|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
19-318 |
2.77e-152 |
|
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: 429.34 E-value: 2.77e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 19 LPGMGCGTWAWGNQLLWGYNESMDAQLQAVFNLCVSNGVTLFDTGDSYGTGRlngrSELLLGKFSQEYQgvNQENICIAT 98
Cdd:cd19093 2 VSPLGLGTWQWGDRLWWGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYGTGR----SERLLGRFLKELG--DRDEVVIAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 99 KLAAYPWRWTRQSMINACKSSAQRLG-RNVDLVQMHWSTANYApwQEVGLLDGLADLYEQGLVKGVGLSNYGTKRLQRVH 177
Cdd:cd19093 76 KFAPLPWRLTRRSVVKALKASLERLGlDSIDLYQLHWPGPWYS--QIEALMDGLADAVEEGLVRAVGVSNYSADQLRRAH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 178 QKFAERGVPIKTLQVQYSLLSTYPVTeLGLKDVCDELGIKLIAYSPLALGILTGKYSEKGPFPRGVRGLLLRQLLPGVRS 257
Cdd:cd19093 154 KALKERGVPLASNQVEYSLLYRDPEQ-NGLLPACDELGITLIAYSPLAQGLLTGKYSPENPPPGGRRRLFGRKNLEKVQP 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17135278 258 LLQCLQDVAQSRNKTMSQVALNWCIAKGTMPIPGARSVKQAQENIGALGWQLNSGEIAELD 318
Cdd:cd19093 233 LLDALEEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
22-321 |
8.60e-88 |
|
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: 265.33 E-value: 8.60e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 22 MGCGTWAWGnqllWGYNESMDAQLQAVFNLCVSNGVTLFDTGDSYGtgrlNGRSELLLGKFSQEYqGVNQENICIATKL- 100
Cdd:pfam00248 1 IGLGTWQLG----GGWGPISKEEALEALRAALEAGINFIDTAEVYG----DGKSEELLGEALKDY-PVKRDKVVIATKVp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 101 ---AAYPWRWTRQSMINACKSSAQRLGRN-VDLVQMHWSTANYaPWQEVglLDGLADLYEQGLVKGVGLSNYGTKRLQRV 176
Cdd:pfam00248 72 dgdGPWPSGGSKENIRKSLEESLKRLGTDyIDLYYLHWPDPDT-PIEET--WDALEELKKEGKIRAIGVSNFDAEQIEKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 177 HQKfaeRGVPIKTLQVQYSLLstYPVTELGLKDVCDELGIKLIAYSPLALGILTGKYSEKGPFPRGVRGLLLRQLLPGVR 256
Cdd:pfam00248 149 LTK---GKIPIVAVQVEYNLL--RRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPGERRRLLKKGTPLNL 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17135278 257 SLLQCLQDVAQSRNKTMSQVALNWCIA--KGTMPIPGARSVKQAQENIGALGWQLNSGEIAELDKAA 321
Cdd:pfam00248 224 EALEALEEIAKEHGVSPAQVALRWALSkpGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
17-322 |
1.64e-79 |
|
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: 245.09 E-value: 1.64e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 17 LSLPGMGCGTWAWGNqlLWGYNEsmDAQLQAVFNLCVSNGVTLFDTGDSYGtgrlNGRSELLLGKFSQEYqgvNQENICI 96
Cdd:COG0667 11 LKVSRLGLGTMTFGG--PWGGVD--EAEAIAILDAALDAGINFFDTADVYG----PGRSEELLGEALKGR---PRDDVVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 97 ATK----LAAYPWRW--TRQSMINACKSSAQRLGRN-VDLVQMHWSTANyAPWQEVglLDGLADLYEQGLVKGVGLSNYG 169
Cdd:COG0667 80 ATKvgrrMGPGPNGRglSREHIRRAVEASLRRLGTDyIDLYQLHRPDPD-TPIEET--LGALDELVREGKIRYIGVSNYS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 170 TKRLQRVHqKFAERGVPIKTLQVQYSLLSTYPvtELGLKDVCDELGIKLIAYSPLALGILTGKYSEKGPFP---RGVRGL 246
Cdd:COG0667 157 AEQLRRAL-AIAEGLPPIVAVQNEYSLLDRSA--EEELLPAARELGVGVLAYSPLAGGLLTGKYRRGATFPegdRAATNF 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17135278 247 LLRQLLPGVRSLLQCLQDVAQSRNKTMSQVALNWCIAKG--TMPIPGARSVKQAQENIGALGWQLNSGEIAELDKAAA 322
Cdd:COG0667 234 VQGYLTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPgvTSVIPGARSPEQLEENLAAADLELSAEDLAALDAALA 311
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
16-318 |
2.27e-62 |
|
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: 200.44 E-value: 2.27e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 16 ELSLPGMGCGTWAWGNQllwGYNESMDAQLQAVFNLCVSNGVTLFDTGDSYGtgrlNGRSELLLGKFSQEYQgvnqENIC 95
Cdd:cd19084 1 DLKVSRIGLGTWAIGGT---WWGEVDDQESIEAIKAAIDLGINFFDTAPVYG----FGHSEEILGKALKGRR----DDVV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 96 IATKLAAypwRW----------TRQSMINACKSSAQRLGRN-VDLVQMHW---STanyaPWQEVglLDGLADLYEQGLVK 161
Cdd:cd19084 70 IATKCGL---RWdggkgvtkdlSPESIRKEVEQSLRRLQTDyIDLYQIHWpdpNT----PIEET--AEALEKLKKEGKIR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 162 GVGLSNYGTKRLQRvhqkfAERGVPIKTLQVQYSLLSTYPVTELgLKdVCDELGIKLIAYSPLALGILTGKYSEKGPFPR 241
Cdd:cd19084 141 YIGVSNFSVEQLEE-----ARKYGPIVSLQPPYSMLEREIEEEL-LP-YCRENGIGVLPYGPLAQGLLTGKYKKEPTFPP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 242 G-VR---GLLLRQLLPGVRSLLQCLQDVAQSRNKTMSQVALNWCIAK--GTMPIPGARSVKQAQENIGALGWQLNSGEIA 315
Cdd:cd19084 214 DdRRsrfPFFRGENFEKNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQpgVTSAIVGAKNPEQLEENAGALDWELTEEELK 293
|
...
gi 17135278 316 ELD 318
Cdd:cd19084 294 EID 296
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
17-321 |
3.69e-60 |
|
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: 194.73 E-value: 3.69e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 17 LSLPGMGCgtWAWGNQLLWGYNEsmDAQLQAVFNLCVSNGVTLFDTGDSYGtgrlNGRSELLLGKFsqeYQGVNqENICI 96
Cdd:cd19085 1 VSRLGLGC--WQFGGGYWWGDQD--DEESIATIHAALDAGINFFDTAEAYG----DGHSEEVLGKA---LKGRR-DDVVI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 97 ATKlaAYPWRWTRQSMINACKSSAQRLGRN-VDLVQMHWstanyaPWQEVGL---LDGLADLYEQGLVKGVGLSNYGTKR 172
Cdd:cd19085 69 ATK--VSPDNLTPEDVRKSCERSLKRLGTDyIDLYQIHW------PSSDVPLeetMEALEKLKEEGKIRAIGVSNFGPAQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 173 LQRVHqkfaERGvPIKTLQVQYSLLSTYPvtELGLKDVCDELGIKLIAYSPLALGILTGKYSEKGPFPRG-VRGLLLRQL 251
Cdd:cd19085 141 LEEAL----DAG-RIDSNQLPYNLLWRAI--EYEILPFCREHGIGVLAYSPLAQGLLTGKFSSAEDFPPGdARTRLFRHF 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17135278 252 LPG----VRSLLQCLQDVAQSRNKTMSQVALNWCIAKG--TMPIPGARSVKQAQENIGALGWQLNSGEIAELDKAA 321
Cdd:cd19085 214 EPGaeeeTFEALEKLKEIADELGVTMAQLALAWVLQQPgvTSVIVGARNPEQLEENAAAVDLELSPSVLERLDEIS 289
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-322 |
2.75e-56 |
|
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: 184.84 E-value: 2.75e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 16 ELSLPGMGCGTWAWGNQLLWGY----NESMDAQLQAVFNLCVSNGVTLFDTGDSYGTGRlngrSELLLGKFSQEYqgvNQ 91
Cdd:cd19103 1 DKKLPKIALGTWSWGSGGAGGDqvfgNHLDEDTLKAVFDKAMAAGLNLWDTAAVYGMGA----SEKILGEFLKRY---PR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 92 ENICIATKL---AAYPwrwTRQSMINACKSSAQRLGRN-VDLVQMHwSTANYAPWqevglLDGLADLYEQGLVKGVGLSN 167
Cdd:cd19103 74 EDYIISTKFtpqIAGQ---SADPVADMLEGSLARLGTDyIDIYWIH-NPADVERW-----TPELIPLLKSGKVKHVGVSN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 168 YGTKRLQRVHQKFAERGVPIKTLQVQYSLLSTYPvTELGLKDVCDELGIKLIAYSPLALGILTGKYSEKGPFPRGV-RGL 246
Cdd:cd19103 145 HNLAEIKRANEILAKAGVSLSAVQNHYSLLYRSS-EEAGILDYCKENGITFFAYMVLEQGALSGKYDTKHPLPEGSgRAE 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17135278 247 LLRQLLPGVRSLLQCLQDVAQSRNKTMSQVALNWCIAKGTMPIPGARSVKQAQENIGALGWQLNSGEIAELDKAAA 322
Cdd:cd19103 224 TYNPLLPQLEELTAVMAEIGAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDDEIKELEQLAD 299
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
18-318 |
6.17e-53 |
|
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: 175.11 E-value: 6.17e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 18 SLPGMGCGTWAWGNQLLWGYNEsmDAQLQAVFNLCVSNGVTLFDTGDSYGtgrlNGRSELLLGkfsQEYQGVNQENICIA 97
Cdd:cd19072 3 EVPVLGLGTWGIGGGMSKDYSD--DKKAIEALRYAIELGINLIDTAEMYG----GGHAEELVG---KAIKGFDREDLFIT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 98 TKLaaYPWRWTRQSMINACKSSAQRLGRN-VDLVQMHWStaNYA-PWQEVglLDGLADLYEQGLVKGVGLSNYGTKRLQR 175
Cdd:cd19072 74 TKV--SPDHLKYDDVIKAAKESLKRLGTDyIDLYLIHWP--NPSiPIEET--LRAMEELVEEGKIRYIGVSNFSLEELEE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 176 VhQKFAERGvPIKTLQVQYSLLSTYPvtELGLKDVCDELGIKLIAYSPLALGILTGKYsekgpfprgvrglllrqllpgv 255
Cdd:cd19072 148 A-QSYLKKG-PIVANQVEYNLFDREE--ESGLLPYCQKNGIAIIAYSPLEKGKLSNAK---------------------- 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17135278 256 rsLLQCLQDVAQSRNKTMSQVALNWCIAK-GTMPIPGARSVKQAQENIGALGWQLNSGEIAELD 318
Cdd:cd19072 202 --GSPLLDEIAKKYGKTPAQIALNWLISKpNVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
30-318 |
8.48e-51 |
|
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: 170.86 E-value: 8.48e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 30 GNQLLWGYNEsmdAQLQAVFNLCVSNGVTLFDTGDSYGT---GRLNGRSELLLGKFSQeyQGVNQENICIATKLAAYPWR 106
Cdd:cd19081 16 TMVFGWTADE---ETSFALLDAFVDAGGNFIDTADVYSAwvpGNAGGESETIIGRWLK--SRGKRDRVVIATKVGFPMGP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 107 ----WTRQSMINACKSSAQRLGRN-VDLVQMHWSTANyAPWQEVglLDGLADLYEQGLVKGVGLSNYGTKRLQRVHQKFA 181
Cdd:cd19081 91 ngpgLSRKHIRRAVEASLRRLQTDyIDLYQAHWDDPA-TPLEET--LGALNDLIRQGKVRYIGASNYSAWRLQEALELSR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 182 ERGVP-IKTLQVQYSLLSTYPvTELGLKDVCDELGIKLIAYSPLALGILTGKYSEKGPFPRGVR-GLLLRQLL-PGVRSL 258
Cdd:cd19081 168 QHGLPrYVSLQPEYNLVDRES-FEGELLPLCREEGIGVIPYSPLAGGFLTGKYRSEADLPGSTRrGEAAKRYLnERGLRI 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17135278 259 LQCLQDVAQSRNKTMSQVALNWCIAKG--TMPIPGARSVKQAQENIGALGWQLNSGEIAELD 318
Cdd:cd19081 247 LDALDEVAAEHGATPAQVALAWLLARPgvTAPIAGARTVEQLEDLLAAAGLRLTDEEVARLD 308
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
16-320 |
5.27e-46 |
|
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: 158.55 E-value: 5.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 16 ELSLpgmGCGTWAwGNQLLWGYNESMDAQL-QAVFNLCVSNGVTLFDTGDSYGtgrlNGRSELLLGKFSQEYQgvnqENI 94
Cdd:cd19091 15 ELAL---GTMTFG-GGGGFFGAWGGVDQEEaDRLVDIALDAGINFFDTADVYS----EGESEEILGKALKGRR----DDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 95 CIATKLAAYPWR------WTRQSMINACKSSAQRLGRN-VDLVQMHWSTAnYAPWQEVglLDGLADLYEQGLVKGVGLSN 167
Cdd:cd19091 83 LIATKVRGRMGEgpndvgLSRHHIIRAVEASLKRLGTDyIDLYQLHGFDA-LTPLEET--LRALDDLVRQGKVRYIGVSN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 168 YGTKRLQRVHQKFAERG-VPIKTLQVQYSLLSTYpvTELGLKDVCDELGIKLIAYSPLALGILTGKYSEKGPFPRGVRGL 246
Cdd:cd19091 160 FSAWQIMKALGISERRGlARFVALQAYYSLLGRD--LEHELMPLALDQGVGLLVWSPLAGGLLSGKYRRGQPAPEGSRLR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 247 LLRQLLPGV-----RSLLQCLQDVAQSRNKTMSQVALNWCIAKGTMP--IPGARSVKQAQENIGALGWQLNSGEIAELDK 319
Cdd:cd19091 238 RTGFDFPPVdrergYDVVDALREIAKETGATPAQVALAWLLSRPTVSsvIIGARNEEQLEDNLGAAGLSLTPEEIARLDK 317
|
.
gi 17135278 320 A 320
Cdd:cd19091 318 V 318
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
22-304 |
1.45e-43 |
|
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: 149.94 E-value: 1.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 22 MGCGTWAWGNQLlWGYNEsmDAQLQAVFNLCVSNGVTLFDTGDSYGtgrlNGRSELLLGKFSQEyqgvNQENICIATKL- 100
Cdd:cd19086 6 IGFGTWGLGGDW-WGDVD--DAEAIRALRAALDLGINFFDTADVYG----DGHSERLLGKALKG----RRDKVVIATKFg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 101 ------AAYPWRWTRQSMINACKSSAQRLGRN-VDLVQMHWSTANYAPWQEVglLDGLADLYEQGLVKGVGLSnygTKRL 173
Cdd:cd19086 75 nrfdggPERPQDFSPEYIREAVEASLKRLGTDyIDLYQLHNPPDEVLDNDEL--FEALEKLKQEGKIRAYGVS---VGDP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 174 QRVHQkfAERGVPIKTLQVQYSLLSTYPvtELGLKDVCDELGIKLIAYSPLALGILTGKysekgpfprgvrglllrqllp 253
Cdd:cd19086 150 EEALA--ALRRGGIDVVQVIYNLLDQRP--EEELFPLAEEHGVGVIARVPLASGLLTGK--------------------- 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 17135278 254 gvrsllqclqdvaqsrnktMSQVALNWCIAKG--TMPIPGARSVKQAQENIGA 304
Cdd:cd19086 205 -------------------LAQAALRFILSHPavSTVIPGARSPEQVEENAAA 238
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
15-317 |
1.65e-41 |
|
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: 146.59 E-value: 1.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 15 QELSLPGMGCGtwAWGnqLLWGYNESMDAQLQAVFNLCVSNGVTLFDTGDSYGtgrlNGRSELLLGKFSQEyqgvNQENI 94
Cdd:cd19076 8 QGLEVSALGLG--CMG--MSAFYGPADEEESIATLHRALELGVTFLDTADMYG----PGTNEELLGKALKD----RRDEV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 95 CIATKlaaYPWRWTRQSMIN-----------ACKSSAQRLGRNV-DLVQMHWSTANyAPWQE-VGlldGLADLYEQGLVK 161
Cdd:cd19076 76 VIATK---FGIVRDPGSGFRgvdgrpeyvraACEASLKRLGTDViDLYYQHRVDPN-VPIEEtVG---AMAELVEEGKVR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 162 GVGLSNYGT---KRLQRVHqkfaergvPIKTLQVQYSLLSTYPvtELGLKDVCDELGIKLIAYSPLALGILTGKYSEKGP 238
Cdd:cd19076 149 YIGLSEASAdtiRRAHAVH--------PITAVQSEYSLWTRDI--EDEVLPTCRELGIGFVAYSPLGRGFLTGAIKSPED 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 239 FPRGVRglllRQLLPgvR----------SLLQCLQDVAQSRNKTMSQVALNWCIAKG--TMPIPGARSVKQAQENIGALG 306
Cdd:cd19076 219 LPEDDF----RRNNP--RfqgenfdknlKLVEKLEAIAAEKGCTPAQLALAWVLAQGddIVPIPGTKRIKYLEENVGALD 292
|
330
....*....|.
gi 17135278 307 WQLNSGEIAEL 317
Cdd:cd19076 293 VVLTPEELAEI 303
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
16-306 |
1.20e-40 |
|
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: 143.89 E-value: 1.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 16 ELSLpgmgcGTWAW-GNQLlwgynESMDAQlqAVFNLCVSNGVTLFDTGDSYGtgrlNGRSELLLGKFSQEYqgvNQENI 94
Cdd:cd19074 6 ELSL-----GTWLTfGGQV-----DDEDAK--ACVRKAYDLGINFFDTADVYA----AGQAEEVLGKALKGW---PRESY 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 95 CIATKLaaypwRW-----------TRQSMINACKSSAQRLGRN-VDLVQMHWSTANyAPWQEVglLDGLADLYEQGLVKG 162
Cdd:cd19074 67 VISTKV-----FWptgpgpndrglSRKHIFESIHASLKRLQLDyVDIYYCHRYDPE-TPLEET--VRAMDDLIRQGKILY 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 163 VGLSNYGTKRLQRVHQKFAERG-VPIKTLQVQYSLLSTYPVTELglKDVCDELGIKLIAYSPLALGILTGKYSEKGPFPR 241
Cdd:cd19074 139 WGTSEWSAEQIAEAHDLARQFGlIPPVVEQPQYNMLWREIEEEV--IPLCEKNGIGLVVWSPLAQGLLTGKYRDGIPPPS 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17135278 242 G-------VRGLLLRQLLPGVRSLLQCLQDVAQSRNKTMSQVALNWCIAK--GTMPIPGARSVKQAQENIGALG 306
Cdd:cd19074 217 RsratdedNRDKKRRLLTDENLEKVKKLKPIADELGLTLAQLALAWCLRNpaVSSAIIGASRPEQLEENVKASG 290
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
25-305 |
2.08e-40 |
|
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: 144.24 E-value: 2.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 25 GTWAWGNQllwgyNESMDAQLQavFNLCVSNGVTLFDTGDSY---GTGRLNGRSELLLGKFSQeyQGVNQENICIATKLA 101
Cdd:cd19094 7 GTMTWGEQ-----NTEAEAHEQ--LDYAFDEGVNFIDTAEMYpvpPSPETQGRTEEIIGSWLK--KKGNRDKVVLATKVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 102 AY--PWRW--------TRQSMINACKSSAQRLGRN-VDLVQMHW--------STANYAPWQEVG-------LLDGLADLY 155
Cdd:cd19094 78 GPgeGITWprgggtrlDRENIREAVEGSLKRLGTDyIDLYQLHWpdrytplfGGGYYTEPSEEEdsvsfeeQLEALGELV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 156 EQGLVKGVGLSN---YGTKRLQRvhqkFAER-GVP-IKTLQVQYSLLS-TYpvtELGLKDVCDELGIKLIAYSPLALGIL 229
Cdd:cd19094 158 KAGKIRHIGLSNetpWGVMKFLE----LAEQlGLPrIVSIQNPYSLLNrNF---EEGLAEACHRENVGLLAYSPLAGGVL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 230 TGKYSEKGPFPRGVRGLLLRQLLP---GVRSLLQC--LQDVAQSRNKTMSQVALNWCIAKG--TMPIPGARSVKQAQENI 302
Cdd:cd19094 231 TGKYLDGAARPEGGRLNLFPGYMAryrSPQALEAVaeYVKLARKHGLSPAQLALAWVRSRPfvTSTIIGATTLEQLKENI 310
|
...
gi 17135278 303 GAL 305
Cdd:cd19094 311 DAF 313
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
25-303 |
3.62e-40 |
|
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: 140.73 E-value: 3.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 25 GTWAWGNQLlwgynesMDAQLQAVFNLCVSNGVTLFDTGDSYGtgrlNGRSELLLGKFSQEYQgvNQENICIATKLAAYP 104
Cdd:cd06660 6 GTMTFGGDG-------DEEEAFALLDAALEAGGNFFDTADVYG----DGRSERLLGRWLKGRG--NRDDVVIATKGGHPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 105 W------RWTRQSMINACKSSAQRLGRN-VDLVQMHWSTANyAPWQEVglLDGLADLYEQGLVKGVGLSNYGTKRLQRVH 177
Cdd:cd06660 73 GgdpsrsRLSPEHIRRDLEESLRRLGTDyIDLYYLHRDDPS-TPVEET--LEALNELVREGKIRYIGVSNWSAERLAEAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 178 QKFAERG-VPIKTLQVQYSLLSTYPVTElGLKDVCDELGIKLIAYSPLALGiltgkysekgpfprgvrglllrqllpgvr 256
Cdd:cd06660 150 AYAKAHGlPGFAAVQPQYSLLDRSPMEE-ELLDWAEENGLPLLAYSPLARG----------------------------- 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 17135278 257 sllqclqdvaqsrnktMSQVALNWCIAK--GTMPIPGARSVKQAQENIG 303
Cdd:cd06660 200 ----------------PAQLALAWLLSQpfVTVPIVGARSPEQLEENLA 232
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
23-321 |
4.17e-40 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 142.81 E-value: 4.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 23 GCGTWA---------WGNQllwGYNESMDAQLQAVfnlcvSNGVTLFDTGDSYGTGRlngrSELLLGKFSQEYQgvnqEN 93
Cdd:cd19102 5 GLGTWAiggggwgggWGPQ---DDRDSIAAIRAAL-----DLGINWIDTAAVYGLGH----SEEVVGRALKGLR----DR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 94 ICIATKLA------AYPWRW-TRQSMINACKSSAQRLGR-NVDLVQMHWstanyaPWQEVGLLDG---LADLYEQGLVKG 162
Cdd:cd19102 69 PIVATKCGllwdeeGRIRRSlKPASIRAECEASLRRLGVdVIDLYQIHW------PDPDEPIEEAwgaLAELKEEGKVRA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 163 VGLSNYGT---KRLQRVHqkfaergvPIKTLQVQYSLLSTYPVTELGlkDVCDELGIKLIAYSPLALGILTGKYSEK--G 237
Cdd:cd19102 143 IGVSNFSVdqmKRCQAIH--------PIASLQPPYSLLRRGIEAEIL--PFCAEHGIGVIVYSPMQSGLLTGKMTPErvA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 238 PFPRGVRGLLLRQLLPGVRS----LLQCLQDVAQSRNKTMSQVALNWCIAKG--TMPIPGARSVKQAQENIGALGWQLNS 311
Cdd:cd19102 213 SLPADDWRRRSPFFQEPNLArnlaLVDALRPIAERHGRTVAQLAIAWVLRRPevTSAIVGARRPDQIDETVGAADLRLTP 292
|
330
....*....|
gi 17135278 312 GEIAELDKAA 321
Cdd:cd19102 293 EELAEIEALL 302
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
18-322 |
7.95e-40 |
|
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: 142.58 E-value: 7.95e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 18 SLPGMGCGtwAWGNQLLWGYNESmDAQLQAVFNLCVSNGVTLFDTGDSYGTgrlngrSELLLGKFSQEYQGvNQENICIA 97
Cdd:cd19144 12 SVPALGFG--AMGLSAFYGPPKP-DEERFAVLDAAFELGCTFWDTADIYGD------SEELIGRWFKQNPG-KREKIFLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 98 TKLAAY-----PWRWTRQS---MINACKSSAQRLGRN-VDLVQMHWSTANYAPWQEVGlldGLADLYEQGLVKGVGLSNY 168
Cdd:cd19144 82 TKFGIEknvetGEYSVDGSpeyVKKACETSLKRLGVDyIDLYYQHRVDGKTPIEKTVA---AMAELVQEGKIKHIGLSEC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 169 GTKRLQRVHQKFaergvPIKTLQVQYSLLST-YPVTELGLKDVCDELGIKLIAYSPLALGILTGKYSEKGPFPRG-VRGL 246
Cdd:cd19144 159 SAETLRRAHAVH-----PIAAVQIEYSPFSLdIERPEIGVLDTCRELGVAIVAYSPLGRGFLTGAIRSPDDFEEGdFRRM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 247 LLR---QLLPGVRSLLQCLQDVAQSRNKTMSQVALNWCIAKGT--MPIPGARSVKQAQENIGALGWQLNSGEIAELDKAA 321
Cdd:cd19144 234 APRfqaENFPKNLELVDKIKAIAKKKNVTAGQLTLAWLLAQGDdiIPIPGTTKLKRLEENLGALKVKLTEEEEKEIREIA 313
|
.
gi 17135278 322 A 322
Cdd:cd19144 314 E 314
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
25-321 |
3.07e-39 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 140.42 E-value: 3.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 25 GTWawgnQLL--WGYNESMDAQLQAVFNLcVSNGVTLFDTGDSYGtgrlngRSELLLGKFSQEYQGVNQ--ENICIATKL 100
Cdd:cd19101 8 GMW----QLSggHGGIRDEDAAVRAMAAY-VDAGLTTFDCADIYG------PAEELIGEFRKRLRRERDaaDDVQIHTKW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 101 AAYPWRW--TRQSMINACKSSAQRLGRN-VDLVQMHWstANYAPWQEVGLLDGLADLYEQGLVKGVGLSNYGTKRLQRVh 177
Cdd:cd19101 77 VPDPGELtmTRAYVEAAIDRSLKRLGVDrLDLVQFHW--WDYSDPGYLDAAKHLAELQEEGKIRHLGLTNFDTERLREI- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 178 qkfAERGVPIKTLQVQYSLLSTYPvtELGLKDVCDELGIKLIAYSPLALGILTGKY---SEKGPFPRGVRGLLL-RQLL- 252
Cdd:cd19101 154 ---LDAGVPIVSNQVQYSLLDRRP--ENGMAALCEDHGIKLLAYGTLAGGLLSEKYlgvPEPTGPALETRSLQKyKLMId 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17135278 253 -----PGVRSLLQCLQDVAQSRNKTMSQVALNW-----CIAKgtmPIPGARSVKQAQENIGALGWQLNSGEIAELDKAA 321
Cdd:cd19101 229 ewggwDLFQELLRTLKAIADKHGVSIANVAVRWvldqpGVAG---VIVGARNSEHIDDNVRAFSFRLDDEDRAAIDAVL 304
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
55-320 |
4.00e-38 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 136.34 E-value: 4.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 55 NGVTLFDTGDSYGtgrlngrSELLLGKFSQEyQGVNQENICIATKLaaYPWRWTRQSMINACKSSAQRLGRN-VDLVQMH 133
Cdd:COG0656 30 AGYRHIDTAAMYG-------NEEGVGEAIAA-SGVPREELFVTTKV--WNDNHGYDDTLAAFEESLERLGLDyLDLYLIH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 134 W--STANYAPWQevglldGLADLYEQGLVKGVGLSNYGTKRLQRVhqkFAERGVPIKTLQVQYSLLSTypvtELGLKDVC 211
Cdd:COG0656 100 WpgPGPYVETWR------ALEELYEEGLIRAIGVSNFDPEHLEEL---LAETGVKPAVNQVELHPYLQ----QRELLAFC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 212 DELGIKLIAYSPLAlgiltgkysekgpfprgvRGLLLRQLLpgvrsllqcLQDVAQSRNKTMSQVALNWCIAKGTMPIPG 291
Cdd:COG0656 167 REHGIVVEAYSPLG------------------RGKLLDDPV---------LAEIAEKHGKTPAQVVLRWHLQRGVVVIPK 219
|
250 260
....*....|....*....|....*....
gi 17135278 292 ARSVKQAQENIGALGWQLNSGEIAELDKA 320
Cdd:COG0656 220 SVTPERIRENLDAFDFELSDEDMAAIDAL 248
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
34-305 |
5.27e-38 |
|
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: 137.39 E-value: 5.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 34 LW---GYNESMDAQLQAVFNLcVSNGVTLFDTGDSYGtgRLNGRSELLLGKFSQEYQGVNQENICIATKLAAYPW----- 105
Cdd:cd19089 18 LWhnfGDYTSPEEARELLRTA-FDLGITHFDLANNYG--PPPGSAEENFGRILKRDLRPYRDELVISTKAGYGMWpgpyg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 106 RW-TRQSMINACKSSAQRLGRN-VDLVQMHWSTANyAPWQEvgLLDGLADLYEQGLVKGVGLSNYGTKRLQRVHQKFAER 183
Cdd:cd19089 95 DGgSRKYLLASLDQSLKRMGLDyVDIFYHHRYDPD-TPLEE--TMTALADAVRSGKALYVGISNYPGAKARRAIALLREL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 184 GVPIKTLQVQYSLLSTYPvtELGLKDVCDELGIKLIAYSPLALGILTGKYSeKGPFP-----RGVRGLLLRQLLPGVRSL 258
Cdd:cd19089 172 GVPLIIHQPRYSLLDRWA--EDGLLEVLEEAGIGFIAFSPLAQGLLTDKYL-NGIPPdsrraAESKFLTEEALTPEKLEQ 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 17135278 259 LQCLQDVAQSRNKTMSQVALNWCIAKG--TMPIPGARSVKQAQENIGAL 305
Cdd:cd19089 249 LRKLNKIAAKRGQSLAQLALSWVLRDPrvTSVLIGASSPSQLEDNVAAL 297
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
32-318 |
5.92e-38 |
|
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: 136.99 E-value: 5.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 32 QLLWGYNESMDAQLQAVFNLCVSNGVTLFDTGDSYGTGRLNGrSELLLGKFSQEYQGVNQE-NICI--ATKLAAYPWRWT 108
Cdd:cd19077 14 GLTWRPNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHA-NLKLLARFFRKYPEYADKvVLSVkgGLDPDTLRPDGS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 109 RQSMINACKSSAQRLG--RNVDLVQMHWSTANyAPWQEVglLDGLADLYEQGLVKGVGLSNYGTKRLQRVHQKfaergVP 186
Cdd:cd19077 93 PEAVRKSIENILRALGgtKKIDIFEPARVDPN-VPIEET--IKALKELVKEGKIRGIGLSEVSAETIRRAHAV-----HP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 187 IKTLQVQYSLLSTYPVTElGLKDVCDELGIKLIAYSPLALGILTGKYSEKGPFPRG-VRGLLLR---QLLPGVRSLLQCL 262
Cdd:cd19077 165 IAAVEVEYSLFSREIEEN-GVLETCAELGIPIIAYSPLGRGLLTGRIKSLADIPEGdFRRHLDRfngENFEKNLKLVDAL 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 17135278 263 QDVAQSRNKTMSQVALNWCIAKGT---MPIPGARSVKQAQENIGALGWQLNSGEIAELD 318
Cdd:cd19077 244 QELAEKKGCTPAQLALAWILAQSGpkiIPIPGSTTLERVEENLKAANVELTDEELKEIN 302
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
16-318 |
2.42e-36 |
|
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: 133.11 E-value: 2.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 16 ELSLPGMGCGT-WAWGnqllWGYNESmdaqlQAVFNLCVSNGVTLFDTGDSYgtgrLNGRSELLLGKFSQEyqgvNQENI 94
Cdd:cd19080 12 PLALGTMTFGTeWGWG----ADREEA-----RAMFDAYVEAGGNFIDTANNY----TNGTSERLLGEFIAG----NRDRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 95 CIATKlaaYPWRWT----------RQSMINACKSSAQRLGRN-VDLVQMHW---STanyaPWQEVglLDGLADLYEQGLV 160
Cdd:cd19080 75 VLATK---YTMNRRpgdpnaggnhRKNLRRSVEASLRRLQTDyIDLLYVHAwdfTT----PVEEV--MRALDDLVRAGKV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 161 KGVGLSNYGTKRLQRVhQKFAE-RGV-PIKTLQVQYSLLSTYPvtELGLKDVCDELGIKLIAYSPLALGILTGKYSeKGP 238
Cdd:cd19080 146 LYVGISDTPAWVVARA-NTLAElRGWsPFVALQIEYSLLERTP--ERELLPMARALGLGVTPWSPLGGGLLTGKYQ-RGE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 239 FPRGVRGLLLRQ----LLPGVRSLLQCLQDVAQSRNKTMSQVALNWCIAK--GTMPIPGARSVKQAQENIGALGWQLNSG 312
Cdd:cd19080 222 EGRAGEAKGVTVgfgkLTERNWAIVDVVAAVAEELGRSAAQVALAWVRQKpgVVIPIIGARTLEQLKDNLGALDLTLSPE 301
|
....*.
gi 17135278 313 EIAELD 318
Cdd:cd19080 302 QLARLD 307
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
19-318 |
1.08e-35 |
|
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: 129.70 E-value: 1.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 19 LPGMGCGTWawgnQLlwgyneSMDAQLQAVfNLCVSNGVTLFDTGDSYGTgrlngrsELLLGKFSQEYqGVNQENICIAT 98
Cdd:cd19073 1 IPALGLGTW----QL------RGDDCANAV-KEALELGYRHIDTAEIYNN-------EAEVGEAIAES-GVPREDLFITT 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 99 KLaaYPWRWTRQSMINACKSSAQRLGRN-VDLVQMHWSTANYAPwQEVglLDGLADLYEQGLVKGVGLSNYGTKRLQrvh 177
Cdd:cd19073 62 KV--WRDHLRPEDLKKSVDRSLEKLGTDyVDLLLIHWPNPTVPL-EET--LGALKELKEAGKVKSIGVSNFTIELLE--- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 178 qkFAER--GVPIKTLQVQYS-LLStypvtELGLKDVCDELGIKLIAYSPLAlgiltgkysekgpfprgvRGLLLRqllpg 254
Cdd:cd19073 134 --EALDisPLPIAVNQVEFHpFLY-----QAELLEYCRENDIVITAYSPLA------------------RGEVLR----- 183
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17135278 255 vrslLQCLQDVAQSRNKTMSQVALNWCIAKGTMPIPGARSVKQAQENIGALGWQLNSGEIAELD 318
Cdd:cd19073 184 ----DPVIQEIAEKYDKTPAQVALRWLVQKGIVVIPKASSEDHLKENLAIFDWELTSEDVAKID 243
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
19-318 |
1.14e-34 |
|
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this family. It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381364 [Multi-domain] Cd Length: 266 Bit Score: 127.36 E-value: 1.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 19 LPGMGCGTWAWGNQllwgyNESMDAQLQAVfNLCVSNGVTLFDTGDSYGtgrlNGRSELLLGKFSQEYQgvnqENICIAT 98
Cdd:cd19138 11 VPALGQGTWYMGED-----PAKRAQEIEAL-RAGIDLGMTLIDTAEMYG----DGGSEELVGEAIRGRR----DKVFLVS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 99 KLaaYPWRWTRQSMINACKSSAQRLGRN-VDLVQMHWSTAnyAPWQEVglLDGLADLYEQGLVKGVGLSNYGTKRLQRVH 177
Cdd:cd19138 77 KV--LPSNASRQGTVRACERSLRRLGTDyLDLYLLHWRGG--VPLAET--VAAMEELKKEGKIRAWGVSNFDTDDMEELW 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 178 QkfAERGVPIKTLQVQYSLLSTYPvtELGLKDVCDELGIKLIAYSPLALGiltgkysekgpfprgvrGLLLRQLLPGVRs 257
Cdd:cd19138 151 A--VPGGGNCAANQVLYNLGSRGI--EYDLLPWCREHGVPVMAYSPLAQG-----------------GLLRRGLLENPT- 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17135278 258 llqcLQDVAQSRNKTMSQVALNWCIA-KGTMPIPGARSVKQAQENIGALGWQLNSGEIAELD 318
Cdd:cd19138 209 ----LKEIAARHGATPAQVALAWVLRdGNVIAIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
47-319 |
3.35e-34 |
|
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: 127.30 E-value: 3.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 47 AVFNLCVSNGVTLFDTGDSYGtgrlNGRSELLLGKFSQEyqgvNQENICIATK----LAAYPWR--WTRQSMINACKSSA 120
Cdd:cd19087 34 AIMDRALDAGINFFDTADVYG----GGRSEEIIGRWIAG----RRDDIVLATKvfgpMGDDPNDrgLSRRHIRRAVEASL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 121 QRLGRN-VDLVQMHwSTANYAPWQEVglLDGLADLYEQGLVKGVGLSNYGTKRLQRVHQKFAERGV-PIKTLQVQYSLLS 198
Cdd:cd19087 106 RRLQTDyIDLYQMH-HFDRDTPLEET--LRALDDLVRQGKIRYIGVSNFAAWQIAKAQGIAARRGLlRFVSEQPMYNLLK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 199 TYPvtELGLKDVCDELGIKLIAYSPLALGILTGKY--SEKGPFPRGVRGLL--LRQLLPGVRSLLQCLQDVAQSRNKTMS 274
Cdd:cd19087 183 RQA--ELEILPAARAYGLGVIPYSPLAGGLLTGKYgkGKRPESGRLVERARyqARYGLEEYRDIAERFEALAAEAGLTPA 260
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 17135278 275 QVALNWCIAKG--TMPIPGARSVKQAQENIGALGWQLNSGEIAELDK 319
Cdd:cd19087 261 SLALAWVLSHPavTSPIIGPRTLEQLEDSLAALEITLTPELLAEIDE 307
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
56-320 |
3.92e-34 |
|
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: 126.96 E-value: 3.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 56 GVTLFDTGDSYGTgRLNgrsELLLGKFSQEYQgvnqENICIATKLAAYPWRWTRQSMI---------NACKSSAQRLGRN 126
Cdd:cd19078 38 GITFFDTAEVYGP-YTN---EELVGEALKPFR----DQVVIATKFGFKIDGGKPGPLGldsrpehirKAVEGSLKRLQTD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 127 -VDLVQMHWSTANyAPWQEVGllDGLADLYEQGLVKGVGLSNYGTKRLQRVHQKFaergvPIKTLQVQYSLLSTYPVTEL 205
Cdd:cd19078 110 yIDLYYQHRVDPN-VPIEEVA--GTMKELIKEGKIRHWGLSEAGVETIRRAHAVC-----PVTAVQSEYSMMWREPEKEV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 206 gLKdVCDELGIKLIAYSPLALGILTGKYSEKGPFPRG-VRGLLLR---QLLPGVRSLLQCLQDVAQSRNKTMSQVALNWC 281
Cdd:cd19078 182 -LP-TLEELGIGFVPFSPLGKGFLTGKIDENTKFDEGdDRASLPRftpEALEANQALVDLLKEFAEEKGATPAQIALAWL 259
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 17135278 282 IAKG--TMPIPGARSVKQAQENIGALGWQLNSGEIAELDKA 320
Cdd:cd19078 260 LAKKpwIVPIPGTTKLSRLEENIGAADIELTPEELREIEDA 300
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
19-318 |
5.94e-34 |
|
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: 125.38 E-value: 5.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 19 LPGMGCGTWAWGNQLLWGYneSMDAQLQAVFNLCVSNGVTLFDTGDSYGtgrlNGRSELLLGKFSQEYQgvnQENICIAT 98
Cdd:cd19137 4 IPALGLGTWGIGGFLTPDY--SRDEEMVELLKTAIELGYTHIDTAEMYG----GGHTEELVGKAIKDFP---REDLFIVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 99 KLaaYPWRWTRQSMINACKSSAQRLGRN-VDLVQMHWSTANYaPWQEVglLDGLADLYEQGLVKGVGLSNYGTKRLQRVH 177
Cdd:cd19137 75 KV--WPTNLRYDDLLRSLQNSLRRLDTDyIDLYLIHWPNPNI-PLEET--LSAMAEGVRQGLIRYIGVSNFNRRLLEEAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 178 QKFAErgvPIKTLQVQYSLLSTYPVtELGLKDVCDELGIKLIAYSPLAlgiltgkysekgpfprgvRGLLLRQLLpgvrs 257
Cdd:cd19137 150 SKSQT---PIVCNQVKYNLEDRDPE-RDGLLEYCQKNGITVVAYSPLR------------------RGLEKTNRT----- 202
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17135278 258 llqcLQDVAQSRNKTMSQVALNWCIAK-GTMPIPGARSVKQAQENIGALGWQLNSGEIAELD 318
Cdd:cd19137 203 ----LEEIAKNYGKTIAQIALAWLIQKpNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
25-318 |
9.81e-33 |
|
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: 123.46 E-value: 9.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 25 GTWAWGNQLLWGYNESMDAQLQaVFNLCVSNGVTLFDTGDSYGtgrlNGRSELLLGKFSQEYqgVNQENICIATKLAaYP 104
Cdd:cd19079 18 GCMSFGDPKWRPWVLDEEESRP-IIKRALDLGINFFDTANVYS----GGASEEILGRALKEF--APRDEVVIATKVY-FP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 105 WR-------WTRQSMINACKSSAQRLGRN-VDLVQMHWSTANyAPWQEVglLDGLADLYEQGLVKGVGLSNYGTKRLQRV 176
Cdd:cd19079 90 MGdgpngrgLSRKHIMAEVDASLKRLGTDyIDLYQIHRWDYE-TPIEET--LEALHDVVKSGKVRYIGASSMYAWQFAKA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 177 hQKFAER--GVPIKTLQVQYSLLstYPVTELGLKDVCDELGIKLIAYSPLALGILTGKYSEKGPFPRGVR---GLLLRQL 251
Cdd:cd19079 167 -LHLAEKngWTKFVSMQNHYNLL--YREEEREMIPLCEEEGIGVIPWSPLARGRLARPWGDTTERRRSTTdtaKLKYDYF 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17135278 252 LPGVRSLLQCLQDVAQSRNKTMSQVALNWCIAKG--TMPIPGARSVKQAQENIGALGWQLNSGEIAELD 318
Cdd:cd19079 244 TEADKEIVDRVEEVAKERGVSMAQVALAWLLSKPgvTAPIVGATKLEHLEDAVAALDIKLSEEEIKYLE 312
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
10-319 |
1.55e-32 |
|
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: 123.15 E-value: 1.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 10 TMQI-HQELSLPGMGCGTWAWGNQLLWG---YNESMDAqLQAVFNLcvsnGVTLFDTGDSYGTGRlngrSELLLGKFSQE 85
Cdd:cd19149 1 YRKLgKSGIEASVIGLGTWAIGGGPWWGgsdDNESIRT-IHAALDL----GINLIDTAPAYGFGH----SEEIVGKAIKG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 86 YQgvnqENICIATKLAAYpWRWTR------------------QSMINACKSSAQRLGRNV-DLVQMHWStANYAPWQEVg 146
Cdd:cd19149 72 RR----DKVVLATKCGLR-WDREGgsfffvrdgvtvyknlspESIREEVEQSLKRLGTDYiDLYQTHWQ-DVETPIEET- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 147 lLDGLADLYEQGLVKGVGLSNYGTKRLQRvhqkfAERGVPIKTLQVQYSLLStyPVTELGLKDVCDELGIKLIAYSPLAL 226
Cdd:cd19149 145 -MEALEELKRQGKIRAIGASNVSVEQIKE-----YVKAGQLDIIQEKYSMLD--RGIEKELLPYCKKNNIAFQAYSPLEQ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 227 GILTGKYSEKGPFP----RGVRGLLLRQLLPGVRSLLQCLQDVAQSRNKTMSQVALNWCIAKG--TMPIPGARSVKQAQE 300
Cdd:cd19149 217 GLLTGKITPDREFDagdaRSGIPWFSPENREKVLALLEKWKPLCEKYGCTLAQLVIAWTLAQPgiTSALCGARKPEQAEE 296
|
330
....*....|....*....
gi 17135278 301 NIGALGWQLNSGEIAELDK 319
Cdd:cd19149 297 NAKAGDIRLSAEDIATMRS 315
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
19-318 |
1.15e-31 |
|
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. The family includes AKR1A/B/C/D/E/G/I, AKR2A/B/C/D/E, AKR3A/B/C/D/E/G, AKR4A/B/C, AKR5A/B/C/D/E/F/G/H, and similar proteins.
Pssm-ID: 381297 [Multi-domain] Cd Length: 251 Bit Score: 119.12 E-value: 1.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 19 LPGMGCGTWawgnqllWGYNESM-DAQLQAVfnlcvSNGVTLFDTGDSYGTgrlngrsELLLGKFSQEYqGVNQENICIA 97
Cdd:cd19071 1 MPLIGLGTY-------KLKPEETaEAVLAAL-----EAGYRHIDTAAAYGN-------EAEVGEAIRES-GVPREELFIT 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 98 TKLAayPWRWTRQSMINACKSSAQRLGRN-VDLVQMHWSTANYAPWQEVGLLD---GLADLYEQGLVKGVGLSNYGTKRL 173
Cdd:cd19071 61 TKLW--PTDHGYERVREALEESLKDLGLDyLDLYLIHWPVPGKEGGSKEARLEtwrALEELVDEGLVRSIGVSNFNVEHL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 174 QRVhqkFAERGVPIKTLQVQYSLLSTYPvtelGLKDVCDELGIKLIAYSPLAlgiltgkysekgpfprgvrglllrqllP 253
Cdd:cd19071 139 EEL---LAAARIKPAVNQIELHPYLQQK----ELVEFCKEHGIVVQAYSPLG---------------------------R 184
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17135278 254 GVRSLLQC--LQDVAQSRNKTMSQVALNWCIAKGTMPIPGARSVKQAQENIGALGWQLNSGEIAELD 318
Cdd:cd19071 185 GRRPLLDDpvLKEIAKKYGKTPAQVLLRWALQRGVVVIPKSSNPERIKENLDVFDFELSEEDMAAID 251
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
17-326 |
1.41e-30 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 118.55 E-value: 1.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 17 LSLPGMGCGTWAwgnqlLWGYNESMDAQ---LQAVFNLcvsnGVTLFDTGDSYGTGrlNGRSELLLGKFSQEYQGVNQEN 93
Cdd:PRK09912 23 LRLPALSLGLWH-----NFGHVNALESQraiLRKAFDL----GITHFDLANNYGPP--PGSAEENFGRLLREDFAAYRDE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 94 ICIATKLAAYPWRW------TRQSMINACKSSAQRLGRN-VDLVQMHWSTANyAPWQEVGllDGLADLYEQGLVKGVGLS 166
Cdd:PRK09912 92 LIISTKAGYDMWPGpygsggSRKYLLASLDQSLKRMGLEyVDIFYSHRVDEN-TPMEETA--SALAHAVQSGKALYVGIS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 167 NYGTKRLQRVHQKFAERGVPIKTLQVQYSLLSTYpVTELGLKDVCDELGIKLIAYSPLALGILTGKYSEKGP-------F 239
Cdd:PRK09912 169 SYSPERTQKMVELLREWKIPLLIHQPSYNLLNRW-VDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPqdsrmhrE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 240 PRGVRGLLLRQLLPGVRSLLQCLQDVAQSRNKTMSQVALNWCI--AKGTMPIPGARSVKQAQENIGAL-GWQLNSGEIAE 316
Cdd:PRK09912 248 GNKVRGLTPKMLTEANLNSLRLLNEMAQQRGQSMAQMALSWLLkdERVTSVLIGASRAEQLEENVQALnNLTFSTEELAQ 327
|
330
....*....|....*....
gi 17135278 317 LDKAA---------ASSDK 326
Cdd:PRK09912 328 IDQHIadgelnlwqASSDK 346
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
22-309 |
5.73e-30 |
|
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: 114.62 E-value: 5.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 22 MGCGTWAWGNQLLWGynESMD-AQLQAVFNLCVSNGVTLFDTGDSYGTGRlngrSELLLGKFSQEYQgvnqENICIATKL 100
Cdd:cd19088 4 LGYGAMRLTGPGIWG--PPADrEEAIAVLRRALELGVNFIDTADSYGPDV----NERLIAEALHPYP----DDVVIATKG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 101 AAY---PWRWTR----QSMINACKSSAQRLGRNV-DLVQMHWSTANYAPWQEVGlldGLADLYEQGLVKGVGLSNYGTKR 172
Cdd:cd19088 74 GLVrtgPGWWGPdgspEYLRQAVEASLRRLGLDRiDLYQLHRIDPKVPFEEQLG---ALAELQDEGLIRHIGLSNVTVAQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 173 LQRvhqkfAERGVPIKTLQVQYSLLSTypvTELGLKDVCDELGIKLIAYSPLAlgiltgkysekgpfprgvRGLLLRQLL 252
Cdd:cd19088 151 IEE-----ARAIVRIVSVQNRYNLANR---DDEGVLDYCEAAGIAFIPWFPLG------------------GGDLAQPGG 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 17135278 253 PgvrsllqcLQDVAQSRNKTMSQVALNWCIAKG--TMPIPGARSVKQAQENIGALGWQL 309
Cdd:cd19088 205 L--------LAEVAARLGATPAQVALAWLLARSpvMLPIPGTSSVEHLEENLAAAGLRL 255
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
14-306 |
1.44e-29 |
|
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: 114.86 E-value: 1.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 14 HQELSLPGMGCGTWawgnqllwgYN-------ESMDAQLQAVFNLcvsnGVTLFDTGDSYGTGRlnGRSELLLGK-FSQE 85
Cdd:cd19150 7 KSGLKLPALSLGLW---------HNfgddtplETQRAILRTAFDL----GITHFDLANNYGPPP--GSAEENFGRiLRED 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 86 YQGVNQENIcIATKLAAYPW-----RW-TRQSMINACKSSAQRLGRN-VDLVQMHWSTANyAPWQEVglLDGLADLYEQG 158
Cdd:cd19150 72 FAGYRDELI-ISTKAGYDMWpgpygEWgSRKYLLASLDQSLKRMGLDyVDIFYSHRFDPD-TPLEET--MGALDHAVRSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 159 LVKGVGLSNYGTKRLQRVHQKFAERGVPIKTLQVQYSLLSTYpVTELGLKDVCDELGIKLIAYSPLALGILTGKYseKGP 238
Cdd:cd19150 148 KALYVGISSYSPERTREAAAILRELGTPLLIHQPSYNMLNRW-VEESGLLDTLQELGVGCIAFTPLAQGLLTDKY--LNG 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17135278 239 FPRGVR-----GLLLRQLLPGVRSLLQCLQDVAQSRNKTMSQVALNWCIAKG--TMPIPGARSVKQAQENIGALG 306
Cdd:cd19150 225 IPEGSRaskerSLSPKMLTEANLNSIRALNEIAQKRGQSLAQMALAWVLRDGrvTSALIGASRPEQLEENVGALD 299
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
22-320 |
2.12e-29 |
|
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: 114.44 E-value: 2.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 22 MGCGTWAWGNQLLwgYNESMDAQLQAVFNLCVSNGVTLFDTGDSYGTGRlngrSELLLGKFSQEYqgvNQENICIATKLA 101
Cdd:cd19083 14 IGLGTNAVGGHNL--YPNLDEEEGKDLVREALDNGVNLLDTAFIYGLGR----SEELVGEVLKEY---NRNEVVIATKGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 102 AYpwRWTRQSMIN--------ACKSSAQRLGRN-VDLVQMHWSTANYAPWQEVGlldGLADLYEQGLVKGVGLSNYGTKR 172
Cdd:cd19083 85 HK--FGGDGSVLNnspeflrsAVEKSLKRLNTDyIDLYYIHFPDGETPKAEAVG---ALQELKDEGKIRAIGVSNFSLEQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 173 LQrvhqKFAERGVpIKTLQVQYSLLSTYpvTELGLKDVCDELGIKLIAYSPLALGILTGKYSEKGPFPRG--------VR 244
Cdd:cd19083 160 LK----EANKDGY-VDVLQGEYNLLQRE--AEEDILPYCVENNISFIPYFPLASGLLAGKYTKDTKFPDNdlrndkplFK 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17135278 245 GLLLRQLLPGVRSllqcLQDVAQSRNKTMSQVALNWCIAKGTMP--IPGARSVKQAQENIGALGWQLNSGEIAELDKA 320
Cdd:cd19083 233 GERFSENLDKVDK----LKSIADEKGVTVAHLALAWYLTRPAIDvvIPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
22-305 |
6.26e-28 |
|
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: 110.34 E-value: 6.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 22 MGCGTWAWGNQLLWGynesmdAQLQAVFNLCVSNGVTLFDTGDSYGtgrlNGRSELLLGKFSQEYQGVNqenicIATKla 101
Cdd:cd19075 5 LGTMTFGSQGRFTTA------EAAAELLDAFLERGHTEIDTARVYP----DGTSEELLGELGLGERGFK-----IDTK-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 102 AYPW---RWTRQSMINACKSSAQRLGRN-VDLVQMHwstanyAPWQEVGL---LDGLADLYEQGLVKGVGLSNYGTKRLQ 174
Cdd:cd19075 68 ANPGvggGLSPENVRKQLETSLKRLKVDkVDVFYLH------APDRSTPLeetLAAIDELYKEGKFKEFGLSNYSAWEVA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 175 RVHQKFAERGVPIKTL-QVQYSLLSTYPVTELglKDVCDELGIKLIAYSPLALGILTGKYSEKGPFPRGVR-------GL 246
Cdd:cd19075 142 EIVEICKENGWVLPTVyQGMYNAITRQVETEL--FPCLRKLGIRFYAYSPLAGGFLTGKYKYSEDKAGGGRfdpnnalGK 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17135278 247 LLRQL--LPGVRSLLQCLQDVAQSRNKTMSQVALNWCI-------AKGTMPIPGARSVKQAQENIGAL 305
Cdd:cd19075 220 LYRDRywKPSYFEALEKVEEAAEKEGISLAEAALRWLYhhsaldgEKGDGVILGASSLEQLEENLAAL 287
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
10-318 |
3.92e-26 |
|
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: 104.71 E-value: 3.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 10 TMQIHQELSLPGMGCGTWAWGnqllwGYneSMDAQLQAVFNlCvsnGVTLFDTGDSYGTgrlngrsELLLGKFSQEyQGV 89
Cdd:cd19135 4 TVRLSNGVEMPILGLGTSHSG-----GY--SHEAVVYALKE-C---GYRHIDTAKRYGC-------EELLGKAIKE-SGV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 90 NQENICIATKLaaYPWRWTRQSMINACKSSAQRLGRN-VDLVQMHW----------STANYAPWQevglldGLADLYEQG 158
Cdd:cd19135 65 PREDLFLTTKL--WPSDYGYESTKQAFEASLKRLGVDyLDLYLLHWpdcpssgknvKETRAETWR------ALEELYDEG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 159 LVKGVGLSNYGTKRLQrvhQKFAERGVPIKTLQVQYSLLsTYPVTelgLKDVCDELGIKLIAYSPLAlgiltgkysekgp 238
Cdd:cd19135 137 LCRAIGVSNFLIEHLE---QLLEDCSVVPHVNQVEFHPF-QNPVE---LIEYCRDNNIVFEGYCPLA------------- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 239 fprgvRGLLLRQllPGVrsllqclQDVAQSRNKTMSQVALNWCIAKGTMPIPGARSVKQAQENIGALGWQLNSGEIAELD 318
Cdd:cd19135 197 -----KGKALEE--PTV-------TELAKKYQKTPAQILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLD 262
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
19-319 |
2.92e-25 |
|
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: 102.75 E-value: 2.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 19 LPGMGCGTWawgnqLLWGYNESMDAQLQAVfnlcvSNGVTLFDTGDSYGTgrlngrsELLLGKFSQEY---QGVNQENIC 95
Cdd:cd19116 11 IPAIALGTW-----KLKDDEGVRQAVKHAI-----EAGYRHIDTAYLYGN-------EAEVGEAIREKiaeGVVKREDLF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 96 IATKLaaypwrW----TRQSMINACKSSAQRLGRN-VDLVQMHWSTA------NYAP----WQEVGLLD---GLADLYEQ 157
Cdd:cd19116 74 ITTKL------WnsyhEREQVEPALRESLKRLGLDyVDLYLIHWPVAfkenndSESNgdgsLSDIDYLEtwrGMEDLVKL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 158 GLVKGVGLSNYGTKRLQRVhqkFAERGVPIKTLQVQYSLlstyPVTELGLKDVCDELGIKLIAYSPLalgiltGKysekg 237
Cdd:cd19116 148 GLTRSIGVSNFNSEQINRL---LSNCNIKPAVNQIEVHP----TLTQEKLVAYCQSNGIVVMAYSPF------GR----- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 238 PFPRgvrglllRQLLPGVRSLLQCLQDVAQSRNKTMSQVALNWCIAKGTMPIPGARSVKQAQENIGALGWQLNSGEIAEL 317
Cdd:cd19116 210 LVPR-------GQTNPPPRLDDPTLVAIAKKYGKTTAQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAAL 282
|
..
gi 17135278 318 DK 319
Cdd:cd19116 283 NS 284
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
53-306 |
6.13e-25 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 102.02 E-value: 6.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 53 VSNGVTLFDTGDSYGT---GRLNGRSELLLGKFSQEyQGvNQENICIATKLAAYPWRW----------TRQSMINACKSS 119
Cdd:cd19752 27 VAAGGNFLDTANNYAFwteGGVGGESERLIGRWLKD-RG-NRDDVVIATKVGAGPRDPdggpespeglSAETIEQEIDKS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 120 AQRLGRN-VDLVQMHWSTANYaPWQEVglLDGLADLYEQGLVKGVGLSNYGTKRLQRVHQKFAERGVPIKT-LQVQYSLL 197
Cdd:cd19752 105 LRRLGTDyIDLYYAHVDDRDT-PLEET--LEAFNELVKAGKVRAIGASNFAAWRLERARQIARQQGWAEFSaIQQRHSYL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 198 STYPVTELG--------LKDVCDELG-IKLIAYSPLalgiLTGKYS-EKGPFPRGVRGlllrqllPGVRSLLQCLQDVAQ 267
Cdd:cd19752 182 RPRPGADFGvqrivtdeLLDYASSRPdLTLLAYSPL----LSGAYTrPDRPLPEQYDG-------PDSDARLAVLEEVAG 250
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 17135278 268 SRNKTMSQVALNWCIAK--GTMPIPGARSVKQAQENIGALG 306
Cdd:cd19752 251 ELGATPNQVVLAWLLHRtpAIIPLLGASTVEQLEENLAALD 291
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
16-317 |
5.09e-24 |
|
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: 99.81 E-value: 5.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 16 ELSLPGMGCgtwawgNQLLWGYNESM-DAQLQAVFNLCVSNGVTLFDTGDSYGTGRlngrSELLLGKfsqEYQGVNQENI 94
Cdd:cd19145 11 EVSAQGLGC------MGLSGDYGAPKpEEEGIALIHHAFNSGVTFLDTSDIYGPNT----NEVLLGK---ALKDGPREKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 95 CIATKLA-AYP------WRWTRQSMINACKSSAQRLGRN-VDLVQMHWSTANYAPWQEVGlldGLADLYEQGLVKGVGLS 166
Cdd:cd19145 78 QLATKFGiHEIggsgveVRGDPAYVRAACEASLKRLDVDyIDLYYQHRIDTTVPIEITMG---ELKKLVEEGKIKYIGLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 167 NYGTKRLQRVHQKFaergvPIKTLQVQYSLLStypvtelglKDV-------CDELGIKLIAYSPLALGILTGKysekgpf 239
Cdd:cd19145 155 EASADTIRRAHAVH-----PITAVQLEWSLWT---------RDIeeeiiptCRELGIGIVPYSPLGRGFFAGK------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 240 PRGVRGL---LLRQLLPGVRS--------LLQCLQDVAQSRNKTMSQVALNWCIAKG--TMPIPGARSVKQAQENIGALG 306
Cdd:cd19145 214 AKLEELLensDVRKSHPRFQGenleknkvLYERVEALAKKKGCTPAQLALAWVLHQGedVVPIPGTTKIKNLNQNIGALS 293
|
330
....*....|.
gi 17135278 307 WQLNSGEIAEL 317
Cdd:cd19145 294 VKLTKEDLKEI 304
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
17-305 |
1.35e-23 |
|
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: 98.63 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 17 LSLPGMGCGTW-AWGNQLLWgynESMDAQLQAVFNLcvsnGVTLFDTGDSYGTgrLNGRSELLLGK-FSQEYQGVNQENI 94
Cdd:cd19151 10 LKLPAISLGLWhNFGDVDRY---ENSRAMLRRAFDL----GITHFDLANNYGP--PPGSAEENFGRiLKEDLKPYRDELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 95 cIATKLAAYPWR-----W-TRQSMINACKSSAQRLGRN-VDLVQMHWSTANyAPWQEVglLDGLADLYEQGLVKGVGLSN 167
Cdd:cd19151 81 -ISTKAGYTMWPgpygdWgSKKYLIASLDQSLKRMGLDyVDIFYHHRPDPE-TPLEET--MGALDQIVRQGKALYVGISN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 168 YGTKRLQRVHQKFAERGVPIKTLQVQYSLLSTYPvtELGLKDVCDELGIKLIAYSPLALGILTGKYSeKGpFPRGVR--- 244
Cdd:cd19151 157 YPPEEAREAAAILKDLGTPCLIHQPKYSMFNRWV--EEGLLDVLEEEGIGCIAFSPLAQGLLTDRYL-NG-IPEDSRaak 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17135278 245 -GLLLR--QLLPGVRSLLQCLQDVAQSRNKTMSQVALNWCIAKGTMP--IPGARSVKQAQENIGAL 305
Cdd:cd19151 233 gSSFLKpeQITEEKLAKVRRLNEIAQARGQKLAQMALAWVLRNKRVTsvLIGASKPSQIEDAVGAL 298
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
23-319 |
1.40e-23 |
|
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: 98.53 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 23 GCGTWAWGNQLlWGYNEsmDAQLQAVFNLCVSNGVTLFDTGDSYGTGRlngrSELLLGKFSQEYQGVNQenICIATKLA- 101
Cdd:cd19148 8 ALGTWAIGGWM-WGGTD--EKEAIETIHKALDLGINLIDTAPVYGFGL----SEEIVGKALKEYGKRDR--VVIATKVGl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 102 -----AYPWR-WTRQSMINACKSSAQRLGRN-VDLVQMHWSTANyAPWQEVGLLdgLADLYEQGLVKGVGLSNYGTKRLQ 174
Cdd:cd19148 79 ewdegGEVVRnSSPARIRKEVEDSLRRLQTDyIDLYQVHWPDPL-VPIEETAEA--LKELLDEGKIRAIGVSNFSPEQME 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 175 RVhqkfaERGVPIKTLQVQYSLLstypvtELGL-KDV---CDELGIKLIAYSPLALGILTGKYSEKGPFPRGVrgllLRQ 250
Cdd:cd19148 156 TF-----RKVAPLHTVQPPYNLF------EREIeKDVlpyARKHNIVTLAYGALCRGLLSGKMTKDTKFEGDD----LRR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 251 LLPGVRS-----LLQC---LQDVAQSR-NKTMSQVALNWCIAKGTMPIP--GARSVKQAQENIGALGWQLNSGEIAELDK 319
Cdd:cd19148 221 TDPKFQEprfsqYLAAveeLDKLAQERyGKSVIHLAVRWLLDQPGVSIAlwGARKPEQLDAVDEVFGWSLNDEDMKEIDA 300
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
22-312 |
1.77e-22 |
|
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: 94.93 E-value: 1.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 22 MGCGTWAWGNqlLWGyNESMDAQLQAVFnLCVSNGVTLFDTGDSYGtgrlngRSELLLGKFSQEYQGvnqENICIATKLA 101
Cdd:cd19090 3 LGLGTAGLGG--VFG-GVDDDEAVATIR-AALDLGINYIDTAPAYG------DSEERLGLALAELPR---EPLVLSTKVG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 102 AYP---WRWTRQSMINACKSSAQRLGRN-VDLVQMHwsTANYAPWQEV----GLLDGLADLYEQGLVKGVGLSNYGTkrl 173
Cdd:cd19090 70 RLPedtADYSADRVRRSVEESLERLGRDrIDLLMIH--DPERVPWVDIlapgGALEALLELKEEGLIKHIGLGGGPP--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 174 qRVHQKFAERGVPIKTLQVQ-YSLLSTYPVTELglKDVCDELGIKLIAYSPLALGILTGKYSEKGPFPRgvrglllRQLL 252
Cdd:cd19090 145 -DLLRRAIETGDFDVVLTANrYTLLDQSAADEL--LPAAARHGVGVINASPLGMGLLAGRPPERVRYTY-------RWLS 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17135278 253 PGVRSLLQCLQDVAQSRNKTMSQVALNWCIAkgtMP-----IPGARSVKQAQENIGALGWQLNSG 312
Cdd:cd19090 215 PELLDRAKRLYELCDEHGVPLPALALRFLLR---DPristvLVGASSPEELEQNVAAAEGPLPEE 276
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
14-318 |
4.19e-22 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 95.31 E-value: 4.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 14 HQELSLPGMGCGTWAWGNQllwgyNESMDAQLQavFNLCVSNGVTLFDTGDSYGTG---RLNGRSELLLGKFSQEYQgvN 90
Cdd:PRK10625 8 HSSLEVSTLGLGTMTFGEQ-----NSEADAHAQ--LDYAVAQGINLIDVAEMYPVPprpETQGLTETYIGNWLAKRG--S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 91 QENICIATKLAAyPWRWT-----------RQSMINACKSSAQRLGRN-VDLVQMHW--------STANYApWQE----VG 146
Cdd:PRK10625 79 REKLIIASKVSG-PSRNNdkgirpnqaldRKNIREALHDSLKRLQTDyLDLYQVHWpqrptncfGKLGYS-WTDsapaVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 147 LLDGLADLYEQ---GLVKGVGLSN---YGTKRLQRVHQKfaeRGVP-IKTLQVQYSLLSTypVTELGLKDVCDELGIKLI 219
Cdd:PRK10625 157 LLETLDALAEQqraGKIRYIGVSNetaFGVMRYLHLAEK---HDLPrIVTIQNPYSLLNR--SFEVGLAEVSQYEGVELL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 220 AYSPLALGILTGKYSeKGPFPRGVRGLLL----RQLLPGVRSLLQCLQDVAQSRNKTMSQVALNWC-----IAKGTMpip 290
Cdd:PRK10625 232 AYSCLAFGTLTGKYL-NGAKPAGARNTLFsrftRYSGEQTQKAVAAYVDIAKRHGLDPAQMALAFVrrqpfVASTLL--- 307
|
330 340
....*....|....*....|....*...
gi 17135278 291 GARSVKQAQENIGALGWQLNSGEIAELD 318
Cdd:PRK10625 308 GATTMEQLKTNIESLHLTLSEEVLAEIE 335
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
14-319 |
2.48e-21 |
|
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: 91.17 E-value: 2.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 14 HQELSLPGMGCGTWawgnqllwgynESMDAQLQAVFNLCVSNGVTLFDTGDSYG----TGRLNGRSelllgkfsqeyqGV 89
Cdd:cd19140 3 VNGVRIPALGLGTY-----------PLTGEECTRAVEHALELGYRHIDTAQMYGneaqVGEAIAAS------------GV 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 90 NQENICIATKLaaYPWRWTRQSMINACKSSAQRLGRN-VDLVQMHWstanyaPWQEVGL---LDGLADLYEQGLVKGVGL 165
Cdd:cd19140 60 PRDELFLTTKV--WPDNYSPDDFLASVEESLRKLRTDyVDLLLLHW------PNKDVPLaetLGALNEAQEAGLARHIGV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 166 SNYGTKRLQRVHqkfAERGVPIKTLQVQYS-LLSTYPVtelglKDVCDELGIKLIAYSPLAlgiltgkysekgpfprgvR 244
Cdd:cd19140 132 SNFTVALLREAV---ELSEAPLFTNQVEYHpYLDQRKL-----LDAAREHGIALTAYSPLA------------------R 185
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17135278 245 GLLLRQLLpgvrsllqcLQDVAQSRNKTMSQVALNWCIAK-GTMPIPGARSVKQAQENIGALGWQLNSGEIAELDK 319
Cdd:cd19140 186 GEVLKDPV---------LQEIGRKHGKTPAQVALRWLLQQeGVAAIPKATNPERLEENLDIFDFTLSDEEMARIAA 252
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
23-304 |
2.40e-20 |
|
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: 88.45 E-value: 2.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 23 GCGTW-AWGNqllWGYNEsmDAQLQAVFNLCVSNGVTLFDTGDSYgtgrlnGRSELLLGKFSQEYQGvnqENICIATKlA 101
Cdd:cd19095 4 GLGTSgIGRV---WGVPS--EAEAARLLNTALDLGINLIDTAPAY------GRSEERLGRALAGLRR---DDLFIATK-V 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 102 AYPWR-------WTRQSMINACKSSAQRLGRN-VDLVQMHwstaNYAPWQEVG-LLDGLADLYEQGLVKGVGLSNYGTkr 172
Cdd:cd19095 69 GTHGEggrdrkdFSPAAIRASIERSLRRLGTDyIDLLQLH----GPSDDELTGeVLETLEDLKAAGKVRYIGVSGDGE-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 173 lqrVHQKFAERGVpIKTLQVQYSLLSTypvTELGLKDVCDELGIKLIAYSPLAlgiltgkyseKGPFPRGVRGlllrqlL 252
Cdd:cd19095 143 ---ELEAAIASGV-FDVVQLPYNVLDR---EEEELLPLAAEAGLGVIVNRPLA----------NGRLRRRVRR------R 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 17135278 253 PGVRSLLQCLQDVAQSRNKTMSQVALNWCIAKG--TMPIPGARSVKQAQENIGA 304
Cdd:cd19095 200 PLYADYARRPEFAAEIGGATWAQAALRFVLSHPgvSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
16-321 |
4.73e-20 |
|
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: 88.38 E-value: 4.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 16 ELSLPGMGCgtwaWGnqlLWGYNESmDAQLQAVFNLCVSNGVTLFDTGDSYGtgrlNGRSELLLGKFSQEYQGVnQENIC 95
Cdd:cd19092 5 EVSRLVLGC----MR---LADWGES-AEELLSLIEAALELGITTFDHADIYG----GGKCEELFGEALALNPGL-REKIE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 96 IATK----LAAYPWRWTRQS-------MINACKSSAQRLGRN-VDLVQMHWSTANYAPWqEVGllDGLADLYEQGLVKGV 163
Cdd:cd19092 72 IQTKcgirLGDDPRPGRIKHydtskehILASVEGSLKRLGTDyLDLLLLHRPDPLMDPE-EVA--EAFDELVKSGKVRYF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 164 GLSNYGTKRLQ----RVHQkfaergvPIKTLQVQYSLLSTYPVTElGLKDVCDELGIKLIAYSPLALGILTGKYSEKgpF 239
Cdd:cd19092 149 GVSNFTPSQIEllqsYLDQ-------PLVTNQIELSLLHTEAIDD-GTLDYCQLLDITPMAWSPLGGGRLFGGFDER--F 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 240 PRgvrglllrqllpgvrsLLQCLQDVAQSRNKTMSQVALNWcIAK---GTMPIPGARSVKQAQENIGALGWQLNSGEIAE 316
Cdd:cd19092 219 QR----------------LRAALEELAEEYGVTIEAIALAW-LLRhpaRIQPILGTTNPERIRSAVKALDIELTREEWYE 281
|
....*
gi 17135278 317 LDKAA 321
Cdd:cd19092 282 IYEAA 286
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
61-319 |
3.14e-19 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 85.48 E-value: 3.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 61 DTGDSYGTgrlngrsELLLGKFSQEyQGVNQENICIATKLaaypW--RWTRQSMINACKSSAQRLGRN-VDLVQMHW-ST 136
Cdd:cd19139 32 DTAQIYDN-------EAAVGQAIAE-SGVPRDELFITTKI----WidNLSKDKLLPSLEESLEKLRTDyVDLTLIHWpSP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 137 ANYAPWQEVglLDGLADLYEQGLVKGVGLSNYGTKRLQRVHQKFAERgvPIKTLQVQyslLSTYpVTELGLKDVCDELGI 216
Cdd:cd19139 100 NDEVPVEEY--IGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVGAG--AIATNQIE---LSPY-LQNRKLVAHCKQHGI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 217 KLIAYSPLAlgiltgkysekgpfprgvRGLLLRQllpgvrsllQCLQDVAQSRNKTMSQVALNWCIAKGTMPIPGARSVK 296
Cdd:cd19139 172 HVTSYMTLA------------------YGKVLDD---------PVLAAIAERHGATPAQIALAWAMARGYAVIPSSTKRE 224
|
250 260
....*....|....*....|...
gi 17135278 297 QAQENIGALGWQLNSGEIAELDK 319
Cdd:cd19139 225 HLRSNLLALDLTLDADDMAAIAA 247
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
16-305 |
1.38e-18 |
|
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: 84.96 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 16 ELSLpgmgcGTW-AWGNQLLWGYNESMdaqLQAVFNlcvsNGVTLFDTGDSYGtgrlNGRSELLLGKFSQEYqGVNQENI 94
Cdd:cd19143 15 ALSF-----GSWvTFGNQVDVDEAKEC---MKAAYD----AGVNFFDNAEVYA----NGQSEEIMGQAIKEL-GWPRSDY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 95 CIATKLAaypWRW----------TRQSMINACKSSAQRLGRN-VDLVQMHWSTANyAPWQEVglLDGLADLYEQGLVKGV 163
Cdd:cd19143 78 VVSTKIF---WGGggpppndrglSRKHIVEGTKASLKRLQLDyVDLVFCHRPDPA-TPIEET--VRAMNDLIDQGKAFYW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 164 GLSNYGTKRLQRVHQkFAERGVPIKTL--QVQYSLLSTYPVtELGLKDVCDELGIKLIAYSPLALGILTGKYSEKgpFPR 241
Cdd:cd19143 152 GTSEWSAQQIEEAHE-IADRLGLIPPVmeQPQYNLFHRERV-EVEYAPLYEKYGLGTTTWSPLASGLLTGKYNNG--IPE 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17135278 242 GVRGLL---------LRQLLPGVRSLLQCLQDVAQSRNKTMSQVALNWCIAKgtmP-----IPGARSVKQAQENIGAL 305
Cdd:cd19143 228 GSRLALpgyewlkdrKEELGQEKIEKVRKLKPIAEELGCSLAQLAIAWCLKN---PnvstvITGATKVEQLEENLKAL 302
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
20-322 |
1.74e-18 |
|
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: 83.82 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 20 PGMGCGTWAWGNQLLWGYNESMDAQLQAVfnlcvSNGVTLFDTGDSYGTgrlngrsELLLGKFSQEYqGVNQENICIATK 99
Cdd:cd19120 7 IAFGTGTAWYKSGDDDIQRDLVDSVKLAL-----KAGFRHIDTAEMYGN-------EKEVGEALKES-GVPREDLFITTK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 100 LaaypwrWTRQSMIN-ACKSSAQRLGRN-VDLVQMH--WSTANYAP-----WQEvglldgLADLYEQGLVKGVGLSNYGT 170
Cdd:cd19120 74 V------SPGIKDPReALRKSLAKLGVDyVDLYLIHspFFAKEGGPtlaeaWAE------LEALKDAGLVRSIGVSNFRI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 171 KRLQRVhqkFAERGVPIKTLQVQYS--LLSTYPvtelGLKDVCDELGIKLIAYSPLAlgiltgkysekgPFPRGVRGlll 248
Cdd:cd19120 142 EDLEEL---LDTAKIKPAVNQIEFHpyLYPQQP----ALLEYCREHGIVVSAYSPLS------------PLTRDAGG--- 199
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17135278 249 rqllpgvrSLLQCLQDVAQSRNKTMSQVALNWCIAKGTMPIPGARSVKQAQENIGALGWQLNSGEIAELDKAAA 322
Cdd:cd19120 200 --------PLDPVLEKIAEKYGVTPAQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEIDKAGK 265
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
19-319 |
3.08e-18 |
|
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: 83.06 E-value: 3.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 19 LPGMGCGTWAwgnqlLWGYNESMDAQLQAVfnlcvSNGVTLFDTGDSYGTGRLNGRS-ELLLGKFsqeyqGVNQENICIA 97
Cdd:cd19136 1 MPILGLGTFR-----LRGEEEVRQAVDAAL-----KAGYRLIDTASVYRNEADIGKAlRDLLPKY-----GLSREDIFIT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 98 TKLAayPWRWTRQSMINACKSSAQRLGRN-VDLVQMHW---------STANYA----PWQEvglldgLADLYEQGLVKGV 163
Cdd:cd19136 66 SKLA--PKDQGYEKARAACLGSLERLGTDyLDLYLIHWpgvqglkpsDPRNAElrreSWRA------LEDLYKEGKLRAI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 164 GLSNYGTKRLQRVhQKFAErgVPIKTLQVQYSLLstYPVTELglKDVCDELGIKLIAYSPLALGiltgkysekgpfprgv 243
Cdd:cd19136 138 GVSNYTVRHLEEL-LKYCE--VPPAVNQVEFHPH--LVQKEL--LKFCKDHGIHLQAYSSLGSG---------------- 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17135278 244 RGLLLRQllPGVrsllqclQDVAQSRNKTMSQVALNWCIAKGTMPIPGARSVKQAQENIGALGWQLNSGEIAELDK 319
Cdd:cd19136 195 DLRLLED--PTV-------LAIAKKYGRTPAQVLLRWALQQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNA 261
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
47-305 |
6.54e-18 |
|
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: 82.60 E-value: 6.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 47 AVFNLCVSNGVTLFDTGDSYGTGRLNGRSELLLGKFSQEYQgvNQENICIATKLAAYP------WRWTRQSMINACKSSA 120
Cdd:cd19082 21 ALLDAFVELGGNFIDTARVYGDWVERGASERVIGEWLKSRG--NRDKVVIATKGGHPDledmsrSRLSPEDIRADLEESL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 121 QRLGRN-VDLVQMHwstaNYAPWQEVG-LLDGLADLYEQGLVKGVGLSNYGTKRLQRVhQKFAER--GVPIKTLQVQYSL 196
Cdd:cd19082 99 ERLGTDyIDLYFLH----RDDPSVPVGeIVDTLNELVRAGKIRAFGASNWSTERIAEA-NAYAKAhgLPGFAASSPQWSL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 197 LSTYPVTELGLKDVC---------DELGIKLIAYSPLALGILTGKYSEKGPFPRGVRGLLLRqllPGVRSLLQCLQDVAQ 267
Cdd:cd19082 174 ARPNEPPWPGPTLVAmdeemrawhEENQLPVFAYSSQARGFFSKRAAGGAEDDSELRRVYYS---EENFERLERAKELAE 250
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 17135278 268 SRNKTMSQVALNWCIAKG--TMPIPGARSVKQAQENIGAL 305
Cdd:cd19082 251 EKGVSPTQIALAYVLNQPfpTVPIIGPRTPEQLRDSLAAA 290
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-305 |
2.31e-17 |
|
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: 80.32 E-value: 2.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 15 QELSLPGMGCGTWAWGNQLLwgynesmdaqLQAVFNLcvsnGVTLFDTGDSYGtgrlNGRSELLLGKFsqeYQGVNQENI 94
Cdd:cd19105 11 LKVSRLGFGGGGLPRESPEL----------LRRALDL----GINYFDTAEGYG----NGNSEEIIGEA---LKGLRRDKV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 95 CIATKLAAYPWRWTRQSMINACKSSAQRLGRN-VDLVQMHWSTANYAPWQEVGLLDGLADLYEQGLVKGVGLSNYGTkrL 173
Cdd:cd19105 70 FLATKASPRLDKKDKAELLKSVEESLKRLQTDyIDIYQLHGVDTPEERLLNEELLEALEKLKKEGKVRFIGFSTHDN--M 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 174 QRVHQKFAERGvPIKTLQVQYSLLStYPVTELGLKDVCDELGIKLIAYSPLA---LGILTGKYSEKGPFPRgvrglllrq 250
Cdd:cd19105 148 AEVLQAAIESG-WFDVIMVAYNFLN-QPAELEEALAAAAEKGIGVVAMKTLAggyLQPALLSVLKAKGFSL--------- 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 17135278 251 llpgvrsllqclqdvaqsrnktmSQVALNWCIAKGTM--PIPGARSVKQAQENIGAL 305
Cdd:cd19105 217 -----------------------PQAALKWVLSNPRVdtVVPGMRNFAELEENLAAA 250
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
18-318 |
3.46e-17 |
|
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: 79.62 E-value: 3.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 18 SLPGMGCGTWawgnqLLWGYN--ESMDAQLQAvfnlcvsnGVTLFDTGDSY----GTGRLNGRSelllgkfsqeyqGVNQ 91
Cdd:cd19132 6 QIPAIGFGTY-----PLKGDEgvEAVVAALQA--------GYRLLDTAFNYenegAVGEAVRRS------------GVPR 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 92 ENICIATKLAAYPWRwtRQSMINACKSSAQRLGRN-VDLVQMHW---STANY-APWQEvglldgLADLYEQGLVKGVGLS 166
Cdd:cd19132 61 EELFVTTKLPGRHHG--YEEALRTIEESLYRLGLDyVDLYLIHWpnpSRDLYvEAWQA------LIEAREEGLVRSIGVS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 167 NYGTKRLQRVHQkfaERGVPIKTLQVQysLLSTYPVTELglKDVCDELGIKLIAYSPLAlgiltgkysekgpfpRGVRgl 246
Cdd:cd19132 133 NFLPEHLDRLID---ETGVTPAVNQIE--LHPYFPQAEQ--RAYHREHGIVTQSWSPLG---------------RGSG-- 188
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17135278 247 LLRQllpgvrsllQCLQDVAQSRNKTMSQVALNWCIAKGTMPIPGARSVKQAQENIGALGWQLNSGEIAELD 318
Cdd:cd19132 189 LLDE---------PVIKAIAEKHGKTPAQVVLRWHVQLGVVPIPKSANPERQRENLAIFDFELSDEDMAAIA 251
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
22-305 |
1.08e-16 |
|
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: 79.41 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 22 MGCGTWA-WGNQLlwgynesMDAQLQAVFNLCVSNGVTLFDTGDSYGTGRlngrSELLLGKFSQEyQGVNQENICIATKL 100
Cdd:cd19141 15 LGLGTWVtFGSQI-------SDEVAEELVTLAYENGINLFDTAEVYAAGK----AEIVLGKILKK-KGWRRSSYVITTKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 101 -----AAYPWRWTRQSMINACKSSAQRLGRN-VDLVQMHWSTANyAPWQEVglLDGLADLYEQGLVKGVGLSNYGTKRLQ 174
Cdd:cd19141 83 fwggkAETERGLSRKHIIEGLKASLERLQLEyVDIVFANRPDPN-TPMEEI--VRAFTHVINQGMAMYWGTSRWSAMEIM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 175 RVH---QKFaeRGVPIKTLQVQYSLLSTYPVtELGLKDVCDELGIKLIAYSPLALGILTGKYSEKGPF-PRG-------V 243
Cdd:cd19141 160 EAYsvaRQF--NLIPPIVEQAEYHLFQREKV-EMQLPELFHKIGVGAMTWSPLACGILSGKYDDGVPEySRAslkgyqwL 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17135278 244 RGLLLRQLLPGVRSLLQCLQDVAQSRNKTMSQVALNWCIAKGTMP--IPGARSVKQAQENIGAL 305
Cdd:cd19141 237 KEKILSEEGRRQQAKLKELQIIADRLGCTLPQLAIAWCLKNEGVSsvLLGASSTEQLYENLQAI 300
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
128-319 |
1.78e-16 |
|
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a founding member of aldo-keto reductase family 3 member G1 (AKR3G1). It is an aldo/keto reductase that catalyzes the NADPH-dependent reduction of aldehyde- and ketone-groups of different classes of carbonyl compounds to the corresponding alcohols.
Pssm-ID: 381349 [Multi-domain] Cd Length: 297 Bit Score: 78.61 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 128 DLVQMHW------------STANYAPWQEVGLLD---GLADLYEQGLVKGVGLSNYGTKRLQRVHQKfaERGVPIKTlQV 192
Cdd:cd19123 105 DLYLMHWpvalkkgvgfpeSGEDLLSLSPIPLEDtwrAMEELVDKGLCRHIGVSNFSVKKLEDLLAT--ARIKPAVN-QV 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 193 QyslLSTYpVTELGLKDVCDELGIKLIAYSPLAlgiltgkysekgpfpRGVRGLLLRQllPGVRSLLQ--CLQDVAQSRN 270
Cdd:cd19123 182 E---LHPY-LQQPELLAFCRDNGIHLTAYSPLG---------------SGDRPAAMKA--EGEPVLLEdpVINKIAEKHG 240
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17135278 271 KTMSQVALNWCIAKGTMPIPGARSVKQAQENIGALGWQLNSGE---IAELDK 319
Cdd:cd19123 241 ASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDmatIAALDR 292
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
22-318 |
4.93e-16 |
|
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: 77.72 E-value: 4.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 22 MGCGTW-AWGNQLlwgynesMDAQLQAVFNLCVSNGVTLFDTGDSYGTGRlngrSELLLGKFSQEyQGVNQENICIATKL 100
Cdd:cd19160 18 LGLGTWvTFGSQI-------SDETAEDLLTVAYEHGVNLFDTAEVYAAGK----AERTLGNILKS-KGWRRSSYVVTTKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 101 -----AAYPWRWTRQSMINACKSSAQRLGRN-VDLVQMHWSTANyAPWQEVglLDGLADLYEQGLVKGVGLSNYGTKRLQ 174
Cdd:cd19160 86 ywggqAETERGLSRKHIIEGLRGSLDRLQLEyVDIVFANRSDPN-SPMEEI--VRAMTYVINQGMAMYWGTSRWSAMEIM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 175 RVHQKFAERG-VPIKTLQVQYSLLSTYPVtELGLKDVCDELGIKLIAYSPLALGILTGKYSEKGPFP-----RGVRGLLL 248
Cdd:cd19160 163 EAYSVARQFNlIPPVCEQAEYHLFQREKV-EMQLPELYHKIGVGSVTWSPLACGLITGKYDGRVPDTcraavKGYQWLKE 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17135278 249 R-QLLPGVR--SLLQCLQDVAQSRNKTMSQVALNWCI-AKGTMPI-PGARSVKQAQENIGALG--WQLNSGEIAELD 318
Cdd:cd19160 242 KvQSEEGKKqqAKVKELHPIADRLGCTVAQLAIAWCLrSEGVSSVlLGVSSAEQLIENLGSIQvlSQLTPQTVMEID 318
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
17-318 |
8.98e-16 |
|
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: 77.05 E-value: 8.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 17 LSLPGMGCGTW-AWGNQLlwgynesMDAQLQAVFNLCVSNGVTLFDTGDSYGTGRlngrSELLLGKFSQEyQGVNQENIC 95
Cdd:cd19158 11 LRVSCLGLGTWvTFGGQI-------TDEMAEHLMTLAYDNGINLFDTAEVYAAGK----AEVVLGNIIKK-KGWRRSSLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 96 IATKL-----AAYPWRWTRQSMINACKSSAQRLG-RNVDLVQMHWSTANyAPWQEVglLDGLADLYEQGLVKGVGLSNYG 169
Cdd:cd19158 79 ITTKIfwggkAETERGLSRKHIIEGLKASLERLQlEYVDVVFANRPDPN-TPMEET--VRAMTHVINQGMAMYWGTSRWS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 170 TKRLQRVHQKFAERG-VPIKTLQVQYSLLSTYPVtELGLKDVCDELGIKLIAYSPLALGILTGKY-SEKGPFPRG----- 242
Cdd:cd19158 156 SMEIMEAYSVARQFNlIPPICEQAEYHMFQREKV-EVQLPELFHKIGVGAMTWSPLACGIVSGKYdSGIPPYSRAslkgy 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 243 --VRGLLLRQLLPGVRSLLQCLQDVAQSRNKTMSQVALNWCIAKGTMP--IPGARSVKQAQENIGALGW--QLNSGEIAE 316
Cdd:cd19158 235 qwLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSsvLLGASNAEQLMENIGAIQVlpKLSSSIVHE 314
|
..
gi 17135278 317 LD 318
Cdd:cd19158 315 ID 316
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
10-318 |
1.85e-15 |
|
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: 75.10 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 10 TMQIHQELSLPGMGCGTWawgnqllwgynESMDAQLQAVFNLCVSNGVTLFDTGDSYGtgrlngrSELLLGKfSQEYQGV 89
Cdd:cd19131 1 TITLNDGNTIPQLGLGVW-----------QVSNDEAASAVREALEVGYRSIDTAAIYG-------NEEGVGK-AIRASGV 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 90 NQENICIATKLaaypwrWT----RQSMINACKSSAQRLGRN-VDLVQMHWStanyAPWQE--VGLLDGLADLYEQGLVKG 162
Cdd:cd19131 62 PREELFITTKL------WNsdqgYDSTLRAFDESLRKLGLDyVDLYLIHWP----VPAQDkyVETWKALIELKKEGRVKS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 163 VGLSNYGTKRLQRVhqkFAERGVPIKTLQVQysllsTYP-VTELGLKDVCDELGIKLIAYSPLAlgiltgkysekgpfpr 241
Cdd:cd19131 132 IGVSNFTIEHLQRL---IDETGVVPVVNQIE-----LHPrFQQRELRAFHAKHGIQTESWSPLG---------------- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 242 gvRGLLLRQLLpgvrsllqcLQDVAQSRNKTMSQVALNWCIAKGTMPIPgaRSVKQA--QENIGALGWQLNS---GEIAE 316
Cdd:cd19131 188 --QGGLLSDPV---------IGEIAEKHGKTPAQVVIRWHLQNGLVVIP--KSVTPSriAENFDVFDFELDAddmQAIAG 254
|
..
gi 17135278 317 LD 318
Cdd:cd19131 255 LD 256
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
42-305 |
1.94e-15 |
|
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: 74.87 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 42 DAQLQAVFNLCVSNGVTLFDTGDSYGTgrlngrSELLLGKFSQEYQGVNqenicIATKLAAYPW--RWTRQSMINACKSS 119
Cdd:cd19097 25 EKEAKKILEYALKAGINTLDTAPAYGD------SEKVLGKFLKRLDKFK-----IITKLPPLKEdkKEDEAAIEASVEAS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 120 AQRLGRN-VDLVQMHWSTANYAPWQEVglLDGLADLYEQGLVKGVGLSNYGTKRLQRVHQKFaergvPIKTLQVQYSLLS 198
Cdd:cd19097 94 LKRLKVDsLDGLLLHNPDDLLKHGGKL--VEALLELKKEGLIRKIGVSVYSPEELEKALESF-----KIDIIQLPFNILD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 199 TYPVTElglkDVCDEL---GIKLIAYSPLALGILTGKYSEKGPFPRGVRGLLLRqllpgvrsllqcLQDVAQSRNKTMSQ 275
Cdd:cd19097 167 QRFLKS----GLLAKLkkkGIEIHARSVFLQGLLLMEPDKLPAKFAPAKPLLKK------------LHELAKKLGLSPLE 230
|
250 260 270
....*....|....*....|....*....|....*..
gi 17135278 276 VALNWCIAkgtmpIP-------GARSVKQAQENIGAL 305
Cdd:cd19097 231 LALGFVLS-----LPeidkivvGVDSLEQLKEIIAAF 262
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
16-322 |
2.81e-15 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 75.63 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 16 ELSLPGMGCgtwawgnqllWGYNESMDAQLQAVFNLCVSNGVTLFDTGDSYGTgrlngrSELLLGKFSQEYqgvnQENIC 95
Cdd:COG1453 12 EVSVLGFGG----------MRLPRKDEEEAEALIRRAIDNGINYIDTARGYGD------SEEFLGKALKGP----RDKVI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 96 IATKLAayPWRWTRQSMINACKSSAQRLGRN-VDLVQMHW-STANYAPW--QEVGLLDGLADLYEQGLVKGVGLSNYGtk 171
Cdd:COG1453 72 LATKLP--PWVRDPEDMRKDLEESLKRLQTDyIDLYLIHGlNTEEDLEKvlKPGGALEALEKAKAEGKIRHIGFSTHG-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 172 RLQrVHQKFAERGvPIKTLQVQYSLLSTYPVTELGLKDVCDELGIKLIAYSPLalgiltgkysekgpfprgvRGLLLRQL 251
Cdd:COG1453 148 SLE-VIKEAIDTG-DFDFVQLQYNYLDQDNQAGEEALEAAAEKGIGVIIMKPL-------------------KGGRLANP 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17135278 252 LPGVRSLLqclqdvaqSRNKTMSQVALNWCIAKG--TMPIPGARSVKQAQENIGAL--GWQLNSGEIAELDKAAA 322
Cdd:COG1453 207 PEKLVELL--------CPPLSPAEWALRFLLSHPevTTVLSGMSTPEQLDENLKTAdnLEPLTEEELAILERLAE 273
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
17-305 |
3.22e-15 |
|
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: 75.08 E-value: 3.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 17 LSLPGMGCGTW-AWGNQLlwgynesMDAQLQAVFNLCVSNGVTLFDTGDSYGTGRlngrSELLLGKFSQEyQGVNQENIC 95
Cdd:cd19159 11 LRVSCLGLGTWvTFGGQI-------SDEVAERLMTIAYESGVNLFDTAEVYAAGK----AEVILGSIIKK-KGWRRSSLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 96 IATKL-----AAYPWRWTRQSMINACKSSAQRLG-RNVDLVQMHWSTANyAPWQEVglLDGLADLYEQGLVKGVGLSNYG 169
Cdd:cd19159 79 ITTKLywggkAETERGLSRKHIIEGLKGSLQRLQlEYVDVVFANRPDSN-TPMEEI--VRAMTHVINQGMAMYWGTSRWS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 170 TKRLQR---VHQKFaeRGVPIKTLQVQYSLLSTYPVtELGLKDVCDELGIKLIAYSPLALGILTGKYsEKGpFPRGVRGL 246
Cdd:cd19159 156 AMEIMEaysVARQF--NMIPPVCEQAEYHLFQREKV-EVQLPELYHKIGVGAMTWSPLACGIISGKY-GNG-VPESSRAS 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17135278 247 L-----LRQLLPG-----VRSLLQCLQDVAQSRNKTMSQVALNWCIAKGTMP--IPGARSVKQAQENIGAL 305
Cdd:cd19159 231 LkcyqwLKERIVSeegrkQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSsvLLGSSTPEQLIENLGAI 301
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
10-318 |
1.01e-14 |
|
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are founding members of aldo-keto reductase family 3 member A1 (AKR3A1) and A2 (AKR3A2), respectively. Gcy1p, also called galactose-inducible crystallin-like protein 1, is a glycerol dehydrogenase involved in glycerol catabolism under microaerobic conditions. It has mRNA binding activity. Ypr1p acts as a 2-methylbutyraldehyde reductase that displays high specific activity towards 2-methylbutyraldehyde, as well as other aldehydes such as hexanal.
Pssm-ID: 381343 [Multi-domain] Cd Length: 284 Bit Score: 73.30 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 10 TMQIHQELSLPGMGCGTWawgnqllwgynESMDAQLQAVFNLCVSNGVTLFDTGDSYGTGRLNGRSElllgKFSqeyqGV 89
Cdd:cd19117 5 TFKLNTGAEIPAVGLGTW-----------QSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGI----KDS----GV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 90 NQENICIATKLAAypwrwTRQSMINAC-KSSAQRLGRN-VDLVQMHW------------------STANYAPWQEVGLLD 149
Cdd:cd19117 66 PREEIFITTKLWC-----TWHRRVEEAlDQSLKKLGLDyVDLYLMHWpvpldpdgndflfkkddgTKDHEPDWDFIKTWE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 150 GLADLYEQGLVKGVGLSNYGTKRLQRVHQKFAERGVPiKTLQVQYSLLSTYPvtelGLKDVCDELGIKLIAYSPLAlgil 229
Cdd:cd19117 141 LMQKLPATGKVKAIGVSNFSIKNLEKLLASPSAKIVP-AVNQIELHPLLPQP----KLVDFCKSKGIHATAYSPLG---- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 230 tgkySEKGPfprgvrglLLRqllpgvrslLQCLQDVAQSRNKTMSQVALNWCIAKGTMPIPGARSVKQAQENIGAlgWQL 309
Cdd:cd19117 212 ----STNAP--------LLK---------EPVIIKIAKKHGKTPAQVIISWGLQRGYSVLPKSVTPSRIESNFKL--FTL 268
|
....*....
gi 17135278 310 NSGEIAELD 318
Cdd:cd19117 269 SDEEFKEID 277
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
20-305 |
2.02e-14 |
|
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: 72.64 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 20 PGMGCGTWAWGNqllwGYNESMDAQLQAVFNLCVSNGVTLFDTGDSYGtgrlNGRSELLLGKFSQEYqgvNQENICIATK 99
Cdd:cd19152 1 PKLGFGTAPLGN----LYEAVSDEEAKATLVAAWDLGIRYFDTAPWYG----AGLSEERLGAALREL---GREDYVISTK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 100 L-----------------------AAYPWRWTRQSMINACKSSAQRLGRN-VDLVQMH---------WSTANYAPWQEVG 146
Cdd:cd19152 70 VgrllvplqeveptfepgfwnplpFDAVFDYSYDGILRSIEDSLQRLGLSrIDLLSIHdpdedlagaESDEHFAQAIKGA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 147 LLdGLADLYEQGLVKGVGLsnyGTKRLQrVHQKFAERGVP-IKTLQVQYSLLSTYPVTElgLKDVCDELGIKLIAYSPLA 225
Cdd:cd19152 150 FR-ALEELREEGVIKAIGL---GVNDWE-VILRILEEADLdWVMLAGRYTLLDHSAARE--LLPECEKRGVKVVNAGPFN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 226 LGILTGkysekGPFPRGVRGlllRQLLPGVRSLLQCLQDVAQSRNKTMSQVALNWCIAkgtmP------IPGARSVKQAQ 299
Cdd:cd19152 223 SGFLAG-----GDNFDYYEY---GPAPPELIARRDRIEALCEQHGVSLAAAALQFALA----PpavasvAPGASSPERVE 290
|
....*.
gi 17135278 300 ENIGAL 305
Cdd:cd19152 291 ENVALL 296
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
56-315 |
2.58e-14 |
|
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: 72.20 E-value: 2.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 56 GVTLFDTGDSYGtgrlNGRSELLLGKFsqeYQGVNQENICIATKLAAYPWRW----------TRQSMinacKSSAQRLGR 125
Cdd:cd19163 46 GINYIDTAPWYG----QGRSETVLGKA---LKGIPRDSYYLATKVGRYGLDPdkmfdfsaerITKSV----EESLKRLGL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 126 N-VDLVQMHwsTANYAPWQEVGL---LDGLADLYEQGLVKGVGLSNYGTKRLQRVhqkfAERG-VPIKTLQV--QYSLLS 198
Cdd:cd19163 115 DyIDIIQVH--DIEFAPSLDQILnetLPALQKLKEEGKVRFIGITGYPLDVLKEV----LERSpVKIDTVLSycHYTLND 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 199 TypvTELGLKDVCDELGIKLIAYSPLALGILTgkysEKGPFPrgvrgllLRQLLPGVRSLLQCLQDVAQSRNKTMSQVAL 278
Cdd:cd19163 189 T---SLLELLPFFKEKGVGVINASPLSMGLLT----ERGPPD-------WHPASPEIKEACAKAAAYCKSRGVDISKLAL 254
|
250 260 270
....*....|....*....|....*....|....*....
gi 17135278 279 NWCIAKGTMP--IPGARSVKQAQENIGALGWQLNSGEIA 315
Cdd:cd19163 255 QFALSNPDIAttLVGTASPENLRKNLEAAEEPLDAHLLA 293
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-232 |
2.59e-14 |
|
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: 71.36 E-value: 2.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 16 ELSLPGMGCGTWAWGNQllwgynesmdAQLQAVFNLCVSNGVTLFDTGDSYgtgrlnGRSELLLGKFSQEYqgvnQENIC 95
Cdd:cd19100 10 KVSRLGFGGGPLGRLSQ----------EEAAAIIRRALDLGINYFDTAPSY------GDSEEKIGKALKGR----RDKVF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 96 IATKLAAypwrWTRQSMINACKSSAQRLGRN-VDLVQMHwsTANYAPWQEV-----GLLDGLADLYEQGLVKGVGLSNYG 169
Cdd:cd19100 70 LATKTGA----RDYEGAKRDLERSLKRLGTDyIDLYQLH--AVDTEEDLDQvfgpgGALEALLEAKEEGKIRFIGISGHS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17135278 170 TKrlqrVHQKFAERGvPIKTLQVQYSLLST-YPVTELGLKDVCDELGIKLIAYSPLALGILTGK 232
Cdd:cd19100 144 PE----VLLRALETG-EFDVVLFPINPAGDhIDSFREELLPLAREKGVGVIAMKVLAGGRLLSG 202
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
10-318 |
5.03e-14 |
|
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 70.88 E-value: 5.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 10 TMQIHQELSLPGMGCGTWAWGNQllwgyNESMDAQLQAVfnlcvSNGVTLFDTGDSYGtgrlngrSELLLGKFSQEyQGV 89
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEEG-----SEVVNAVKTAL-----KNGYRSIDTAAIYG-------NEEGVGKGIKE-SGI 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 90 NQENICIATKLaaypwrWTR----QSMINACKSSAQRLGRN-VDLVQMHW--STANYAPWQevglldGLADLYEQGLVKG 162
Cdd:cd19157 63 PREELFITSKV------WNAdqgyDSTLKAFEASLERLGLDyLDLYLIHWpvKGKYKETWK------ALEKLYKDGRVRA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 163 VGLSNYGTKRLQRVHQKfAERgVPIKTlQVQYsllstYP-VTELGLKDVCDELGIKLIAYSPLALGiltgkysekgpfpr 241
Cdd:cd19157 131 IGVSNFQVHHLEDLLAD-AEI-VPMVN-QVEF-----HPrLTQKELRDYCKKQGIQLEAWSPLMQG-------------- 188
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17135278 242 gvrglllrQLLPgvrslLQCLQDVAQSRNKTMSQVALNWCIAKGTMPIPgaRSVKQAQ--ENIGALGWQLNSGEIAELD 318
Cdd:cd19157 189 --------QLLD-----NPVLKEIAEKYNKSVAQVILRWDLQNGVVTIP--KSIKEHRiiENADVFDFELSQEDMDKID 252
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
17-319 |
6.95e-14 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381380 [Multi-domain] Cd Length: 303 Bit Score: 70.90 E-value: 6.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 17 LSLPGMGCGTWawgnqllwgynESMDAQLQAVFNLCVSNGVTLFDTGDSYgtgrlngRSELLLGKFSQEY--QGV-NQEN 93
Cdd:cd19154 10 VKMPLIGLGTW-----------QSKGAEGITAVRTALKAGYRLIDTAFLY-------QNEEAIGEALAELleEGVvKRED 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 94 ICIATKLAayPWRWTRQSMINACKSSAQRLGRN-VDLVQMH--WST----ANYAPWQ-------EVGLLD---GLADLYE 156
Cdd:cd19154 72 LFITTKLW--THEHAPEDVEEALRESLKKLQLEyVDLYLIHapAAFkddeGESGTMEngmsihdAVDVEDvwrGMEKVYD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 157 QGLVKGVGLSNYGTKRLQRVhqkFAERGVPIKTLQVQYSLLstYPVTElgLKDVCDELGIKLIAYSPLalgiltgkysek 236
Cdd:cd19154 150 EGLTKAIGVSNFNNDQIQRI---LDNARVKPHNNQVECHLY--FPQKE--LVEFCKKHNISVTSYATL------------ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 237 gpfprGVRGLLLRQLLPGVRSLLQCLQD-----VAQSRNKTMSQVALNWCIAKGTMPIPGARSVKQAQENIGALGWQLNS 311
Cdd:cd19154 211 -----GSPGRANFTKSTGVSPAPNLLQDpivkaIAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSE 285
|
....*...
gi 17135278 312 GEIAELDK 319
Cdd:cd19154 286 EDMATLEE 293
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
127-319 |
2.57e-13 |
|
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase (ALR) from Hordeum vulgare (AKR4C1), Bromus inermis (AKR4C2), Avena fatua (AKR4C3), and Xerophyta viscosa (AKR4C4), two aldose reductases, DpAR1 (AKR4C5) and DpAR2(AKR4C6), from Digitalis purpurea, aldehyde reductase from Zea mays (AKR4C7), four aldo-keto reductases from Arabidopsis thaliana (AKR4C8-11), and another three aldo-keto reductases from Aloe arborescens (AKR4C12) and Oryza sativa (AKR4C14/15). ALR (EC 1.1.1.21), also called AR, aldehyde reductase, or polyol dehydrogenase (NADP(+)), is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. Both DpAR1 and DpAR2 reduce the ketone group of steroid structures. They may be involved in plant steroid metabolism in general and in cardenolide biosynthesis in particular. Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops.
Pssm-ID: 381351 [Multi-domain] Cd Length: 287 Bit Score: 69.30 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 127 VDLVQMHW-----------STANYAPWQEVGLLDGLADLYEQGLVKGVGLSNYGTKRLQRVhqkFAERGVPIKTLQVQys 195
Cdd:cd19125 103 LDLYLIHWpvrlkkgahmpEPEEVLPPDIPSTWKAMEKLVDSGKVRAIGVSNFSVKKLEDL---LAVARVPPAVNQVE-- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 196 llsTYPV-TELGLKDVCDELGIKLIAYSPLAlgiltgkysekGPFPRGVRGLLLRQLLpgvrsllqcLQDVAQSRNKTMS 274
Cdd:cd19125 178 ---CHPGwQQDKLHEFCKSKGIHLSAYSPLG-----------SPGTTWVKKNVLKDPI---------VTKVAEKLGKTPA 234
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17135278 275 QVALNWCIAKGTMPIPgaRSVKQA--QENIGALGWQLNSGEIAELDK 319
Cdd:cd19125 235 QVALRWGLQRGTSVLP--KSTNEEriKENIDVFDWSIPEEDFAKFSS 279
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
53-318 |
3.30e-13 |
|
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: 68.59 E-value: 3.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 53 VSNGVTLFDTGDSYGTGRLNGRSelllgkfsQEYQGVNQENICIATKLaaypW--RWTRQSMINACKSSAQRLGRN-VDL 129
Cdd:cd19127 32 LADGYRLIDTAAAYGNEREVGEG--------IRRSGVDRSDIFVTTKL----WisDYGYDKALRGFDASLRRLGLDyVDL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 130 VQMHWSTANY-----APWQevglldGLADLYEQGLVKGVGLSNYGTKRLQRVhqkFAERGVPIKTLQVQyslLSTYpVTE 204
Cdd:cd19127 100 YLLHWPVPNDfdrtiQAYK------ALEKLLAEGRVRAIGVSNFTPEHLERL---IDATTVVPAVNQVE---LHPY-FSQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 205 LGLKDVCDELGIKLIAYSPLAlGILTgkYSEKGPfprgvrglllrqllPGVRSLLQ--CLQDVAQSRNKTMSQVALNWCI 282
Cdd:cd19127 167 KDLRAFHRRLGIVTQAWSPIG-GVMR--YGASGP--------------TGPGDVLQdpTITGLAEKYGKTPAQIVLRWHL 229
|
250 260 270
....*....|....*....|....*....|....*...
gi 17135278 283 AKGTMPIPgaRSVKQAQ--ENIGALGWQLNSGEIAELD 318
Cdd:cd19127 230 QNGVSAIP--KSVHPERiaENIDIFDFALSAEDMAAID 265
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
10-318 |
5.25e-13 |
|
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: 67.96 E-value: 5.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 10 TMQIHQELSLPGMGCGTWawgnqllwgynESMDAQLQAVFNLCVSNGVTLFDTGDSYGTGRLNGRSellLGKfsqeyQGV 89
Cdd:cd19134 2 TVTLNDDNTMPVIGLGVG-----------ELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRA---IAA-----SGI 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 90 NQENICIATKLAAYPWRWTRQsmINACKSSAQRLGRN-VDLVQMHWSTANYAPWqeVGLLDGLADLYEQGLVKGVGLSNY 168
Cdd:cd19134 63 PRGELFVTTKLATPDQGFTAS--QAACRASLERLGLDyVDLYLIHWPAGREGKY--VDSWGGLMKLREEGLARSIGVSNF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 169 GTKRLQRVhqkFAERGVPIKTLQVQYSLLstypVTELGLKDVCDELGIKLIAYSPLALGILTGKysekgpfprgvrglll 248
Cdd:cd19134 139 TAEHLENL---IDLTFFTPAVNQIELHPL----LNQAELRKVNAQHGIVTQAYSPLGVGRLLDN---------------- 195
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 249 rqllPGVRSLlqclqdvAQSRNKTMSQVALNWCIAKGTMPIPGARSVKQAQENIGALGWQLNSGEIAELD 318
Cdd:cd19134 196 ----PAVTAI-------AAAHGRTPAQVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDALD 254
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
18-305 |
1.80e-12 |
|
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: 66.43 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 18 SLPGMGCGTWawgnQLLWGYNESMDaQLQAVFNLCVSNGVTLFDTGDSYGtgrlNGRSELLLGK-FSQEYqgvnQENICI 96
Cdd:cd19096 1 SVLGFGTMRL----PESDDDSIDEE-KAIEMIRYAIDAGINYFDTAYGYG----GGKSEEILGEaLKEGP----REKFYL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 97 ATKLAayPWR-WTRQSMINACKSSAQRLGRN-VDLVQMHW-STANYAPW-QEVGLLDGLADLYEQGLVKGVGLSNYGTKR 172
Cdd:cd19096 68 ATKLP--PWSvKSAEDFRRILEESLKRLGVDyIDFYLLHGlNSPEWLEKaRKGGLLEFLEKAKKEGLIRHIGFSFHDSPE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 173 LqrvhqkfaergvpIKTL---------QVQYSLLSTYPVTELGLKDVCDELGIKLIAYSPLalgiltgkyseKGpfprgv 243
Cdd:cd19096 146 L-------------LKEIldsydfdfvQLQYNYLDQENQAGRPGIEYAAKKGMGVIIMEPL-----------KG------ 195
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17135278 244 rGLLLRqlLPGVRSLLQClqdvaqSRNKTMSQVALNWCIAKG--TMPIPGARSVKQAQENIGAL 305
Cdd:cd19096 196 -GGLAN--NPPEALAILC------GAPLSPAEWALRFLLSHPevTTVLSGMSTPEQLDENIAAA 250
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
22-323 |
3.02e-12 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 66.15 E-value: 3.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 22 MGCGTWAWGNQLLWGYNESMDAQLqAVFNLCVSNGVTLFDTGDSYGTGRLNG--RSELllgkfsQEYQgvnqENICIATK 99
Cdd:PRK10376 20 LGYGAMQLAGPGVFGPPKDRDAAI-AVLREAVALGVNHIDTSDFYGPHVTNQliREAL------HPYP----DDLTIVTK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 100 L-------AAYPWRWTRQSMINACKSSAQRLGRNV-DLVQMHWSTANYAPwQEVGL---LDGLADLYEQGLVKGVGLSNY 168
Cdd:PRK10376 89 VgarrgedGSWLPAFSPAELRRAVHDNLRNLGLDVlDVVNLRLMGDGHGP-AEGSIeepLTVLAELQRQGLVRHIGLSNV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 169 GTKRLQRvhqkfAERGVPIKTLQVQYSLlstypvTELGLKDVCDELGIKLIAYSPLalgiltgkysekgpFPRGvrGLll 248
Cdd:PRK10376 168 TPTQVAE-----ARKIAEIVCVQNHYNL------AHRADDALIDALARDGIAYVPF--------------FPLG--GF-- 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17135278 249 rqllpgvrSLLQC--LQDVAQSRNKTMSQVALNWCI--AKGTMPIPGARSVKQAQENIGALGWQLNSGEIAELDKAAAS 323
Cdd:PRK10376 219 --------TPLQSstLSDVAASLGATPMQVALAWLLqrSPNILLIPGTSSVAHLRENLAAAELVLSEEVLAELDGIARE 289
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
89-331 |
6.80e-12 |
|
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: 65.20 E-value: 6.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 89 VNQENICIATKLaaypWRWTRQSMINACKSSAQRLGRN-VDLVQMHWSTANY--------APWQEVGLLD---------- 149
Cdd:cd19112 66 VKREDLFITTKL----WNSDHGHVIEACKDSLKKLQLDyLDLYLVHFPVATKhtgvgttgSALGEDGVLDidvtislett 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 150 --GLADLYEQGLVKGVGLSNYgtkRLQRVHQKFAERGVPIKTLQVQysllsTYPVTEL-GLKDVCDELGIKLIAYSPLAl 226
Cdd:cd19112 142 whAMEKLVSAGLVRSIGISNY---DIFLTRDCLAYSKIKPAVNQIE-----THPYFQRdSLVKFCQKHGISVTAHTPLG- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 227 giltGKYSEKGPFprgvrglllrqllpGVRSLLQ--CLQDVAQSRNKTMSQVALNWCIAKGTMPIPGARSVKQAQENIGA 304
Cdd:cd19112 213 ----GAAANAEWF--------------GSVSPLDdpVLKDLAKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDV 274
|
250 260
....*....|....*....|....*..
gi 17135278 305 LGWQLNSGEIaeldKAAASSDKKMVQN 331
Cdd:cd19112 275 FDFQLSKEDM----KLIKSLDRKYRTN 297
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
19-328 |
2.31e-11 |
|
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: 63.29 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 19 LPGMGCGTWawgnqllwgynESMDAQLQAVFNLCVSNGVTLFDTGDSYGtgrlngrSELLLGKFSQEY--QG-VNQENIC 95
Cdd:cd19111 4 MPVIGLGTY-----------QSPPEEVRAAVDYALFVGYRHIDTALSYQ-------NEKAIGEALKWWlkNGkLKREEVF 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 96 IATKLAAYPWRwtRQSMINACKSSAQRLGRN-VDLVQMHWSTANYAPWQEVGLLDGLAD----------LYEQGLVKGVG 164
Cdd:cd19111 66 ITTKLPPVYLE--FKDTEKSLEKSLENLKLPyVDLYLIHHPCGFVNKKDKGERELASSDvtsvwrameaLVSEGKVKSIG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 165 LSNYGTKRLQRVhqkFAERGVPIKTLQVQyslLSTYpVTELGLKDVCDELGIKLIAYSPLALGILTGKYSEkGPFPrgvr 244
Cdd:cd19111 144 LSNFNPRQINKI---LAYAKVKPSNLQLE---CHAY-LQQRELRKFCNKKNIVVTAYAPLGSPGRANQSLW-PDQP---- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 245 glllrqllpgvrSLLQ---CLQdVAQSRNKTMSQVALNWCIAKGTMPIPGARSVKQAQENIGALGWQLNSGEIAELDkaa 321
Cdd:cd19111 212 ------------DLLEdptVLA-IAKELDKTPAQVLLRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLK--- 275
|
....*..
gi 17135278 322 aSSDKKM 328
Cdd:cd19111 276 -TLDRNM 281
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
19-318 |
2.37e-11 |
|
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381381 [Multi-domain] Cd Length: 307 Bit Score: 63.70 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 19 LPGMGCGTWawgnqllwgynESMDAQLQAVFNLCVSNGVTLFDTGDSYgtgrlngRSELLLGKFSQEY---QGVNQENIC 95
Cdd:cd19155 12 MPVVGLGTW-----------QSSPEEIETAVDTALEAGYRHIDTAYVY-------RNEAAIGNVLKKWidsGKVKREELF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 96 IATKLaayPWRWTRQSMINAC-KSSAQRLGRN-VDLVQMHWS-TANY--------APWQEV------GLLD---GLADLY 155
Cdd:cd19155 74 IVTKL---PPGGNRREKVEKFlLKSLEKLQLDyVDLYLIHFPvGSLSkeddsgklDPTGEHkqdyttDLLDiwkAMEAQV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 156 EQGLVKGVGLSNYGTKRLQRVHQKFAERGVpikTLQVQyslLSTYpVTELGLKDVCDELGIKLIAYSPLALGILTGKYSE 235
Cdd:cd19155 151 DQGLTRSIGLSNFNREQMARILKNARIKPA---NLQVE---LHVY-LQQKDLVDFCSTHSITVTAYAPLGSPGAAHFSPG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 236 KGPFPRGVRGLLLrqlLPGVRSllqclqdVAQSRNKTMSQVALNWCIAKGTMPIPGARSVKQAQENIGALGWQLNSGEIA 315
Cdd:cd19155 224 TGSPSGSSPDLLQ---DPVVKA-------IAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMA 293
|
...
gi 17135278 316 ELD 318
Cdd:cd19155 294 KLS 296
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
19-319 |
6.94e-11 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 62.01 E-value: 6.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 19 LPGMGCGTWAWGNQllwgynESMDAQLQAVfnlcvSNGVTLFDTGDSYgtgrlngRSELLLGKFSQEyQGVNQENICIAT 98
Cdd:PRK11565 15 MPQLGLGVWQASNE------EVITAIHKAL-----EVGYRSIDTAAIY-------KNEEGVGKALKE-ASVAREELFITT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 99 KLaaypWRWTRQSMINACKSSAQRLGRN-VDLVQMHWStanyAPWQE--VGLLDGLADLYEQGLVKGVGLSNYGTKRLQR 175
Cdd:PRK11565 76 KL----WNDDHKRPREALEESLKKLQLDyVDLYLMHWP----VPAIDhyVEAWKGMIELQKEGLIKSIGVCNFQIHHLQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 176 VhqkFAERGVPIKTLQV------QYSLLSTYPVTElglkdvcdelGIKLIAYSPLALGiltgkysEKGPFPRGVrglllr 249
Cdd:PRK11565 148 L---IDETGVTPVINQIelhplmQQRQLHAWNATH----------KIQTESWSPLAQG-------GKGVFDQKV------ 201
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17135278 250 qllpgvrsllqcLQDVAQSRNKTMSQVALNWCIAKGTMPIPGARSVKQAQENIGALGWQLNS---GEIAELDK 319
Cdd:PRK11565 202 ------------IRDLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRLDKdelGEIAKLDQ 262
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
88-319 |
1.77e-10 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 60.81 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 88 GVNQENICIATKLaaypwrWT----RQSMINACKSSAQRLGRN-VDLVQMHWStanyAPWQEVGL---LDGLADLYEQGL 159
Cdd:PRK11172 53 GVPRDELFITTKI------WIdnlaKDKLIPSLKESLQKLRTDyVDLTLIHWP----SPNDEVSVeefMQALLEAKKQGL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 160 VKGVGLSNYGTKRLQrvhQKFAERGV-PIKTLQVQyslLSTYpVTELGLKDVCDELGIKLIAYSPLALG-ILtgkyseKG 237
Cdd:PRK11172 123 TREIGISNFTIALMK---QAIAAVGAeNIATNQIE---LSPY-LQNRKVVAFAKEHGIHVTSYMTLAYGkVL------KD 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 238 PFprgvrglllrqllpgvrsllqcLQDVAQSRNKTMSQVALNWCIAKGTMPIPGARSVKQAQENIGALGWQLNS---GEI 314
Cdd:PRK11172 190 PV----------------------IARIAAKHNATPAQVILAWAMQLGYSVIPSSTKRENLASNLLAQDLQLDAedmAAI 247
|
....*
gi 17135278 315 AELDK 319
Cdd:PRK11172 248 AALDR 252
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
55-318 |
2.02e-10 |
|
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: 60.28 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 55 NGVTLFDTGDSYGtgrlngrSELLLGKFSQEyQGVNQENICIATKLaaypwrWTRQSMINACKS----SAQRLGRN-VDL 129
Cdd:cd19133 35 AGYRLIDTAAAYG-------NEEAVGRAIKK-SGIPREELFITTKL------WIQDAGYEKAKKaferSLKRLGLDyLDL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 130 VQMHWSTAN-YAPWQevglldGLADLYEQGLVKGVGLSNYGTKRLQRvHQKFAErgVPIKTLQVQysllsTYPV-TELGL 207
Cdd:cd19133 101 YLIHQPFGDvYGAWR------AMEELYKEGKIRAIGVSNFYPDRLVD-LILHNE--VKPAVNQIE-----THPFnQQIEA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 208 KDVCDELGIKLIAYSPLAlgiltgkysekgpfpRGVRGLLLRQLLpgvrsllqclQDVAQSRNKTMSQVALNWCIAKGTM 287
Cdd:cd19133 167 VEFLKKYGVQIEAWGPFA---------------EGRNNLFENPVL----------TEIAEKYGKSVAQVILRWLIQRGIV 221
|
250 260 270
....*....|....*....|....*....|....*.
gi 17135278 288 PIPgaRSVKQA--QENIGALGWQLNSGE---IAELD 318
Cdd:cd19133 222 VIP--KSVRPEriAENFDIFDFELSDEDmeaIAALD 255
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
19-318 |
2.57e-10 |
|
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: 60.14 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 19 LPGMGCGTWawgnQLLWGyNESMDAQLQAVfnlcvSNGVTLFDTGDSYgtgrlngRSELLLGKFSQEyQGVNQENICIAT 98
Cdd:cd19126 9 MPWLGLGVF----QTPDG-DETERAVQTAL-----ENGYRSIDTAAIY-------KNEEGVGEAIRE-SGVPREELFVTT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 99 KLAAYPWRWTRQSmiNACKSSAQRLGRN-VDLVQMHWSTANYapWQEVglLDGLADLYEQGLVKGVGLSNYGTKRLQRVh 177
Cdd:cd19126 71 KLWNDDQRARRTE--DAFQESLDRLGLDyVDLYLIHWPGKDK--FIDT--WKALEKLYASGKVKAIGVSNFQEHHLEEL- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 178 qkFAERGVPIKTLQVQYSLLSTYPvtelGLKDVCDELGIKLIAYSPLALGILTgkySEKgpfprgvrglllrqllpgvrs 257
Cdd:cd19126 144 --LAHADVVPAVNQVEFHPYLTQK----ELRGYCKSKGIVVEAWSPLGQGGLL---SNP--------------------- 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17135278 258 llqCLQDVAQSRNKTMSQVALNWCIAKGTMPIPGARSVKQAQENIGALGWQLNSGEIAELD 318
Cdd:cd19126 194 ---VLAAIGEKYGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAID 251
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
19-317 |
4.77e-10 |
|
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) from Mus musculus (liver, AKR1E1) and Homo sapiens (AKR1E2). 1,5-anhydro-D-fructose reductase), also called AF reductase, or aldo-keto reductase family 1 member C-like protein 2 (AKR1CL2), catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. AKR1E2 is a testis aldo-keto reductase (tAKR), which is also known as testis-specific protein (TSP), or LoopADR.
Pssm-ID: 381336 [Multi-domain] Cd Length: 301 Bit Score: 59.59 E-value: 4.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 19 LPGMGCGTWawgnqllwgynESMDAQLQAVFNLCVSNGVTLFDTGDSYgtgrlNGRSELLLGKFSQEYQG-VNQENICIA 97
Cdd:cd19110 4 IPAVGLGTW-----------KASPGEVTEAVKVAIDAGYRHFDCAYLY-----HNESEVGAGIREKIKEGvVRREDLFIV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 98 TKLaaypwrWT---RQSMI-NACKSSAQRLGRN-VDLVQMHWSTANYAPWQEVGL-------------LD---GLADLYE 156
Cdd:cd19110 68 SKL------WCtchKKSLVkTACTRSLKALKLNyLDLYLIHWPMGFKPGEPDLPLdrsgmvipsdtdfLDtweAMEDLVI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 157 QGLVKGVGLSNYGTKRLQRVHQKFAERGVPIkTLQVQysllsTYP-VTELGLKDVCDELGIKLIAYSPLalgiltGKYSE 235
Cdd:cd19110 142 EGLVKNIGVSNFNHEQLERLLNKPGLRVKPV-TNQIE-----CHPyLTQKKLISFCQSRNVSVTAYRPL------GGSCE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 236 KGPfprgvrglLLRQLLpgvrsllqcLQDVAQSRNKTMSQVALNWCIAKGTMPIPGARSVKQAQENIGALGWQLNSGEIA 315
Cdd:cd19110 210 GVD--------LIDDPV---------IQRIAKKHGKSPAQILIRFQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMD 272
|
..
gi 17135278 316 EL 317
Cdd:cd19110 273 NL 274
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
21-305 |
5.19e-10 |
|
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: 59.29 E-value: 5.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 21 GMGCGTwawgnqlLWGYNESMDAQLQAVFNLCVSNGVTLFDTGDSYGtgrlNGRSELLLGKFSQEYQGvnqENICIATKL 100
Cdd:cd19162 4 GLGAAS-------LGNLARAGEDEAAATLDAAWDAGIRYFDTAPLYG----LGLSERRLGAALARHPR---AEYVVSTKV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 101 AAYP--------------WRWTRQSMINACKSSAQRLGRN-VDLV-----QMHWSTAnyapwqEVGLLDGLADLYEQGLV 160
Cdd:cd19162 70 GRLLepgaagrpagadrrFDFSADGIRRSIEASLERLGLDrLDLVflhdpDRHLLQA------LTDAFPALEELRAEGVV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 161 KGVGLSNYGTKRLQRvhqkFAERGVP-IKTLQVQYSLLSTYPVTElgLKDVCDELGIKLIAYSPLALGILTGKYSEKGPF 239
Cdd:cd19162 144 GAIGVGVTDWAALLR----AARRADVdVVMVAGRYTLLDRRAATE--LLPLCAAKGVAVVAAGVFNSGILATDDPAGDRY 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17135278 240 prgvrglLLRQLLPGVRSLLQCLQDVAQSRNKTMSQVALNWCI---AKGTMPIpGARSVKQAQENIGAL 305
Cdd:cd19162 218 -------DYRPATPEVLARARRLAAVCRRYGVPLPAAALQFPLrhpAVASVVV-GAASPAELRDNLALL 278
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
21-326 |
5.45e-10 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 59.59 E-value: 5.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 21 GMGCGtwawGNQLLWGyNESMDAQLQAVfNLCVSNGVTLFDTGDSYGtgrlNGRSELLLGKFSQEyqgvNQENICIATK- 99
Cdd:cd19104 16 TFGGG----GIGGLMG-RTTREEQIAAV-RRALDLGINFFDTAPSYG----DGKSEENLGRALKG----LPAGPYITTKv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 100 -LAAYPWRWTRQSMINACKSSAQRLGRN-VDLVQMH--------WSTANYAPWQEV----GLLDGLADLYEQGLVKGVGL 165
Cdd:cd19104 82 rLDPDDLGDIGGQIERSVEKSLKRLKRDsVDLLQLHnrigderdKPVGGTLSTTDVlglgGVADAFERLRSEGKIRFIGI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 166 SNYG-TKRLQRV--HQKFAergvpikTLQVQYSLL------STYPVTEL----GLKDVCDELGIKLIAYSPLALGILTGK 232
Cdd:cd19104 162 TGLGnPPAIRELldSGKFD-------AVQVYYNLLnpsaaeARPRGWSAqdygGIIDAAAEHGVGVMGIRVLAAGALTTS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 233 ySEKGPFPRGVRGLLLRQllpGVRSlLQCLQDVAQSRNKTMSQVALNWCIAkgtmpIPGARSVkqaqenIGALgwqlnsG 312
Cdd:cd19104 235 -LDRGREAPPTSDSDVAI---DFRR-AAAFRALAREWGETLAQLAHRFALS-----NPGVSTV------LVGV------K 292
|
330
....*....|....
gi 17135278 313 EIAELDKAAASSDK 326
Cdd:cd19104 293 NREELEEAVAAEAA 306
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
60-301 |
5.55e-10 |
|
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family.
Pssm-ID: 381355 [Multi-domain] Cd Length: 295 Bit Score: 59.39 E-value: 5.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 60 FDTGDSYgtgrlngRSELLLGKFSQEY---QGVNQENICIATKLAAYPWRWTRqsMINACKSSAQRLGRN-VDLVQMHWS 135
Cdd:cd19129 36 FDCAERY-------RNEAEVGEAMQEVfkaGKIRREDLFVTTKLWNTNHRPER--VKPAFEASLKRLQLDyLDLYLIHTP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 136 TAnYAPWQE---------------VGLLD---GLADLYEQGLVKGVGLSNYGTKRLQRVHQkfAERgvpIKTLQVQYSLL 197
Cdd:cd19129 107 FA-FQPGDEqdprdangnviyddgVTLLDtwrAMERLVDEGRCKAIGLSDVSLEKLREIFE--AAR---IKPAVVQVESH 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 198 STYPVTELglKDVCDELGIKLIAYSPLalgiltGKYSEKGPFPRGVrglllrqllpgvrsllqcLQDVAQSRNKTMSQVA 277
Cdd:cd19129 181 PYLPEWEL--LDFCKNHGIVLQAFAPL------GHGMEPKLLEDPV------------------ITAIARRVNKTPAQVL 234
|
250 260
....*....|....*....|....
gi 17135278 278 LNWCIAKGTMPIPGARSVKQAQEN 301
Cdd:cd19129 235 LAWAIQRGTALLTTSKTPSRIREN 258
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
17-319 |
1.06e-09 |
|
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: 58.63 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 17 LSLPGMGCGTW-AWGNQLlwgynesMDAQLQAVFNLCVSNGVTLFDTGDSYgtgrLNGRSELLLGKFSQEyQGVNQENIC 95
Cdd:cd19142 11 LRVSNVGLGTWsTFSTAI-------SEEQAEEIVTLAYENGINYFDTSDAF----TSGQAETELGRILKK-KGWKRSSYI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 96 IATKLAaypWRWT-------RQSMINACKSSAQRLG-RNVDLVQMHWSTAnYAPWQEVglLDGLADLYEQGLVkgvglSN 167
Cdd:cd19142 79 VSTKIY---WSYGseerglsRKHIIESVRASLRRLQlDYIDIVIIHKADP-MCPMEEV--VRAMSYLIDNGLI-----MY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 168 YGTKRLQRVHQKFA-----ERGVPIKTL-QVQYSLLSTYPVtELGLKDVCDELGIKLIAYSPLALGILTGKYSEKGPFPR 241
Cdd:cd19142 148 WGTSRWSPVEIMEAfsiarQFNCPTPICeQSEYHMFCREKM-ELYMPELYNKVGVGLITWSPLSLGLDPGISEETRRLVT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 242 GVRGLLLRQLLPGVRSL-----------LQCLQDVAQSRNKTMSQVALNWCIAKGTMP--IPGARSVKQAQENIGALGW- 307
Cdd:cd19142 227 KLSFKSSKYKVGSDGNGiheetrrashkLRELSLIAERLGCDLTQLLIAWSLKNENVQcvLIGASSLEQLYSQLNSLQLl 306
|
330
....*....|...
gi 17135278 308 -QLNSGEIAELDK 319
Cdd:cd19142 307 pKLNSAVMEELER 319
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
60-309 |
1.62e-09 |
|
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes Glycine max NAD(P)H-dependent 6'-deoxychalcone synthase (6DCS, EC 3.1.170), chalcone reductase (CHR, EC 2.3.1.74) from Medicago sativa, Glycyrrhiza echinate, and Glycyrrhiza glabra, which are founding members of aldo-keto reductase family 4 member A1 (AKR4A1), A2 (AKR4A2), A3 (AKR4A3), and A4 (AKR4A4), respectively. NAD(P)H-6DCS co-acts with chalcone synthase in formation of 4,2',4'-trihydroxychalcone, involved in the biosynthesis of glyceollin type phytoalexins. CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. The AKR4B family of AKR includes Sesbania rostrate chalcone reductase (CHR, AKR4B1), Papaver somniferum codeinone reductase (COR, AKR4B2/ AKR4B3), Fragaria x ananassa D-galacturonate reductase (GalUR, AKR4B4), deoxymugineic acid synthase 1 (DMAS1) from Zea mays (AKR4B5), Oryza sativa (AKR4B6), Hordeum vulgare (AKR4B7), Triticum aestivum (AKR4B8), and Erythroxylum coca methylecgonone reductase (MecgoR, AKR4B10). CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. NADPH-dependent COR and non-functional NADPH-dependent COR from Papaver somniferum are founding members of aldo-keto reductase family 4 member B2 (AKR4B2) and B3 (AKR4B3), respectively. NADPH-dependent COR (EC 1.1.1.247) reduces codeinone to codeine in the penultimate step in morphine biosynthesis. It can use morphinone, hydrocodone, and hydromorphone as substrates during reductive reaction with NADPH as cofactor, and morphine and dihydrocodeine as substrates during oxidative reaction with NADP as cofactor. GalUR (EC 1.1.1.365), also called aldo-keto reductase 2 (AKR2), is involved in ascorbic acid (vitamin C) biosynthesis by catalyzing the conversion from L-galactonate and NADP(+) to D-galacturonate and NADPH. DMAS1 (EC 1.1.1.285) catalyzes the reduction of a 3''-keto intermediate during the biosynthesis of 2'-deoxymugineic acid (DMA) from L-Met. It is involved in the formation of phytosiderophores (MAs) belonging to the mugineic acid family and required to acquire iron. MecgoR catalyzes the stereospecific reduction of methylecgonone to methylecgonine, the penultimate step in cocaine biosynthesis.
Pssm-ID: 381350 [Multi-domain] Cd Length: 281 Bit Score: 58.05 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 60 FDTGDSYGTgrlngrsELLLGKFSQE---YQGVNQ-ENICIATKLA---AYPWRwtrqsMINACKSSAQRLGRN-VDLVQ 131
Cdd:cd19124 37 FDTAAAYGT-------EEALGEALAEalrLGLVKSrDELFVTSKLWcsdAHPDL-----VLPALKKSLRNLQLEyVDLYL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 132 MHWST-----ANYAPWQEVGLLD--------GLADLYEQGLVKGVGLSNYGTKRLQRVHQkFAErgVPIKTLQVQYSlls 198
Cdd:cd19124 105 IHWPVslkpgKFSFPIEEEDFLPfdikgvweAMEECQRLGLTKAIGVSNFSCKKLQELLS-FAT--IPPAVNQVEMN--- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 199 tyPVTELG-LKDVCDELGIKLIAYSPLalgiltGKYSEKGpfprgvrglllrqllpGVRSLL--QCLQDVAQSRNKTMSQ 275
Cdd:cd19124 179 --PAWQQKkLREFCKANGIHVTAYSPL------GAPGTKW----------------GSNAVMesDVLKEIAAAKGKTVAQ 234
|
250 260 270
....*....|....*....|....*....|....
gi 17135278 276 VALNWCIAKGTMPIPGARSVKQAQENIGALGWQL 309
Cdd:cd19124 235 VSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWEL 268
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
88-318 |
4.83e-09 |
|
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from Leishmania major and Trypanosoma brucei are founding members of aldo-keto reductase family 5 member A1 (AKR5A1) and A2 (AKR5A2), respectively. PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity toward the synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde.
Pssm-ID: 381382 [Multi-domain] Cd Length: 266 Bit Score: 56.37 E-value: 4.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 88 GVNQENICIATKLaaypWRWTR--QSMINACKSSAQRLGRN-VDLVQMHWSTAN--YAPWQevglldGLADLYEQGLVKG 162
Cdd:cd19156 60 GVPREEVFVTTKL----WNSDQgyESTLAAFEESLEKLGLDyVDLYLIHWPVKGkfKDTWK------AFEKLYKEKKVRA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 163 VGLSNYGTKRLQRVhqkFAERGVPIKTLQVQ-YSLLSTYPvtelgLKDVCDELGIKLIAYSPLALGiltgkysekgpfpr 241
Cdd:cd19156 130 IGVSNFHEHHLEEL---LKSCKVAPMVNQIElHPLLTQEP-----LRKFCKEKNIAVEAWSPLGQG-------------- 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17135278 242 gvrglllrQLLPGVRsllqcLQDVAQSRNKTMSQVALNWCIAKGTMPIPGARSVKQAQENIGALGWQLNSGEIAELD 318
Cdd:cd19156 188 --------KLLSNPV-----LKAIGKKYGKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQID 251
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
17-304 |
6.11e-09 |
|
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: 56.39 E-value: 6.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 17 LSLPGMGCGTWAWGNQllWGYNESMDaQLQAVFNLCVSNGVTLFDTGDSYGtgrlNGRSELLLGKFSQEYQgVNQENICI 96
Cdd:cd19153 10 GNVSPVGLGTAALGGV--YGDGLEQD-EAVAIVAEAFAAGINHFDTSPYYG----AESSEAVLGKALAALQ-VPRSSYTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 97 ATKLAAY---PWRWTRQSMINACKSSAQRLGRN-VDLVQMH-WSTANYAP-WQEVglLDGLADLYEQGLVKGVGLSNYGT 170
Cdd:cd19153 82 ATKVGRYrdsEFDYSAERVRASVATSLERLHTTyLDVVYLHdIEFVDYDTlVDEA--LPALRTLKDEGVIKRIGIAGYPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 171 KRLQRVHQKfaergVPIKTLQVQYSLlSTYPVTELGLKDVCDEL----GIKLIAYSPLALGILTgkysEKGPFPrgvrgl 246
Cdd:cd19153 160 DTLTRATRR-----CSPGSLDAVLSY-CHLTLQDARLESDAPGLvrgaGPHVINASPLSMGLLT----SQGPPP------ 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17135278 247 lLRQLLPGVRSLLQCLQDVAQSRNKTMSQVALNWCIA----KGTMpIPGARSVKQAQENIGA 304
Cdd:cd19153 224 -WHPASGELRHYAAAADAVCASVEASLPDLALQYSLAahagVGTV-LLGPSSLAQLRSMLAA 283
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
13-318 |
1.57e-08 |
|
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol dehydrogenase [NADP(+)] (ALR, EC 1.1.1.2) from Homo sapiens (AKR1A1), Sus scrofa (AKR1A2), Rattus norvegicus (liver, AKR1A3), and Mus musculus (AKR1A4). ALR, also known as aldehyde reductase, or ALDR1, catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid.
Pssm-ID: 381332 [Multi-domain] Cd Length: 305 Bit Score: 55.08 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 13 IHQELSLPGMGCGTWawgnqllwgynESMDAQLQAVFNLCVSNGVTLFDTGDSYGtgrlngrSELLLGKFSQE----YQG 88
Cdd:cd19106 1 LHTGQKMPLIGLGTW-----------KSKPGQVKAAVKYALDAGYRHIDCAAVYG-------NEQEVGEALKEkvgpGKA 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 89 VNQENICIATKLaaypWRwTR---QSMINACKSSAQRLGRN-VDLVQMHWSTA-----NYAPWQEVGLL----------- 148
Cdd:cd19106 63 VPREDLFVTSKL----WN-TKhhpEDVEPALRKTLKDLQLDyLDLYLIHWPYAfergdNPFPKNPDGTIrydsthyketw 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 149 DGLADLYEQGLVKGVGLSNYGTKRLQRVHQKfaergVPIK--TLQVQysllsTYP-VTELGLKDVCDELGIKLIAYSPLA 225
Cdd:cd19106 138 KAMEKLVDKGLVKAIGLSNFNSRQIDDILSV-----ARIKpaVLQVE-----CHPyLAQNELIAHCKARGLVVTAYSPLG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 226 lgiltgkySEKGPFPRGVRGLLLRQllPGVRSLlqclqdvAQSRNKTMSQVALNWCIAKGTMPIPgaRSVKQA--QENIG 303
Cdd:cd19106 208 --------SPDRPWAKPDEPVLLEE--PKVKAL-------AKKYNKSPAQILLRWQVQRGVVVIP--KSVTPSriKQNIQ 268
|
330
....*....|....*
gi 17135278 304 ALGWQLNSGEIAELD 318
Cdd:cd19106 269 VFDFTLSPEEMKQLD 283
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
87-317 |
2.46e-08 |
|
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase (AR, EC 1.1.1.21) from Homo sapiens (AKR1B1), Oryctolagus cuniculus (kidney, AKR1B2), Mus musculus (AKR1B3), Rattus norvegicus (lens, AKR1B4), Bos taurus (lens/testis, AKR1B5), and Sus scrofa (lens, AKR1B6), aldose reductase-related protein 1 (ALD1, EC1.1.1.21) from Mus musculus (AKR1B7), Rattus norvegicus (AKR1B14), and Homo sapiens (AKR1B15), Mus musculus fibroblast growth factor induced protein (FR-1 or AKR1B8, EC 1.1.1.21), Cricetulus griseus aldose reductase-related protein 2 (ALD2 or AKR1B9, EC 1.1.1.21), aldose reductase-like from Homo sapiens (ARL-1 or AKR1B10) and Rattus norvegicus (AKR1B13), aldo-keto reductase from Gallus domesticus (eye, tongue, esophagus, AKR1B12), and Oryctolagus cuniculus AR-like protein (3beta-HSD, AKR1B19). AR, also called aldehyde reductase, catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. ALD1 reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. It may play a role in the metabolism of xenobiotic aromatic aldehydes. FR-1, also called aldose reductase-related protein 2, or fibroblast growth factor-regulated protein (FGFRP), is induced by fibroblast growth factor-1. It may play a role in the regulation of the cell cycle. FR-1 belongs to the NADPH-dependent aldo-keto reductase family. ALD2 is an inducible aldo-keto reductase with a preference for aliphatic substrates. It can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. ARL-1, also called aldose reductase-like, or aldose reductase-related protein (ARP), or small intestine reductase, or SI reductase, acts as all-trans-retinaldehyde reductase that can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). It may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. AKR1B15, also called estradiol 17-beta-dehydrogenase AKR1B15, is a mitochondrial aldo-keto reductase that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. It has a strong selectivity towards NADP(H). AKR1B19 is aldose reductase-like that may show 3-beta-hydroxysteroid dehydrogenase (3beta-HSD) activity.
Pssm-ID: 381333 [Multi-domain] Cd Length: 307 Bit Score: 54.73 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 87 QGVNQENICIATKLaaYPWRWTRQSMINACKSSAQRLGRN-VDLVQMHWSTA-----NYAPWQEVG--------LLD--- 149
Cdd:cd19107 57 QVVKREDLFIVSKL--WCTFHEKGLVKGACQKTLSDLKLDyLDLYLIHWPTGfkpgkELFPLDESGnvipsdttFLDtwe 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 150 GLADLYEQGLVKGVGLSNYGTKRLQRVHQKFAERGVPIkTLQVQysllsTYP-VTELGLKDVCDELGIKLIAYSPLAlgi 228
Cdd:cd19107 135 AMEELVDEGLVKAIGVSNFNHLQIERILNKPGLKYKPA-VNQIE-----CHPyLTQEKLIQYCQSKGIVVTAYSPLG--- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 229 ltgkySEKGPFPRgvrglllrqllPGVRSLLQ--CLQDVAQSRNKTMSQVALNWCIAKGTMPIPGARSVKQAQENIGALG 306
Cdd:cd19107 206 -----SPDRPWAK-----------PEDPSLLEdpKIKEIAAKHNKTTAQVLIRFPIQRNLVVIPKSVTPERIAENFKVFD 269
|
250
....*....|.
gi 17135278 307 WQLNSGEIAEL 317
Cdd:cd19107 270 FELSSEDMATI 280
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
17-302 |
2.92e-08 |
|
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, EC 1.1.1.365), also called D-galacturonic acid reductase, or GalUR, is a founding member of aldo-keto reductase family 3 member D1 (AKR3D1). It mediates the reduction of D-galacturonate to L-galactonate, the first step in D-galacturonate catabolic process. It also has activity with D-glucuronate and DL-glyceraldehyde. Its activity is seen only with NADPH and not with NADH.
Pssm-ID: 381347 [Multi-domain] Cd Length: 279 Bit Score: 54.07 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 17 LSLPGMGCGTWAWGNqllwgyNESMDAQLQAVfnlcvSNGVTLFDTGDSYGTgrlngRSELLLGKFSQEYQGVNQENICI 96
Cdd:cd19121 10 ASIPAVGLGTWQAKA------GEVKAAVAHAL-----KIGYRHIDGALCYQN-----EDEVGEGIKEAIAGGVKREDLFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 97 ATKLaaypWRWTRQSMINACKSSAQRLGRN-VDLVQMHWSTA------------------NYAP-WQEVGLLDGLADLYE 156
Cdd:cd19121 74 TTKL----WSTYHRRVELCLDRSLKSLGLDyVDLYLVHWPVLlnpngnhdlfptlpdgsrDLDWdWNHVDTWKQMEKVLK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 157 QGLVKGVGLSNYGTKRLQRVhqkfaergvpIKTLQV-----QYSLLSTYPVTELglKDVCDELGIKLIAYSPLAlgiltg 231
Cdd:cd19121 150 TGKTKAIGVSNYSIPYLEEL----------LKHATVvpavnQVENHPYLPQQEL--VDFCKEKGILIEAYSPLG------ 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17135278 232 kySEKGPfprgvrglLLRQllPGVrsllqclQDVAQSRNKTMSQVALNWCIAKGTMPIPGARSVKQAQENI 302
Cdd:cd19121 212 --STGSP--------LISD--EPV-------VEIAKKHNVGPGTVLISYQVARGAVVLPKSVTPDRIKSNL 263
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
39-326 |
3.55e-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: 381324 [Multi-domain] Cd Length: 318 Bit Score: 54.27 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 39 ESMDAQLQAVFNLCVSNGVTLFDTGDSYgtgrlnGRSELLLGKFSQEyQGVNQENICIATKLA-AYPWRWTRQSMINACK 117
Cdd:cd19098 31 EAMRAHTHAVLDAAWAAGVRYFDAARSY------GRAEEFLGSWLRS-RNIAPDAVFVGSKWGyTYTADWQVDAAVHEVK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 118 ------------SSAQRLGRNVDLVQMHWSTANYAPWQEVGLLDGLADLYEQGLvkGVGLSNYGTKRLQRVHQKFAER-- 183
Cdd:cd19098 104 dhslarllkqweETRSLLGKHLDLYQIHSATLESGVLEDADVLAALAELKAEGV--KIGLSLSGPQQAETLRRALEIEid 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 184 GVPI-KTLQVQYSLLSTYPVTELGLkdvCDELGIKLIAYSPLALGILTGkysekgpfprgvrglllRQLLPGVRSLLQCL 262
Cdd:cd19098 182 GARLfDSVQATWNLLEQSAGEALEE---AHEAGMGVIVKEALANGRLTD-----------------RNPSPELAPLMAVL 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17135278 263 QDVAQSRNKTMSQVALNWCIAKGTMPI--PGARSVKQAQENIGALGWQLNSGEIAELDKAAASSDK 326
Cdd:cd19098 242 KAVADRLGVTPDALALAAVLAQPFVDVvlSGAATPEQLRSNLRALDVSLDLELLAALADLAEPPED 307
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
18-319 |
1.47e-07 |
|
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar proteins; Saccharomyces cerevisiae Ara1p (EC 1.1.1.117), also called D-arabinose 1-dehydrogenase (NAD(P)(+)), is a founding members of aldo-keto reductase family 3 member C1 (AKR3C1). It catalyzes the oxidation of D-arabinose, L-xylose, L-fucose, and L-galactose in the presence of NADP(+).
Pssm-ID: 381345 [Multi-domain] Cd Length: 294 Bit Score: 52.11 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 18 SLPGMGCGTWAWGNQLlwgynesmdAQLQAVFNLCVSNGVTLFDTGDSYGTgrlngrsELLLGKFSQEY---QGVNQENI 94
Cdd:cd19119 11 SIPALGLGTASPHEDR---------AEVKEAVEAAIKEGYRHIDTAYAYET-------EDFVGEAIKRAiddGSIKREEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 95 CIATKLaaYPWRWTRqsMINACKSSAQRLGRN-VDLVQMHWSTANYAPWQEVGLL------DG----------------L 151
Cdd:cd19119 75 FITTKV--WPTFYDE--VERSLDESLKALGLDyVDLLLVHWPVCFEKDSDDSGKPftpvndDGktryaasgdhittykqL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 152 ADLYEQGLVKGVGLSNYGTKRLQRVHQKfaergVPIKTLQVQYSLLSTYPvtELGLKDVCDELGIKLIAYSPLAlgiltg 231
Cdd:cd19119 151 EKIYLDGRAKAIGVSNYSIVYLERLIKE-----CKVVPAVNQVELHPHLP--QMDLRDFCFKHGILVTAYSPLG------ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 232 kysekgpfprGVRGLLLRQLLpgvrsllqcLQDVAQSRNKTMSQVALNWCIAKGTMPIPGARSVKQAQENIGALGwqLNS 311
Cdd:cd19119 218 ----------SHGAPNLKNPL---------VKKIAEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKIVS--LTK 276
|
....*...
gi 17135278 312 GEIAELDK 319
Cdd:cd19119 277 EDLQKLDD 284
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
150-319 |
1.74e-07 |
|
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose reductase xyl1 (XR, EC 1.1.1.307) is a founding member of aldo-keto reductase family 2 member D1 (AKR2D1). It catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol in a NAD(P)H dependent manner.
Pssm-ID: 381341 [Multi-domain] Cd Length: 311 Bit Score: 52.04 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 150 GLADLYEQGLVKGVGLSNYGTKRLQRVhqkfaERGVPIK--TLQVQYsllstYP-VTELGLKDVCDELGIKLIAYS---P 223
Cdd:cd19115 149 AMEKLVDKGLARSIGVSNFSAQLLMDL-----LRYARIRpaTLQIEH-----HPyLTQPRLVKYAQKEGIAVTAYSsfgP 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 224 LALGILTGKYSEKGPfprgvrgLLLRQllPGVRSLlqclqdvAQSRNKTMSQVALNWCIAKGTMPIPGARSVKQAQENIG 303
Cdd:cd19115 219 QSFLELDLPGAKDTP-------PLFEH--DVIKSI-------AEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLD 282
|
170
....*....|....*....
gi 17135278 304 ALGWQLNSGE---IAELDK 319
Cdd:cd19115 283 VTGFDLEAEEikaISALDI 301
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-302 |
7.89e-07 |
|
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: 50.01 E-value: 7.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 17 LSLPGMGCGTWawgnqlLWGYNESMDAQLQAVFNLCVSNGVTLFDTGDSYGtgrlNGRSELLLGKF---SQEYQGVNQEN 93
Cdd:cd19099 1 LTLSSLGLGTY------RGDSDDETDEEYREALKAALDSGINVIDTAINYR----GGRSERLIGKAlreLIEKGGIKRDE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 94 ICIATK---------------------LAAYPWRWT-----RQSM-----INACKSSAQRLGRN-VDLVQMH---WSTAN 138
Cdd:cd19099 71 VVIVTKagyipgdgdeplrplkyleekLGRGLIDVAdsaglRHCIspaylEDQIERSLKRLGLDtIDLYLLHnpeEQLLE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 139 YAPWQEVGLLDGLADLYE----QGLVKGVGLS----------NYGTKRLQRVHQKFAERGVP---IKTLQVQYSLLSTYP 201
Cdd:cd19099 151 LGEEEFYDRLEEAFEALEeavaEGKIRYYGIStwdgfrappaLPGHLSLEKLVAAAEEVGGDnhhFKVIQLPLNLLEPEA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 202 VTELGLK--------DVCDELGIKLIAYSPLAlgiltgkysekgpfprgvRGLLLRQLLPGVRsllqclqdVAQSRNKTM 273
Cdd:cd19099 231 LTEKNTVkgealsllEAAKELGLGVIASRPLN------------------QGQLLGELRLADL--------LALPGGATL 284
|
330 340 350
....*....|....*....|....*....|.
gi 17135278 274 SQVALNWCIA-KG-TMPIPGARSVKQAQENI 302
Cdd:cd19099 285 AQRALQFARStPGvDSALVGMRRPEHVDENL 315
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
56-304 |
1.39e-06 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 49.39 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 56 GVTLFDTGDSYGtgrlNGRSELLLGKfSQEYQGVNQENICIATKLAAYP--WRWTRQSMINACKSSAQRLGRN-VDLVQM 132
Cdd:PLN02587 44 GINFFDTSPYYG----GTLSEKVLGK-ALKALGIPREKYVVSTKCGRYGegFDFSAERVTKSVDESLARLQLDyVDILHC 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 133 HWStanyapwqEVGLLD--------GLADLYEQGLVKGVGLSNYGTKRLQRVHQKFAERGVPIKTLQVQYSLLSTypvTE 204
Cdd:PLN02587 119 HDI--------EFGSLDqivnetipALQKLKESGKVRFIGITGLPLAIFTYVLDRVPPGTVDVILSYCHYSLNDS---SL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 205 LGLKDVCDELGIKLIAYSPLALGILTGK-YSEKGPFPrgvrglllrqllPGVRSLLQCLQDVAQSRNKTMSQVALNWCIA 283
Cdd:PLN02587 188 EDLLPYLKSKGVGVISASPLAMGLLTENgPPEWHPAP------------PELKSACAAAATHCKEKGKNISKLALQYSLS 255
|
250 260
....*....|....*....|...
gi 17135278 284 KGTMPIP--GARSVKQAQENIGA 304
Cdd:PLN02587 256 NKDISTTlvGMNSVQQVEENVAA 278
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
154-301 |
1.44e-06 |
|
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde reductase 1 (ARI, EC 1.1.1.2), Trichosporonoides megachilieni NADPH-dependent erthyrose reductase (ER) 1/2 and 3, are founding members of aldo-keto reductase family 3 member B1 (AKR3B1), B2 (AKR3B2), and B3 (AKR3B3), respectively. Sporidiobolus salmonicolor NADPH-ARI, also called alcohol dehydrogenase [NADP(+)], or aldehyde reductase I, or ALR 1, catalyzes the asymmetric reduction of aliphatic and aromatic aldehydes and ketones to an R-enantiomer. It reduces ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Trichosporonoides megachilieni NADPH-ERs catalyze the reduction of D-erythrose.
Pssm-ID: 381344 [Multi-domain] Cd Length: 283 Bit Score: 48.95 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 154 LYEQGLVKGVGLSNYGTKRLQRVhqkFAERGVPIKTLQVQYSLLstypVTELGLKDVCDELGIKLIAYSPLalgiltGKY 233
Cdd:cd19118 148 LKKTGKVKSIGVSNFSIDHLQAI---IEETGVVPAVNQIEAHPL----LLQDELVDYCKSKNIHITAYSPL------GNN 214
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 234 SEKGPfprgvrgLLLRQllPGVrsllqclQDVAQSRNKTMSQVALNWCIAKGTMPIPgaRSVKQA--QEN 301
Cdd:cd19118 215 LAGLP-------LLVQH--PEV-------KAIAAKLGKTPAQVLIAWGIQRGHSVIP--KSVTPSriRSN 266
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
158-318 |
5.93e-06 |
|
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes 3-oxo-5-beta-steroid 4-dehydrogenase (EC 1.3.1.3) from Homo sapiens (AKR1D1), Rattus norvegicus (liver, AKR1D2), and Oryctolagus cuniculus (AKR1D3). 3-oxo-5-beta-steroid 4-dehydrogenase, also called delta(4)-3-ketosteroid 5-beta-reductase (EC 1.3.99.6), or delta(4)-3-oxosteroid 5-beta-reductase, or 5-beta-reductase, efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites.
Pssm-ID: 381335 [Multi-domain] Cd Length: 308 Bit Score: 47.10 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 158 GLVKGVGLSNYGTKRLQRVHQKFAERGVPIkTLQVQysllsTYP-VTELGLKDVCDELGIKLIAYSPLALgiltgkysek 236
Cdd:cd19109 147 GLVKSIGVSNFNRRQLELILNKPGLKHKPV-SNQVE-----CHPyFTQPKLLEFCQQHDIVIVAYSPLGT---------- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 237 gpfPRGvrGLLLRQLLPgvrSLLQ--CLQDVAQSRNKTMSQVALNWCIAKGTMPIPGARSVKQAQENIGALGWQLNSGEI 314
Cdd:cd19109 211 ---CRD--PIWVNVSSP---PLLEdpLLNSIGKKYNKTAAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEM 282
|
....
gi 17135278 315 AELD 318
Cdd:cd19109 283 KDIE 286
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
256-321 |
6.41e-06 |
|
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: 47.42 E-value: 6.41e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17135278 256 RSLLQCLQDVAQSRNKTMSQVALNWCIAKG--TMPIPGARSVKQAQENIGALGWQLNSGEIAELDKAA 321
Cdd:cd19146 248 RKVSEKLEKVAEEKGTAITSVALAYVMHKApyVFPIVGGRKVEHLKGNIEALGISLSDEEIQEIEDAY 315
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
54-280 |
2.83e-04 |
|
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: 41.88 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 54 SNGVTLFDTGDSYGtgrlngRSELLLGK----FSQEYQgvnQENICIATKLAAY-PW------RWTRQSMinacKSSAQR 122
Cdd:cd19164 45 ELGIRAFDTSPYYG------PSEIILGRalkaLRDEFP---RDTYFIITKVGRYgPDdfdyspEWIRASV----ERSLRR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 123 LGRN-VDLVQMHwsTANYAPWQEVglLDGLADLYE---QGLVKGVGLSNYGTKRLQRV-HQKFAERGVPIK--------T 189
Cdd:cd19164 112 LHTDyLDLVYLH--DVEFVADEEV--LEALKELFKlkdEGKIRNVGISGYPLPVLLRLaELARTTAGRPLDavlsychyT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 190 LQvQYSLLSTYPVTElglkdvcDELGIK-LIAYSPLALGILTgkysEKGPfprgvrglllRQLLPGVRSLLQCLQ---DV 265
Cdd:cd19164 188 LQ-NTTLLAYIPKFL-------AAAGVKvVLNASPLSMGLLR----SQGP----------PEWHPASPELRAAAAkaaEY 245
|
250
....*....|....*
gi 17135278 266 AQSRNKTMSQVALNW 280
Cdd:cd19164 246 CQAKGTDLADVALRY 260
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| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
127-318 |
1.66e-03 |
|
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: 39.74 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 127 VDLVQMHWSTA--------NYAP-----------WQEVGLLD---GLADLYEQGLVKGVGLSNYGTKRLQRVHqkfaeRG 184
Cdd:cd19113 103 VDLFLIHFPIAfkfvpieeKYPPgfycgdgdnfvYEDVPILDtwkALEKLVDAGKIKSIGVSNFPGALILDLL-----RG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17135278 185 VPIK--TLQVQYSLLSTYPvtelglkdvcdelgiKLIAYSPLAlGILTGKYSEKGP--FPRgvrglLLRQLLPGVRSLLQ 260
Cdd:cd19113 178 ATIKpaVLQIEHHPYLQQP---------------KLIEYAQKA-GITITAYSSFGPqsFVE-----LNQGRALNTPTLFE 236
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17135278 261 --CLQDVAQSRNKTMSQVALNWCIAKGTMPIPGARSVKQAQENIGALGWQLNSG---EIAELD 318
Cdd:cd19113 237 hdTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEdfeEIAKLD 299
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