVLSLPEIDKIVVGVDSLEQLKEIIAAFKKPPL 267
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
13-303 |
5.29e-28 |
|
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: 110.73 E-value: 5.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 13 VSEISLGGLFVGKE-SSDTGIQTIRRALELGVNLFDTAPSY-------FGGKAQEILGEAL--NGVKQPHYVSTKV-GP- 80
Cdd:cd19094 1 VSEICLGTMTWGEQnTEAEAHEQLDYAFDEGVNFIDTAEMYpvppspeTQGRTEEIIGSWLkkKGNRDKVVLATKVaGPg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 81 ----CPIFPEPKYDHDSIMQQVEYNLKALKRDKIDLLHIHDPDRY------GDKGNPGNYHAVFGKNMALATLQKLKAQG 150
Cdd:cd19094 81 egitWPRGGGTRLDRENIREAVEGSLKRLGTDYIDLYQLHWPDRYtplfggGYYTEPSEEEDSVSFEEQLEALGELVKAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 151 VIRSIGIG--SLW--LDFQAHCIDTGEFDVILTFNRYGLIWRdaqfqSF-----PFCRRHNVGVMQGTPLHQGVL----- 216
Cdd:cd19094 161 KIRHIGLSneTPWgvMKFLELAEQLGLPRIVSIQNPYSLLNR-----NFeeglaEACHRENVGLLAYSPLAGGVLtgkyl 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 217 --AVPRPEW-VTTPPDWMTvtehdRYR---------RLLDIQKSCGIPLPELALRFILQNPTISATIPGAGNLTELAANV 284
Cdd:cd19094 236 dgAARPEGGrLNLFPGYMA-----RYRspqaleavaEYVKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLKENI 310
|
330
....*....|....*....
gi 1085403013 285 AcSEKGPLPPDVATQIESL 303
Cdd:cd19094 311 D-AFDVPLSDELLAEIDAV 328
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
4-285 |
3.96e-27 |
|
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381379 [Multi-domain] Cd Length: 294 Bit Score: 107.62 E-value: 3.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 4 RSLGRTGWQVSEISLG-----GLFVGKESSDTGIQTIRRALELGVNLFDTAPSYFGGKAQEILGEALNGVKQP---HYVS 75
Cdd:cd19153 3 ETLEIALGNVSPVGLGtaalgGVYGDGLEQDEAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAALQVPrssYTVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 76 TKVGPCPIfPEPKYDHDSIMQQVEYNLKALKRDKIDLLHIHDPDrygdkgnpgnyhavFGK-----NMALATLQKLKAQG 150
Cdd:cd19153 83 TKVGRYRD-SEFDYSAERVRASVATSLERLHTTYLDVVYLHDIE--------------FVDydtlvDEALPALRTLKDEG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 151 VIRSIGIGSLWLDFQAHCID---TGEFDVILTFNRYGLiwRDAQFQS-FPFCRRHN-VGVMQGTPLHQGVLavpRPEwvt 225
Cdd:cd19153 148 VIKRIGIAGYPLDTLTRATRrcsPGSLDAVLSYCHLTL--QDARLESdAPGLVRGAgPHVINASPLSMGLL---TSQ--- 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1085403013 226 TPPDWMTVTEHDRY--RRLLDIQKSCGIPLPELALRFILQN-PTISATIPGAGNLTELAANVA 285
Cdd:cd19153 220 GPPPWHPASGELRHyaAAADAVCASVEASLPDLALQYSLAAhAGVGTVLLGPSSLAQLRSMLA 282
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
1-302 |
6.37e-25 |
|
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: 101.90 E-value: 6.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 1 MKYRSLGRTGWQVSEISLGG--LFVGKESSDTGIQTIRRALELGVNLFDTAPSYFGGKAQEILGEALN--GVKQPHYV-S 75
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSwvTFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKelGWPRSDYVvS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 76 TKV---GPCPiFPEPKY---DHdsIMQQVEYNLKALKRDKIDLLHIHDPDRYGdkgnP-----GNYHAVFGKNMAL--AT 142
Cdd:cd19143 81 TKIfwgGGGP-PPNDRGlsrKH--IVEGTKASLKRLQLDYVDLVFCHRPDPAT----PieetvRAMNDLIDQGKAFywGT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 143 lQKLKAQGVIRSIGIGSLwLDFQAHCIDTGEfdviltfnrYGLIWRDAQFQSF-PFCRRHNVGVMQGTPLHQGVL----- 216
Cdd:cd19143 154 -SEWSAQQIEEAHEIADR-LGLIPPVMEQPQ---------YNLFHRERVEVEYaPLYEKYGLGTTTWSPLASGLLtgkyn 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 217 ---------AVPRPEWVTTPPDWMTVTEHDRYRRLLDIQKSCGIPLPELALRFILQNPTISATIPGAGNLTELAANVACS 287
Cdd:cd19143 223 ngipegsrlALPGYEWLKDRKEELGQEKIEKVRKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEENLKAL 302
|
330
....*....|....*.
gi 1085403013 288 EKGP-LPPDVATQIES 302
Cdd:cd19143 303 EVLPkLTPEVMEKIEA 318
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
15-303 |
6.53e-25 |
|
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: 101.86 E-value: 6.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 15 EISLGGLFVGKESSDTGIQTIRRAL----ELGVNLFDTAPSYFGGKAQEILGEALNGvKQPHYVSTKVgpcPIFPEPKYD 90
Cdd:cd19075 2 KIILGTMTFGSQGRFTTAEAAAELLdaflERGHTEIDTARVYPDGTSEELLGELGLG-ERGFKIDTKA---NPGVGGGLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 91 HDSIMQQVEYNLKALKRDKIDLLHIHDPDRygdkGNPgnyhavfgknMA--LATLQKLKAQGVIRSIGIG--SLWLDFQA 166
Cdd:cd19075 78 PENVRKQLETSLKRLKVDKVDVFYLHAPDR----STP----------LEetLAAIDELYKEGKFKEFGLSnySAWEVAEI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 167 HCIDT-----------GEfdviltfnrYGLIWRDAQFQSFPFCRRHNVGVMQGTPLHQGVLAVPRPEWVTTPPD------ 229
Cdd:cd19075 144 VEICKengwvlptvyqGM---------YNAITRQVETELFPCLRKLGIRFYAYSPLAGGFLTGKYKYSEDKAGGgrfdpn 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 230 --WMTVTeHDRYRR------LLDIQKSC---GIPLPELALRFILQNPTISAT-----IPGAGNLTELAANVACSEKGPLP 293
Cdd:cd19075 215 naLGKLY-RDRYWKpsyfeaLEKVEEAAekeGISLAEAALRWLYHHSALDGEkgdgvILGASSLEQLEENLAALEKGPLP 293
|
330
....*....|
gi 1085403013 294 PDVATQIESL 303
Cdd:cd19075 294 EEVVKAIDEA 303
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
12-274 |
2.61e-24 |
|
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: 100.07 E-value: 2.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 12 QVSEISLG-----GLFVGKESSDTGIQTIRRALELGVNLFDTAPSYFGGKAQEILGEALN--GVKQPHYVSTKVGpCPIF 84
Cdd:cd19148 3 PVSRIALGtwaigGWMWGGTDEKEAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKeyGKRDRVVIATKVG-LEWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 85 PEPKYDHDS----IMQQVEYNLKALKRDKIDLLHIHDPdrygDKGNPGNYHAvfgknmalATLQKLKAQGVIRSIGIGsl 160
Cdd:cd19148 82 EGGEVVRNSsparIRKEVEDSLRRLQTDYIDLYQVHWP----DPLVPIEETA--------EALKELLDEGKIRAIGVS-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 161 wlDFQAHCIDTGEFDVILTFN--RYGLIWRDAQFQSFPFCRRHNVGVMQGTPLHQGVLAVPRPEWVTTPPDWMTVT---- 234
Cdd:cd19148 148 --NFSPEQMETFRKVAPLHTVqpPYNLFEREIEKDVLPYARKHNIVTLAYGALCRGLLSGKMTKDTKFEGDDLRRTdpkf 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1085403013 235 EHDRYRRLLDI--------QKSCGIPLPELALRFILQNPTISATIPGA 274
Cdd:cd19148 226 QEPRFSQYLAAveeldklaQERYGKSVIHLAVRWLLDQPGVSIALWGA 273
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
12-288 |
3.40e-23 |
|
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: 96.14 E-value: 3.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 12 QVSEISLG-GLFVGKESSDTG-----IQTIRRALELGVNLFDTAPSYFGGKAQEILGEALNGVKQPH-YVSTKVgpcpiF 84
Cdd:cd19072 3 EVPVLGLGtWGIGGGMSKDYSddkkaIEALRYAIELGINLIDTAEMYGGGHAEELVGKAIKGFDREDlFITTKV-----S 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 85 PEpKYDHDSIMQQVEYNLKALKRDKIDLLHIHDPdrygdkgnpgNYHAVFGKNMalATLQKLKAQGVIRSIGIGSLWLDF 164
Cdd:cd19072 78 PD-HLKYDDVIKAAKESLKRLGTDYIDLYLIHWP----------NPSIPIEETL--RAMEELVEEGKIRYIGVSNFSLEE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 165 QAHCID-TGEFDVILTFNRYGLIWRDAQFQSFPFCRRHNVGVMQGTPLHQGVLAVPrpewvttppdwmtvtehDRYRRLL 243
Cdd:cd19072 145 LEEAQSyLKKGPIVANQVEYNLFDREEESGLLPYCQKNGIAIIAYSPLEKGKLSNA-----------------KGSPLLD 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1085403013 244 DIQKSCGIPLPELALRFILQNPTISAtIPGAGNLTELAANVACSE 288
Cdd:cd19072 208 EIAKKYGKTPAQIALNWLISKPNVIA-IPKASNIEHLEENAGALG 251
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
16-288 |
1.07e-22 |
|
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: 94.59 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 16 ISLGGLFVGKESSDTGIQTIRRALELGVNLFDTAPSYFGGKAQEILGEALNGVKQPHYVSTKVG---PCPIFPEPKYDHD 92
Cdd:cd19088 11 LTGPGIWGPPADREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHPYPDDVVIATKGGlvrTGPGWWGPDGSPE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 93 SIMQQVEYNLKALKRDKIDL--LHIHDPDR-YGDkgnpgnyhavfgknmALATLQKLKAQGVIRSIGIGSLWLDF--QAH 167
Cdd:cd19088 91 YLRQAVEASLRRLGLDRIDLyqLHRIDPKVpFEE---------------QLGALAELQDEGLIRHIGLSNVTVAQieEAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 168 CIdtgeFDVILTFNRYGLIWRDAqFQSFPFCRRHNVGVMQGTPLHQGVLAVPRpewvttppdwmtvtehdryRRLLDIQK 247
Cdd:cd19088 156 AI----VRIVSVQNRYNLANRDD-EGVLDYCEAAGIAFIPWFPLGGGDLAQPG-------------------GLLAEVAA 211
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1085403013 248 SCGIPLPELALRFILQ-NPTISAtIPGAGNLTELAANVACSE 288
Cdd:cd19088 212 RLGATPAQVALAWLLArSPVMLP-IPGTSSVEHLEENLAAAG 252
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
26-285 |
1.21e-21 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 92.73 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 26 ESSDTgIQTIRRALELGVNLFDTAPSYfgGKAQEILGEALNGVKQPH-----YVSTKVGPCPiFPEPKYDHDSIMQQVEY 100
Cdd:cd19164 32 ESIPP-VDIVRRALELGIRAFDTSPYY--GPSEIILGRALKALRDEFprdtyFIITKVGRYG-PDDFDYSPEWIRASVER 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 101 NLKALKRDKIDLLHIHDPDRYGDKGnpgnyhaVFGknmALATLQKLKAQGVIRSIGIGSLWLDF---QAHCIDT---GEF 174
Cdd:cd19164 108 SLRRLHTDYLDLVYLHDVEFVADEE-------VLE---ALKELFKLKDEGKIRNVGISGYPLPVllrLAELARTtagRPL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 175 DVILTFNRYGLiwrdaQFQSFP-----FCRRHNVG-VMQGTPLHQGVL-AVPRPEWVTTPPDwMTVTEHdryrRLLDIQK 247
Cdd:cd19164 178 DAVLSYCHYTL-----QNTTLLayipkFLAAAGVKvVLNASPLSMGLLrSQGPPEWHPASPE-LRAAAA----KAAEYCQ 247
|
250 260 270
....*....|....*....|....*....|....*....
gi 1085403013 248 SCGIPLPELALRFILQ-NPTISATIPGAGNLTELAANVA 285
Cdd:cd19164 248 AKGTDLADVALRYALReWGGEGPTVVGCSNVDELEEAVE 286
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
3-295 |
2.34e-21 |
|
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: 91.94 E-value: 2.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 3 YRSLGRTGWQVSEISLG--GLFVGKESSDTGIQTIRRALELGVNLFDTAPSYFG--GKAQEILGEALNGVKQPH----YV 74
Cdd:cd19089 1 YRRCGRSGLHLPAISLGlwHNFGDYTSPEEARELLRTAFDLGITHFDLANNYGPppGSAEENFGRILKRDLRPYrdelVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 75 STKVG----PCPI--FPEPKYdhdsIMQQVEYNLKALKRDKIDLLHIHdpdRYgDKGNP-----GN-YHAVF-GK----- 136
Cdd:cd19089 81 STKAGygmwPGPYgdGGSRKY----LLASLDQSLKRMGLDYVDIFYHH---RY-DPDTPleetmTAlADAVRsGKalyvg 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 137 --NMALATLQKLKAqgVIRSIGIgslwldfqahcidtgefDVILTFNRYGLIWRDAQFQSFPFCRRHNVGVMQGTPLHQG 214
Cdd:cd19089 153 isNYPGAKARRAIA--LLRELGV-----------------PLIIHQPRYSLLDRWAEDGLLEVLEEAGIGFIAFSPLAQG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 215 VLA------VPRPEWVTTPPDWMT---VTEH--DRYRRLLDIQKSCGIPLPELALRFILQNPTISATIPGAGNLTELAAN 283
Cdd:cd19089 214 LLTdkylngIPPDSRRAAESKFLTeeaLTPEklEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVTSVLIGASSPSQLEDN 293
|
330
....*....|..
gi 1085403013 284 VACSEKGPLPPD 295
Cdd:cd19089 294 VAALKNLDFSEE 305
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
4-304 |
2.47e-21 |
|
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: 91.90 E-value: 2.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 4 RSLGRTGWQVSEISLGGLFVGKE-----SSDTGIQTIRRALELGVNLFDTAPSYFGGKAQEILGEALNGVKQPHYVSTK- 77
Cdd:cd19080 1 RLLGRSGLRVSPLALGTMTFGTEwgwgaDREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAGNRDRIVLATKy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 78 -VGPCPIFPEPKYDH-DSIMQQVEYNLKALKRDKIDLLHIHDPDRygdkgnpgnyhavfgknMA-----LATLQKLKAQG 150
Cdd:cd19080 81 tMNRRPGDPNAGGNHrKNLRRSVEASLRRLQTDYIDLLYVHAWDF-----------------TTpveevMRALDDLVRAG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 151 VIRSIGIGSL--WLDFQAHCIdtGEFD-----VILTfNRYGLIWRDAQFQSFPFCRRHNVGVMQGTPLHQGVL------- 216
Cdd:cd19080 144 KVLYVGISDTpaWVVARANTL--AELRgwspfVALQ-IEYSLLERTPERELLPMARALGLGVTPWSPLGGGLLtgkyqrg 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 217 -AVPRPEWVTTPPDWMTVTEHDR--YRRLLDIQKSCGIPLPELALRFILQNPTISATIPGAGNLTELAANVACSEKgPLP 293
Cdd:cd19080 221 eEGRAGEAKGVTVGFGKLTERNWaiVDVVAAVAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDL-TLS 299
|
330
....*....|.
gi 1085403013 294 PDvatQIESLG 304
Cdd:cd19080 300 PE---QLARLD 307
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
6-303 |
2.72e-21 |
|
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: 91.89 E-value: 2.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 6 LGRTGWQVSEISLGGLFVGKESS-DTGIQTIRRALELGVNLFDTAPSY-------FGGKAQEILGEAL--NGVKQPHYVS 75
Cdd:cd19081 2 LGRTGLSVSPLCLGTMVFGWTADeETSFALLDAFVDAGGNFIDTADVYsawvpgnAGGESETIIGRWLksRGKRDRVVIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 76 TKVGpCPIFPE-----PKYdhdsIMQQVEYNLKALKRDKIDLLHIHDPDRygdkgnpgnyhAVFGKNMaLATLQKLKAQG 150
Cdd:cd19081 82 TKVG-FPMGPNgpglsRKH----IRRAVEASLRRLQTDYIDLYQAHWDDP-----------ATPLEET-LGALNDLIRQG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 151 VIRSIGIG--SLWLDFQAHCIDTGE----FDVILTfnRYGLIWRD-AQFQSFPFCRRHNVGVMQGTPLHQGVLA------ 217
Cdd:cd19081 145 KVRYIGASnySAWRLQEALELSRQHglprYVSLQP--EYNLVDREsFEGELLPLCREEGIGVIPYSPLAGGFLTgkyrse 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 218 ------VPRPEWV---TTPPDWMTVTEhdryrrLLDIQKSCGIPLPELALRFILQNPTISATIPGAGNLTELAANVACSE 288
Cdd:cd19081 223 adlpgsTRRGEAAkryLNERGLRILDA------LDEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAG 296
|
330
....*....|....*
gi 1085403013 289 kGPLPPDvatQIESL 303
Cdd:cd19081 297 -LRLTDE---EVARL 307
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
2-119 |
3.36e-20 |
|
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: 88.81 E-value: 3.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 2 KYRSLGRTGWQVSEISLG--GL--FVGKESSDTGIQTIRRALELGVNLFDTAPSYFGGKAQEILGEALNGVKQPHYVSTK 77
Cdd:cd19076 1 PTRKLGTQGLEVSALGLGcmGMsaFYGPADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKDRRDEVVIATK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1085403013 78 VG----PCPIFPEPKYDHDSIMQQVEYNLKALKRDKIDLLHIHDPD 119
Cdd:cd19076 81 FGivrdPGSGFRGVDGRPEYVRAACEASLKRLGTDVIDLYYQHRVD 126
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
11-286 |
1.20e-19 |
|
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: 86.90 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 11 WQVSEISLGGlfvGKESSDTGIQTI-RRALELGVNLFDTAPSYFGGKAQEILGEAL--NGVKQPHYVSTKVGPCPifpeP 87
Cdd:cd19093 10 WQWGDRLWWG---YGEYGDEDLQAAfDAALEAGVNLFDTAEVYGTGRSERLLGRFLkeLGDRDEVVIATKFAPLP----W 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 88 KYDHDSIMQQVEYNLKALKRDKIDLLHIHDPDrygdkgnpgnyhAVFGKNMALA-TLQKLKAQGVIRSIGIGSLWLD--F 164
Cdd:cd19093 83 RLTRRSVVKALKASLERLGLDSIDLYQLHWPG------------PWYSQIEALMdGLADAVEEGLVRAVGVSNYSADqlR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 165 QAH-CIDTGEFDVILTFNRYGLIWRDA-QFQSFPFCRRHNVGVMQGTPLHQGVLA-VPRPEwvtTPPdwmtvteHDRYRR 241
Cdd:cd19093 151 RAHkALKERGVPLASNQVEYSLLYRDPeQNGLLPACDELGITLIAYSPLAQGLLTgKYSPE---NPP-------PGGRRR 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1085403013 242 LL----------------DIQKSCGIPLPELALRFILQNPTISatIPGAGNLTELAANVAC 286
Cdd:cd19093 221 LFgrknlekvqplldaleEIAEKYGKTPAQVALNWLIAKGVVP--IPGAKNAEQAEENAGA 279
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
13-217 |
1.21e-19 |
|
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: 87.29 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 13 VSEISLG--GLFVGK---ESSDTGIQTIRRALELGVNLFDTAPSYFGGKAQEILGEALNGVKQPHYVSTKVG-----PCP 82
Cdd:cd19078 4 VSAIGLGcmGMSHGYgppPDKEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKPFRDQVVIATKFGfkidgGKP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 83 IFPEPKYDHDSIMQQVEYNLKALKRDKIDLLHIH--DPDRygdkgnpgNYHAVFGknmalaTLQKLKAQGVIRSIGIGSL 160
Cdd:cd19078 84 GPLGLDSRPEHIRKAVEGSLKRLQTDYIDLYYQHrvDPNV--------PIEEVAG------TMKELIKEGKIRHWGLSEA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1085403013 161 WLDF--QAHCIdtgeFDVILTFNRYGLIWRDAQFQSFPFCRRHNVGVMQGTPLHQGVLA 217
Cdd:cd19078 150 GVETirRAHAV----CPVTAVQSEYSMMWREPEKEVLPTLEELGIGFVPFSPLGKGFLT 204
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-285 |
6.04e-19 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 85.45 E-value: 6.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 11 WQVSEISLGGLFVG--KESSDTGIQTIRRALELGVNLFDTAPSYFGGKAQEILGEALNGVKQPH-------YVSTKVGPC 81
Cdd:cd19099 1 LTLSSLGLGTYRGDsdDETDEEYREALKAALDSGINVIDTAINYRGGRSERLIGKALRELIEKGgikrdevVIVTKAGYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 82 P------------------IFPEPKYDHDS---------IMQQVEYNLKALKRDKIDLLHIHDPDRYGDKGNPGNYHAVF 134
Cdd:cd19099 81 PgdgdeplrplkyleeklgRGLIDVADSAGlrhcispayLEDQIERSLKRLGLDTIDLYLLHNPEEQLLELGEEEFYDRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 135 GKnmALATLQKLKAQGVIRSIGIgSLWLDFQA-------------------------HC------IDTGEFDVILTFNRY 183
Cdd:cd19099 161 EE--AFEALEEAVAEGKIRYYGI-STWDGFRAppalpghlsleklvaaaeevggdnhHFkviqlpLNLLEPEALTEKNTV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 184 GLIWRDAqfqsFPFCRRHNVGVMQGTPLHQGVLA--VPRPEWVTTPPDWmtvtehdryrrlldiqkscgiPLPELALRFI 261
Cdd:cd19099 238 KGEALSL----LEAAKELGLGVIASRPLNQGQLLgeLRLADLLALPGGA---------------------TLAQRALQFA 292
|
330 340
....*....|....*....|....
gi 1085403013 262 LQNPTISATIPGAGNLTELAANVA 285
Cdd:cd19099 293 RSTPGVDSALVGMRRPEHVDENLA 316
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
20-286 |
3.68e-18 |
|
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: 82.14 E-value: 3.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 20 GLFVGKESSDTGIQTIRRALELGVNLFDTAPSYfggKAQEILGEALN--GVKQPH-YVSTKVGPCpifpepKYDHDSIMQ 96
Cdd:cd19071 5 GLGTYKLKPEETAEAVLAALEAGYRHIDTAAAY---GNEAEVGEAIResGVPREElFITTKLWPT------DHGYERVRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 97 QVEYNLKALKRDKIDLLHIHDPDRYGDKGNPGNYHAVFgknmalATLQKLKAQGVIRSIGIGslwlDFQAHCIDT--GEF 174
Cdd:cd19071 76 ALEESLKDLGLDYLDLYLIHWPVPGKEGGSKEARLETW------RALEELVDEGLVRSIGVS----NFNVEHLEEllAAA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 175 DVILTFNrygliwrdaQFQSFP---------FCRRHNVGVMQGTPLHQGVLAVPRPEwvttppdwmtvtehdryrRLLDI 245
Cdd:cd19071 146 RIKPAVN---------QIELHPylqqkelveFCKEHGIVVQAYSPLGRGRRPLLDDP------------------VLKEI 198
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1085403013 246 QKSCGIPLPELALRFILQNPTIsaTIPGAGNLTELAANVAC 286
Cdd:cd19071 199 AKKYGKTPAQVLLRWALQRGVV--VIPKSSNPERIKENLDV 237
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
20-285 |
1.51e-17 |
|
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: 80.39 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 20 GLFVGKESSDTGIQTIRRALELGVNLFDTAPSYfggKAQEILGEALNGVKQPH---YVSTKvgpcpIFPEpKYDHDSIMQ 96
Cdd:cd19073 5 GLGTWQLRGDDCANAVKEALELGYRHIDTAEIY---NNEAEVGEAIAESGVPRedlFITTK-----VWRD-HLRPEDLKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 97 QVEYNLKALKRDKIDLLHIHDPDRygdkgnpgNYHAvfgkNMALATLQKLKAQGVIRSIGIGSLWLDFQAHCIDTG---- 172
Cdd:cd19073 76 SVDRSLEKLGTDYVDLLLIHWPNP--------TVPL----EETLGALKELKEAGKVKSIGVSNFTIELLEEALDISplpi 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 173 -----EFDVILtfNRYGLIwrdaqfqsfPFCRRHNVGVMQGTPLHQG-VLAVPrpewvttppdwmtvtehdryrRLLDIQ 246
Cdd:cd19073 144 avnqvEFHPFL--YQAELL---------EYCRENDIVITAYSPLARGeVLRDP---------------------VIQEIA 191
|
250 260 270
....*....|....*....|....*....|....*....
gi 1085403013 247 KSCGIPLPELALRFILQNPTIsaTIPGAGNLTELAANVA 285
Cdd:cd19073 192 EKYDKTPAQVALRWLVQKGIV--VIPKASSEDHLKENLA 228
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
14-288 |
2.95e-16 |
|
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: 77.59 E-value: 2.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 14 SEISLGGLFVG-KESSDTGIQTIRRALELGVNLFDTAPSY----FGGKAQEILGEAL--NGVKQPHYVSTKvGPCPIFPE 86
Cdd:cd19082 1 SRIVLGTADFGtRIDEEEAFALLDAFVELGGNFIDTARVYgdwvERGASERVIGEWLksRGNRDKVVIATK-GGHPDLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 87 ---PKYDHDSIMQQVEYNLKALKRDKIDL--LHIHDPDRygdkgnpgnyhAV--FgknmaLATLQKLKAQGVIRSIGiGS 159
Cdd:cd19082 80 msrSRLSPEDIRADLEESLERLGTDYIDLyfLHRDDPSV-----------PVgeI-----VDTLNELVRAGKIRAFG-AS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 160 LW-----LDFQAHCIDTGEFDVILTFNRYGL------IWRDAQFQS-----FPFCRRHNVGVMQGTPLHQGVLAVPRPEW 223
Cdd:cd19082 143 NWsteriAEANAYAKAHGLPGFAASSPQWSLarpnepPWPGPTLVAmdeemRAWHEENQLPVFAYSSQARGFFSKRAAGG 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1085403013 224 VTTPPD----WMTVTEHDRYRRLLDIQKSCGIPLPELALRFILQNPTISATIPGAGNLTELAANVACSE 288
Cdd:cd19082 223 AEDDSElrrvYYSEENFERLERAKELAEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAAAD 291
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
9-156 |
4.27e-16 |
|
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: 76.83 E-value: 4.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 9 TGWQVSEISLG--GLFVGKESSDTGIQTIRRALELGVNLFDTAPSYFGGKAQEILGEALNgvKQPHY-----VSTKVGPC 81
Cdd:cd19092 2 EGLEVSRLVLGcmRLADWGESAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALA--LNPGLrekieIQTKCGIR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 82 PIFPEPK-----YD--HDSIMQQVEYNLKALKRDKIDLLHIHDPDrygdkgnpgnyhavfgknmALA-------TLQKLK 147
Cdd:cd19092 80 LGDDPRPgrikhYDtsKEHILASVEGSLKRLGTDYLDLLLLHRPD-------------------PLMdpeevaeAFDELV 140
|
....*....
gi 1085403013 148 AQGVIRSIG 156
Cdd:cd19092 141 KSGKVRYFG 149
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
29-288 |
4.61e-16 |
|
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: 76.46 E-value: 4.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 29 DTGIQTIRRALELGVNLFDTAPSYFGGKAQEILGEA-LNGVKQPHYVSTKVGPCPIfpepkyDHDSIMQQVEYNLKALKR 107
Cdd:cd19137 26 EEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAiKDFPREDLFIVTKVWPTNL------RYDDLLRSLQNSLRRLDT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 108 DKIDLLHIHDPdrygdkgNPGnyhavFGKNMALATLQKLKAQGVIRSIGIGSLWLDFQAHCIDTGEFDVILTFNRYGLIW 187
Cdd:cd19137 100 DYIDLYLIHWP-------NPN-----IPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQTPIVCNQVKYNLED 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 188 RDAQFQS-FPFCRRHNVGVMQGTPLHQGVLAVPrpewvttppdwmtvtehdryRRLLDIQKSCGIPLPELALRFILQNPT 266
Cdd:cd19137 168 RDPERDGlLEYCQKNGITVVAYSPLRRGLEKTN--------------------RTLEEIAKNYGKTIAQIALAWLIQKPN 227
|
250 260
....*....|....*....|..
gi 1085403013 267 IsATIPGAGNLTELAANVACSE 288
Cdd:cd19137 228 V-VAIPKAGRVEHLKENLKATE 248
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
1-285 |
5.00e-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: 76.52 E-value: 5.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 1 MKYRSLGRTGWQVSEislgglfvGKESSDTGIQTIRRALELGVNLFDTAPSYFGGKAQEILGEALNGVKQPHYVSTKVGP 80
Cdd:cd19138 9 TKVPALGQGTWYMGE--------DPAKRAQEIEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIRGRRDKVFLVSKVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 81 cpifpePKYDHDSIMQQVEYNLKALKRDKID--LLHIhdpdrygdkgnPGNYHavFGKNMalATLQKLKAQGVIRSIGIG 158
Cdd:cd19138 81 ------SNASRQGTVRACERSLRRLGTDYLDlyLLHW-----------RGGVP--LAETV--AAMEELKKEGKIRAWGVS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 159 SLWLDfqahciDTGEFDVI-----LTFN--RYGLIWRDAQFQSFPFCRRHNVGVMQGTPLHQGVLavPRPEWVTTPpdwm 231
Cdd:cd19138 140 NFDTD------DMEELWAVpgggnCAANqvLYNLGSRGIEYDLLPWCREHGVPVMAYSPLAQGGL--LRRGLLENP---- 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1085403013 232 tvtehdryrRLLDIQKSCGIPLPELALRFILQNPTISAtIPGAGNLTELAANVA 285
Cdd:cd19138 208 ---------TLKEIAARHGATPAQVALAWVLRDGNVIA-IPKSGSPEHARENAA 251
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
29-285 |
6.72e-15 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 73.17 E-value: 6.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 29 DTGIQTIRRALELGVNLFDTAPSYfggKAQEILGEAL--NGVKQPH-YVSTKVGPcpifpePKYDHDSIMQQVEYNLKAL 105
Cdd:COG0656 18 EEAAAAVRTALEAGYRHIDTAAMY---GNEEGVGEAIaaSGVPREElFVTTKVWN------DNHGYDDTLAAFEESLERL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 106 KRDKIDLLHIHDPdrygdkgNPGNYHAvfgknmALATLQKLKAQGVIRSIGIgSlwlDFQAHCIDT--GEFDVILTFN-- 181
Cdd:COG0656 89 GLDYLDLYLIHWP-------GPGPYVE------TWRALEELYEEGLIRAIGV-S---NFDPEHLEEllAETGVKPAVNqv 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 182 RYGLIWRdaQFQSFPFCRRHNVGVMQGTPLHQG-VLAVPrpewvttppdwmTVTE-HDRYrrlldiQKSCGiplpELALR 259
Cdd:COG0656 152 ELHPYLQ--QRELLAFCREHGIVVEAYSPLGRGkLLDDP------------VLAEiAEKH------GKTPA----QVVLR 207
|
250 260
....*....|....*....|....*.
gi 1085403013 260 FILQNPTIsaTIPGAGNLTELAANVA 285
Cdd:COG0656 208 WHLQRGVV--VIPKSVTPERIRENLD 231
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
1-291 |
2.00e-13 |
|
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: 69.69 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 1 MKYRSLGRTGWQVSEISLGG--LFVGKESSDTGIQTIRRALELGVNLFDTAPSYFGGKAQEILGEAL---NGVKQPHYVS 75
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTwvTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIkkkGWRRSSLVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 76 TKV---GPCPIfpEPKYDHDSIMQQVEYNLKALKRDKIDLLHIHDPDrygdkgnpgnyhavfgKNMALATLqkLKAQGVI 152
Cdd:cd19159 81 TKLywgGKAET--ERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPD----------------SNTPMEEI--VRAMTHV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 153 RSIGIGSLWLDFQAHCIDTGE-FDVILTFN---------RYGLIWRDAQFQSFP-FCRRHNVGVMQGTPLHQGVLA---- 217
Cdd:cd19159 141 INQGMAMYWGTSRWSAMEIMEaYSVARQFNmippvceqaEYHLFQREKVEVQLPeLYHKIGVGAMTWSPLACGIISgkyg 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 218 --VPRPEWVTTPP-DWMT---VTEHDRYRR-----LLDIQKSCGIPLPELALRFILQNPTISATIPGAGNLTELAANVAC 286
Cdd:cd19159 221 ngVPESSRASLKCyQWLKeriVSEEGRKQQnklkdLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 300
|
....*
gi 1085403013 287 SEKGP 291
Cdd:cd19159 301 IQVLP 305
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-284 |
8.92e-13 |
|
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: 67.62 E-value: 8.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 10 GWQVSeislgglfvGKESSDTGIQTIRRAL----ELGVNLFDTAPSYfgGKAQEILGEALNGVKQPHYVSTKVGPCPIF- 84
Cdd:cd19101 9 MWQLS---------GGHGGIRDEDAAVRAMaayvDAGLTTFDCADIY--GPAEELIGEFRKRLRRERDAADDVQIHTKWv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 85 PEPKYDHDSiMQQVEYN----LKALKRDKIDLL--HIHDPD--RYGDkgnpgnyhavfgknmALATLQKLKAQGVIRSIG 156
Cdd:cd19101 78 PDPGELTMT-RAYVEAAidrsLKRLGVDRLDLVqfHWWDYSdpGYLD---------------AAKHLAELQEEGKIRHLG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 157 igslwldfqahcidTGEFDVI-----------LTFNR--YGLIWRDAQFQSFPFCRRHNVGVMQ-GTpLHQGVLA----- 217
Cdd:cd19101 142 --------------LTNFDTErlreildagvpIVSNQvqYSLLDRRPENGMAALCEDHGIKLLAyGT-LAGGLLSekylg 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1085403013 218 VPRPEWVTTPP-----DWMTVTEH---DRYRRLL----DIQKSCGIPLPELALRFILQNPTISATIPGAGNLTELAANV 284
Cdd:cd19101 207 VPEPTGPALETrslqkYKLMIDEWggwDLFQELLrtlkAIADKHGVSIANVAVRWVLDQPGVAGVIVGARNSEHIDDNV 285
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
20-220 |
1.32e-12 |
|
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: 66.63 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 20 GLFVGKESSDTGIQTIRRALELGVNLFDTAPSYfggKAQEILGEALNGVKQPH---YVSTKVGpcpifpEPKYDHDSIMQ 96
Cdd:cd19131 14 GLGVWQVSNDEAASAVREALEVGYRSIDTAAIY---GNEEGVGKAIRASGVPReelFITTKLW------NSDQGYDSTLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 97 QVEYNLKALKRDKIDLLHIHDP----DRYGDkgnpgnyhavfgknmALATLQKLKAQGVIRSIGIGSLWLDFQAHCIDtg 172
Cdd:cd19131 85 AFDESLRKLGLDYVDLYLIHWPvpaqDKYVE---------------TWKALIELKKEGRVKSIGVSNFTIEHLQRLID-- 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1085403013 173 EFDVILTFNRYGLIWRDAQFQSFPFCRRHNVGVMQGTPLHQG-VLAVPR 220
Cdd:cd19131 148 ETGVVPVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGgLLSDPV 196
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
20-284 |
1.68e-12 |
|
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: 66.54 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 20 GLFVGKESsDTGIQTIRRALELGVNLFDTAPSYFGgkaQEILGEAL------NGVKQPH-YVSTKVGpcPIFPEPKydhd 92
Cdd:cd19116 17 GTWKLKDD-EGVRQAVKHAIEAGYRHIDTAYLYGN---EAEVGEAIrekiaeGVVKREDlFITTKLW--NSYHERE---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 93 simqQVEY----NLKALKRDKIDLLHIHDPDRY-GDKGNPGNYHAVFGKNMALAT---LQKLKAQGVIRSIGIGslwlDF 164
Cdd:cd19116 87 ----QVEPalreSLKRLGLDYVDLYLIHWPVAFkENNDSESNGDGSLSDIDYLETwrgMEDLVKLGLTRSIGVS----NF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 165 QAHCIDT-----------GEFDVILTFNRYGLIwrdaqfqsfPFCRRHNVGVMQGTPLHQgvlAVPRPewVTTPPDWMTv 233
Cdd:cd19116 159 NSEQINRllsncnikpavNQIEVHPTLTQEKLV---------AYCQSNGIVVMAYSPFGR---LVPRG--QTNPPPRLD- 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1085403013 234 tehdrYRRLLDIQKSCGIPLPELALRFILQNPTISatIPGAGNLTELAANV 284
Cdd:cd19116 224 -----DPTLVAIAKKYGKTTAQIVLRYLIDRGVVP--IPKSSNKKRIKENI 267
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
1-310 |
1.79e-12 |
|
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: 67.03 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 1 MKYRSLGRTGWQVSEISLGG--LFVGKESSDTGIQTIRRALELGVNLFDTAPSYFGGKAQEILGEALNgvKQPHYVSTKV 78
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTwvTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIK--KKGWRRSSLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 79 GPCPIF------PEPKYDHDSIMQQVEYNLKALKRDKIDLLHIHDPDrygdkgnpgnyhavfgKNMALAtlQKLKAQGVI 152
Cdd:cd19158 79 ITTKIFwggkaeTERGLSRKHIIEGLKASLERLQLEYVDVVFANRPD----------------PNTPME--ETVRAMTHV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 153 RSIGIGSLWLDFQAHCIDTGE-FDVILTFNRYGLIWRDAQFQSF----------PFCRRHNVGVMQGTPLHQGVLAVPRP 221
Cdd:cd19158 141 INQGMAMYWGTSRWSSMEIMEaYSVARQFNLIPPICEQAEYHMFqrekvevqlpELFHKIGVGAMTWSPLACGIVSGKYD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 222 EWVttPP---------DWMT---VTEHDR-----YRRLLDIQKSCGIPLPELALRFILQNPTISATIPGAGNLTELAANV 284
Cdd:cd19158 221 SGI--PPysraslkgyQWLKdkiLSEEGRrqqakLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENI 298
|
330 340
....*....|....*....|....*..
gi 1085403013 285 ACSEKGP-LPPDVATQIEslGILHEDP 310
Cdd:cd19158 299 GAIQVLPkLSSSIVHEID--SILGNKP 323
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
4-285 |
7.40e-12 |
|
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: 64.76 E-value: 7.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 4 RSLGRTGWQVSEISLG--GL--FVGKESSDT-GIQTIRRALELGVNLFDTAPSYfGGKAQEIL-GEAL-NGVKQPHYVST 76
Cdd:cd19145 3 VKLGSQGLEVSAQGLGcmGLsgDYGAPKPEEeGIALIHHAFNSGVTFLDTSDIY-GPNTNEVLlGKALkDGPREKVQLAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 77 KVG---PCPIFPEPKYDHDSIMQQVEYNLKALKRDKIDLLHIHDPDrygdkgnpgnyHAVfGKNMALATLQKLKAQGVIR 153
Cdd:cd19145 82 KFGiheIGGSGVEVRGDPAYVRAACEASLKRLDVDYIDLYYQHRID-----------TTV-PIEITMGELKKLVEEGKIK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 154 SIGIGSLWLDF--QAHCIDTgefdVILTFNRYGLIWRDAQFQSFPFCRRHNVGVMQGTPLHQGVLAvPRPEWVTTPPDWM 231
Cdd:cd19145 150 YIGLSEASADTirRAHAVHP----ITAVQLEWSLWTRDIEEEIIPTCRELGIGIVPYSPLGRGFFA-GKAKLEELLENSD 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1085403013 232 TVTEHDR------------YRRLLDIQKSCGIPLPELALRFILQNPTISATIPGAGNLTELAANVA 285
Cdd:cd19145 225 VRKSHPRfqgenleknkvlYERVEALAKKKGCTPAQLALAWVLHQGEDVVPIPGTTKIKNLNQNIG 290
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
1-119 |
2.81e-11 |
|
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: 63.25 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 1 MKYRSLGRTGWQVSEISLGGL--FVGKESSDTGIQTIRRALELGVNLFDTAPSYFGGKAQEILGEALN--GVKQPHY-VS 75
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGTWstFSTAISEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILKkkGWKRSSYiVS 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1085403013 76 TKV----GPcpifPEPKYDHDSIMQQVEYNLKALKRDKIDLLHIHDPD 119
Cdd:cd19142 81 TKIywsyGS----EERGLSRKHIIESVRASLRRLQLDYIDIVIIHKAD 124
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
15-231 |
1.50e-10 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381380 [Multi-domain] Cd Length: 303 Bit Score: 60.89 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 15 EISLGGLFVGKESSDTGIQTIRRALELGVNLFDTAPSYfggKAQEILGEAL-----NGVKQPH--YVSTKVGPCPIFPEp 87
Cdd:cd19154 11 KMPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLY---QNEEAIGEALaelleEGVVKREdlFITTKLWTHEHAPE- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 88 kydhdSIMQQVEYNLKALKRDKIDLLHIHDP-------DRYGDKGNPGNYHAVFGKNMALATLQKLKAQGVIRSIGIgSL 160
Cdd:cd19154 87 -----DVEEALRESLKKLQLEYVDLYLIHAPaafkddeGESGTMENGMSIHDAVDVEDVWRGMEKVYDEGLTKAIGV-SN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1085403013 161 WLDFQAHCI-DTGEFDVILTFNRYGLIWRdaQFQSFPFCRRHNVGVMQGTPLHQ-GVLAVPRPEWVTTPPDWM 231
Cdd:cd19154 161 FNNDQIQRIlDNARVKPHNNQVECHLYFP--QKELVEFCKKHNISVTSYATLGSpGRANFTKSTGVSPAPNLL 231
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
2-286 |
1.63e-10 |
|
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: 60.88 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 2 KYRSLGRTGWQVSEISLGgL---FVGKESSDTGIQTIRRALELGVNLFDTAPSYfG---GKAQEILGEALNGVKQPH--- 72
Cdd:cd19151 1 KYNRCGRSGLKLPAISLG-LwhnFGDVDRYENSRAMLRRAFDLGITHFDLANNY-GpppGSAEENFGRILKEDLKPYrde 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 73 -YVSTKVGpCPIFPEPKYDHDS---IMQQVEYNLKALKRDKIDLLHIHDPdrygDKGNPgnyhavFGKNM-ALATLQKlk 147
Cdd:cd19151 79 lIISTKAG-YTMWPGPYGDWGSkkyLIASLDQSLKRMGLDYVDIFYHHRP----DPETP------LEETMgALDQIVR-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 148 aQGVIRSIGIGSLWLDfqahciDTGEFDVIL---------------TFNRY---GL--IWRDAQFQSFPFCrrhnvgvmq 207
Cdd:cd19151 146 -QGKALYVGISNYPPE------EAREAAAILkdlgtpclihqpkysMFNRWveeGLldVLEEEGIGCIAFS--------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 208 gtPLHQGVL------AVPRPEWVTTP-----PDWMTVTEHDRYRRLLDIQKSCGIPLPELALRFILQNPTISATIPGAGN 276
Cdd:cd19151 210 --PLAQGLLtdrylnGIPEDSRAAKGssflkPEQITEEKLAKVRRLNEIAQARGQKLAQMALAWVLRNKRVTSVLIGASK 287
|
330
....*....|
gi 1085403013 277 LTELAANVAC 286
Cdd:cd19151 288 PSQIEDAVGA 297
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
1-76 |
9.48e-10 |
|
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: 58.84 E-value: 9.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 1 MKYRSLGRTGWQVSEISLGG--LFVGKESSDTGIQTIRRALELGVNLFDTAPSYFGGKAQEILGEAL--NGVKQPHYVST 76
Cdd:cd19160 3 MKYRNLGKSGLRVSCLGLGTwvTFGSQISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILksKGWRRSSYVVT 82
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
1-303 |
1.16e-09 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 58.71 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 1 MKYRSLGRTGWQVSEISLGGLFVGKESSDTGIQT-IRRALELGVNLFDTAPSY-------FGGKAQEILGEAL--NGVKQ 70
Cdd:PRK10625 1 MQYHRIPHSSLEVSTLGLGTMTFGEQNSEADAHAqLDYAVAQGINLIDVAEMYpvpprpeTQGLTETYIGNWLakRGSRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 71 PHYVSTKV-GPC-----PIFPEPKYDHDSIMQQVEYNLKALKRDKIDLLHIHDPDRygdkgnPGNYHAVFGKNMA----- 139
Cdd:PRK10625 81 KLIIASKVsGPSrnndkGIRPNQALDRKNIREALHDSLKRLQTDYLDLYQVHWPQR------PTNCFGKLGYSWTdsapa 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 140 ---LATLQKLKAQ---GVIRSIGIG--SLWLDFQ-AHCIDTGEFDVILTF-NRYGLIWRDAQFQSFPFCRRHNVGVMQGT 209
Cdd:PRK10625 155 vslLETLDALAEQqraGKIRYIGVSneTAFGVMRyLHLAEKHDLPRIVTIqNPYSLLNRSFEVGLAEVSQYEGVELLAYS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 210 PLHQGVL-------AVP---------RPEWVTTPPDWMTVTEHdryrrlLDIQKSCGIPLPELALRFILQNPTISATIPG 273
Cdd:PRK10625 235 CLAFGTLtgkylngAKPagarntlfsRFTRYSGEQTQKAVAAY------VDIAKRHGLDPAQMALAFVRRQPFVASTLLG 308
|
330 340 350
....*....|....*....|....*....|
gi 1085403013 274 AGNLTELAANVAcSEKGPLPPDVATQIESL 303
Cdd:PRK10625 309 ATTMEQLKTNIE-SLHLTLSEEVLAEIEAV 337
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-156 |
1.43e-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: 381391 [Multi-domain] Cd Length: 291 Bit Score: 58.11 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 14 SEISLGGLFVG-KESSDTGIQTIRRALELGVNLFDTA-------PSYFGGKAQEILGEALN--GVKQPHYVSTKVG-PCP 82
Cdd:cd19752 1 SELCLGTMYFGtRTDEETSFAILDRYVAAGGNFLDTAnnyafwtEGGVGGESERLIGRWLKdrGNRDDVVIATKVGaGPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 83 IFPEPKYD-----HDSIMQQVEYNLKALKRDKIDLL--HIHDPDRYGDKgnpgnyhavfgknmALATLQKLKAQGVIRSI 155
Cdd:cd19752 81 DPDGGPESpeglsAETIEQEIDKSLRRLGTDYIDLYyaHVDDRDTPLEE--------------TLEAFNELVKAGKVRAI 146
|
.
gi 1085403013 156 G 156
Cdd:cd19752 147 G 147
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
29-285 |
1.50e-09 |
|
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: 57.65 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 29 DTGIQTIRRALELGVNLFDTAPSYfgGKAQEIlGEAL--NGVKQPH-YVSTKVGPcpifpePKYDHDSIMQQVEYNLKAL 105
Cdd:cd19140 21 EECTRAVEHALELGYRHIDTAQMY--GNEAQV-GEAIaaSGVPRDElFLTTKVWP------DNYSPDDFLASVEESLRKL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 106 KRDKIDLLHIHDPDRYGDKGNPgnyhavfgknmaLATLQKLKAQGVIRSIGIGSLWLDFQAHCIDTGEFDVILTfnrygl 185
Cdd:cd19140 92 RTDYVDLLLLHWPNKDVPLAET------------LGALNEAQEAGLARHIGVSNFTVALLREAVELSEAPLFTN------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 186 iwrdaQFQSFPF---------CRRHNVGVMQGTPLHQG-VLAVPrpewvttppdwmTVTEHDRYRRLLDIQkscgiplpe 255
Cdd:cd19140 154 -----QVEYHPYldqrklldaAREHGIALTAYSPLARGeVLKDP------------VLQEIGRKHGKTPAQ--------- 207
|
250 260 270
....*....|....*....|....*....|
gi 1085403013 256 LALRFILQNPTISAtIPGAGNLTELAANVA 285
Cdd:cd19140 208 VALRWLLQQEGVAA-IPKATNPERLEENLD 236
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
28-157 |
2.29e-09 |
|
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like protein is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase similar to Bacillus subtilis glyoxal reductase (YvgN) that reduces glyoxal and methylglyoxal (2-oxopropanal).
Pssm-ID: 381362 [Multi-domain] Cd Length: 262 Bit Score: 56.87 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 28 SDTGIQTIRRALELGVNLFDTAPSYfggKAQEILGEALNGVKQPH-------YVSTKVGPcpifpepkYDH--DSIMQQV 98
Cdd:cd19136 14 EEEVRQAVDAALKAGYRLIDTASVY---RNEADIGKALRDLLPKYglsrediFITSKLAP--------KDQgyEKARAAC 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1085403013 99 EYNLKALKRDKIDLLHIHDPDRYGDK-GNPGNyhavfgKNMALAT---LQKLKAQGVIRSIGI 157
Cdd:cd19136 83 LGSLERLGTDYLDLYLIHWPGVQGLKpSDPRN------AELRRESwraLEDLYKEGKLRAIGV 139
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
33-168 |
2.44e-09 |
|
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid reductase (2,5-DKG reductase) is a founding member of aldo-keto reductase family 5 member F1 (AKR5F1). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381359 [Multi-domain] Cd Length: 255 Bit Score: 56.81 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 33 QTIRRALELGVNLFDTAPSYFGGKAqeiLGEAL--NGVKQPH-YVSTKVGPcpifpePKYDHDSIMQQVEYNLKALKRDK 109
Cdd:cd19133 27 RAVLEAIKAGYRLIDTAAAYGNEEA---VGRAIkkSGIPREElFITTKLWI------QDAGYEKAKKAFERSLKRLGLDY 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1085403013 110 IDLLHIHDPdrYGDkgnpgnyhaVFGknmALATLQKLKAQGVIRSIGI----GSLWLDFQAHC 168
Cdd:cd19133 98 LDLYLIHQP--FGD---------VYG---AWRAMEELYKEGKIRAIGVsnfyPDRLVDLILHN 146
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
2-78 |
3.21e-09 |
|
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: 57.07 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 2 KYRSLGRTGWQVSEISLGGL--FVGKESSDTGIQTIRRALELGVNLFDTAPSYFGGKAQEILGEAL--NGVKQPHYV-ST 76
Cdd:cd19141 1 PYRNLGKSGLRVSCLGLGTWvtFGSQISDEVAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILkkKGWRRSSYViTT 80
|
..
gi 1085403013 77 KV 78
Cdd:cd19141 81 KI 82
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
1-285 |
3.58e-09 |
|
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: 57.07 E-value: 3.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 1 MKYRSLGRTGWQVSEISLG--GL--FVGKESSDT-GIQTIRRALELGVNLFDTAPSYfgGKAQEILGE--ALN-GVKQPH 72
Cdd:cd19144 1 IPTRTLGRNGPSVPALGFGamGLsaFYGPPKPDEeRFAVLDAAFELGCTFWDTADIY--GDSEELIGRwfKQNpGKREKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 73 YVSTKVGPCPIFPEPKYDHDS----IMQQVEYNLKALKRDKIDLLHIH--DPDRYGDKgnpgnyhavfgknmALATLQKL 146
Cdd:cd19144 79 FLATKFGIEKNVETGEYSVDGspeyVKKACETSLKRLGVDYIDLYYQHrvDGKTPIEK--------------TVAAMAEL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 147 KAQGVIRSIGIG-----SLWLDFQAHCIDTgefdVILTFNRYGLIWRDAQFQSFPFCRRHNVGVMQGTPLHQGVLAVPrp 221
Cdd:cd19144 145 VQEGKIKHIGLSecsaeTLRRAHAVHPIAA----VQIEYSPFSLDIERPEIGVLDTCRELGVAIVAYSPLGRGFLTGA-- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 222 ewVTTPPDWmtvtEHDRYRR-------------------LLDIQKSCGIPLPELALRFILQNPTISATIPGAGNLTELAA 282
Cdd:cd19144 219 --IRSPDDF----EEGDFRRmaprfqaenfpknlelvdkIKAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEE 292
|
...
gi 1085403013 283 NVA 285
Cdd:cd19144 293 NLG 295
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
6-119 |
1.06e-08 |
|
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: 55.42 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 6 LGRTGWQVSEISLGGLFvGKESSDTGIQTI-RRALELGVNLFDTAPSYFGGKAQEILGEALNGVKQPHY-VSTKVGPCPI 83
Cdd:cd19103 9 LGTWSWGSGGAGGDQVF-GNHLDEDTLKAVfDKAMAAGLNLWDTAAVYGMGASEKILGEFLKRYPREDYiISTKFTPQIA 87
|
90 100 110
....*....|....*....|....*....|....*.
gi 1085403013 84 FPEPkydhDSIMQQVEYNLKALKRDKIDLLHIHDPD 119
Cdd:cd19103 88 GQSA----DPVADMLEGSLARLGTDYIDIYWIHNPA 119
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
20-157 |
1.33e-08 |
|
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: 54.67 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 20 GLFVGKESSDTGIQTIRRALELGVNLFDTAPSYfGGKAQeiLGEAL--NGVKQPH-YVSTKVGpcpifpEPKYDHDSIMQ 96
Cdd:cd19139 5 GLGTFRLKDDVVIDSVRTALELGYRHIDTAQIY-DNEAA--VGQAIaeSGVPRDElFITTKIW------IDNLSKDKLLP 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1085403013 97 QVEYNLKALKRDKIDLLHIHDPDRYgDKGNPGNYhavfgknmaLATLQKLKAQGVIRSIGI 157
Cdd:cd19139 76 SLEESLEKLRTDYVDLTLIHWPSPN-DEVPVEEY---------IGALAEAKEQGLTRHIGV 126
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
32-157 |
1.61e-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: 51.46 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 32 IQTIRRALELGVNLFDTAPSYfggKAQEILGEALN--GVKQPH-YVSTKVGPcpifpepkyDHDSIMQQVEYNLKALKRD 108
Cdd:cd19120 28 VDSVKLALKAGFRHIDTAEMY---GNEKEVGEALKesGVPREDlFITTKVSP---------GIKDPREALRKSLAKLGVD 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1085403013 109 KIDLLHIHDPDRYGDKGNPgnyHAVfgknmALATLQKLKAQGVIRSIGI 157
Cdd:cd19120 96 YVDLYLIHSPFFAKEGGPT---LAE-----AWAELEALKDAGLVRSIGV 136
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
20-157 |
3.41e-07 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 50.84 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 20 GLFVGKESSDTGIQTIRRALELGVNLFDTAPSYfggKAQEILGEALNGVKQPH---YVSTKVGpcpifpepKYDHDSIMQ 96
Cdd:PRK11565 19 GLGVWQASNEEVITAIHKALEVGYRSIDTAAIY---KNEEGVGKALKEASVAReelFITTKLW--------NDDHKRPRE 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1085403013 97 QVEYNLKALKRDKIDLLHIHDPDrygdkgnPGNYHAVfgknMALATLQKLKAQGVIRSIGI 157
Cdd:PRK11565 88 ALEESLKKLQLDYVDLYLMHWPV-------PAIDHYV----EAWKGMIELQKEGLIKSIGV 137
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
20-284 |
4.56e-07 |
|
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: 50.24 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 20 GLFVGKESSDTGIQTIRRALELGVNLFDTAPSYfGGKAQeiLGEALNGVKQPH---YVSTKVGpcpifpEPKYDHDSIMQ 96
Cdd:cd19134 15 GLGVGELSDDEAERSVSAALEAGYRLIDTAAAY-GNEAA--VGRAIAASGIPRgelFVTTKLA------TPDQGFTASQA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 97 QVEYNLKALKRDKIDLLHIHDPdrygdKGNPGNYHAVFGknmalaTLQKLKAQGVIRSIGIGslwlDFQAHCIDtgefDV 176
Cdd:cd19134 86 ACRASLERLGLDYVDLYLIHWP-----AGREGKYVDSWG------GLMKLREEGLARSIGVS----NFTAEHLE----NL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 177 I-LTF-----NRYGLIWRDAQFQSFPFCRRHNVGVMQGTPLHQGVLAvprpewvttppdwmtvtEHDRYRRLLDiqKSCG 250
Cdd:cd19134 147 IdLTFftpavNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGRLL-----------------DNPAVTAIAA--AHGR 207
|
250 260 270
....*....|....*....|....*....|....
gi 1085403013 251 IPlPELALRFILQNPtiSATIPGAGNLTELAANV 284
Cdd:cd19134 208 TP-AQVLLRWSLQLG--NVVISRSSNPERIASNL 238
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
14-267 |
6.31e-07 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381337 [Multi-domain] Cd Length: 286 Bit Score: 49.80 E-value: 6.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 14 SEISLGGLFVGKESSDTGIQTIRRALELGVNLFDTAPSYfggKAQEILGEALN-----GV--KQPHYVSTKVGPcpIFPE 86
Cdd:cd19111 2 FPMPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSY---QNEKAIGEALKwwlknGKlkREEVFITTKLPP--VYLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 87 PKydhdSIMQQVEYNLKALKRDKIDLLHIHDPDRYGDKGNPG-NYHAVFGKNMALATLQKLKAQGVIRSIGIGslwlDFQ 165
Cdd:cd19111 77 FK----DTEKSLEKSLENLKLPYVDLYLIHHPCGFVNKKDKGeRELASSDVTSVWRAMEALVSEGKVKSIGLS----NFN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 166 AHCIDTgefdvILtfnRYGLIWRD-------AQFQS---FPFCRRHNVGVMQGTPLHqgvlAVPRPEWVTTPPDWMTVTE 235
Cdd:cd19111 149 PRQINK-----IL---AYAKVKPSnlqlechAYLQQrelRKFCNKKNIVVTAYAPLG----SPGRANQSLWPDQPDLLED 216
|
250 260 270
....*....|....*....|....*....|..
gi 1085403013 236 hdryRRLLDIQKSCGIPLPELALRFILQNPTI 267
Cdd:cd19111 217 ----PTVLAIAKELDKTPAQVLLRFVLQRGTG 244
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
20-217 |
2.27e-06 |
|
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes prostaglandin F2-alpha synthase (PGFS) from Leishmania major (AKR5A1) and Trypanosoma brucei (AKR5A2). PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity for synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde. The AKR5G family of AKR includes Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase, which corresponds to aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381352 [Multi-domain] Cd Length: 254 Bit Score: 48.20 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 20 GLFVGK-ESSDTGIQTIRRALELGVNLFDTAPSYfggKAQEILGEAL--NGV-KQPHYVSTKVgpcpifpepkYDHD--- 92
Cdd:cd19126 13 GLGVFQtPDGDETERAVQTALENGYRSIDTAAIY---KNEEGVGEAIreSGVpREELFVTTKL----------WNDDqra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 93 -SIMQQVEYNLKALKRDKIDLLHIHDP--DRYGDkgnpgnyhavfgknmALATLQKLKAQGVIRSIGIGslwlDFQAHCI 169
Cdd:cd19126 80 rRTEDAFQESLDRLGLDYVDLYLIHWPgkDKFID---------------TWKALEKLYASGKVKAIGVS----NFQEHHL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1085403013 170 DT--GEFDVILTFNrygliwrdaQFQSFP---------FCRRHNVGVMQGTPLHQGVLA 217
Cdd:cd19126 141 EEllAHADVVPAVN---------QVEFHPyltqkelrgYCKSKGIVVEAWSPLGQGGLL 190
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
2-285 |
7.56e-06 |
|
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: 46.68 E-value: 7.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 2 KYRSLGRTGWQVSEISLGGL--FVGKESSDTGIQTIRRALELGVNLFDTAPSYfG---GKAQE----ILGEALNGVKQPH 72
Cdd:cd19150 1 QYRRCGKSGLKLPALSLGLWhnFGDDTPLETQRAILRTAFDLGITHFDLANNY-GpppGSAEEnfgrILREDFAGYRDEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 73 YVSTKVGpCPIFPEP-------KYDHDSIMQqveyNLKALKRDKIDLLHIH--DPDRYGDKGNPGNYHAV-FGKNM---- 138
Cdd:cd19150 80 IISTKAG-YDMWPGPygewgsrKYLLASLDQ----SLKRMGLDYVDIFYSHrfDPDTPLEETMGALDHAVrSGKALyvgi 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 139 ----------ALATLQKLKAQGVIR--SIGIGSLWLDfqahcidtgEFDVILTFNRYGliwrdaqfqsfpfcrrhnVGVM 206
Cdd:cd19150 155 ssyspertreAAAILRELGTPLLIHqpSYNMLNRWVE---------ESGLLDTLQELG------------------VGCI 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 207 QGTPLHQGVL------AVPRPEWVTTP----PDWMTVTEHDRYRRLLDIQKSCGIPLPELALRFILQNPTISATIPGAGN 276
Cdd:cd19150 208 AFTPLAQGLLtdkylnGIPEGSRASKErslsPKMLTEANLNSIRALNEIAQKRGQSLAQMALAWVLRDGRVTSALIGASR 287
|
....*....
gi 1085403013 277 LTELAANVA 285
Cdd:cd19150 288 PEQLEENVG 296
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
1-285 |
9.37e-06 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 46.52 E-value: 9.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 1 MKYRSLGRTGWQVSEISLG--GLFVGKESSDTGIQTIRRALELGVNLFDTAPSYF--GGKAQEILGEALNGVKQPH---- 72
Cdd:PRK09912 13 MQYRYCGKSGLRLPALSLGlwHNFGHVNALESQRAILRKAFDLGITHFDLANNYGppPGSAEENFGRLLREDFAAYrdel 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 73 YVSTKVGpCPIFPEP-------KYdhdsIMQQVEYNLKALKRDKIDLLHIHDPdrygDKGNPGNYHAVfgknmALA-TLQ 144
Cdd:PRK09912 93 IISTKAG-YDMWPGPygsggsrKY----LLASLDQSLKRMGLEYVDIFYSHRV----DENTPMEETAS-----ALAhAVQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 145 KLKAQGVirsiGIGSLWLDFQAHCID-TGEFDVILTFNR--YGLI--WRDaQFQSFPFCRRHNVGVMQGTPLHQGVL--- 216
Cdd:PRK09912 159 SGKALYV----GISSYSPERTQKMVElLREWKIPLLIHQpsYNLLnrWVD-KSGLLDTLQNNGVGCIAFTPLAQGLLtgk 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 217 ---AVPRPEWVTT--------PPDWMTVTEHDRYRRLLDIQKSCGIPLPELALRFILQNPTISATIPGAGNLTELAANVA 285
Cdd:PRK09912 234 ylnGIPQDSRMHRegnkvrglTPKMLTEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQ 313
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
29-157 |
1.84e-05 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 45.40 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 29 DTGIQTIRRALELGVNLFDTAPSYfGGKAQeiLGEAL--NGVKQPH-YVSTKvgpcpIFPEpKYDHDSIMQQVEYNLKAL 105
Cdd:PRK11172 16 QVVIDSVKTALELGYRAIDTAQIY-DNEAA--VGQAIaeSGVPRDElFITTK-----IWID-NLAKDKLIPSLKESLQKL 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1085403013 106 KRDKIDLLHIHDPdrygdkgNPGNyhavfGKNMA--LATLQKLKAQGVIRSIGI 157
Cdd:PRK11172 87 RTDYVDLTLIHWP-------SPND-----EVSVEefMQALLEAKKQGLTREIGI 128
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
20-276 |
3.33e-05 |
|
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from Leishmania major and Trypanosoma brucei are founding members of aldo-keto reductase family 5 member A1 (AKR5A1) and A2 (AKR5A2), respectively. PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity toward the synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde.
Pssm-ID: 381382 [Multi-domain] Cd Length: 266 Bit Score: 44.43 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 20 GLFVGK-ESSDTGIQTIRRALELGVNLFDTAPSYfggKAQEILGEAL--NGVKQPH-YVSTKVGpcpifpEPKYDHDSIM 95
Cdd:cd19156 13 GLGVWRvQDGAEAENAVKWAIEAGYRHIDTAAIY---KNEEGVGQGIreSGVPREEvFVTTKLW------NSDQGYESTL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 96 QQVEYNLKALKRDKIDLLHIHDP--DRYGDkgnpgnyhavfgknmALATLQKLKAQGVIRSIGIGslwlDFQAHCIDT-- 171
Cdd:cd19156 84 AAFEESLEKLGLDYVDLYLIHWPvkGKFKD---------------TWKAFEKLYKEKKVRAIGVS----NFHEHHLEEll 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 172 GEFDVILTFNRYGLIWRDAQFQSFPFCRRHNVGVMQGTPLHQGVLavprpewvttppdwmtVTEHdryrRLLDIQKSCGI 251
Cdd:cd19156 145 KSCKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGKL----------------LSNP----VLKAIGKKYGK 204
|
250 260
....*....|....*....|....*
gi 1085403013 252 PLPELALRFILQNPTIsaTIPGAGN 276
Cdd:cd19156 205 SAAQVIIRWDIQHGII--TIPKSVH 227
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
15-163 |
1.01e-04 |
|
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent D-xylose reductase (XR) from Pichia stipites, Kluyveromyces lactis, Pachysolen tannophilus, Candida tropicalis, and Candida tenuis, Gre3p from Saccharomyces cerevisiae, XR from Candida tropicalis, Pichia guilliermondii, Debaryomyces hansenli, and Debaryomyces nepalensis, which correspond to aldo-keto reductase family 2 member B1-B10 (AKR2B1-10), respectively. XR (EC1.1.1.307) catalyzes the NAD(P)H dependent reduction of xylose to xylitol.
Pssm-ID: 381339 [Multi-domain] Cd Length: 310 Bit Score: 43.20 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 15 EISLGGLFVGKESSDTGIQTIRRALELGVNLFDTAPSYfgGKAQEIlGEALNGVKQPHYVSTKvgpcPIFPEPK-----Y 89
Cdd:cd19113 10 KMPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDY--GNEKEV-GEGVNRAIDEGLVKRE----ELFLTSKlwnnfH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 90 DHDSIMQQVEYNLKALKRDKIDLLHIHDPDRYG----DKGNPGNYHAVFGKNMALA---------TLQKLKAQGVIRSIG 156
Cdd:cd19113 83 DPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKfvpiEEKYPPGFYCGDGDNFVYEdvpildtwkALEKLVDAGKIKSIG 162
|
170
....*....|.
gi 1085403013 157 I----GSLWLD 163
Cdd:cd19113 163 VsnfpGALILD 173
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
10-285 |
1.96e-04 |
|
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins; Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis.
Pssm-ID: 381372 [Multi-domain] Cd Length: 326 Bit Score: 42.41 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 10 GWQVSEISLGGLFVGKE--------SSDTGIQTIRRALELGVNLFDTAPSYFGGKAQEILGE--ALNGVKQPHYVSTK-- 77
Cdd:cd19146 8 GVRVSPLCLGAMSFGEAwksmmgecDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEwmASRGNRDEMVLATKyt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 78 -----VGPCPIFPEPKYDH-DSIMQQVEYNLKALKRDKIDLLHIHDPDrygdkgnpgnYHAVFGKNMalATLQKLKAQGV 151
Cdd:cd19146 88 tgyrrGGPIKIKSNYQGNHaKSLRLSVEASLKKLQTSYIDILYVHWWD----------YTTSIPELM--QSLNHLVAAGK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 152 IRSIGIGSL--WLdfQAHCIDTGEFDVILTFNRYGLIW----RDAQFQSFPFCRRHNVGVMQGTPLHQGVLAVP--RPEW 223
Cdd:cd19146 156 VLYLGVSDTpaWV--VSKANAYARAHGLTQFVVYQGHWsaafRDFERDILPMCEAEGMALAPWGVLGQGQFRTEeeFKRR 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1085403013 224 VTTPPDWMTVTEHDRY--RRLLDIQKSCGIPLPELALRFILQNPTISATIPGAGNLTELAANVA 285
Cdd:cd19146 234 GRSGRKGGPQTEKERKvsEKLEKVAEEKGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIE 297
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
29-157 |
2.11e-04 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 42.26 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 29 DTGIQTIRRALELGVNLFDTAPSYFGGKAQEILGEALNGVKQPHYVSTKVG---------PcpifpePKYDHDSIMQQVE 99
Cdd:PRK10376 40 DAAIAVLREAVALGVNHIDTSDFYGPHVTNQLIREALHPYPDDLTIVTKVGarrgedgswL------PAFSPAELRRAVH 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1085403013 100 YNLKALKRDKIDLLH------IHDPDrygdkgnPGNYHAvfgknmALATLQKLKAQGVIRSIGI 157
Cdd:PRK10376 114 DNLRNLGLDVLDVVNlrlmgdGHGPA-------EGSIEE------PLTVLAELQRQGLVRHIGL 164
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
35-284 |
2.39e-04 |
|
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 (NADP-dependent D-sorbitol-6-phosphate dehydrogenase or NADP-S6PDH) from Malus domestica, and AKR2A2 (NADPH-dependent mannose-6-phosphate reductase or NADPH-M6PR) from Apium graveolens. NADP-S6PDH (EC 1.1.1.200), also called aldose-6-phosphate reductase [NADPH], synthesizes sorbitol-6-phosphate, a key intermediate in the synthesis of sorbitol which is a major photosynthetic product in many members of the Rosaceae family. NADPH-M6PR (EC 1.1.1.224), also called NADPH-dependent M6P reductase, is a key enzyme involved in mannitol biosynthesis.
Pssm-ID: 381338 [Multi-domain] Cd Length: 308 Bit Score: 42.09 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 35 IRRALELGVNLFDTAPSYfggKAQEILGEALNGV-------KQPHYVSTKVGpcpifpepKYDHDSIMQQVEYNLKALKR 107
Cdd:cd19112 30 ILNAIKIGYRHFDCAADY---KNEKEVGEALAEAfktglvkREDLFITTKLW--------NSDHGHVIEACKDSLKKLQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 108 DKIDLLHIHDP--DRYGDKGNPGNYHA------VFGKNMALAT---LQKLKAQGVIRSIGIGSLWLDFQAHCID------ 170
Cdd:cd19112 99 DYLDLYLVHFPvaTKHTGVGTTGSALGedgvldIDVTISLETTwhaMEKLVSAGLVRSIGISNYDIFLTRDCLAyskikp 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 171 -TGEFDVILTFNRYGLIwrdaqfqsfPFCRRHNVGVMQGTPLHQGVLAVprpEWvttppdWMTVTEHDRyRRLLDIQKSC 249
Cdd:cd19112 179 aVNQIETHPYFQRDSLV---------KFCQKHGISVTAHTPLGGAAANA---EW------FGSVSPLDD-PVLKDLAKKY 239
|
250 260 270
....*....|....*....|....*....|....*
gi 1085403013 250 GIPLPELALRFILQNPTisATIPGAGNLTELAANV 284
Cdd:cd19112 240 GKSAAQIVLRWGIQRNT--AVIPKSSKPERLKENI 272
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
15-157 |
5.98e-04 |
|
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) is a founding member of the aldo-keto reductase family 5 member B1 (AKR5B1). M6DH (EC 1.1.1.218), also called naloxone reductase, oxidizes the C-6 hydroxy group of morphine and codeine.
Pssm-ID: 381353 [Multi-domain] Cd Length: 268 Bit Score: 40.85 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 15 EISLGGLFVGKESSDTGIQTIRRALELGVNLFDTAPSYfGGKAQeiLGEAL--NGVKQPH-YVSTKVGPCpifpepKYDH 91
Cdd:cd19127 8 EMPALGLGVFQTPPEETADAVATALADGYRLIDTAAAY-GNERE--VGEGIrrSGVDRSDiFVTTKLWIS------DYGY 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1085403013 92 DSIMQQVEYNLKALKRDKIDLLHIHDPDRygdkgnpgnyhAVFGKNM-ALATLQKLKAQGVIRSIGI 157
Cdd:cd19127 79 DKALRGFDASLRRLGLDYVDLYLLHWPVP-----------NDFDRTIqAYKALEKLLAEGRVRAIGV 134
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
9-289 |
1.29e-03 |
|
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: 39.91 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 9 TGWQVSEISLG--GLFV--GKESSDTGIQTIRRALELGVNLFDTApSYFGGKAQEI----LGEALNgvKQPHY-----VS 75
Cdd:cd19077 1 NGKLVGPIGLGlmGLTWrpNPTPDEEAFETMKAALDAGSNLWNGG-EFYGPPDPHAnlklLARFFR--KYPEYadkvvLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 76 TKVGPCPIFPEPKYDHDSIMQQVEYNLKALKR-DKIDLLhihdpdrygdkgNPgnyhAVFGKNMAL----ATLQKLKAQG 150
Cdd:cd19077 78 VKGGLDPDTLRPDGSPEAVRKSIENILRALGGtKKIDIF------------EP----ARVDPNVPIeetiKALKELVKEG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 151 VIRSIGIGSLWLD-----FQAHCIDTGEFDviltfnrYGLIWRDAqFQS--FPFCRRHNVGVMQGTPLHQGVL--AVPRP 221
Cdd:cd19077 142 KIRGIGLSEVSAEtirraHAVHPIAAVEVE-------YSLFSREI-EENgvLETCAELGIPIIAYSPLGRGLLtgRIKSL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 222 EwvTTPPDWM---------TVTEHDR--YRRLLDIQKSCGIPLPELALRFILQ--NPTISAtIPGAGNLTELAANVACSE 288
Cdd:cd19077 214 A--DIPEGDFrrhldrfngENFEKNLklVDALQELAEKKGCTPAQLALAWILAqsGPKIIP-IPGSTTLERVEENLKAAN 290
|
.
gi 1085403013 289 K 289
Cdd:cd19077 291 V 291
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
40-214 |
1.44e-03 |
|
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: 39.61 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 40 ELGVNLFDTAPSYfggKAQEILGEAL--NGVKQPH-YVSTKVGPcpifpePKYDHDSIMQQVEYNLKALKRDKIDLLHIH 116
Cdd:cd19135 37 ECGYRHIDTAKRY---GCEELLGKAIkeSGVPREDlFLTTKLWP------SDYGYESTKQAFEASLKRLGVDYLDLYLLH 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 117 DPDRYGDKGNPgnyhavfgKNMALAT---LQKLKAQGVIRSIGIGslwlDFQ-AHCIDTGEF-DVILTFNR--YGLIWRD 189
Cdd:cd19135 108 WPDCPSSGKNV--------KETRAETwraLEELYDEGLCRAIGVS----NFLiEHLEQLLEDcSVVPHVNQveFHPFQNP 175
|
170 180
....*....|....*....|....*
gi 1085403013 190 AQFQSfpFCRRHNVGVMQGTPLHQG 214
Cdd:cd19135 176 VELIE--YCRDNNIVFEGYCPLAKG 198
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
38-216 |
1.89e-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: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 38 ALELGVNLFDTAPSYfgGKAQEIlGEALNGVKQPH---YVSTKVGpcpifpEPKYDHDSIMQQVEYNLKALKRDKIDLLH 114
Cdd:cd19130 32 ALEVGYRHIDTAAIY--GNEEGV-GAAIAASGIPRdelFVTTKLW------NDRHDGDEPAAAFAESLAKLGLDQVDLYL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 115 IHDPdrygdKGNPGNYHAvfgknmALATLQKLKAQGVIRSIGIGslwlDFQAHCID--TGEFDVILTFNRYGLIWRDAQF 192
Cdd:cd19130 103 VHWP-----TPAAGNYVH------TWEAMIELRAAGRTRSIGVS----NFLPPHLEriVAATGVVPAVNQIELHPAYQQR 167
|
170 180
....*....|....*....|....
gi 1085403013 193 QSFPFCRRHNVGVMQGTPLHQGVL 216
Cdd:cd19130 168 TIRDWAQAHDVKIEAWSPLGQGKL 191
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
29-214 |
2.69e-03 |
|
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B (DkgB) from Corynebacterium sp. and 2,5-diketo-D-gluconic acid reductase Zymomonas mobilis are founding members of aldo-keto reductase family 5 member D1 (AKR5D1) and E1 (AKR5E1), respectively. DkgB (EC 1.1.1.274), also called 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381358 [Multi-domain] Cd Length: 255 Bit Score: 38.79 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 29 DTGIQTIRRALELGVNLFDTAPSYfggKAQEILGEAL--NGVKQPH-YVSTKVgpcpifpePKYDH--DSIMQQVEYNLK 103
Cdd:cd19132 20 DEGVEAVVAALQAGYRLLDTAFNY---ENEGAVGEAVrrSGVPREElFVTTKL--------PGRHHgyEEALRTIEESLY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085403013 104 ALKRDKIDLLHIHDPdrygdkgNP--GNYHAVFgknMALATLQKlkaQGVIRSIGIGslwlDFQAHCID-----TGEFDV 176
Cdd:cd19132 89 RLGLDYVDLYLIHWP-------NPsrDLYVEAW---QALIEARE---EGLVRSIGVS----NFLPEHLDrlideTGVTPA 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 1085403013 177 ILTFNRYGLIWRDAQFQsfpFCRRHNVGVMQGTPLHQG 214
Cdd:cd19132 152 VNQIELHPYFPQAEQRA---YHREHGIVTQSWSPLGRG 186
|
|
| |
