|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
2-269 |
1.37e-136 |
|
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: 386.22 E-value: 1.37e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 2 KTLSFA-GREMPVIGAGLWGIGEGIDAHAQ-RRALDAAFDAGLVLLDTAEMYGNGASERVAGAAARSaraQGKDVFVVSK 79
Cdd:cd19138 1 RTVTLPdGTKVPALGQGTWYMGEDPAKRAQeIEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIRG---RRDKVFLVSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 80 VLPSNARPQLMRTALTRSLHNLGLDYLDMYLLHWRSTADLALVAQQMHEFVQEGLIRHWGVSNFDVADMQELLAVPYGEE 159
Cdd:cd19138 78 VLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWRGGVPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVPGGGN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 160 CACDQNLYNLANRGMDHDLMPWLRDHHIPLMAYSPLGDGGPAGtRVMVNNTEVKKVAARHHASAQQVMLAWCVRDGNTLA 239
Cdd:cd19138 158 CAANQVLYNLGSRGIEYDLLPWCREHGVPVMAYSPLAQGGLLR-RGLLENPTLKEIAARHGATPAQVALAWVLRDGNVIA 236
|
250 260 270
....*....|....*....|....*....|
gi 1233716732 240 IPQSANPEHLVQDFHSGSLELDEHDFAALD 269
Cdd:cd19138 237 IPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
8-276 |
1.44e-80 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 243.81 E-value: 1.44e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGAGLWGIGegiDAHAqRRALDAAFDAGLVLLDTAEMYGN----GaservagaaarsaraQG--------KDVF 75
Cdd:COG0656 2 GVEIPALGLGTWQLP---GEEA-AAAVRTALEAGYRHIDTAAMYGNeegvG---------------EAiaasgvprEELF 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 76 VVSKVLPSNARPQLMRTALTRSLHNLGLDYLDMYLLHWRSTADLALVAQQMHEFVQEGLIRHWGVSNFDVADMQELLAVP 155
Cdd:COG0656 63 VTTKVWNDNHGYDDTLAAFEESLERLGLDYLDLYLIHWPGPGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAET 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 156 yGEECACDQNLYNLANRgmDHDLMPWLRDHHIPLMAYSPLGDGGpagtrvMVNNTEVKKVAARHHASAQQVMLAWCVRDG 235
Cdd:COG0656 143 -GVKPAVNQVELHPYLQ--QRELLAFCREHGIVVEAYSPLGRGK------LLDDPVLAEIAEKHGKTPAQVVLRWHLQRG 213
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1233716732 236 nTLAIPQSANPEHLVQDFHSGSLELDEHDFAALDSA------FPAPT 276
Cdd:COG0656 214 -VVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALdrgerlGPDPD 259
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
8-269 |
2.70e-73 |
|
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: 225.57 E-value: 2.70e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGAGLWGIGEG-----IDAHAQRRALDAAFDAGLVLLDTAEMYGNGASERVAgaaarsaraqGK--------DV 74
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGmskdySDDKKAIEALRYAIELGINLIDTAEMYGGGHAEELV----------GKaikgfdreDL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 75 FVVSKVLPSNARPQLMRTALTRSLHNLGLDYLDMYLLHWRSTA-DLALVAQQMHEFVQEGLIRHWGVSNFDVADMQELLA 153
Cdd:cd19072 71 FITTKVSPDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSiPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 154 VPYGEECACDQNLYNLANRGMDHDLMPWLRDHHIPLMAYSPLGDGGPAGTRvmvNNTEVKKVAARHHASAQQVMLAWCVR 233
Cdd:cd19072 151 YLKKGPIVANQVEYNLFDREEESGLLPYCQKNGIAIIAYSPLEKGKLSNAK---GSPLLDEIAKKYGKTPAQIALNWLIS 227
|
250 260 270
....*....|....*....|....*....|....*.
gi 1233716732 234 DGNTLAIPQSANPEHLVQDFHSGSLELDEHDFAALD 269
Cdd:cd19072 228 KPNVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
11-269 |
2.62e-59 |
|
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: 189.23 E-value: 2.62e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 11 MPVIGAGLWGIGEGidahAQRRALDAAFDAGLVLLDTAEMYGNGAservagaaarsarAQGK----------DVFVVSKV 80
Cdd:cd19071 1 MPLIGLGTYKLKPE----ETAEAVLAALEAGYRHIDTAAAYGNEA-------------EVGEairesgvpreELFITTKL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 81 LPSNARPQLMRTALTRSLHNLGLDYLDMYLLHW-----RSTADLALVA--QQMHEFVQEGLIRHWGVSNFDVADMQELLA 153
Cdd:cd19071 64 WPTDHGYERVREALEESLKDLGLDYLDLYLIHWpvpgkEGGSKEARLEtwRALEELVDEGLVRSIGVSNFNVEHLEELLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 154 V----PygeecACDQNLYNLANRgmDHDLMPWLRDHHIPLMAYSPLGdggpAGTRVMVNNTEVKKVAARHHASAQQVMLA 229
Cdd:cd19071 144 AarikP-----AVNQIELHPYLQ--QKELVEFCKEHGIVVQAYSPLG----RGRRPLLDDPVLKEIAKKYGKTPAQVLLR 212
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1233716732 230 WCVRDGnTLAIPQSANPEHLVQDFHSGSLELDEHDFAALD 269
Cdd:cd19071 213 WALQRG-VVVIPKSSNPERIKENLDVFDFELSEEDMAAID 251
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-274 |
6.35e-57 |
|
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: 185.38 E-value: 6.35e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 1 MKTLSFAGREMPVIGAGLWGIGE---GIDAHAQRRALDAAFDAGLVLLDTAEMYGNGASERVAgaaarsaraqGK----- 72
Cdd:COG0667 3 YRRLGRSGLKVSRLGLGTMTFGGpwgGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELL----------GEalkgr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 73 ---DVFVVSKV--------LPSNARPQLMRTALTRSLHNLGLDYLDMYLLHWRSTA-DLALVAQQMHEFVQEGLIRHWGV 140
Cdd:COG0667 73 prdDVVIATKVgrrmgpgpNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDtPIEETLGALDELVREGKIRYIGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 141 SNFDVADMQELLAVPYG-EECACDQNLYNLANRGMDHDLMPWLRDHHIPLMAYSPLGDG-----------GPAGTRVMVN 208
Cdd:COG0667 153 SNYSAEQLRRALAIAEGlPPIVAVQNEYSLLDRSAEEELLPAARELGVGVLAYSPLAGGlltgkyrrgatFPEGDRAATN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 209 NT-------------EVKKVAARHHASAQQVMLAWCV-RDGNTLAIPQSANPEHLVQDFHSGSLELDEHDFAALDSAFPA 274
Cdd:COG0667 233 FVqgylternlalvdALRAIAAEHGVTPAQLALAWLLaQPGVTSVIPGARSPEQLEENLAAADLELSAEDLAALDAALAA 312
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
12-271 |
2.89e-55 |
|
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: 180.09 E-value: 2.89e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 12 PVIGAGLWGIGEGIDAHAQ-----RRALDAAFDAGLVLLDTAEMYGNGASERVAgaaarsaraqGK-------DVFVVSK 79
Cdd:cd19085 2 SRLGLGCWQFGGGYWWGDQddeesIATIHAALDAGINFFDTAEAYGDGHSEEVL----------GKalkgrrdDVVIATK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 80 VLPSNARPQLMRTALTRSLHNLGLDYLDMYLLHW-RSTADLALVAQQMHEFVQEGLIRHWGVSNFDVADMQELLAVpygE 158
Cdd:cd19085 72 VSPDNLTPEDVRKSCERSLKRLGTDYIDLYQIHWpSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDA---G 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 159 ECACDQNLYNLANRGMDHDLMPWLRDHHIPLMAYSPLGDG------------------------GPAGTRVMVNNT--EV 212
Cdd:cd19085 149 RIDSNQLPYNLLWRAIEYEILPFCREHGIGVLAYSPLAQGlltgkfssaedfppgdartrlfrhFEPGAEEETFEAleKL 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 213 KKVAARHHASAQQVMLAWCV-RDGNTLAIPQSANPEHLVQDFHSGSLELDEHDFAALDSA 271
Cdd:cd19085 229 KEIADELGVTMAQLALAWVLqQPGVTSVIVGARNPEQLEENAAAVDLELSPSVLERLDEI 288
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
14-271 |
2.08e-52 |
|
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: 172.88 E-value: 2.08e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 14 IGAGLWGIG---EGIDAHAQRRALDAAFDAGLVLLDTAEMYGNGASERVAGAAARSARAQGKDVFVVSKV------LPSN 84
Cdd:pfam00248 1 IGLGTWQLGggwGPISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKRDKVVIATKVpdgdgpWPSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 85 ARPQLMRTALTRSLHNLGLDYLDMYLLHW--RSTADLALVAqQMHEFVQEGLIRHWGVSNFDVADMQELLAVPYGeECAC 162
Cdd:pfam00248 81 GSKENIRKSLEESLKRLGTDYIDLYYLHWpdPDTPIEETWD-ALEELKKEGKIRAIGVSNFDAEQIEKALTKGKI-PIVA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 163 DQNLYNLANRGMDHDLMPWLRDHHIPLMAYSPLGDG------------GPAGTRVMVNNT---------EVKKVAARHHA 221
Cdd:pfam00248 159 VQVEYNLLRRRQEEELLEYCKKNGIPLIAYSPLGGGlltgkytrdpdkGPGERRRLLKKGtplnlealeALEEIAKEHGV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1233716732 222 SAQQVMLAWCV-RDGNTLAIPQSANPEHLVQDFHSGSLELDEHDFAALDSA 271
Cdd:pfam00248 239 SPAQVALRWALsKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDEL 289
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
8-269 |
3.32e-52 |
|
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: 171.21 E-value: 3.32e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGAGLWGIGEGIDAHAQR-----RALDAAFDAGLVLLDTAEMYGNGASERVAGAAARSARAQgkDVFVVSKVLP 82
Cdd:cd19137 1 GEKIPALGLGTWGIGGFLTPDYSRdeemvELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKDFPRE--DLFIVTKVWP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 83 SNARPQLMRTALTRSLHNLGLDYLDMYLLHW-RSTADLALVAQQMHEFVQEGLIRHWGVSNFDVADMQEllAVPY-GEEC 160
Cdd:cd19137 79 TNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWpNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEE--AISKsQTPI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 161 ACDQNLYNLANRG-MDHDLMPWLRDHHIPLMAYSPLGDGgpagtrVMVNNTEVKKVAARHHASAQQVMLAWCVRDGNTLA 239
Cdd:cd19137 157 VCNQVKYNLEDRDpERDGLLEYCQKNGITVVAYSPLRRG------LEKTNRTLEEIAKNYGKTIAQIALAWLIQKPNVVA 230
|
250 260 270
....*....|....*....|....*....|
gi 1233716732 240 IPQSANPEHLVQDFHSGSLELDEHDFAALD 269
Cdd:cd19137 231 IPKAGRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
1-268 |
6.32e-52 |
|
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: 171.83 E-value: 6.32e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 1 MKTLSFA-GREMPVIGAGLWGIGEGIDAHAQRRALDAafdaGLVLLDTAEMYGNgasERVAGAAARSARAQGK----DVF 75
Cdd:cd19123 1 MKTLPLSnGDLIPALGLGTWKSKPGEVGQAVKQALEA----GYRHIDCAAIYGN---EAEIGAALAEVFKEGKvkreDLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 76 VVSKVLPSNARPQLMRTALTRSLHNLGLDYLDMYLLHW-----------RSTAD--------LALVAQQMHEFVQEGLIR 136
Cdd:cd19123 74 ITSKLWNNSHAPEDVLPALEKTLADLQLDYLDLYLMHWpvalkkgvgfpESGEDllslspipLEDTWRAMEELVDKGLCR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 137 HWGVSNFDVADMQELLA----VPygeecACDQnlYNLANRGMDHDLMPWLRDHHIPLMAYSPLGDGG-PAGTR-----VM 206
Cdd:cd19123 154 HIGVSNFSVKKLEDLLAtariKP-----AVNQ--VELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDrPAAMKaegepVL 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1233716732 207 VNNTEVKKVAARHHASAQQVMLAWCVRDgNTLAIPQSANPEHLVQDFHSGSLELDEHDFAAL 268
Cdd:cd19123 227 LEDPVINKIAEKHGASPAQVLIAWAIQR-GTVVIPKSVNPERIQQNLEAAEVELDASDMATI 287
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
10-269 |
1.04e-48 |
|
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: 163.47 E-value: 1.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 10 EMPVIGAGLWGIGEGIDAHAQR----RALDAAFDAGLVLLDTAEMYGNGASERVAgaaarsaraqGK-------DVFVVS 78
Cdd:cd19084 3 KVSRIGLGTWAIGGTWWGEVDDqesiEAIKAAIDLGINFFDTAPVYGFGHSEEIL----------GKalkgrrdDVVIAT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 79 KV---------LPSNARPQLMRTALTRSLHNLGLDYLDMYLLHWRSTA-DLALVAQQMHEFVQEGLIRHWGVSNFDVADM 148
Cdd:cd19084 73 KCglrwdggkgVTKDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNtPIEETAEALEKLKKEGKIRYIGVSNFSVEQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 149 QEllAVPYGEeCACDQNLYNLANRGMDHDLMPWLRDHHIPLMAYSPLGDG------------GPAGTR---------VMV 207
Cdd:cd19084 153 EE--ARKYGP-IVSLQPPYSMLEREIEEELLPYCRENGIGVLPYGPLAQGlltgkykkeptfPPDDRRsrfpffrgeNFE 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1233716732 208 NNTEV----KKVAARHHASAQQVMLAWCVR-DGNTLAIPQSANPEHLVQDFHSGSLELDEHDFAALD 269
Cdd:cd19084 230 KNLEIvdklKEIAEKYGKSLAQLAIAWTLAqPGVTSAIVGAKNPEQLEENAGALDWELTEEELKEID 296
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
11-269 |
1.40e-48 |
|
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: 161.28 E-value: 1.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 11 MPVIGAGLWGIgEGIDAhaqRRALDAAFDAGLVLLDTAEMYGNgasERVAGAAARSARAQGKDVFVVSKVLPSNARPQLM 90
Cdd:cd19073 1 IPALGLGTWQL-RGDDC---ANAVKEALELGYRHIDTAEIYNN---EAEVGEAIAESGVPREDLFITTKVWRDHLRPEDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 91 RTALTRSLHNLGLDYLDMYLLHW-RSTADLALVAQQMHEFVQEGLIRHWGVSNFDVADMQELLAVpYGEECACDQ----- 164
Cdd:cd19073 74 KKSVDRSLEKLGTDYVDLLLIHWpNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDI-SPLPIAVNQvefhp 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 165 NLYNlanrgmdHDLMPWLRDHHIPLMAYSPLGDGGpagtrvMVNNTEVKKVAARHHASAQQVMLAWCVRDGnTLAIPQSA 244
Cdd:cd19073 153 FLYQ-------AELLEYCRENDIVITAYSPLARGE------VLRDPVIQEIAEKYDKTPAQVALRWLVQKG-IVVIPKAS 218
|
250 260
....*....|....*....|....*
gi 1233716732 245 NPEHLVQDFHSGSLELDEHDFAALD 269
Cdd:cd19073 219 SEDHLKENLAIFDWELTSEDVAKID 243
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
12-251 |
1.16e-47 |
|
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: 158.84 E-value: 1.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 12 PVIGAGLWGIGEGIDAHAQRRALDAAFDAGLVLLDTAEMYGNGASERVAgaaarsaraqGK---------DVFVVSKV-- 80
Cdd:cd06660 1 SRLGLGTMTFGGDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLL----------GRwlkgrgnrdDVVIATKGgh 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 81 ------LPSNARPQLMRTALTRSLHNLGLDYLDMYLLHWR-STADLALVAQQMHEFVQEGLIRHWGVSNFDVADMQELLA 153
Cdd:cd06660 71 ppggdpSRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDdPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 154 V---PYGEECACDQNLYNLANRG-MDHDLMPWLRDHHIPLMAYSPLGdGGPAgtrvmvnntevkkvaarhhasaqQVMLA 229
Cdd:cd06660 151 YakaHGLPGFAAVQPQYSLLDRSpMEEELLDWAEENGLPLLAYSPLA-RGPA-----------------------QLALA 206
|
250 260
....*....|....*....|...
gi 1233716732 230 WCV-RDGNTLAIPQSANPEHLVQ 251
Cdd:cd06660 207 WLLsQPFVTVPIVGARSPEQLEE 229
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
11-270 |
9.96e-44 |
|
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: 149.32 E-value: 9.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 11 MPVIGAGLWGIGEGIDAhaqRRALDAAFDAGLVLLDTAEMYGNGAS-ERVAGAAARSARAQGKDVFVVSKVLPSNARPQL 89
Cdd:cd19136 1 MPILGLGTFRLRGEEEV---RQAVDAALKAGYRLIDTASVYRNEADiGKALRDLLPKYGLSREDIFITSKLAPKDQGYEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 90 MRTALTRSLHNLGLDYLDMYLLHWRSTADLALVA-----------QQMHEFVQEGLIRHWGVSNFDVADMQELLAvpYGE 158
Cdd:cd19136 78 ARAACLGSLERLGTDYLDLYLIHWPGVQGLKPSDprnaelrreswRALEDLYKEGKLRAIGVSNYTVRHLEELLK--YCE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 159 -ECACDQNLYNlaNRGMDHDLMPWLRDHHIPLMAYSPLGDGGPagtrVMVNNTEVKKVAARHHASAQQVMLAWCVRDGnT 237
Cdd:cd19136 156 vPPAVNQVEFH--PHLVQKELLKFCKDHGIHLQAYSSLGSGDL----RLLEDPTVLAIAKKYGRTPAQVLLRWALQQG-I 228
|
250 260 270
....*....|....*....|....*....|...
gi 1233716732 238 LAIPQSANPEHLVQDFHSGSLELDEHDFAALDS 270
Cdd:cd19136 229 GVIPKSTNPERIAENIKVFDFELSEEDMAELNA 261
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
8-271 |
1.74e-43 |
|
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: 148.92 E-value: 1.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGaglWGIG----EGIDAHAQRRALD---AAFDAGLVLLDTAEMYGNgasERVAGAAARSARAQGKDVFVVSKV 80
Cdd:cd19120 1 GSKIPAIA---FGTGtawyKSGDDDIQRDLVDsvkLALKAGFRHIDTAEMYGN---EKEVGEALKESGVPREDLFITTKV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 81 LPSNARPqlmRTALTRSLHNLGLDYLDMYLLHWR-----STADLALVAQQMHEFVQEGLIRHWGVSNFDVADMQELLA-- 153
Cdd:cd19120 75 SPGIKDP---REALRKSLAKLGVDYVDLYLIHSPffakeGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDta 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 154 --VPygeecACDQNLYNLANRGMDHDLMPWLRDHHIPLMAYSPL-----GDGGPAgtrvmvnNTEVKKVAARHHASAQQV 226
Cdd:cd19120 152 kiKP-----AVNQIEFHPYLYPQQPALLEYCREHGIVVSAYSPLspltrDAGGPL-------DPVLEKIAEKYGVTPAQV 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1233716732 227 MLAWCvRDGNTLAIPQSANPEHLVQDFHSGSLELDEHDFAALDSA 271
Cdd:cd19120 220 LLRWA-LQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEIDKA 263
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
10-269 |
1.82e-43 |
|
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: 149.69 E-value: 1.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 10 EMPVIGAGLWGIG-------EGIDAHAQRRALDAAFDAGLVLLDTAEMYGNGASERVAGAAARSARAQgKDVFVVSKV-- 80
Cdd:cd19093 1 EVSPLGLGTWQWGdrlwwgyGEYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELGDR-DEVVIATKFap 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 81 LPSNARPQLMRTALTRSLHNLGLDYLDMYLLHWrSTADLALVAQQMH---EFVQEGLIRHWGVSNFDVADMQELLAV--P 155
Cdd:cd19093 80 LPWRLTRRSVVKALKASLERLGLDSIDLYQLHW-PGPWYSQIEALMDglaDAVEEGLVRAVGVSNYSADQLRRAHKAlkE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 156 YGEECACDQNLYNLANRGMD-HDLMPWLRDHHIPLMAYSPLGDG---G-------PAGTRVMVNN-----------TEVK 213
Cdd:cd19093 159 RGVPLASNQVEYSLLYRDPEqNGLLPACDELGITLIAYSPLAQGlltGkyspenpPPGGRRRLFGrknlekvqpllDALE 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1233716732 214 KVAARHHASAQQVMLAWCVRDGnTLAIPQSANPEHLVQDFHSGSLELDEHDFAALD 269
Cdd:cd19093 239 EIAEKYGKTPAQVALNWLIAKG-VVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
11-269 |
1.27e-42 |
|
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: 146.34 E-value: 1.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 11 MPVIGAGLWGIGEGIDAHAQRRALDAAFDAglvlLDTAEMYGNgasERVAGAAARSARAQGKDVFVVSKVLPSNARPQLM 90
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRH----IDTAQIYDN---EAAVGQAIAESGVPRDELFITTKIWIDNLSKDKL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 91 RTALTRSLHNLGLDYLDMYLLHWRSTAD---LALVAQQMHEFVQEGLIRHWGVSNFDVADMQELLAVPYGEECACDQ--- 164
Cdd:cd19139 74 LPSLEESLEKLRTDYVDLTLIHWPSPNDevpVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVGAGAIATNQiel 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 165 NLYnLANRGmdhdLMPWLRDHHIPLMAYSPLGDGgpagtRVMVNNTeVKKVAARHHASAQQVMLAWCVRDGnTLAIPQSA 244
Cdd:cd19139 154 SPY-LQNRK----LVAHCKQHGIHVTSYMTLAYG-----KVLDDPV-LAAIAERHGATPAQIALAWAMARG-YAVIPSST 221
|
250 260
....*....|....*....|....*
gi 1233716732 245 NPEHLVQDFHSGSLELDEHDFAALD 269
Cdd:cd19139 222 KREHLRSNLLALDLTLDADDMAAIA 246
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
8-270 |
2.48e-42 |
|
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: 145.48 E-value: 2.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGAGLWGIgEGIDAHaqrRALDAAFDAGLVLLDTAEMYGNgasERVAGAAARSARAQGKDVFVVSKVLPSNARP 87
Cdd:cd19140 5 GVRIPALGLGTYPL-TGEECT---RAVEHALELGYRHIDTAQMYGN---EAQVGEAIAASGVPRDELFLTTKVWPDNYSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 88 QLMRTALTRSLHNLGLDYLDMYLLHW-RSTADLALVAQQMHEFVQEGLIRHWGVSNFDVADMQEllAVPYGEE-CACDQN 165
Cdd:cd19140 78 DDFLASVEESLRKLRTDYVDLLLLHWpNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLRE--AVELSEApLFTNQV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 166 LYN--LANRgmdhDLMPWLRDHHIPLMAYSPLGDGgpagtRVMvNNTEVKKVAARHHASAQQVMLAWCVRDGNTLAIPQS 243
Cdd:cd19140 156 EYHpyLDQR----KLLDAAREHGIALTAYSPLARG-----EVL-KDPVLQEIGRKHGKTPAQVALRWLLQQEGVAAIPKA 225
|
250 260
....*....|....*....|....*..
gi 1233716732 244 ANPEHLVQDFHSGSLELDEHDFAALDS 270
Cdd:cd19140 226 TNPERLEENLDIFDFTLSDEEMARIAA 252
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
8-270 |
5.91e-40 |
|
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: 140.50 E-value: 5.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGAGLWGigeGIDAHAQRRALDAAFDAGLVLLDTAEMYGNgasERVAGAAARSARAQG----KDVFVVSKVLPS 83
Cdd:cd19116 8 GNEIPAIALGTWK---LKDDEGVRQAVKHAIEAGYRHIDTAYLYGN---EAEVGEAIREKIAEGvvkrEDLFITTKLWNS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 84 NARPQLMRTALTRSLHNLGLDYLDMYLLHW---------------RSTADLALVA--QQMHEFVQEGLIRHWGVSNFDVA 146
Cdd:cd19116 82 YHEREQVEPALRESLKRLGLDYVDLYLIHWpvafkenndsesngdGSLSDIDYLEtwRGMEDLVKLGLTRSIGVSNFNSE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 147 DMQELLA----VPYGEECACDQNLYNLanrgmdhDLMPWLRDHHIPLMAYSPLG----DGGPAGTRVMvNNTEVKKVAAR 218
Cdd:cd19116 162 QINRLLSncniKPAVNQIEVHPTLTQE-------KLVAYCQSNGIVVMAYSPFGrlvpRGQTNPPPRL-DDPTLVAIAKK 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1233716732 219 HHASAQQVMLAWCVrDGNTLAIPQSANPEHLVQDFHSGSLELDEHDFAALDS 270
Cdd:cd19116 234 YGKTTAQIVLRYLI-DRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNS 284
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
11-261 |
2.23e-39 |
|
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: 138.12 E-value: 2.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 11 MPVIGAGLWGIGEgiDAHAQRRALDAAFDAGLVLLDTAEMYGNGASERVAGAAARSAraqGKDVFVVSKV---------L 81
Cdd:cd19088 9 MRLTGPGIWGPPA--DREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHPY---PDDVVIATKGglvrtgpgwW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 82 PSNARPQLMRTALTRSLHNLGLDYLDMYLLHWRSTA-DLALVAQQMHEFVQEGLIRHWGVSNFDVADMQELLAVPygeEC 160
Cdd:cd19088 84 GPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKvPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAIV---RI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 161 ACDQNLYNLANRGmDHDLMPWLRDHHIPLMAYSPLGDGGPAGtrvmvNNTEVKKVAARHHASAQQVMLAWCVRDG-NTLA 239
Cdd:cd19088 161 VSVQNRYNLANRD-DEGVLDYCEAAGIAFIPWFPLGGGDLAQ-----PGGLLAEVAARLGATPAQVALAWLLARSpVMLP 234
|
250 260
....*....|....*....|..
gi 1233716732 240 IPQSANPEHLVQDFHSGSLELD 261
Cdd:cd19088 235 IPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
8-270 |
2.31e-38 |
|
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: 135.39 E-value: 2.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGAGLWGIGEGIDAhaqRRALDAAFDAGLVLLDTAEMYGNgasERVAGAAARSARAQGKDVFVVSKVLPSNARP 87
Cdd:cd19133 6 GVEMPILGFGVFQIPDPEEC---ERAVLEAIKAGYRLIDTAAAYGN---EEAVGRAIKKSGIPREELFITTKLWIQDAGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 88 QLMRTALTRSLHNLGLDYLDMYLLH---------WRStadlalvaqqMHEFVQEGLIRHWGVSNFDVADMQELLA----V 154
Cdd:cd19133 80 EKAKKAFERSLKRLGLDYLDLYLIHqpfgdvygaWRA----------MEELYKEGKIRAIGVSNFYPDRLVDLILhnevK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 155 PygeecACDQ---NLYNlanrgMDHDLMPWLRDHHIPLMAYSPLGDGGPAgtrvMVNNTEVKKVAARHHASAQQVMLAWC 231
Cdd:cd19133 150 P-----AVNQietHPFN-----QQIEAVEFLKKYGVQIEAWGPFAEGRNN----LFENPVLTEIAEKYGKSVAQVILRWL 215
|
250 260 270
....*....|....*....|....*....|....*....
gi 1233716732 232 VRDGnTLAIPQSANPEHLVQDFHSGSLELDEHDFAALDS 270
Cdd:cd19133 216 IQRG-IVVIPKSVRPERIAENFDIFDFELSDEDMEAIAA 253
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
8-270 |
2.41e-38 |
|
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: 137.02 E-value: 2.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGAGLWGIGEG-----IDAHAQRRALDAAFDAGLVLLDTAEMYGNGASER-----------------------V 59
Cdd:cd19149 8 GIEASVIGLGTWAIGGGpwwggSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEivgkaikgrrdkvvlatkcglrwD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 60 AGAAARSARAQGKDVFvvskvlpSNARPQLMRTALTRSLHNLGLDYLDMYLLHWRS-TADLALVAQQMHEFVQEGLIRHW 138
Cdd:cd19149 88 REGGSFFFVRDGVTVY-------KNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDvETPIEETMEALEELKRQGKIRAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 139 GVSNFDVADMQEllAVPYGeECACDQNLYNLANRGMDHDLMPWLRDHHIPLMAYSPLGDG---GPAG------------- 202
Cdd:cd19149 161 GASNVSVEQIKE--YVKAG-QLDIIQEKYSMLDRGIEKELLPYCKKNNIAFQAYSPLEQGlltGKITpdrefdagdarsg 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1233716732 203 ---------TRVMVNNTEVKKVAARHHASAQQVMLAWCV-RDGNTLAIPQSANPEHLVQDFHSGSLELDEHDFAALDS 270
Cdd:cd19149 238 ipwfspenrEKVLALLEKWKPLCEKYGCTLAQLVIAWTLaQPGITSALCGARKPEQAEENAKAGDIRLSAEDIATMRS 315
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
8-270 |
2.30e-37 |
|
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: 133.78 E-value: 2.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGAGLWGI-GEGIdahaqRRALDAAFDAGLVLLDTAEMYGNgasERVAGAAARSARAQGK----DVFVVSKVLP 82
Cdd:cd19111 1 GFPMPVIGLGTYQSpPEEV-----RAAVDYALFVGYRHIDTALSYQN---EKAIGEALKWWLKNGKlkreEVFITTKLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 83 SNARPQLMRTALTRSLHNLGLDYLDMYLLH--WRST------------ADLALVAQQMHEFVQEGLIRHWGVSNFDVADM 148
Cdd:cd19111 73 VYLEFKDTEKSLEKSLENLKLPYVDLYLIHhpCGFVnkkdkgerelasSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 149 QELLAV----PYGEECACdqNLYNlanrgMDHDLMPWLRDHHIPLMAYSPLGDGG------PAGTRVMVNNTEVKKVAAR 218
Cdd:cd19111 153 NKILAYakvkPSNLQLEC--HAYL-----QQRELRKFCNKKNIVVTAYAPLGSPGranqslWPDQPDLLEDPTVLAIAKE 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1233716732 219 HHASAQQVMLAWCVrDGNTLAIPQSANPEHLVQDFHSGSLELDEHDFAALDS 270
Cdd:cd19111 226 LDKTPAQVLLRFVL-QRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKT 276
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-271 |
1.50e-36 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 132.03 E-value: 1.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 14 IGAGLWGIGEGI-DAHAQRRALDAAFDAGLVLLDTAEMYGNGASERVAGAAARSAraqGKDVFVVSKV--LPSNA----- 85
Cdd:cd19102 11 IGGGGWGGGWGPqDDRDSIAAIRAALDLGINWIDTAAVYGLGHSEEVVGRALKGL---RDRPIVATKCglLWDEEgrirr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 86 --RPQLMRTALTRSLHNLGLDYLDMYLLHWRS-TADLALVAQQMHEFVQEGLIRHWGVSNFDVADMQELLAVpygEECAC 162
Cdd:cd19102 88 slKPASIRAECEASLRRLGVDVIDLYQIHWPDpDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQAI---HPIAS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 163 DQNLYNLANRGMDHDLMPWLRDHHIPLMAYSPLGDG---------------------------GPAGTRVMVNNTEVKKV 215
Cdd:cd19102 165 LQPPYSLLRRGIEAEILPFCAEHGIGVIVYSPMQSGlltgkmtpervaslpaddwrrrspffqEPNLARNLALVDALRPI 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1233716732 216 AARHHASAQQVMLAWCVR-DGNTLAIPQSANPEHLVQDFHSGSLELDEHDFAALDSA 271
Cdd:cd19102 245 AERHGRTVAQLAIAWVLRrPEVTSAIVGARRPDQIDETVGAADLRLTPEELAEIEAL 301
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
8-269 |
2.14e-36 |
|
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: 130.36 E-value: 2.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGAGLWGIGegiDAHAQRrALDAAFDAGLVLLDTAEMYGNgasERVAGAAARSARAQGKDVFVVSKVLPSNARP 87
Cdd:cd19134 8 DNTMPVIGLGVGELS---DDEAER-SVSAALEAGYRLIDTAAAYGN---EAAVGRAIAASGIPRGELFVTTKLATPDQGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 88 QLMRTALTRSLHNLGLDYLDMYLLHWRSTADLALVAQ--QMHEFVQEGLIRHWGVSNFDVADMQELLAVPYgEECACDQ- 164
Cdd:cd19134 81 TASQAACRASLERLGLDYVDLYLIHWPAGREGKYVDSwgGLMKLREEGLARSIGVSNFTAEHLENLIDLTF-FTPAVNQi 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 165 NLYNLANRGMdhdlmpwLRD----HHIPLMAYSPLGDGgpagtrVMVNNTEVKKVAARHHASAQQVMLAWCVRDGNTlAI 240
Cdd:cd19134 160 ELHPLLNQAE-------LRKvnaqHGIVTQAYSPLGVG------RLLDNPAVTAIAAAHGRTPAQVLLRWSLQLGNV-VI 225
|
250 260
....*....|....*....|....*....
gi 1233716732 241 PQSANPEHLVQDFHSGSLELDEHDFAALD 269
Cdd:cd19134 226 SRSSNPERIASNLDVFDFELTADHMDALD 254
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
8-270 |
4.17e-36 |
|
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: 131.11 E-value: 4.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGAGLW-GIGEGIDAhaqrrALDAAFDAGLVLLDTAEMYGNgasERVAGAAARSARAQGK----DVFVVSKVLP 82
Cdd:cd19155 9 GEKMPVVGLGTWqSSPEEIET-----AVDTALEAGYRHIDTAYVYRN---EAAIGNVLKKWIDSGKvkreELFIVTKLPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 83 SNARPQLMRTALTRSLHNLGLDYLDMYLLH-------------WRS---------TADLALVAQQMHEFVQEGLIRHWGV 140
Cdd:cd19155 81 GGNRREKVEKFLLKSLEKLQLDYVDLYLIHfpvgslskeddsgKLDptgehkqdyTTDLLDIWKAMEAQVDQGLTRSIGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 141 SNFDVADMQELLAV----PYGEECACdqNLYnLANRgmdhDLMPWLRDHHIPLMAYSPLGD----------GGPAGTRV- 205
Cdd:cd19155 161 SNFNREQMARILKNarikPANLQVEL--HVY-LQQK----DLVDFCSTHSITVTAYAPLGSpgaahfspgtGSPSGSSPd 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1233716732 206 MVNNTEVKKVAARHHASAQQVMLAWCVRDGnTLAIPQSANPEHLVQDFHSGSLELDEHDFAALDS 270
Cdd:cd19155 234 LLQDPVVKAIAERHGKSPAQVLLRWLMQRG-VVVIPKSTNAARIKENFQVFDFELTEADMAKLSS 297
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
8-270 |
6.38e-35 |
|
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: 127.53 E-value: 6.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGAGLWGIGEgidaHAQRRALDAAFDAGLVLLDTAEMYGNgasERVAGAAARSARAQGK----DVFVVSKVLPS 83
Cdd:cd19154 9 GVKMPLIGLGTWQSKG----AEGITAVRTALKAGYRLIDTAFLYQN---EEAIGEALAELLEEGVvkreDLFITTKLWTH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 84 NARPQLMRTALTRSLHNLGLDYLDMYLLH--W------------------RSTADLALVAQQMHEFVQEGLIRHWGVSNF 143
Cdd:cd19154 82 EHAPEDVEEALRESLKKLQLEYVDLYLIHapAafkddegesgtmengmsiHDAVDVEDVWRGMEKVYDEGLTKAIGVSNF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 144 DVADMQELLAV----PYGEECACdqNLYNlanrgMDHDLMPWLRDHHIPLMAYSPLG---------DGGPAGTRVMVNNT 210
Cdd:cd19154 162 NNDQIQRILDNarvkPHNNQVEC--HLYF-----PQKELVEFCKKHNISVTSYATLGspgranftkSTGVSPAPNLLQDP 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 211 EVKKVAARHHASAQQVMLAWCVRDGnTLAIPQSANPEHLVQDFHSGSLELDEHDFAALDS 270
Cdd:cd19154 235 IVKAIAEKHGKTPAQVLLRYLLQRG-IAVIPKSATPSRIKENFNIFDFSLSEEDMATLEE 293
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
8-269 |
7.56e-35 |
|
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: 126.01 E-value: 7.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGAGLWGIGEGIDAhaqRRALDAAFDAGLVLLDTAEMYGNgasERVAGAAARSARAQGKDVFVVSKVLPSNARP 87
Cdd:cd19126 6 GTRMPWLGLGVFQTPDGDET---ERAVQTALENGYRSIDTAAIYKN---EEGVGEAIRESGVPREELFVTTKLWNDDQRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 88 QLMRTALTRSLHNLGLDYLDMYLLHWRSTADLALVAQQMHEFVQEGLIRHWGVSNFDVADMQELLA----VPygeecACD 163
Cdd:cd19126 80 RRTEDAFQESLDRLGLDYVDLYLIHWPGKDKFIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAhadvVP-----AVN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 164 QNLYN--LANRgmdhDLMPWLRDHHIPLMAYSPLGDGGpagtrvMVNNTEVKKVAARHHASAQQVMLAWCVRDGnTLAIP 241
Cdd:cd19126 155 QVEFHpyLTQK----ELRGYCKSKGIVVEAWSPLGQGG------LLSNPVLAAIGEKYGKSAAQVVLRWDIQHG-VVTIP 223
|
250 260
....*....|....*....|....*...
gi 1233716732 242 QSANPEHLVQDFHSGSLELDEHDFAALD 269
Cdd:cd19126 224 KSVHASRIKENADIFDFELSEDDMTAID 251
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
8-268 |
1.17e-34 |
|
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: 125.56 E-value: 1.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGAGLWGIGegiDAHAqRRALDAAFDAGLVLLDTAEMYGNgasERVAGAAARSARAQGKDVFVVSKVLPSNARP 87
Cdd:cd19131 7 GNTIPQLGLGVWQVS---NDEA-ASAVREALEVGYRSIDTAAIYGN---EEGVGKAIRASGVPREELFITTKLWNSDQGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 88 QLMRTALTRSLHNLGLDYLDMYLLHWRSTADLALVA--QQMHEFVQEGLIRHWGVSNFDVADMQELL----AVPygeecA 161
Cdd:cd19131 80 DSTLRAFDESLRKLGLDYVDLYLIHWPVPAQDKYVEtwKALIELKKEGRVKSIGVSNFTIEHLQRLIdetgVVP-----V 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 162 CDQnlYNLANRGMDHDLMPWLRDHHIPLMAYSPLGDGGpagtrvMVNNTEVKKVAARHHASAQQVMLAWCVRDGNtLAIP 241
Cdd:cd19131 155 VNQ--IELHPRFQQRELRAFHAKHGIQTESWSPLGQGG------LLSDPVIGEIAEKHGKTPAQVVIRWHLQNGL-VVIP 225
|
250 260
....*....|....*....|....*..
gi 1233716732 242 QSANPEHLVQDFHSGSLELDEHDFAAL 268
Cdd:cd19131 226 KSVTPSRIAENFDVFDFELDADDMQAI 252
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
8-270 |
4.53e-34 |
|
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: 124.36 E-value: 4.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGAGLWGIGeGIDAHAQRRALDaafDAGLVLLDTAEMYGNgasERVAGAAARSARAQGKDVFVVSKVLPSNARP 87
Cdd:cd19135 10 GVEMPILGLGTSHSG-GYSHEAVVYALK---ECGYRHIDTAKRYGC---EELLGKAIKESGVPREDLFLTTKLWPSDYGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 88 QLMRTALTRSLHNLGLDYLDMYLLHWRSTAD--------LALVAQQMHEFVQEGLIRHWGVSNFDVADMQELLavpygEE 159
Cdd:cd19135 83 ESTKQAFEASLKRLGVDYLDLYLLHWPDCPSsgknvketRAETWRALEELYDEGLCRAIGVSNFLIEHLEQLL-----ED 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 160 CA----CDQNLYNLANRGMdhDLMPWLRDHHIPLMAYSPLGDGGPagtrvmVNNTEVKKVAARHHASAQQVMLAWCVRDG 235
Cdd:cd19135 158 CSvvphVNQVEFHPFQNPV--ELIEYCRDNNIVFEGYCPLAKGKA------LEEPTVTELAKKYQKTPAQILIRWSIQNG 229
|
250 260 270
....*....|....*....|....*....|....*
gi 1233716732 236 nTLAIPQSANPEHLVQDFHSGSLELDEHDFAALDS 270
Cdd:cd19135 230 -VVTIPKSTKEERIKENCQVFDFSLSEEDMATLDS 263
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
8-270 |
6.94e-34 |
|
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: 124.38 E-value: 6.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGAGLWGIGEGIDAHAqrraLDAAFDAGLVLLDTAEMYGNgasERVAGAAARSARAQG----KDVFVVSKVLPS 83
Cdd:cd19125 8 GAKIPAVGLGTWQADPGVVGNA----VKTAIKEGYRHIDCAAIYGN---EKEIGKALKKLFEDGvvkrEDLFITSKLWCT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 84 NARPQLMRTALTRSLHNLGLDYLDMYLLHW---------RSTA------DLALVAQQMHEFVQEGLIRHWGVSNFDVADM 148
Cdd:cd19125 81 DHAPEDVPPALEKTLKDLQLDYLDLYLIHWpvrlkkgahMPEPeevlppDIPSTWKAMEKLVDSGKVRAIGVSNFSVKKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 149 QELLAV----PygeecACDQNLYNLANRgmDHDLMPWLRDHHIPLMAYSPLGDGG-PAGTRVMVNNTEVKKVAARHHASA 223
Cdd:cd19125 161 EDLLAVarvpP-----AVNQVECHPGWQ--QDKLHEFCKSKGIHLSAYSPLGSPGtTWVKKNVLKDPIVTKVAEKLGKTP 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1233716732 224 QQVMLAWCVRDGNTLaIPQSANPEHLVQDFHSGSLELDEHDFAALDS 270
Cdd:cd19125 234 AQVALRWGLQRGTSV-LPKSTNEERIKENIDVFDWSIPEEDFAKFSS 279
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
8-269 |
7.94e-34 |
|
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: 123.53 E-value: 7.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGAGLWGIgegiDAHAQRRALDAAFDAGLVLLDTAEMYGNgasERVAGAAARSARAQGKDVFVVSKVLPSNARP 87
Cdd:cd19132 4 GTQIPAIGFGTYPL----KGDEGVEAVVAALQAGYRLLDTAFNYEN---EGAVGEAVRRSGVPREELFVTTKLPGRHHGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 88 QLMRTALTRSLHNLGLDYLDMYLLHW-RSTADLALVA-QQMHEFVQEGLIRHWGVSNFdVADMQELLAVPYGEECACDQN 165
Cdd:cd19132 77 EEALRTIEESLYRLGLDYVDLYLIHWpNPSRDLYVEAwQALIEAREEGLVRSIGVSNF-LPEHLDRLIDETGVTPAVNQI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 166 -LYNLANRgmdHDLMPWLRDHHIPLMAYSPLGdggpAGTRVMVNNTeVKKVAARHHASAQQVMLAWCVRDGnTLAIPQSA 244
Cdd:cd19132 156 eLHPYFPQ---AEQRAYHREHGIVTQSWSPLG----RGSGLLDEPV-IKAIAEKHGKTPAQVVLRWHVQLG-VVPIPKSA 226
|
250 260
....*....|....*....|....*
gi 1233716732 245 NPEHLVQDFHSGSLELDEHDFAALD 269
Cdd:cd19132 227 NPERQRENLAIFDFELSDEDMAAIA 251
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
8-269 |
1.52e-33 |
|
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: 123.68 E-value: 1.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGAGLWGIGEGidahAQRRALDAAFDAGLVLLDTAEMYGNgASERVAGAAARSARAQG---KDVFVVSKVLPSN 84
Cdd:cd19118 4 GNKIPAIGLGTWQAEPG----EVGAAVKIALKAGYRHLDLAKVYQN-QHEVGQALKELLKEEPGvkrEDLFITSKLWNNS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 85 ARPQLMRTALTRSLHNLGLDYLDMYLLHW----RSTAD-------------------LALVA--QQMHEFVQEGLIRHWG 139
Cdd:cd19118 79 HRPEYVEPALDDTLKELGLDYLDLYLIHWpvafKPTGDlnpltavptnggevdldlsVSLVDtwKAMVELKKTGKVKSIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 140 VSNFDVADMQELLAVPyGEECACDQNLYnlanrgmdHDLMPW--LRDHH----IPLMAYSPLGdGGPAGTRVMVNNTEVK 213
Cdd:cd19118 159 VSNFSIDHLQAIIEET-GVVPAVNQIEA--------HPLLLQdeLVDYCksknIHITAYSPLG-NNLAGLPLLVQHPEVK 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1233716732 214 KVAARHHASAQQVMLAWCVRDGNTLaIPQSANPEHLVQDFHsgSLELDEHDFAALD 269
Cdd:cd19118 229 AIAAKLGKTPAQVLIAWGIQRGHSV-IPKSVTPSRIRSNFE--QVELSDDEFNAVT 281
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
13-249 |
1.09e-32 |
|
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: 119.89 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 13 VIGAGLWGIGEGI-----DAHAqRRALDAAFDAGLVLLDTAEMYGNGASERVAgaaarsaraqGK-------DVFVVSKV 80
Cdd:cd19086 5 EIGFGTWGLGGDWwgdvdDAEA-IRALRAALDLGINFFDTADVYGDGHSERLL----------GKalkgrrdKVVIATKF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 81 ---------LPSNARPQLMRTALTRSLHNLGLDYLDMYLLH--WRSTADLALVAQQMHEFVQEGLIRHWGVSnfdVADMQ 149
Cdd:cd19086 74 gnrfdggpeRPQDFSPEYIREAVEASLKRLGTDYIDLYQLHnpPDEVLDNDELFEALEKLKQEGKIRAYGVS---VGDPE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 150 ELLAVPYGEECACDQNLYNLANRGMDHDLMPWLRDHHIPLMAYSPLGDGGPAGTRVmvnntevkkvaarhhasaqQVMLA 229
Cdd:cd19086 151 EALAALRRGGIDVVQVIYNLLDQRPEEELFPLAEEHGVGVIARVPLASGLLTGKLA-------------------QAALR 211
|
250 260
....*....|....*....|.
gi 1233716732 230 WCV-RDGNTLAIPQSANPEHL 249
Cdd:cd19086 212 FILsHPAVSTVIPGARSPEQV 232
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
3-271 |
2.58e-32 |
|
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: 121.18 E-value: 2.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 3 TLSFAGREmpvigaGLWGIGEGIDAHAQRRALDAAFDAGLVLLDTAEMYGNGASERVAgaaarsaraqGK-------DVF 75
Cdd:cd19091 20 TMTFGGGG------GFFGAWGGVDQEEADRLVDIALDAGINFFDTADVYSEGESEEIL----------GKalkgrrdDVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 76 VVSKVL------PSN---ARPQLMRtALTRSLHNLGLDYLDMYLLH-WRSTADLALVAQQMHEFVQEGLIRHWGVSNFDV 145
Cdd:cd19091 84 IATKVRgrmgegPNDvglSRHHIIR-AVEASLKRLGTDYIDLYQLHgFDALTPLEETLRALDDLVRQGKVRYIGVSNFSA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 146 ADMQELLAVP--YG-EECACDQNLYNLANRGMDHDLMPWLRDHHIPLMAYSPLGDG-----------GPAGTR------- 204
Cdd:cd19091 163 WQIMKALGISerRGlARFVALQAYYSLLGRDLEHELMPLALDQGVGLLVWSPLAGGllsgkyrrgqpAPEGSRlrrtgfd 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1233716732 205 -VMVNNT-------EVKKVAARHHASAQQVMLAWCV-RDGNTLAIPQSANPEHLVQDFHSGSLELDEHDFAALDSA 271
Cdd:cd19091 243 fPPVDRErgydvvdALREIAKETGATPAQVALAWLLsRPTVSSVIIGARNEEQLEDNLGAAGLSLTPEEIARLDKV 318
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
6-270 |
5.45e-32 |
|
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: 119.80 E-value: 5.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 6 FAGREMPVIGAGLWGIGEGidahAQRRALDAAFDAGLVLLDTAEMYGNGAS--ERVAGAAARSARAQGKDVFVVSKVLPS 83
Cdd:cd19106 2 HTGQKMPLIGLGTWKSKPG----QVKAAVKYALDAGYRHIDCAAVYGNEQEvgEALKEKVGPGKAVPREDLFVTSKLWNT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 84 NARPQLMRTALTRSLHNLGLDYLDMYLLHW--------------------RSTADLALVAQQMHEFVQEGLIRHWGVSNF 143
Cdd:cd19106 78 KHHPEDVEPALRKTLKDLQLDYLDLYLIHWpyafergdnpfpknpdgtirYDSTHYKETWKAMEKLVDKGLVKAIGLSNF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 144 DVADMQELLAV----PYGEECACDQNLYNlanrgmdHDLMPWLRDHHIPLMAYSPLGDGGPA----GTRVMVNNTEVKKV 215
Cdd:cd19106 158 NSRQIDDILSVarikPAVLQVECHPYLAQ-------NELIAHCKARGLVVTAYSPLGSPDRPwakpDEPVLLEEPKVKAL 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1233716732 216 AARHHASAQQVMLAWCVRDGnTLAIPQSANPEHLVQDFHSGSLELDEHDFAALDS 270
Cdd:cd19106 231 AKKYNKSPAQILLRWQVQRG-VVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDA 284
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
8-249 |
7.55e-32 |
|
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: 119.20 E-value: 7.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGAGLWGIGE-GIDAHAQRRALDAAFDAGLVLLDTAEMYGNGASERVAGAAARSARAQGKDVFVVSK---VLPS 83
Cdd:cd19092 3 GLEVSRLVLGCMRLADwGESAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPGLREKIEIQTKcgiRLGD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 84 NARPQL----------MRTALTRSLHNLGLDYLDMYLLHwRSTA--DLALVAQQMHEFVQEGLIRHWGVSNFDVADMqEL 151
Cdd:cd19092 83 DPRPGRikhydtskehILASVEGSLKRLGTDYLDLLLLH-RPDPlmDPEEVAEAFDELVKSGKVRYFGVSNFTPSQI-EL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 152 LAVPYGEECACDQNLYNLANRGMDHD-LMPWLRDHHIPLMAYSPLGDG---GPAGTRVMVNNTEVKKVAARHHASAQQVM 227
Cdd:cd19092 161 LQSYLDQPLVTNQIELSLLHTEAIDDgTLDYCQLLDITPMAWSPLGGGrlfGGFDERFQRLRAALEELAEEYGVTIEAIA 240
|
250 260
....*....|....*....|...
gi 1233716732 228 LAWCVRD-GNTLAIPQSANPEHL 249
Cdd:cd19092 241 LAWLLRHpARIQPILGTTNPERI 263
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
1-249 |
1.68e-31 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 118.33 E-value: 1.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 1 MKTLSFA--GREMPVIGAGLWGIGEGiDAHAQ--RRALDAAFDAGLVLLDTAEMYGNGASERVAGAAARSARAQGKDVFV 76
Cdd:COG4989 1 MKRIKLGasGLSVSRIVLGCMRLGEW-DLSPAeaAALIEAALELGITTFDHADIYGGYTCEALFGEALKLSPSLREKIEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 77 VSK---VLPSNARPQLM----------RTALTRSLHNLGLDYLDMYLLHWRST-ADLALVAQQMHEFVQEGLIRHWGVSN 142
Cdd:COG4989 80 QTKcgiRLPSEARDNRVkhydtskehiIASVEGSLRRLGTDYLDLLLLHRPDPlMDPEEVAEAFDELKASGKVRHFGVSN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 143 FDVADMqELLavpygeECACDQNL------YNLANRGM-DHDLMPWLRDHHIPLMAYSPLGDG---GPAGTRVMVNNTEV 212
Cdd:COG4989 160 FTPSQF-ELL------QSALDQPLvtnqieLSLLHTDAfDDGTLDYCQLNGITPMAWSPLAGGrlfGGFDEQFPRLRAAL 232
|
250 260 270
....*....|....*....|....*....|....*...
gi 1233716732 213 KKVAARHHASAQQVMLAWCVR-DGNTLAIPQSANPEHL 249
Cdd:COG4989 233 DELAEKYGVSPEAIALAWLLRhPAGIQPVIGTTNPERI 270
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
2-269 |
2.05e-31 |
|
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: 117.62 E-value: 2.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 2 KTLSfAGREMPVIGAGLWGIGEGIDAhaqRRALDAAFDAGLVLLDTAEMYGNgasERVAGAAARSARAQGKDVFVVSKVL 81
Cdd:cd19156 1 VKLA-NGVEMPRLGLGVWRVQDGAEA---ENAVKWAIEAGYRHIDTAAIYKN---EEGVGQGIRESGVPREEVFVTTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 82 PSNARPQLMRTALTRSLHNLGLDYLDMYLLHWRSTADLALVAQQMHEFVQEGLIRHWGVSNFDVADMQELLavpygEECA 161
Cdd:cd19156 74 NSDQGYESTLAAFEESLEKLGLDYVDLYLIHWPVKGKFKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELL-----KSCK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 162 ----CDQ-NLYNLANRgmdHDLMPWLRDHHIPLMAYSPLGDGGpagtrvMVNNTEVKKVAARHHASAQQVMLAWCVRDGn 236
Cdd:cd19156 149 vapmVNQiELHPLLTQ---EPLRKFCKEKNIAVEAWSPLGQGK------LLSNPVLKAIGKKYGKSAAQVIIRWDIQHG- 218
|
250 260 270
....*....|....*....|....*....|...
gi 1233716732 237 TLAIPQSANPEHLVQDFHSGSLELDEHDFAALD 269
Cdd:cd19156 219 IITIPKSVHEERIQENFDVFDFELTAEEIRQID 251
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
12-268 |
3.46e-31 |
|
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), also called aldehyde reductase, is the prototype of this family. It catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
Pssm-ID: 381354 [Multi-domain] Cd Length: 277 Bit Score: 117.24 E-value: 3.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 12 PVIGAGLWGIGEGIDahaqRRALDAAFDAGLVLLDTAEMYGNGAS-ERVAGAAARSARAQGKDVFVVSKVLPSNARPQLM 90
Cdd:cd19128 2 PRLGFGTYKITESES----KEAVKNAIKAGYRHIDCAYYYGNEAFiGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 91 RTALTRSLHNLGLDYLDMYLLHWR--------------------STADLALVAQQMHEFVQEGLIRHWGVSNFDVADMQE 150
Cdd:cd19128 78 KEQLLITLQDLQLEYLDLFLIHWPlafdmdtdgdprddnqiqslSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 151 LLAV----PYGEECACDQNLYNLAnrgmdhdLMPWLRDHHIPLMAYSPLGDGGPAGTRVMVNNTEVKKVAARHHASAQQV 226
Cdd:cd19128 158 LLNYckikPFMNQIECHPYFQNDK-------LIKFCIENNIHVTAYRPLGGSYGDGNLTFLNDSELKALATKYNTTPPQV 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1233716732 227 MLAWCVR--DGNTLAIPQSANPEHLVQDFHSGSLELDEHDFAAL 268
Cdd:cd19128 231 IIAWHLQkwPKNYSVIPKSANKSRCQQNFDINDLALTKEDMDAI 274
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
7-264 |
1.88e-29 |
|
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: 112.75 E-value: 1.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 7 AGREMPVIGAGlwGIGEGIDAHAQRRALDAAFDAGLVLLDTAEMYGngaSERVAGAAARSARAQG-----KDVFVVSKVL 81
Cdd:cd19124 1 SGQTMPVIGMG--TASDPPSPEDIKAAVLEAIEVGYRHFDTAAAYG---TEEALGEALAEALRLGlvksrDELFVTSKLW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 82 PSNARPQLMRTALTRSLHNLGLDYLDMYLLHW--RSTA---------------DLALVAQQMHEFVQEGLIRHWGVSNFD 144
Cdd:cd19124 76 CSDAHPDLVLPALKKSLRNLQLEYVDLYLIHWpvSLKPgkfsfpieeedflpfDIKGVWEAMEECQRLGLTKAIGVSNFS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 145 VADMQELLAV----PygeecACDQNLYNLAnrgmdhdlmpW----LRD----HHIPLMAYSPLGDGG-PAGTRVMVNNTE 211
Cdd:cd19124 156 CKKLQELLSFatipP-----AVNQVEMNPA----------WqqkkLREfckaNGIHVTAYSPLGAPGtKWGSNAVMESDV 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1233716732 212 VKKVAARHHASAQQVMLAWCVRDGNTLaIPQSANPEHLVQDFHSGSLELDEHD 264
Cdd:cd19124 221 LKEIAAAKGKTVAQVSLRWVYEQGVSL-VVKSFNKERMKQNLDIFDWELTEED 272
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
10-273 |
4.49e-29 |
|
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: 112.36 E-value: 4.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 10 EMPVIGAGLWGIGEGidahAQRRALDAAFDAGLVLLDTAEMYGNgasERVAGAAARSARAQG----KDVFVVSKVLPSNA 85
Cdd:cd19110 3 DIPAVGLGTWKASPG----EVTEAVKVAIDAGYRHFDCAYLYHN---ESEVGAGIREKIKEGvvrrEDLFIVSKLWCTCH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 86 RPQLMRTALTRSLHNLGLDYLDMYLLHW--------------------RSTADLALVAQQMHEFVQEGLIRHWGVSNFDV 145
Cdd:cd19110 76 KKSLVKTACTRSLKALKLNYLDLYLIHWpmgfkpgepdlpldrsgmviPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 146 ADMQELL------AVPYGEECACDQNLynlanrgMDHDLMPWLRDHHIPLMAYSPLgdGGPAGTRVMVNNTEVKKVAARH 219
Cdd:cd19110 156 EQLERLLnkpglrVKPVTNQIECHPYL-------TQKKLISFCQSRNVSVTAYRPL--GGSCEGVDLIDDPVIQRIAKKH 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1233716732 220 HASAQQVMLAWCVRDgNTLAIPQSANPEHLVQDFHSGSLELDEHDFA---ALD-----SAFP 273
Cdd:cd19110 227 GKSPAQILIRFQIQR-NVIVIPKSVTPSRIKENIQVFDFELTEHDMDnllSLDrnlrlATFP 287
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
2-270 |
7.25e-29 |
|
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: 111.05 E-value: 7.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 2 KTLSF-AGREMPVIGAGLWGIGEGIDAHAqrraLDAAFDAGLVLLDTAEMYGNgasERVAGAAARSARAQGKDVFVVSKV 80
Cdd:cd19117 4 KTFKLnTGAEIPAVGLGTWQSKPNEVAKA----VEAALKAGYRHIDTAAIYGN---EEEVGQGIKDSGVPREEIFITTKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 81 LPS-NARPQlmrTALTRSLHNLGLDYLDMYLLHWRSTADLALVA----------------------QQMHEFVQEGLIRH 137
Cdd:cd19117 77 WCTwHRRVE---EALDQSLKKLGLDYVDLYLMHWPVPLDPDGNDflfkkddgtkdhepdwdfiktwELMQKLPATGKVKA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 138 WGVSNFDVADMQELLA------VPYGEECACDQNLynlanrgMDHDLMPWLRDHHIPLMAYSPLGD-GGPagtrvMVNNT 210
Cdd:cd19117 154 IGVSNFSIKNLEKLLAspsakiVPAVNQIELHPLL-------PQPKLVDFCKSKGIHATAYSPLGStNAP-----LLKEP 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 211 EVKKVAARHHASAQQVMLAWCVRDGnTLAIPQSANPEHLVQDFHsgSLELDEHDFAALDS 270
Cdd:cd19117 222 VIIKIAKKHGKTPAQVIISWGLQRG-YSVLPKSVTPSRIESNFK--LFTLSDEEFKEIDE 278
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
14-269 |
9.52e-28 |
|
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: 108.84 E-value: 9.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 14 IGAGLWGIGEGIDAHAQRRALDAAFDAGLVLLDTAEMYG-------NGASErvaGAAARSARAQGK--DVFVVSKV--LP 82
Cdd:cd19081 12 LCLGTMVFGWTADEETSFALLDAFVDAGGNFIDTADVYSawvpgnaGGESE---TIIGRWLKSRGKrdRVVIATKVgfPM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 83 SNARPQL----MRTALTRSLHNLGLDYLDMYLLHWRSTA-DLALVAQQMHEFVQEGLIRHWGVSNFDVADMQELLAVPYG 157
Cdd:cd19081 89 GPNGPGLsrkhIRRAVEASLRRLQTDYIDLYQAHWDDPAtPLEETLGALNDLIRQGKVRYIGASNYSAWRLQEALELSRQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 158 EECA---CDQNLYNLANRGM-DHDLMPWLRDHHIPLMAYSPLGDG--------------------------GPAGTRVMv 207
Cdd:cd19081 169 HGLPryvSLQPEYNLVDRESfEGELLPLCREEGIGVIPYSPLAGGfltgkyrseadlpgstrrgeaakrylNERGLRIL- 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1233716732 208 nnTEVKKVAARHHASAQQVMLAWCV-RDGNTLAIPQSANPEHLVQDFHSGSLELDEHDFAALD 269
Cdd:cd19081 248 --DALDEVAAEHGATPAQVALAWLLaRPGVTAPIAGARTVEQLEDLLAAAGLRLTDEEVARLD 308
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
8-270 |
1.25e-27 |
|
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: 107.48 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGAGLWGIGEGIDAhaqRRALDAAFDAGLVLLDTAEMYGNgasERVAGAAARSARAQGKDVFVVSKVLPSNARP 87
Cdd:cd19157 7 GVKMPWLGLGVFKVEEGSEV---VNAVKTALKNGYRSIDTAAIYGN---EEGVGKGIKESGIPREELFITSKVWNADQGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 88 QLMRTALTRSLHNLGLDYLDMYLLHWRSTADLALVAQQMHEFVQEGLIRHWGVSNFDVADMQELLAVPygeECACDQNLY 167
Cdd:cd19157 81 DSTLKAFEASLERLGLDYLDLYLIHWPVKGKYKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADA---EIVPMVNQV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 168 NLANRGMDHDLMPWLRDHHIPLMAYSPLGDGGpagtrvMVNNTEVKKVAARHHASAQQVMLAWCVRDGnTLAIPQSANPE 247
Cdd:cd19157 158 EFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQ------LLDNPVLKEIAEKYNKSVAQVILRWDLQNG-VVTIPKSIKEH 230
|
250 260
....*....|....*....|...
gi 1233716732 248 HLVQDFHSGSLELDEHDFAALDS 270
Cdd:cd19157 231 RIIENADVFDFELSQEDMDKIDA 253
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
2-268 |
2.27e-27 |
|
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: 107.69 E-value: 2.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 2 KTLSFAGREMPVIGAGLWGIGE---GIDAHAQRRALDAAFDAGLVLLDTAEMYGNGASERVAgaaarsaraqGK------ 72
Cdd:cd19076 3 RKLGTQGLEVSALGLGCMGMSAfygPADEEESIATLHRALELGVTFLDTADMYGPGTNEELL----------GKalkdrr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 73 -DVFVVSK----------VLPSNARPQLMRTALTRSLHNLGLDYLDMYLLHwRSTADLAL--VAQQMHEFVQEGLIRHWG 139
Cdd:cd19076 73 dEVVIATKfgivrdpgsgFRGVDGRPEYVRAACEASLKRLGTDVIDLYYQH-RVDPNVPIeeTVGAMAELVEEGKVRYIG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 140 VSNFDVADMQELLAV-PygeeCACDQNLYNLANRGMDHDLMPWLRDHHIPLMAYSPLGDGGPAGT--------------- 203
Cdd:cd19076 152 LSEASADTIRRAHAVhP----ITAVQSEYSLWTRDIEDEVLPTCRELGIGFVAYSPLGRGFLTGAikspedlpeddfrrn 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1233716732 204 --RVMVNN--------TEVKKVAARHHASAQQVMLAWCVRDG-NTLAIPQSANPEHLVQDFHSGSLELDEHDFAAL 268
Cdd:cd19076 228 npRFQGENfdknlklvEKLEAIAAEKGCTPAQLALAWVLAQGdDIVPIPGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
24-272 |
2.42e-27 |
|
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: 107.50 E-value: 2.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 24 GIDAHAQRRALDAAFDAGLVLLDTAEMYGNGASE-------RVAGAAARSARAQGKDVFVVSKVLPSNaRPQLMRTALTR 96
Cdd:cd19083 29 NLDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEelvgevlKEYNRNEVVIATKGAHKFGGDGSVLNN-SPEFLRSAVEK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 97 SLHNLGLDYLDMYLLHWRS-TADLALVAQQMHEFVQEGLIRHWGVSNFDVADMQELLAVPYGEECacdQNLYNLANRGMD 175
Cdd:cd19083 108 SLKRLNTDYIDLYYIHFPDgETPKAEAVGALQELKDEGKIRAIGVSNFSLEQLKEANKDGYVDVL---QGEYNLLQREAE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 176 HDLMPWLRDHHIPLMAYSPLGDG-------------------------GPAGTRVMVNNTEVKKVAARHHASAQQVMLAW 230
Cdd:cd19083 185 EDILPYCVENNISFIPYFPLASGllagkytkdtkfpdndlrndkplfkGERFSENLDKVDKLKSIADEKGVTVAHLALAW 264
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1233716732 231 CV-RDGNTLAIPQSANPEHLVQDFHSGSLELDEHDFAALDSAF 272
Cdd:cd19083 265 YLtRPAIDVVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDALF 307
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
8-270 |
2.81e-27 |
|
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; Corynebacterium sp. DkgA is a founding member of aldo-keto reductase family 5 member C1 (AKR5C1). DkgA (EC 1.1.1.346), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates.
Pssm-ID: 381356 [Multi-domain] Cd Length: 256 Bit Score: 106.15 E-value: 2.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGAGLWGIGEGidahAQRRALDAAFDAGLVLLDTAEMYGNgasERVAGAAARSARAQGKDVFVVSKVLPSNARP 87
Cdd:cd19130 7 GNSIPQLGYGVFKVPPA----DTQRAVATALEVGYRHIDTAAIYGN---EEGVGAAIAASGIPRDELFVTTKLWNDRHDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 88 QLMRTALTRSLHNLGLDYLDMYLLHWRSTA--DLALVAQQMHEFVQEGLIRHWGVSNFDVADMqELLAVPYGEECACDQn 165
Cdd:cd19130 80 DEPAAAFAESLAKLGLDQVDLYLVHWPTPAagNYVHTWEAMIELRAAGRTRSIGVSNFLPPHL-ERIVAATGVVPAVNQ- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 166 lYNLANRGMDHDLMPWLRDHHIPLMAYSPLGDGGpagtrvMVNNTEVKKVAARHHASAQQVMLAWCVRDGNTLaIPQSAN 245
Cdd:cd19130 158 -IELHPAYQQRTIRDWAQAHDVKIEAWSPLGQGK------LLGDPPVGAIAAAHGKTPAQIVLRWHLQKGHVV-FPKSVR 229
|
250 260
....*....|....*....|....*
gi 1233716732 246 PEHLVQDFHSGSLELDEHDFAALDS 270
Cdd:cd19130 230 RERMEDNLDVFDFDLTDTEIAAIDA 254
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
37-268 |
1.52e-26 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 104.72 E-value: 1.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 37 AFDAGLVLLDTAEMYGNgasERVAGAAARSARAQGKDVFVVSKVLPSNARPQLMRTALTRSLHNLGLDYLDMYLLHWRST 116
Cdd:PRK11172 25 ALELGYRAIDTAQIYDN---EAAVGQAIAESGVPRDELFITTKIWIDNLAKDKLIPSLKESLQKLRTDYVDLTLIHWPSP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 117 AD---LALVAQQMHEFVQEGLIRHWGVSNFDVADMQELLAVPYGEECACDQ---NLYnLANRgmdhDLMPWLRDHHIPLM 190
Cdd:PRK11172 102 NDevsVEEFMQALLEAKKQGLTREIGISNFTIALMKQAIAAVGAENIATNQielSPY-LQNR----KVVAFAKEHGIHVT 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1233716732 191 AYSPLGDGGPAGTRVMvnntevKKVAARHHASAQQVMLAWCVRDGNTLaIPQSANPEHLVQDFHSGSLELDEHDFAAL 268
Cdd:PRK11172 177 SYMTLAYGKVLKDPVI------ARIAAKHNATPAQVILAWAMQLGYSV-IPSSTKRENLASNLLAQDLQLDAEDMAAI 247
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
22-273 |
3.04e-26 |
|
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: 104.58 E-value: 3.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 22 GEGIDAHAQRRALDAAFDAGLVLLDTAEMYGNGASERVAgaaarsaraqGK-------DVFVVSKV-LPSNARPQLM--- 90
Cdd:cd19087 24 GGRTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEII----------GRwiagrrdDIVLATKVfGPMGDDPNDRgls 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 91 ----RTALTRSLHNLGLDYLDMYLLH-WRSTADLALVAQQMHEFVQEGLIRHWGVSNF---DVADMQELLAVPYGEECAC 162
Cdd:cd19087 94 rrhiRRAVEASLRRLQTDYIDLYQMHhFDRDTPLEETLRALDDLVRQGKIRYIGVSNFaawQIAKAQGIAARRGLLRFVS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 163 DQNLYNLANRGMDHDLMPWLRDHHIPLMAYSPLGDG----------GPAGTRVMVNNTEVKK--------VAARHHASAQ 224
Cdd:cd19087 174 EQPMYNLLKRQAELEILPAARAYGLGVIPYSPLAGGlltgkygkgkRPESGRLVERARYQARygleeyrdIAERFEALAA 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1233716732 225 -------QVMLAWCV-RDGNTLAIPQSANPEHLVQDFHSGSLELDEHDFAALDSAFP 273
Cdd:cd19087 254 eagltpaSLALAWVLsHPAVTSPIIGPRTLEQLEDSLAALEITLTPELLAEIDELFP 310
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
8-269 |
5.21e-26 |
|
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: 103.26 E-value: 5.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGAGLWGIG--EGIDAHAqrraldAAFDAGLVLLDTAEMYGNgasERVAGAAARSARAQGKDVFVVSKVLPSNA 85
Cdd:cd19127 6 GVEMPALGLGVFQTPpeETADAVA------TALADGYRLIDTAAAYGN---EREVGEGIRRSGVDRSDIFVTTKLWISDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 86 RPQLMRTALTRSLHNLGLDYLDMYLLHWRSTADL-ALVA--QQMHEFVQEGLIRHWGVSNFDVADMQELLA----VPyge 158
Cdd:cd19127 77 GYDKALRGFDASLRRLGLDYVDLYLLHWPVPNDFdRTIQayKALEKLLAEGRVRAIGVSNFTPEHLERLIDattvVP--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 159 ecACDQnlYNLANRGMDHDLMPWLRDHHIPLMAYSPLG-------DGGPAGTRVMVNNTeVKKVAARHHASAQQVMLAWC 231
Cdd:cd19127 154 --AVNQ--VELHPYFSQKDLRAFHRRLGIVTQAWSPIGgvmrygaSGPTGPGDVLQDPT-ITGLAEKYGKTPAQIVLRWH 228
|
250 260 270
....*....|....*....|....*....|....*...
gi 1233716732 232 VRDGnTLAIPQSANPEHLVQDFHSGSLELDEHDFAALD 269
Cdd:cd19127 229 LQNG-VSAIPKSVHPERIAENIDIFDFALSAEDMAAID 265
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
25-269 |
7.10e-26 |
|
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: 103.82 E-value: 7.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 25 IDAHAQRRALDAAFDAGLVLLDTAEMYGNGASERVAgaaarsaraqGK---------DVFVVSKVLP-----SNA----R 86
Cdd:cd19079 32 LDEEESRPIIKRALDLGINFFDTANVYSGGASEEIL----------GRalkefaprdEVVIATKVYFpmgdgPNGrglsR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 87 PQLMRtALTRSLHNLGLDYLDMYLLHW--RSTaDLALVAQQMHEFVQEGLIRHWGVSNFDVADMQELLAVP--YG-EECA 161
Cdd:cd19079 102 KHIMA-EVDASLKRLGTDYIDLYQIHRwdYET-PIEETLEALHDVVKSGKVRYIGASSMYAWQFAKALHLAekNGwTKFV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 162 CDQNLYNLANRGMDHDLMPWLRDHHIPLMAYSPLGDGGPAGTRVMVNNTE------------------------VKKVAA 217
Cdd:cd19079 180 SMQNHYNLLYREEEREMIPLCEEEGIGVIPWSPLARGRLARPWGDTTERRrsttdtaklkydyfteadkeivdrVEEVAK 259
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1233716732 218 RHHASAQQVMLAW-CVRDGNTLAIPQSANPEHLVQDFHSGSLELDEHDFAALD 269
Cdd:cd19079 260 ERGVSMAQVALAWlLSKPGVTAPIVGATKLEHLEDAVAALDIKLSEEEIKYLE 312
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
13-198 |
1.22e-25 |
|
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1/AKR7A3/AFAR) from Rattus norvegicus, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR1/AFAR) and aflatoxin B1 aldehyde reductase member 3 (AKR7A3/AFAR2) from Homo sapiens, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR2) from Rattus norvegicus, and aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AKR7A5/AFAR) from Mus musculus, are founding members of aldo-keto reductase family 7 member A1-5 (AKR7A1-5), respectively. AKR7A2 (EC 1.1.1.n11), also called AFB1 aldehyde reductase 1, or AFB1-AR 1, or aldoketoreductase 7, or succinic semialdehyde reductase, or SSA reductase, catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate (GHB). It has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). AKR7A2, AKR7A3 (also called AFB1 aldehyde reductase 2 or AFB1-AR 2), and AKR7A4 (also called AFB1 aldehyde reductase 3, or AFB1-AR 3, or aldoketoreductase 7-like), may be involved in protection of liver against the toxic and carcinogenic effects of aflatoxin B1 (AFB1), a potent hepatocarcinogen. They can reduce the dialdehyde protein-binding form of AFB1 to the non-binding AFB1 dialcohol.
Pssm-ID: 381301 [Multi-domain] Cd Length: 304 Bit Score: 103.02 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 13 VIGAGLWGIGEGI-DAHAQRRALDAAFDAGLVLLDTAEMYGNGASErvagAAARSARAQGKDVFVVSKVLPSNA---RPQ 88
Cdd:cd19075 4 ILGTMTFGSQGRFtTAEAAAELLDAFLERGHTEIDTARVYPDGTSE----ELLGELGLGERGFKIDTKANPGVGgglSPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 89 LMRTALTRSLHNLGLDYLDMYLLHW--RSTaDLALVAQQMHEFVQEGLIRHWGVSNF---DVADMQELlavpygeecaCD 163
Cdd:cd19075 80 NVRKQLETSLKRLKVDKVDVFYLHApdRST-PLEETLAAIDELYKEGKFKEFGLSNYsawEVAEIVEI----------CK 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1233716732 164 QN----------LYNLANRGMDHDLMPWLRDHHIPLMAYSPLGDG 198
Cdd:cd19075 149 ENgwvlptvyqgMYNAITRQVETELFPCLRKLGIRFYAYSPLAGG 193
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
14-198 |
2.46e-25 |
|
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: 102.00 E-value: 2.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 14 IGAGLWGIGE----GIDAHAQRRALDAAFDAGLVLLDTAEMYGNGASERVAGAAARSARAQGKdVFVVSKV--------- 80
Cdd:cd19148 7 IALGTWAIGGwmwgGTDEKEAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKEYGKRDR-VVIATKVglewdegge 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 81 LPSNARPQLMRTALTRSLHNLGLDYLDMYLLHW-RSTADLALVAQQMHEFVQEGLIRHWGVSNFDVADMQEL-LAVPYge 158
Cdd:cd19148 86 VVRNSSPARIRKEVEDSLRRLQTDYIDLYQVHWpDPLVPIEETAEALKELLDEGKIRAIGVSNFSPEQMETFrKVAPL-- 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1233716732 159 ecACDQNLYNLANRGMDHDLMPWLRDHHIPLMAYSPLGDG 198
Cdd:cd19148 164 --HTVQPPYNLFEREIEKDVLPYARKHNIVTLAYGALCRG 201
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
34-230 |
4.59e-25 |
|
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: 101.09 E-value: 4.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 34 LDAAFDAGLVLLDTAEMYGN----GASERVAgaaarsaraqGK---------DVFVVSK----VLPSNARPQL----MRT 92
Cdd:cd19082 23 LDAFVELGGNFIDTARVYGDwverGASERVI----------GEwlksrgnrdKVVIATKgghpDLEDMSRSRLspedIRA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 93 ALTRSLHNLGLDYLDMYLLHwRStaDLAL----VAQQMHEFVQEGLIRHWGVSNFDVADMQEllAVPYGEE-----CACD 163
Cdd:cd19082 93 DLEESLERLGTDYIDLYFLH-RD--DPSVpvgeIVDTLNELVRAGKIRAFGASNWSTERIAE--ANAYAKAhglpgFAAS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 164 QNLYNLA--NRG---------MDHDLMPWLRDHHIPLMAYSPLGDG---GPAGTRVMVNNTE---------------VKK 214
Cdd:cd19082 168 SPQWSLArpNEPpwpgptlvaMDEEMRAWHEENQLPVFAYSSQARGffsKRAAGGAEDDSELrrvyyseenferlerAKE 247
|
250
....*....|....*.
gi 1233716732 215 VAARHHASAQQVMLAW 230
Cdd:cd19082 248 LAEEKGVSPTQIALAY 263
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
8-269 |
5.86e-25 |
|
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: 101.37 E-value: 5.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGAGLWGIGEGIDAHAQRRALDAafdaGLVLLDTAEMYGNgasERVAGAAARSARAQG----KDVFVVSKVLPS 83
Cdd:cd19113 8 GYKMPSVGFGCWKLDNATAADQIYQAIKA----GYRLFDGAEDYGN---EKEVGEGVNRAIDEGlvkrEELFLTSKLWNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 84 NARPQLMRTALTRSLHNLGLDYLDMYLLHWR------------------------STADLALVA--QQMHEFVQEGLIRH 137
Cdd:cd19113 81 FHDPKNVETALNKTLSDLKLDYVDLFLIHFPiafkfvpieekyppgfycgdgdnfVYEDVPILDtwKALEKLVDAGKIKS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 138 WGVSNFDVADMQELL--AVPYGEECACDQNLYNLANRgmdhdLMPWLRDHHIPLMAYSPLG-------DGGPA-GTRVMV 207
Cdd:cd19113 161 IGVSNFPGALILDLLrgATIKPAVLQIEHHPYLQQPK-----LIEYAQKAGITITAYSSFGpqsfvelNQGRAlNTPTLF 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1233716732 208 NNTEVKKVAARHHASAQQVMLAWCVRDGNTLaIPQSANPEHLVQDFHSGSLELDEHDF---AALD 269
Cdd:cd19113 236 EHDTIKSIAAKHNKTPAQVLLRWATQRGIAV-IPKSNLPERLLQNLSVNDFDLTKEDFeeiAKLD 299
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
8-270 |
8.22e-25 |
|
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: 100.96 E-value: 8.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGAGLWGIGEGidahAQRRALDAAFDAGLVLLDTAEMYGNgasERVAGAAARSARAQG----KDVFVVSKVLPS 83
Cdd:cd19107 1 GAKMPILGLGTWKSPPG----QVTEAVKVAIDAGYRHIDCAYVYQN---ENEVGEAIQEKIKEQvvkrEDLFIVSKLWCT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 84 NARPQLMRTALTRSLHNLGLDYLDMYLLHW--------------------RSTADLALVAQQMHEFVQEGLIRHWGVSNF 143
Cdd:cd19107 74 FHEKGLVKGACQKTLSDLKLDYLDLYLIHWptgfkpgkelfpldesgnviPSDTTFLDTWEAMEELVDEGLVKAIGVSNF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 144 DVADMQELLAVPyGEEcacdqnlYNLANRGMD-------HDLMPWLRDHHIPLMAYSPLGDG----GPAGTRVMVNNTEV 212
Cdd:cd19107 154 NHLQIERILNKP-GLK-------YKPAVNQIEchpyltqEKLIQYCQSKGIVVTAYSPLGSPdrpwAKPEDPSLLEDPKI 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1233716732 213 KKVAARHHASAQQVMLAWCVRDgNTLAIPQSANPEHLVQDFHSGSLELDEHDFAALDS 270
Cdd:cd19107 226 KEIAAKHNKTTAQVLIRFPIQR-NLVVIPKSVTPERIAENFKVFDFELSSEDMATILS 282
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
8-270 |
1.53e-24 |
|
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.
Pssm-ID: 381340 [Multi-domain] Cd Length: 302 Bit Score: 99.94 E-value: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGAGLWGIgegiDAHAQRRALDAAFDAGLVLLDTAEMYGNgasERVAGAAARSARAQG----KDVFVVSKVLPS 83
Cdd:cd19114 1 GDKMPLVGFGTAKI----KANETEEVIYNAIKVGYRLIDGALLYGN---EAEVGRGIRKAIQEGlvkrEDLFIVTKLWNN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 84 NARPQLMRTALTRSLHNLGLDYLDMYLLHW-------------------RSTADLALVAQQMHE-------FVQEGLIRH 137
Cdd:cd19114 74 FHGKDHVREAFDRQLKDYGLDYIDLYLIHFpipaayvdpaenypflwkdKELKKFPLEQSPMQEcwremekLVDAGLVRN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 138 WGVSNFDVADMQELLAVPYGEECACDQNLYNLANRgmdHDLMPWLRDHHIPLMAYSPLGDGG----PAGTRVMVNNTE-- 211
Cdd:cd19114 154 IGIANFNVQLILDLLTYAKIKPAVLQIEHHPYLQQ---KRLIDWAKKQGIQITAYSSFGNAVytkvTKHLKHFTNLLEhp 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 212 -VKKVAARHHASAQQVMLAWCVrDGNTLAIPQSANPEHLVQDFHSGSLELDEHDFAALDS 270
Cdd:cd19114 231 vVKKLADKHKRDTGQVLLRWAV-QRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYE 289
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
3-268 |
1.60e-24 |
|
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: 100.21 E-value: 1.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 3 TLSFAGREMPVIGAGLWGIGEGI-----DAHAQRrALDAAFDAGLVLLDTAEMYGNgaSERVAGAAARSARAQGKDVFVV 77
Cdd:cd19144 5 TLGRNGPSVPALGFGAMGLSAFYgppkpDEERFA-VLDAAFELGCTFWDTADIYGD--SEELIGRWFKQNPGKREKIFLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 78 SKV----------LPSNARPQLMRTALTRSLHNLGLDYLDMYLLH-WRSTADLALVAQQMHEFVQEGLIRHWGVSNFDVA 146
Cdd:cd19144 82 TKFgieknvetgeYSVDGSPEYVKKACETSLKRLGVDYIDLYYQHrVDGKTPIEKTVAAMAELVQEGKIKHIGLSECSAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 147 DMQELLAVpygEECACDQNLYN---LANRGMDHDLMPWLRDHHIPLMAYSPLGDGGPAGT-----------------RVM 206
Cdd:cd19144 162 TLRRAHAV---HPIAAVQIEYSpfsLDIERPEIGVLDTCRELGVAIVAYSPLGRGFLTGAirspddfeegdfrrmapRFQ 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1233716732 207 VNN--------TEVKKVAARHHASAQQVMLAWCVRDGN-TLAIPQSANPEHLVQDFHSGSLELDEHDFAAL 268
Cdd:cd19144 239 AENfpknlelvDKIKAIAKKKNVTAGQLTLAWLLAQGDdIIPIPGTTKLKRLEENLGALKVKLTEEEEKEI 309
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
8-268 |
2.71e-24 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 98.61 E-value: 2.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGAGLWGIGEGIDAHAQRRALDAAFDAglvlLDTAEMYGNgasERVAGAAARSARAQGKDVFVVSKVLpsNARP 87
Cdd:PRK11565 12 GNVMPQLGLGVWQASNEEVITAIHKALEVGYRS----IDTAAIYKN---EEGVGKALKEASVAREELFITTKLW--NDDH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 88 QLMRTALTRSLHNLGLDYLDMYLLHWRSTADLALVA--QQMHEFVQEGLIRHWGVSNFDVADMQELL----AVPygeecA 161
Cdd:PRK11565 83 KRPREALEESLKKLQLDYVDLYLMHWPVPAIDHYVEawKGMIELQKEGLIKSIGVCNFQIHHLQRLIdetgVTP-----V 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 162 CDQ-NLYNLANRgmdHDLMPWLRDHHIPLMAYSPLGDGGPAgtrvMVNNTEVKKVAARHHASAQQVMLAWCVrDGNTLAI 240
Cdd:PRK11565 158 INQiELHPLMQQ---RQLHAWNATHKIQTESWSPLAQGGKG----VFDQKVIRDLADKYGKTPAQIVIRWHL-DSGLVVI 229
|
250 260
....*....|....*....|....*...
gi 1233716732 241 PQSANPEHLVQDFHSGSLELDEHDFAAL 268
Cdd:PRK11565 230 PKSVTPSRIAENFDVFDFRLDKDELGEI 257
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
8-270 |
7.18e-24 |
|
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: 97.60 E-value: 7.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGAGLWGIGEGidahAQRRALDAAFDAGLVLLDTAEMYGNGASERVAGAAARSARAQGKDVFVVSKVLPS-NAR 86
Cdd:cd19121 9 GASIPAVGLGTWQAKAG----EVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAIAGGVKREDLFVTTKLWSTyHRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 87 PQLmrtALTRSLHNLGLDYLDMYLLHW------RSTADL-----------------ALVAQQMHEFVQEGLIRHWGVSNF 143
Cdd:cd19121 85 VEL---CLDRSLKSLGLDYVDLYLVHWpvllnpNGNHDLfptlpdgsrdldwdwnhVDTWKQMEKVLKTGKTKAIGVSNY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 144 DVADMQELLA----VPygeecACDQnlYNLANRGMDHDLMPWLRDHHIPLMAYSPLGD-GGPagtrvMVNNTEVKKVAAR 218
Cdd:cd19121 162 SIPYLEELLKhatvVP-----AVNQ--VENHPYLPQQELVDFCKEKGILIEAYSPLGStGSP-----LISDEPVVEIAKK 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1233716732 219 HHASAQQVMLAWCVRDGNTLaIPQSANPEHLVQDFHsgSLELDEHDFAALDS 270
Cdd:cd19121 230 HNVGPGTVLISYQVARGAVV-LPKSVTPDRIKSNLE--IIDLDDEDMNKLND 278
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
3-270 |
8.34e-24 |
|
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: 97.94 E-value: 8.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 3 TLSfAGREMPVIGAGLWGIgegiDAHAQRRALDAAFDAGLVLLDTAEMYGNgasERVAGAAARSARAQG----KDVFVVS 78
Cdd:cd19112 4 TLN-SGHKMPVIGLGVWRM----EPGEIKELILNAIKIGYRHFDCAADYKN---EKEVGEALAEAFKTGlvkrEDLFITT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 79 KVLpsNARPQLMRTALTRSLHNLGLDYLDMYLLH----WRSTA------------------DLALVA--QQMHEFVQEGL 134
Cdd:cd19112 76 KLW--NSDHGHVIEACKDSLKKLQLDYLDLYLVHfpvaTKHTGvgttgsalgedgvldidvTISLETtwHAMEKLVSAGL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 135 IRHWGVSNFDVADMQELLAvpYGE-ECACDQ-NLYNLANRgmdHDLMPWLRDHHIPLMAYSPLGdGGPA-----GTRVMV 207
Cdd:cd19112 154 VRSIGISNYDIFLTRDCLA--YSKiKPAVNQiETHPYFQR---DSLVKFCQKHGISVTAHTPLG-GAAAnaewfGSVSPL 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1233716732 208 NNTEVKKVAARHHASAQQVMLAWCVRDgNTLAIPQSANPEHLVQDFHSGSLELDEHDFAALDS 270
Cdd:cd19112 228 DDPVLKDLAKKYGKSAAQIVLRWGIQR-NTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKS 289
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-271 |
1.01e-23 |
|
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: 97.79 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 13 VIGAGLWG---------IGEGIDAHAQRRALDAAFDAGLVLLDTAEMYGNGASERVAGAAARSARAQgkDVFVVSKVLPS 83
Cdd:cd19103 8 ALGTWSWGsggaggdqvFGNHLDEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEFLKRYPRE--DYIISTKFTPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 84 NA--RPQLMRTALTRSLHNLGLDYLDMYLLHwrSTADLALVAQQMHEFVQEGLIRHWGVSNFDVADM---QELLAvPYGE 158
Cdd:cd19103 86 IAgqSADPVADMLEGSLARLGTDYIDIYWIH--NPADVERWTPELIPLLKSGKVKHVGVSNHNLAEIkraNEILA-KAGV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 159 ECACDQNLYNLANRGMDHD-LMPWLRDHHIPLMAYSPLGDGG-----------PAGT-RVMVNN---------TEV-KKV 215
Cdd:cd19103 163 SLSAVQNHYSLLYRSSEEAgILDYCKENGITFFAYMVLEQGAlsgkydtkhplPEGSgRAETYNpllpqleelTAVmAEI 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1233716732 216 AARHHASAQQVMLAWCVRDGnTLAIPQSANPEHLVQDFHSGSLELDEHDFAALDSA 271
Cdd:cd19103 243 GAKHGASIAQVAIAWAIAKG-TTPIIGVTKPHHVEDAARAASITLTDDEIKELEQL 297
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
13-262 |
1.27e-23 |
|
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: 97.28 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 13 VIGAGLWG-IGEGIDAHAQRRALDAAFDAGLVLLDTAEMYGNGASERVAgaaarsaraqGK-------DVFVVS-KVL-- 81
Cdd:cd19074 6 ELSLGTWLtFGGQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVL----------GKalkgwprESYVIStKVFwp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 82 ---PSN----ARPQLMRtALTRSLHNLGLDYLDMYLLH-WRSTADLALVAQQMHEFVQEGLIRHWGVSNFDVADMQELLA 153
Cdd:cd19074 76 tgpGPNdrglSRKHIFE-SIHASLKRLQLDYVDIYYCHrYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 154 VPYGEECA---CDQNLYNLANRGMDHDLMPWLRDHHIPLMAYSPL---------GDGGPAGTRVMVNNTEV--------- 212
Cdd:cd19074 155 LARQFGLIppvVEQPQYNMLWREIEEEVIPLCEKNGIGLVVWSPLaqglltgkyRDGIPPPSRSRATDEDNrdkkrrllt 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1233716732 213 ----------KKVAARHHASAQQVMLAWCVR-DGNTLAIPQSANPEHLVQDFHSGSLELDE 262
Cdd:cd19074 235 denlekvkklKPIADELGLTLAQLALAWCLRnPAVSSAIIGASRPEQLEENVKASGVKLSP 295
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
19-269 |
1.75e-23 |
|
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: 97.29 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 19 WGIGEGIDAhaQRRALDAAFDAGLVLLDTAEMYGNGASERVAGAAARSAraqgKDVFVVSKVLPSNARPQL--------- 89
Cdd:cd19080 24 WGWGADREE--ARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAGN----RDRIVLATKYTMNRRPGDpnaggnhrk 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 90 -MRTALTRSLHNLGLDYLDMYLLH-WRSTADLALVAQQMHEFVQEGLIRHWGVSNFD---VADMQELlAVPYGEECACD- 163
Cdd:cd19080 98 nLRRSVEASLRRLQTDYIDLLYVHaWDFTTPVEEVMRALDDLVRAGKVLYVGISDTPawvVARANTL-AELRGWSPFVAl 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 164 QNLYNLANRGMDHDLMPWLRDHHIPLMAYSPLGDG----------------GPAGTRVMVNNTE--------VKKVAARH 219
Cdd:cd19080 177 QIEYSLLERTPERELLPMARALGLGVTPWSPLGGGlltgkyqrgeegrageAKGVTVGFGKLTErnwaivdvVAAVAEEL 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1233716732 220 HASAQQVMLAWCV-RDGNTLAIPQSANPEHLVQDFHSGSLELDEHDFAALD 269
Cdd:cd19080 257 GRSAAQVALAWVRqKPGVVIPIIGARTLEQLKDNLGALDLTLSPEQLARLD 307
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
8-272 |
2.18e-23 |
|
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli aldehyde reductase (AKR13C1) and Thermotoga maritima aldo-keto reductase (AKR13C2). Aldehyde reductase (EC 1.1.1.21), also called aldose reductase, is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides.
Pssm-ID: 381304 [Multi-domain] Cd Length: 301 Bit Score: 96.92 E-value: 2.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGAGLWGIGEGIDAHAQR----RALDAAFDAGLVLLDTAEMYGNGASERVAgaaarsaraqGK-------DVFV 76
Cdd:cd19078 1 GLEVSAIGLGCMGMSHGYGPPPDKeemiELIRKAVELGITFFDTAEVYGPYTNEELV----------GEalkpfrdQVVI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 77 VSK-----------VLPSNARPQLMRTALTRSLHNLGLDYLDMYLLHwRSTADLAL--VAQQMHEFVQEGLIRHWGVSNF 143
Cdd:cd19078 71 ATKfgfkidggkpgPLGLDSRPEHIRKAVEGSLKRLQTDYIDLYYQH-RVDPNVPIeeVAGTMKELIKEGKIRHWGLSEA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 144 DVADM------QELLAVpygeecacdQNLYNLANRGMDHDLMPWLRDHHIPLMAYSPLGDGGPAGT-------------R 204
Cdd:cd19078 150 GVETIrrahavCPVTAV---------QSEYSMMWREPEKEVLPTLEELGIGFVPFSPLGKGFLTGKidentkfdegddrA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 205 VMVNNTE------------VKKVAARHHASAQQVMLAWCVRDG-NTLAIPQSANPEHLVQDFHSGSLELDEHDFAALDSA 271
Cdd:cd19078 221 SLPRFTPealeanqalvdlLKEFAEEKGATPAQIALAWLLAKKpWIVPIPGTTKLSRLEENIGAADIELTPEELREIEDA 300
|
.
gi 1233716732 272 F 272
Cdd:cd19078 301 L 301
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
26-231 |
2.60e-22 |
|
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: 94.17 E-value: 2.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 26 DAHAQrraLDAAFDAGLVLLDTAEMY-------GNGASERVAgaaarsaraqGK---------DVFVVSKVLPSNARPQL 89
Cdd:cd19094 19 EAHEQ---LDYAFDEGVNFIDTAEMYpvppspeTQGRTEEII----------GSwlkkkgnrdKVVLATKVAGPGEGITW 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 90 MR---TALTR---------SLHNLGLDYLDMYLLHW-------------------RSTADLALVAQQMHEFVQEGLIRHW 138
Cdd:cd19094 86 PRgggTRLDRenireavegSLKRLGTDYIDLYQLHWpdrytplfgggyytepseeEDSVSFEEQLEALGELVKAGKIRHI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 139 GVSN---FDVADMQEL---LAVPygeECACDQNLYNLANRGMDHDLMPWLRDHHIPLMAYSPLGDG-----------GPA 201
Cdd:cd19094 166 GLSNetpWGVMKFLELaeqLGLP---RIVSIQNPYSLLNRNFEEGLAEACHRENVGLLAYSPLAGGvltgkyldgaaRPE 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1233716732 202 GTR---------------VMVNNTEVKKVAARHHASAQQVMLAWC 231
Cdd:cd19094 243 GGRlnlfpgymaryrspqALEAVAEYVKLARKHGLSPAQLALAWV 287
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
12-249 |
6.72e-21 |
|
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: 89.22 E-value: 6.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 12 PVIGAGLWGIGE---GIDAHAQRRALDAAFDAGLVLLDTAEMYGNgaSERVAgaaarsaraqGK--------DVFVVSKV 80
Cdd:cd19095 1 SVLGLGTSGIGRvwgVPSEAEAARLLNTALDLGINLIDTAPAYGR--SEERL----------GRalaglrrdDLFIATKV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 81 --------LPSNARPQLMRTALTRSLHNLGLDYLDMYLLH----WRSTADlalVAQQMHEFVQEGLIRHWGVSNFDvadm 148
Cdd:cd19095 69 gthgeggrDRKDFSPAAIRASIERSLRRLGTDYIDLLQLHgpsdDELTGE---VLETLEDLKAAGKVRYIGVSGDG---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 149 QELLAVpygeeCACD-----QNLYNLANRGMDhDLMPWLRDHHIPLMAYSPLGdGGPAGTRVMVNNTEVKKVAARHHA-- 221
Cdd:cd19095 142 EELEAA-----IASGvfdvvQLPYNVLDREEE-ELLPLAAEAGLGVIVNRPLA-NGRLRRRVRRRPLYADYARRPEFAae 214
|
250 260 270
....*....|....*....|....*....|...
gi 1233716732 222 ----SAQQVMLAWCVRD-GNTLAIPQSANPEHL 249
Cdd:cd19095 215 iggaTWAQAALRFVLSHpGVSSAIVGTTNPEHL 247
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
8-265 |
8.24e-21 |
|
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: 89.48 E-value: 8.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGAGLWGIGEgiDAHAQRRALDAAFDAGLVLLDTAEMYGngaSERVAGAAARSARAQGK----DVFVVSKVLPS 83
Cdd:cd19119 9 GASIPALGLGTASPHE--DRAEVKEAVEAAIKEGYRHIDTAYAYE---TEDFVGEAIKRAIDDGSikreELFITTKVWPT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 84 NARPqlMRTALTRSLHNLGLDYLDMYLLHW-----RSTADLALVA---------------------QQMHEFVQEGLIRH 137
Cdd:cd19119 84 FYDE--VERSLDESLKALGLDYVDLLLVHWpvcfeKDSDDSGKPFtpvnddgktryaasgdhittyKQLEKIYLDGRAKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 138 WGVSNFDVADMQELL----AVPYGEECACDQNLYNLanrgmdhDLMPWLRDHHIPLMAYSPLGDGGPAgtrvMVNNTEVK 213
Cdd:cd19119 162 IGVSNYSIVYLERLIkeckVVPAVNQVELHPHLPQM-------DLRDFCFKHGILVTAYSPLGSHGAP----NLKNPLVK 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1233716732 214 KVAARHHASAQQVMLAWCVRDGnTLAIPQSANPEHLVQDFHSGSLELDEHDF 265
Cdd:cd19119 231 KIAEKYNVSTGDILISYHVRQG-VIVLPKSLKPVRIVSNGKIVSLTKEDLQK 281
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
8-269 |
1.03e-20 |
|
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis.
Pssm-ID: 381348 [Multi-domain] Cd Length: 291 Bit Score: 89.22 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGAGLWGiGEGIDAHAQRrALDAAFDAGLVLLDTAEMYGNG--ASERVAGAAARSARAQGKDVFVVSKVLPSNA 85
Cdd:cd19122 6 GVKIPAVGFGTFA-NEGAKGETYA-AVTKALDVGYRHLDCAWFYLNEdeVGDAVRDFLKENPSVKREDLFICTKVWNHLH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 86 RPQLMRTALTRSLHNLGLDYLDMYLLHWRSTA------------DLALVAQQ------------MHEFVQEGLIRHWGVS 141
Cdd:cd19122 84 EPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAekndqrspklgpDGKYVILKdltenpeptwraMEEIYESGKAKAIGVS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 142 NFDVADMQELLAV----PYGEECACDQNLYN--LANRGMDHDLMPwlrdhhiplMAYSPLGDGG---PAGTRVMVNNTeV 212
Cdd:cd19122 164 NWTIPGLKKLLSFakvkPHVNQIEIHPFLPNeeLVDYCFSNDILP---------EAYSPLGSQNqvpSTGERVSENPT-L 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1233716732 213 KKVAARHHASAQQVMLAWCVRDGnTLAIPQSANPEHLVQDFHsgSLELDEHDFAALD 269
Cdd:cd19122 234 NEVAEKGGYSLAQVLIAWGLRRG-YVVLPKSSTPSRIESNFK--SIELSDEDFEAIN 287
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-271 |
3.99e-20 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 88.04 E-value: 3.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 10 EMPVIGAGLW----GIGEGIDAHAQRRALDAAFDAGLVLLDTAEMYGnGASERVAGAAARSARAQGK--DVFVVSKVLPS 83
Cdd:cd19101 1 TISRVINGMWqlsgGHGGIRDEDAAVRAMAAYVDAGLTTFDCADIYG-PAEELIGEFRKRLRRERDAadDVQIHTKWVPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 84 NAR----PQLMRTALTRSLHNLGLDYLDMYLLHWRSTADLALV--AQQMHEFVQEGLIRHWGVSNFDVADMQELLAVpyG 157
Cdd:cd19101 80 PGEltmtRAYVEAAIDRSLKRLGVDRLDLVQFHWWDYSDPGYLdaAKHLAELQEEGKIRHLGLTNFDTERLREILDA--G 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 158 EECACDQNLYNLANRGMDHDLMPWLRDHHIPLMAYSPLGdGG---------PAGTRVMVNNTEVKK-------------- 214
Cdd:cd19101 158 VPIVSNQVQYSLLDRRPENGMAALCEDHGIKLLAYGTLA-GGllsekylgvPEPTGPALETRSLQKyklmidewggwdlf 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1233716732 215 ---------VAARHHASAQQVMLAWcvrdgnTLAIPQSA-------NPEHLVQDFHSGSLELDEHDFAALDSA 271
Cdd:cd19101 237 qellrtlkaIADKHGVSIANVAVRW------VLDQPGVAgvivgarNSEHIDDNVRAFSFRLDDEDRAAIDAV 303
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
8-253 |
8.96e-20 |
|
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: 86.74 E-value: 8.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGaglwgIGEGI-DAHAQRRALDAAFDAGLVLLDTAEMYGNgasERVAGAAARSARAQGK----DVFVVSKVLP 82
Cdd:cd19129 3 SGAIPALG-----FGTLIpDPSATRNAVKAALEAGFRHFDCAERYRN---EAEVGEAMQEVFKAGKirreDLFVTTKLWN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 83 SNARPQLMRTALTRSLHNLGLDYLDMYLLH---------------------WRSTADLALVAQQMHEFVQEGLIRHWGVS 141
Cdd:cd19129 75 TNHRPERVKPAFEASLKRLQLDYLDLYLIHtpfafqpgdeqdprdangnviYDDGVTLLDTWRAMERLVDEGRCKAIGLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 142 NFDVADMQELLAV-------------PYGEECacdqnlynlanrgmdhDLMPWLRDHHIPLMAYSPLGDGGPAGtrvMVN 208
Cdd:cd19129 155 DVSLEKLREIFEAarikpavvqveshPYLPEW----------------ELLDFCKNHGIVLQAFAPLGHGMEPK---LLE 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1233716732 209 NTEVKKVAARHHASAQQVMLAWCVRDGNTLaIPQSANPEHLVQDF 253
Cdd:cd19129 216 DPVITAIARRVNKTPAQVLLAWAIQRGTAL-LTTSKTPSRIRENF 259
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
7-269 |
3.40e-19 |
|
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: 85.55 E-value: 3.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 7 AGREMPVIGAGLWGIGEGIDAHAQRRALDAafdaGLVLLDTAEMYGNgasERVAGAAARSARAQG----KDVFVVSKVLP 82
Cdd:cd19115 9 SGYDMPLVGFGLWKVNNDTCADQVYNAIKA----GYRLFDGACDYGN---EVEAGQGVARAIKEGivkrEDLFIVSKLWN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 83 SNARPQLMRTALTRSLHNLGLDYLDMYLLH-------------------------WRSTADLALVAQQMHEFVQEGLIRH 137
Cdd:cd19115 82 TFHDGERVEPICRKQLADWGIDYFDLFLIHfpialkyvdpavryppgwfydgkkvEFSNAPIQETWTAMEKLVDKGLARS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 138 WGVSNFdvadmqellavpygeecaCDQNLYNL--------ANRGMDH-------DLMPWLRDHHIPLMAYSPLG------ 196
Cdd:cd19115 162 IGVSNF------------------SAQLLMDLlryarirpATLQIEHhpyltqpRLVKYAQKEGIAVTAYSSFGpqsfle 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 197 ---DGGPAGTRVMVNNTeVKKVAARHHASAQQVMLAWCVRDGntLA-IPQSANPEHLVQDFHSGSLELDEHD---FAALD 269
Cdd:cd19115 224 ldlPGAKDTPPLFEHDV-IKSIAEKHGKTPAQVLLRWATQRG--IAvIPKSNNPKRLAQNLDVTGFDLEAEEikaISALD 300
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
3-270 |
1.50e-18 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 83.48 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 3 TLSFAGREMPVIG------AGLWGIGEGIDAHAQRRALDAAFDAGLVLLDTAEMYGNGASERVAGAAARSAraqGKDVFV 76
Cdd:PRK10376 9 TFTLGGRSVNRLGygamqlAGPGVFGPPKDRDAAIAVLREAVALGVNHIDTSDFYGPHVTNQLIREALHPY---PDDLTI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 77 VSKV----------LPSNaRPQLMRTALTRSLHNLGLDYLD------MYLLHWRSTADLALVAQQMHEFVQEGLIRHWGV 140
Cdd:PRK10376 86 VTKVgarrgedgswLPAF-SPAELRRAVHDNLRNLGLDVLDvvnlrlMGDGHGPAEGSIEEPLTVLAELQRQGLVRHIGL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 141 SNFDVADMQELLAVPygeECACDQNLYNLANRGmDHDLMPWLRDHHIPLMAYSPLGDGGPagtrvmVNNTEVKKVAARHH 220
Cdd:PRK10376 165 SNVTPTQVAEARKIA---EIVCVQNHYNLAHRA-DDALIDALARDGIAYVPFFPLGGFTP------LQSSTLSDVAASLG 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1233716732 221 ASAQQVMLAWCV-RDGNTLAIPQSANPEHLVQDFHSGSLELDEHDFAALDS 270
Cdd:PRK10376 235 ATPMQVALAWLLqRSPNILLIPGTSSVAHLRENLAAAELVLSEEVLAELDG 285
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
10-275 |
2.00e-17 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 81.05 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 10 EMPVIGAGLWGIGEG---IDAHAQrraLDAAFDAGLVLLDTAEMY-------GNGASERVAGAAARSARAQGKdVFVVSK 79
Cdd:PRK10625 12 EVSTLGLGTMTFGEQnseADAHAQ---LDYAVAQGINLIDVAEMYpvpprpeTQGLTETYIGNWLAKRGSREK-LIIASK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 80 VL-PSNA-----RPQL------MRTALTRSLHNLGLDYLDMYLLHW-------------RSTADLALVA-----QQMHEF 129
Cdd:PRK10625 88 VSgPSRNndkgiRPNQaldrknIREALHDSLKRLQTDYLDLYQVHWpqrptncfgklgySWTDSAPAVSlletlDALAEQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 130 VQEGLIRHWGVSN---------FDVADMQELLAVpygeecACDQNLYNLANRGMDHDLMPWLRDHHIPLMAYSPLGDG-- 198
Cdd:PRK10625 168 QRAGKIRYIGVSNetafgvmryLHLAEKHDLPRI------VTIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLAFGtl 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 199 --------GPAGTRvmvnNT------------------EVKKVAARHHASAQQVMLAWCVRD---GNTLAipQSANPEHL 249
Cdd:PRK10625 242 tgkylngaKPAGAR----NTlfsrftrysgeqtqkavaAYVDIAKRHGLDPAQMALAFVRRQpfvASTLL--GATTMEQL 315
|
330 340 350
....*....|....*....|....*....|.
gi 1233716732 250 VQDFHSGSLELDEHDFAALDSA-----FPAP 275
Cdd:PRK10625 316 KTNIESLHLTLSEEVLAEIEAVhqvytYPAP 346
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
8-270 |
3.62e-17 |
|
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: 79.84 E-value: 3.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGAGLWGIGEGIDAHAQRRALDAAFDAGLVLLDTAEMYGNgasERVAGAAARSARAQGK----DVFVVSKVLPS 83
Cdd:cd19109 1 GNSIPIIGLGTYSEPKTTPKGACAEAVKVAIDTGYRHIDGAYIYQN---EHEVGQAIREKIAEGKvkreDIFYCGKLWNT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 84 NARPQLMRTALTRSLHNLGLDYLDMYLLH-------------------WR-STADLALVAQQMHEFVQEGLIRHWGVSNF 143
Cdd:cd19109 78 CHPPELVRPTLERTLKVLQLDYVDLYIIEmpmafkpgdeiyprdengkWLyHKTNLCATWEALEACKDAGLVKSIGVSNF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 144 DVADMQELLAVP-YGEECACDQ---NLYNLANRgmdhdLMPWLRDHHIPLMAYSPLGDGGpAGTRVMVN------NTEVK 213
Cdd:cd19109 158 NRRQLELILNKPgLKHKPVSNQvecHPYFTQPK-----LLEFCQQHDIVIVAYSPLGTCR-DPIWVNVSspplleDPLLN 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1233716732 214 KVAARHHASAQQVMLAWCVRDGnTLAIPQSANPEHLVQDFHSGSLELDEHDFAALDS 270
Cdd:cd19109 232 SIGKKYNKTAAQVVLRFNIQRG-VVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEA 287
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
8-249 |
1.06e-16 |
|
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: 78.45 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGAGLW-GIGEGIDAHAQRRALDAAFDAGLVLLDTAEMYG--NGASERVAGAAARSARAQGKDVFVVS-KV--- 80
Cdd:cd19089 8 GLHLPAISLGLWhNFGDYTSPEEARELLRTAFDLGITHFDLANNYGppPGSAEENFGRILKRDLRPYRDELVIStKAgyg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 81 -LPS-----NARPQLMRTaLTRSLHNLGLDYLDMYLLHwR--STADLALVAQQMHEFVQEGLIRHWGVSNFDVADMQELL 152
Cdd:cd19089 88 mWPGpygdgGSRKYLLAS-LDQSLKRMGLDYVDIFYHH-RydPDTPLEETMTALADAVRSGKALYVGISNYPGAKARRAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 153 AV--PYGEECACDQNLYNLANRGMDHDLMPWLRDHHIPLMAYSPLG---------DGGPAGTRVMVNNTEVK-------- 213
Cdd:cd19089 166 ALlrELGVPLIIHQPRYSLLDRWAEDGLLEVLEEAGIGFIAFSPLAqglltdkylNGIPPDSRRAAESKFLTeealtpek 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1233716732 214 --------KVAARHHASAQQVMLAWCVRDGN-TLAIPQSANPEHL 249
Cdd:cd19089 246 leqlrklnKIAAKRGQSLAQLALSWVLRDPRvTSVLIGASSPSQL 290
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
8-141 |
2.97e-16 |
|
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: 76.08 E-value: 2.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGAGlwgiGEGIDAHAQRrALDAAFDAGLVLLDTAEMYGNGASErvAGAAARSARAQGKDVFVVSKVLP---SN 84
Cdd:cd19105 10 GLKVSRLGFG----GGGLPRESPE-LLRRALDLGINYFDTAEGYGNGNSE--EIIGEALKGLRRDKVFLATKASPrldKK 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1233716732 85 ARPQLMRtALTRSLHNLGLDYLDMYLLHWRSTADLALVAQQMHEFV----QEGLIRHWGVS 141
Cdd:cd19105 83 DKAELLK-SVEESLKRLQTDYIDIYQLHGVDTPEERLLNEELLEALeklkKEGKVRFIGFS 142
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
33-269 |
1.38e-15 |
|
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: 74.97 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 33 ALDAAFDAGLVLLDTAEMYGNG---ASERVAGAAARSARAQGKDVFVVSK--VLPSNARPQLMRTALTRSLHNL-----G 102
Cdd:cd19077 30 TMKAALDAGSNLWNGGEFYGPPdphANLKLLARFFRKYPEYADKVVLSVKggLDPDTLRPDGSPEAVRKSIENIlralgG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 103 LDYLDMYLLHwRSTADLAL--VAQQMHEFVQEGLIRHWGVSNFDVADMQELLAVpygEECACDQNLYNLANRGMDH-DLM 179
Cdd:cd19077 110 TKKIDIFEPA-RVDPNVPIeeTIKALKELVKEGKIRGIGLSEVSAETIRRAHAV---HPIAAVEVEYSLFSREIEEnGVL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 180 PWLRDHHIPLMAYSPLGDGGPAGT------------RVMVNN-------------TEVKKVAARHHASAQQVMLAWCVRD 234
Cdd:cd19077 186 ETCAELGIPIIAYSPLGRGLLTGRiksladipegdfRRHLDRfngenfeknlklvDALQELAEKKGCTPAQLALAWILAQ 265
|
250 260 270
....*....|....*....|....*....|....*..
gi 1233716732 235 GNT--LAIPQSANPEHLVQDFHSGSLELDEHDFAALD 269
Cdd:cd19077 266 SGPkiIPIPGSTTLERVEENLKAANVELTDEELKEIN 302
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
8-270 |
1.54e-15 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 74.96 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGAGLWGIGEgidaHAQRRALDA---AFDAGLVLLDTAEMYGNgasERVAGAAARSARAQG----KDVFVVSKV 80
Cdd:cd19108 8 GHFIPVLGFGTYAPEE----VPKSKALEAtklAIDAGFRHIDSAYLYQN---EEEVGQAIRSKIADGtvkrEDIFYTSKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 81 LPSNARPQLMRTALTRSLHNLGLDYLDMYLLHWR--------------------STADLALVAQQMHEFVQEGLIRHWGV 140
Cdd:cd19108 81 WCTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPvalkpgeelfpkdengklifDTVDLCATWEAMEKCKDAGLAKSIGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 141 SNFDVADMQELLAVP---YgeECACDQ---NLYNlaNRGmdhDLMPWLRDHHIPLMAYSPLGDGGPAG-----TRVMVNN 209
Cdd:cd19108 161 SNFNRRQLEMILNKPglkY--KPVCNQvecHPYL--NQS---KLLDFCKSKDIVLVAYSALGSQRDKEwvdqnSPVLLED 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1233716732 210 TEVKKVAARHHASAQQVMLAWCVRDGnTLAIPQSANPEHLVQDFHSGSLELDEHDFAALDS 270
Cdd:cd19108 234 PVLCALAKKHKRTPALIALRYQLQRG-VVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDG 293
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
15-262 |
2.23e-15 |
|
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: 74.13 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 15 GAGLWGIGEGIDAHAQRRALDAAFDAGLVLLDTAEMYGNgaSErvAGAAARSARAQGKDVFVVSKVLPSNAR-----PQL 89
Cdd:cd19090 7 TAGLGGVFGGVDDDEAVATIRAALDLGINYIDTAPAYGD--SE--ERLGLALAELPREPLVLSTKVGRLPEDtadysADR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 90 MRTALTRSLHNLGLDYLDMYLLH------WRSTADLALVAQQMHEFVQEGLIRHWGVSNFDVADMQELLAVpyGE-ECAC 162
Cdd:cd19090 83 VRRSVEESLERLGRDRIDLLMIHdpervpWVDILAPGGALEALLELKEEGLIKHIGLGGGPPDLLRRAIET--GDfDVVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 163 DQNLYNLANRGMDHDLMPWLRDHHIPLMAYSPLGDGGPAG-------------TRVMVNNTE-VKKVAARHHASAQQVML 228
Cdd:cd19090 161 TANRYTLLDQSAADELLPAAARHGVGVINASPLGMGLLAGrppervrytyrwlSPELLDRAKrLYELCDEHGVPLPALAL 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 1233716732 229 AWCVRD---GNTLAIPqsANPEHLVQDFHSGSLELDE 262
Cdd:cd19090 241 RFLLRDpriSTVLVGA--SSPEELEQNVAAAEGPLPE 275
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-171 |
4.21e-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: 381330 [Multi-domain] Cd Length: 321 Bit Score: 73.84 E-value: 4.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 16 AGLWGIGegiDAHAQRRALDAAFDAGLVLLDTAEMYGNGASErvaGAAARSARAQGKDVFVVSKVLPSNARPQLMRTALT 95
Cdd:cd19104 23 GGLMGRT---TREEQIAAVRRALDLGINFFDTAPSYGDGKSE---ENLGRALKGLPAGPYITTKVRLDPDDLGDIGGQIE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 96 RSLH----NLGLDYLDMYLLHWR--------------STADLAL--VAQQMHEFVQEGLIRHWGVSNFDVAD-MQELLAv 154
Cdd:cd19104 97 RSVEkslkRLKRDSVDLLQLHNRigderdkpvggtlsTTDVLGLggVADAFERLRSEGKIRFIGITGLGNPPaIRELLD- 175
|
170
....*....|....*..
gi 1233716732 155 pyGEECACDQNLYNLAN 171
Cdd:cd19104 176 --SGKFDAVQVYYNLLN 190
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
34-153 |
5.01e-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: 72.95 E-value: 5.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 34 LDAAFDAGLVLLDTAEMYGNgaSERVAGAAARsaraQGKDVFVVSKVLPSNA----RPQLMRTALTRSLHNLGLDYLDMY 109
Cdd:cd19097 32 LEYALKAGINTLDTAPAYGD--SEKVLGKFLK----RLDKFKIITKLPPLKEdkkeDEAAIEASVEASLKRLKVDSLDGL 105
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1233716732 110 LLHwrSTADLAL----VAQQMHEFVQEGLIRHWGVSNFDVADMQELLA 153
Cdd:cd19097 106 LLH--NPDDLLKhggkLVEALLELKKEGLIRKIGVSVYSPEELEKALE 151
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
12-249 |
1.14e-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: 381391 [Multi-domain] Cd Length: 291 Bit Score: 72.36 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 12 PVIGAGLWGIGEGIDAHAQRRALDAAFDAGLVLLDTAEMYG-------NGASERVAGAAARSARAQGkDVFVVSKV---- 80
Cdd:cd19752 1 SELCLGTMYFGTRTDEETSFAILDRYVAAGGNFLDTANNYAfwteggvGGESERLIGRWLKDRGNRD-DVVIATKVgagp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 81 -----LPSNAR---PQLMRTALTRSLHNLGLDYLDMYLLHW--RSTaDLALVAQQMHEFVQEGLIRHWGVSNFD---VAD 147
Cdd:cd19752 80 rdpdgGPESPEglsAETIEQEIDKSLRRLGTDYIDLYYAHVddRDT-PLEETLEAFNELVKAGKVRAIGASNFAawrLER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 148 MQELLAVPYGEECACDQNLYNL--ANRGMDH--------DLMPWLRDH-HIPLMAYSPLGDG--------------GPAG 202
Cdd:cd19752 159 ARQIARQQGWAEFSAIQQRHSYlrPRPGADFgvqrivtdELLDYASSRpDLTLLAYSPLLSGaytrpdrplpeqydGPDS 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1233716732 203 TRVMvnnTEVKKVAARHHASAQQVMLAWCV-RDGNTLAIPQSANPEHL 249
Cdd:cd19752 239 DARL---AVLEEVAGELGATPNQVVLAWLLhRTPAIIPLLGASTVEQL 283
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
22-260 |
1.17e-14 |
|
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: 72.63 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 22 GEGIDAHAQRRALDAAFDAGLVLLDTAEMYGNGASERVAGAAARSARAQGKDVFVVSKVLPSNARPQLMRTALTR----- 96
Cdd:cd19143 25 GNQVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELGWPRSDYVVSTKIFWGGGGPPPNDRGLSRkhive 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 97 ----SLHNLGLDYLDMYLLHwRSTADLAL--VAQQMHEFVQEGLIRHWGVSNFDVADMQELLAV--------PygeecAC 162
Cdd:cd19143 105 gtkaSLKRLQLDYVDLVFCH-RPDPATPIeeTVRAMNDLIDQGKAFYWGTSEWSAQQIEEAHEIadrlglipP-----VM 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 163 DQNLYNLANRG-MDHDLMPWLRDHHIPLMAYSPL---------GDGGPAGTRVMVNNTE-------------------VK 213
Cdd:cd19143 179 EQPQYNLFHRErVEVEYAPLYEKYGLGTTTWSPLasglltgkyNNGIPEGSRLALPGYEwlkdrkeelgqekiekvrkLK 258
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1233716732 214 KVAARHHASAQQVMLAWCVRDGN-TLAIPQSANPEHLVQDFhsGSLEL 260
Cdd:cd19143 259 PIAEELGCSLAQLAIAWCLKNPNvSTVITGATKVEQLEENL--KALEV 304
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
8-271 |
1.53e-14 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 72.54 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGAGLWGIgEGIDAHAQRRALDAAFDAGLVLLDTAEMYGNgaSERVAgaaarsaraqGK-------DVFVVSKV 80
Cdd:COG1453 10 GLEVSVLGFGGMRL-PRKDEEEAEALIRRAIDNGINYIDTARGYGD--SEEFL----------GKalkgprdKVILATKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 81 LPSNARPQLMRTALTRSLHNLGLDYLDMYLLH---WRSTADLALVAQQMHEFVQ----EGLIRHWGVSNFDVAD-MQELL 152
Cdd:COG1453 77 PPWVRDPEDMRKDLEESLKRLQTDYIDLYLIHglnTEEDLEKVLKPGGALEALEkakaEGKIRHIGFSTHGSLEvIKEAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 153 A--------VPYgeeCACDQNlYNLANRGMDHdlmpwLRDHHIPLMAYSPLGDGGpagtrvMVNNTEVKKVAARHHASAQ 224
Cdd:COG1453 157 DtgdfdfvqLQY---NYLDQD-NQAGEEALEA-----AAEKGIGVIIMKPLKGGR------LANPPEKLVELLCPPLSPA 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1233716732 225 QVMLAWCV-RDGNTLAIPQSANPEHLVQDFHSGSLE--LDEHDFAALDSA 271
Cdd:COG1453 222 EWALRFLLsHPEVTTVLSGMSTPEQLDENLKTADNLepLTEEELAILERL 271
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-251 |
7.43e-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: 381325 [Multi-domain] Cd Length: 316 Bit Score: 70.42 E-value: 7.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 14 IGAGLWGIGEGIDAHAQ-RRALDAAFDAGLVLLDTAEMYGNGASERVAGAAARSARAQGK----DVFVVSK--------- 79
Cdd:cd19099 6 LGLGTYRGDSDDETDEEyREALKAALDSGINVIDTAINYRGGRSERLIGKALRELIEKGGikrdEVVIVTKagyipgdgd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 80 -------------------VLPSNARPQLM-----RTALTRSLHNLGLDYLDMYLLHWRSTADLALVAQQ---------- 125
Cdd:cd19099 86 eplrplkyleeklgrglidVADSAGLRHCIspaylEDQIERSLKRLGLDTIDLYLLHNPEEQLLELGEEEfydrleeafe 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 126 -MHEFVQEGLIRHWGVSNFDV----ADMQELLAVPYGEECACD-----------QNLYNLANRGMDHD----------LM 179
Cdd:cd19099 166 aLEEAVAEGKIRYYGISTWDGfrapPALPGHLSLEKLVAAAEEvggdnhhfkviQLPLNLLEPEALTEkntvkgealsLL 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1233716732 180 PWLRDHHIPLMAYSPLGDGGPAGtrvmvNNTEVKKVAARHHASAQQVMLAWCV-RDGNTLAIPQSANPEHLVQ 251
Cdd:cd19099 246 EAAKELGLGVIASRPLNQGQLLG-----ELRLADLLALPGGATLAQRALQFARsTPGVDSALVGMRRPEHVDE 313
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
8-198 |
1.30e-12 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 65.97 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 8 GREMPVIGAGLWGIGEGIDAHAQRrALDAAFDAGLVLLDTAEMYGNgaSERVAgaaarsaraqGK-------DVFVVSKv 80
Cdd:cd19100 8 GLKVSRLGFGGGPLGRLSQEEAAA-IIRRALDLGINYFDTAPSYGD--SEEKI----------GKalkgrrdKVFLATK- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 81 lpSNAR-PQLMRTALTRSLHNLGLDYLDMYLLHW-RSTADLALVA------QQMHEFVQEGLIRHWGVSNFDVADMQELL 152
Cdd:cd19100 74 --TGARdYEGAKRDLERSLKRLGTDYIDLYQLHAvDTEEDLDQVFgpggalEALLEAKEEGKIRFIGISGHSPEVLLRAL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1233716732 153 AVPygeECACDQNLYNLANRGMD---HDLMPWLRDHHIPLMAYSPLGDG 198
Cdd:cd19100 152 ETG---EFDVVLFPINPAGDHIDsfrEELLPLAREKGVGVIAMKVLAGG 197
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
2-255 |
1.58e-12 |
|
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: 66.72 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 2 KTLSFAGREMPVIGAGLW-GIGEGIDAHAQRRALDAAFDAGLVLLDTAEMYGNGASERVAGAAARSARAQGKDVFVVSKV 80
Cdd:cd19142 4 RNLGKSGLRVSNVGLGTWsTFSTAISEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILKKKGWKRSSYIVSTKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 81 LPSNaRPQ---LMRT----ALTRSLHNLGLDYLDMYLLHwrsTAD----LALVAQQMHEFVQEGLIRHWGVSNFDVADMQ 149
Cdd:cd19142 84 YWSY-GSEergLSRKhiieSVRASLRRLQLDYIDIVIIH---KADpmcpMEEVVRAMSYLIDNGLIMYWGTSRWSPVEIM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 150 ELLAVPYGEECA---CDQNLYNLANRGMDHDLMPWLrdHH---IPLMAYSPL---------------------------- 195
Cdd:cd19142 160 EAFSIARQFNCPtpiCEQSEYHMFCREKMELYMPEL--YNkvgVGLITWSPLslgldpgiseetrrlvtklsfksskykv 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1233716732 196 ---GDGGPAGTRVMVNN-TEVKKVAARHHASAQQVMLAWCVRDGNTLAIPQSA-NPEHLVQDFHS 255
Cdd:cd19142 238 gsdGNGIHEETRRASHKlRELSLIAERLGCDLTQLLIAWSLKNENVQCVLIGAsSLEQLYSQLNS 302
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
37-268 |
2.13e-12 |
|
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381371 [Multi-domain] Cd Length: 304 Bit Score: 65.92 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 37 AFDAGLVLLDTAEMYGNGASERVAGAAARSARAQGKDV---FVVSKVLPSNAR----PQLMRTALTRSLHNLGLDYLDMY 109
Cdd:cd19145 42 AFNSGVTFLDTSDIYGPNTNEVLLGKALKDGPREKVQLatkFGIHEIGGSGVEvrgdPAYVRAACEASLKRLDVDYIDLY 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 110 LLHwR--STADLALVAQQMHEFVQEGLIRHWGVSNFDVADMQELLAVpygEECACDQNLYNLANRGMDHDLMPWLRDHHI 187
Cdd:cd19145 122 YQH-RidTTVPIEITMGELKKLVEEGKIKYIGLSEASADTIRRAHAV---HPITAVQLEWSLWTRDIEEEIIPTCRELGI 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 188 PLMAYSPLGDGGPAGTRVMVNNTE-------------------------VKKVAARHHASAQQVMLAWCVRDGNTLA-IP 241
Cdd:cd19145 198 GIVPYSPLGRGFFAGKAKLEELLEnsdvrkshprfqgenleknkvlyerVEALAKKKGCTPAQLALAWVLHQGEDVVpIP 277
|
250 260
....*....|....*....|....*..
gi 1233716732 242 QSANPEHLVQDFHSGSLELDEHDFAAL 268
Cdd:cd19145 278 GTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
34-251 |
2.42e-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: 65.28 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 34 LDAAFDAGLVLLDTAEMYGNGASERVAgaaarsaraqGK--------DVFVVSKVLP-SNARPQLMRTALTRSLHNLGLD 104
Cdd:cd19096 27 IRYAIDAGINYFDTAYGYGGGKSEEIL----------GEalkegpreKFYLATKLPPwSVKSAEDFRRILEESLKRLGVD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 105 YLDMYLLHWRSTADLALVAQQ------MHEFVQEGLIRHWGVSNFD-VADMQELLAVPYGEECACDQNLYNLANRGMdHD 177
Cdd:cd19096 97 YIDFYLLHGLNSPEWLEKARKggllefLEKAKKEGLIRHIGFSFHDsPELLKEILDSYDFDFVQLQYNYLDQENQAG-RP 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1233716732 178 LMPWLRDHHIPLMAYSPLGDGGPAgtrvmVNNTEVKKVAARHHASAQQVMLAWCVRDGN-TLAIPQSANPEHLVQ 251
Cdd:cd19096 176 GIEYAAKKGMGVIIMEPLKGGGLA-----NNPPEALAILCGAPLSPAEWALRFLLSHPEvTTVLSGMSTPEQLDE 245
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
7-269 |
1.45e-11 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 63.86 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 7 AGREMPVIGAGLW---GIGEGIDAhaQRRALDAAFDAGLVLLDTAEMYG--NGASERVAGAAARSARAQGKDVFVVSKVL 81
Cdd:PRK09912 21 SGLRLPALSLGLWhnfGHVNALES--QRAILRKAFDLGITHFDLANNYGppPGSAEENFGRLLREDFAAYRDELIISTKA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 82 PSNARP---------QLMRTALTRSLHNLGLDYLDMYLLHwRSTADLAL--VAQQMHEFVQEGLIRHWGVSNFD---VAD 147
Cdd:PRK09912 99 GYDMWPgpygsggsrKYLLASLDQSLKRMGLEYVDIFYSH-RVDENTPMeeTASALAHAVQSGKALYVGISSYSperTQK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 148 MQELL---AVPYgeecACDQNLYNLANRGMDHD-LMPWLRDHHIPLMAYSPLG---------DGGPAGTRVMVNNTEVK- 213
Cdd:PRK09912 178 MVELLrewKIPL----LIHQPSYNLLNRWVDKSgLLDTLQNNGVGCIAFTPLAqglltgkylNGIPQDSRMHREGNKVRg 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1233716732 214 ------------------KVAARHHASAQQVMLAWCVRDGNTLAIPQSAN-PEHLVQDFHS-GSLELDEHDFAALD 269
Cdd:PRK09912 254 ltpkmlteanlnslrllnEMAQQRGQSMAQMALSWLLKDERVTSVLIGASrAEQLEENVQAlNNLTFSTEELAQID 329
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
7-267 |
6.70e-11 |
|
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: 61.70 E-value: 6.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 7 AGREMPVIGAGLWGIGEGIDAHAQRRA-LDAAFDAGLVLLDTAEMYG--NGASERVAGAAARSARAQGKDVFVVSKVLPS 83
Cdd:cd19150 8 SGLKLPALSLGLWHNFGDDTPLETQRAiLRTAFDLGITHFDLANNYGppPGSAEENFGRILREDFAGYRDELIISTKAGY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 84 NARP---------QLMRTALTRSLHNLGLDYLDMYLLHwRSTADLAL--VAQQMHEFVQEGLIRHWGVSNFDVADMQELL 152
Cdd:cd19150 88 DMWPgpygewgsrKYLLASLDQSLKRMGLDYVDIFYSH-RFDPDTPLeeTMGALDHAVRSGKALYVGISSYSPERTREAA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 153 AV--PYGEECACDQNLYNLANRGMDHD-LMPWLRDHHIPLMAYSPLG---------DGGPAGTRV---------MVNNTE 211
Cdd:cd19150 167 AIlrELGTPLLIHQPSYNMLNRWVEESgLLDTLQELGVGCIAFTPLAqglltdkylNGIPEGSRAskerslspkMLTEAN 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1233716732 212 VKKV------AARHHASAQQVMLAWCVRDGN-TLAIPQSANPEHLVQDFHSgsleLDEHDFAA 267
Cdd:cd19150 247 LNSIralneiAQKRGQSLAQMALAWVLRDGRvTSALIGASRPEQLEENVGA----LDNLTFSA 305
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
2-253 |
3.76e-10 |
|
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: 59.67 E-value: 3.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 2 KTLSFAGREMPVIGAGLW-GIGEGIDAHAQRRALDAAFDAGLVLLDTAEMYGNGASERVAGAAARSARAQGKDVFVVSKV 80
Cdd:cd19159 4 RNLGKSGLRVSCLGLGTWvTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 81 L---PSNARPQLMRT----ALTRSLHNLGLDYLDMYLLHW-RSTADLALVAQQMHEFVQEGLIRHWGVSNFDVADMQELL 152
Cdd:cd19159 84 YwggKAETERGLSRKhiieGLKGSLQRLQLEYVDVVFANRpDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 153 AVPYGEEC---ACDQNLYNLANRGMDHDLMPWLRdHHIPL--MAYSPL---------GDGGPAGTRVMVNN--------- 209
Cdd:cd19159 164 SVARQFNMippVCEQAEYHLFQREKVEVQLPELY-HKIGVgaMTWSPLacgiisgkyGNGVPESSRASLKCyqwlkeriv 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1233716732 210 -----------TEVKKVAARHHASAQQVMLAWCVR-DGNTLAIPQSANPEHLVQDF 253
Cdd:cd19159 243 seegrkqqnklKDLSPIAERLGCTLPQLAVAWCLRnEGVSSVLLGSSTPEQLIENL 298
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
7-249 |
3.39e-09 |
|
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: 56.64 E-value: 3.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 7 AGREMPVIGAGLWGIGEGIDAHAQRRAL-DAAFDAGLVLLDTAEMYG--NGASERVAGAAARSARAQGKDVFVVS----- 78
Cdd:cd19151 8 SGLKLPAISLGLWHNFGDVDRYENSRAMlRRAFDLGITHFDLANNYGppPGSAEENFGRILKEDLKPYRDELIIStkagy 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 79 KVLPS-----NARPQLMrTALTRSLHNLGLDYLDMYLLHwRSTADLAL--VAQQMHEFVQEGLIRHWGVSNFDVADMQEL 151
Cdd:cd19151 88 TMWPGpygdwGSKKYLI-ASLDQSLKRMGLDYVDIFYHH-RPDPETPLeeTMGALDQIVRQGKALYVGISNYPPEEAREA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 152 LAV--PYGEECACDQNLYNLANRGMDHDLMPWLRDHHIPLMAYSPLGDG--------G-PAGTRVMVNNTEVK------- 213
Cdd:cd19151 166 AAIlkDLGTPCLIHQPKYSMFNRWVEEGLLDVLEEEGIGCIAFSPLAQGlltdrylnGiPEDSRAAKGSSFLKpeqitee 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1233716732 214 ---------KVAARHHASAQQVMLAWCVRDGN-TLAIPQSANPEHL 249
Cdd:cd19151 246 klakvrrlnEIAQARGQKLAQMALAWVLRNKRvTSVLIGASKPSQI 291
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
2-263 |
1.48e-08 |
|
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: 54.99 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 2 KTLSFAGREMPVIGAGLW-GIGEGIDAHAQRRALDAAFDAGLVLLDTAEMYGNGASERVAGAAARSARAQGKDVFVVSKV 80
Cdd:cd19160 6 RNLGKSGLRVSCLGLGTWvTFGSQISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVVTTKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 81 L---PSNARPQLMRT----ALTRSLHNLGLDYLDMYLLHwRSTADLAL--VAQQMHEFVQEGLIRHWGVSNFDVADMQEL 151
Cdd:cd19160 86 YwggQAETERGLSRKhiieGLRGSLDRLQLEYVDIVFAN-RSDPNSPMeeIVRAMTYVINQGMAMYWGTSRWSAMEIMEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 152 LAVPYGEEC---ACDQNLYNLANRGMDHDLMPWLRdHHIPL--MAYSPLGDG---------------------------- 198
Cdd:cd19160 165 YSVARQFNLippVCEQAEYHLFQREKVEMQLPELY-HKIGVgsVTWSPLACGlitgkydgrvpdtcraavkgyqwlkekv 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1233716732 199 -GPAGTRVMVNNTEVKKVAARHHASAQQVMLAWCVR-DGNTLAIPQSANPEHLVQdfHSGSLELDEH 263
Cdd:cd19160 244 qSEEGKKQQAKVKELHPIADRLGCTVAQLAIAWCLRsEGVSSVLLGVSSAEQLIE--NLGSIQVLSQ 308
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
2-252 |
1.83e-08 |
|
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: 54.38 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 2 KTLSFAGREMPVIGAGLWGI--GEGIDAHAQRrALDAAFDAGLVLLDTAEMYGNGASERVAGAAARSARAQGKDVFVVSK 79
Cdd:cd19141 3 RNLGKSGLRVSCLGLGTWVTfgSQISDEVAEE-LVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKGWRRSSYVITTK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 80 VLPSN--------ARPQLMRtALTRSLHNLGLDYLDMYLLHwRS--TADLALVAQQMHEFVQEGLIRHWGVSNFDVADMQ 149
Cdd:cd19141 82 IFWGGkaeterglSRKHIIE-GLKASLERLQLEYVDIVFAN-RPdpNTPMEEIVRAFTHVINQGMAMYWGTSRWSAMEIM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 150 ELLAV--------PygeecACDQNLYNLANRGMDHDLMPWLrdHH---IPLMAYSPL---------GDGGPAGTRVMVNN 209
Cdd:cd19141 160 EAYSVarqfnlipP-----IVEQAEYHLFQREKVEMQLPEL--FHkigVGAMTWSPLacgilsgkyDDGVPEYSRASLKG 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1233716732 210 --------------------TEVKKVAARHHASAQQVMLAWCVR-DGNTLAIPQSANPEHLVQD 252
Cdd:cd19141 233 yqwlkekilseegrrqqaklKELQIIADRLGCTLPQLAIAWCLKnEGVSSVLLGASSTEQLYEN 296
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
2-252 |
1.08e-07 |
|
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: 52.01 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 2 KTLSFAGREMPVIGAGLW-GIGEGIDAHAQRRALDAAFDAGLVLLDTAEMYGNGASERVAGAAARSARAQGKDVFVVSKV 80
Cdd:cd19158 4 RNLGKSGLRVSCLGLGTWvTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 81 L---PSNARPQLMRT----ALTRSLHNLGLDYLDMYLLHwRSTADLAL--VAQQMHEFVQEGLIRHWGVSNFDVADMQEL 151
Cdd:cd19158 84 FwggKAETERGLSRKhiieGLKASLERLQLEYVDVVFAN-RPDPNTPMeeTVRAMTHVINQGMAMYWGTSRWSSMEIMEA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 152 LAVPYGEECA---CDQNLYNLANRGMDHDLMPWLRdHHIPL--MAYSPLGDG---------------------------- 198
Cdd:cd19158 163 YSVARQFNLIppiCEQAEYHMFQREKVEVQLPELF-HKIGVgaMTWSPLACGivsgkydsgippysraslkgyqwlkdki 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1233716732 199 -GPAGTRVMVNNTEVKKVAARHHASAQQVMLAWCVR-DGNTLAIPQSANPEHLVQD 252
Cdd:cd19158 242 lSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRnEGVSSVLLGASNAEQLMEN 297
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
12-254 |
2.00e-07 |
|
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: 51.21 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 12 PVIGAGLWGIGE--GIDAHAQRRALDAAFDAGLVLLDTAEMYGNGASERVAGAAARSARaqGKDVFVVSKV--------- 80
Cdd:cd19162 1 PRLGLGAASLGNlaRAGEDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALARHP--RAEYVVSTKVgrllepgaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 81 -LPSNARPQL------MRTALTRSLHNLGLDYLDMYLLHWRSTADLALVAQQ---MHEFVQEGLIRHWGVSnfdVADMQE 150
Cdd:cd19162 79 gRPAGADRRFdfsadgIRRSIEASLERLGLDRLDLVFLHDPDRHLLQALTDAfpaLEELRAEGVVGAIGVG---VTDWAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 151 LLAVpyGEECACDQNL----YNLANRGMDHDLMPWLRDHHIPLMAYSPLGDG--------------GPAGTRVMVNNTEV 212
Cdd:cd19162 156 LLRA--ARRADVDVVMvagrYTLLDRRAATELLPLCAAKGVAVVAAGVFNSGilatddpagdrydyRPATPEVLARARRL 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1233716732 213 KKVAARHHASAQQVMLAWCVRD---GNTLAIPQSanPEHLVQDFH 254
Cdd:cd19162 234 AAVCRRYGVPLPAAALQFPLRHpavASVVVGAAS--PAELRDNLA 276
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
31-198 |
1.42e-06 |
|
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: 48.70 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 31 RRALDAAFDAGLVLLDTAEMYGNGASERVAgaaarsaraqGK-------DVFVVS-KVLPSNARPQLM--------RTAL 94
Cdd:cd19163 36 IRTVHEALDSGINYIDTAPWYGQGRSETVL----------GKalkgiprDSYYLAtKVGRYGLDPDKMfdfsaeriTKSV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 95 TRSLHNLGLDYLDMYLLHWRSTADL-------ALVAqqMHEFVQEGLIRHWGVSNFDVADMQELLA-VPYGEECACDQNL 166
Cdd:cd19163 106 EESLKRLGLDYIDIIQVHDIEFAPSldqilneTLPA--LQKLKEEGKVRFIGITGYPLDVLKEVLErSPVKIDTVLSYCH 183
|
170 180 190
....*....|....*....|....*....|..
gi 1233716732 167 YNLANRGMDhDLMPWLRDHHIPLMAYSPLGDG 198
Cdd:cd19163 184 YTLNDTSLL-ELLPFFKEKGVGVINASPLSMG 214
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
37-143 |
1.53e-05 |
|
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: 45.60 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 37 AFDAGLVLLDTAEMYGNGASERVAGAAARSARAQGKDVFVVSKV-----LPSNARPQLMRTALTRSLHNLGLDYLDMYLL 111
Cdd:cd19153 42 AFAAGINHFDTSPYYGAESSEAVLGKALAALQVPRSSYTVATKVgryrdSEFDYSAERVRASVATSLERLHTTYLDVVYL 121
|
90 100 110
....*....|....*....|....*....|....*.
gi 1233716732 112 HWRSTADLALVAQQ----MHEFVQEGLIRHWGVSNF 143
Cdd:cd19153 122 HDIEFVDYDTLVDEalpaLRTLKDEGVIKRIGIAGY 157
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
32-269 |
8.13e-05 |
|
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; Phanerochaete chrysosporium ADD (EC1.1.1.91) is a founding member of aldo-keto reductase family 9 member A3. It is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). This family also includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381373 [Multi-domain] Cd Length: 319 Bit Score: 43.27 E-value: 8.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 32 RALDAAFDAGLVLLDTAEMYGNGASERVAGAAARSARAQGKdVFVVSKVLPSNARPQL---------------MRTALTR 96
Cdd:cd19147 38 ELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRKNRDQ-IVIATKFTTDYKAYEVgkgkavnycgnhkrsLHVSVRD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 97 SLHNLGLDYLDMYLLH-WRSTADLALVAQQMHEFVQEGLIRHWGVSNFD--VADMQELLAVPYGE-ECACDQNLYNLANR 172
Cdd:cd19147 117 SLRKLQTDWIDILYVHwWDYTTSIEEVMDSLHILVQQGKVLYLGVSDTPawVVSAANYYATAHGKtPFSVYQGRWNVLNR 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 173 GMDHDLMPWLRDHHIPLMAYSPLGDG-------------GPAGTRVMVNNTE-----------VKKVAARHH-ASAQQVM 227
Cdd:cd19147 197 DFERDIIPMARHFGMALAPWDVLGGGkfqskkaveerkkNGEGLRSFVGGTEqtpeevkiseaLEKVAEEHGtESVTAIA 276
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1233716732 228 LAWcVRDG--NTLAIPQSANPEHLVQDFHSGSLELDEHDFAALD 269
Cdd:cd19147 277 LAY-VRSKapNVFPLVGGRKIEHLKDNIEALSIKLTPEEIEYLE 319
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
13-141 |
8.93e-05 |
|
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: 43.03 E-value: 8.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 13 VIGAGLWGIGEGIDAHAQR--RALDAAFDAGLVLLDTAEMYGNgaSERVAgaaarsaraqGK------------DVFVVS 78
Cdd:cd19164 17 IFGAATFSYQYTTDPESIPpvDIVRRALELGIRAFDTSPYYGP--SEIIL----------GRalkalrdefprdTYFIIT 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1233716732 79 KV---LPS--NARPQLMRTALTRSLHNLGLDYLDMYLLH---WRSTADLALVAQQMHEFVQEGLIRHWGVS 141
Cdd:cd19164 85 KVgryGPDdfDYSPEWIRASVERSLRRLHTDYLDLVYLHdveFVADEEVLEALKELFKLKDEGKIRNVGIS 155
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
15-220 |
4.92e-04 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 40.77 E-value: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 15 GAGLWGIGEGIDAHAQRRALDAAFDAGLVLLDTAEMYGNGASERVAGAAARSAraqGKDVFVVS-KV--LPSNARPQ--- 88
Cdd:cd19161 7 TAGLGNLYTAVSNADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREK---PRDEFVLStKVgrLLKPAREGsvp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 89 ---------------------LMRTaLTRSLHNLGLDYLDMYLLH---------------WRSTADLALVAqqMHEFVQE 132
Cdd:cd19161 84 dpngfvdplpfeivydysydgIMRS-FEDSLQRLGLNRIDILYVHdigvythgdrkerhhFAQLMSGGFKA--LEELKKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 133 GLIRHW--GVSNFDVAD--MQEllavpYGEECACDQNLYNLANRGMDHDLMPWLRDHHIPLMAYSPLGDG---------- 198
Cdd:cd19161 161 GVIKAFglGVNEVQICLeaLDE-----ADLDCFLLAGRYSLLDQSAEEEFLPRCEQRGTSLVIGGVFNSGilatgtksga 235
|
250 260
....*....|....*....|....*.
gi 1233716732 199 ----GPAGTRVMVNNTEVKKVAARHH 220
Cdd:cd19161 236 kfnyGDAPAEIISRVMEIEKICDAYN 261
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
19-273 |
1.03e-03 |
|
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: 40.10 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 19 WGIGEG-IDAHAQRRALDAAFDAGLVLLDTAEMYGNGASErvAGAAARSARAQGKDVFVVSKVLPSNARP---------- 87
Cdd:cd19146 25 WKSMMGeCDKETAFKLLDAFYEQGGNFIDTANNYQGEESE--RWVGEWMASRGNRDEMVLATKYTTGYRRggpikiksny 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 88 -----QLMRTALTRSLHNLGLDYLDMYLLH-WRSTADLALVAQQMHEFVQEGLIRHWGVSNfdvadmQELLAVPYGEECA 161
Cdd:cd19146 103 qgnhaKSLRLSVEASLKKLQTSYIDILYVHwWDYTTSIPELMQSLNHLVAAGKVLYLGVSD------TPAWVVSKANAYA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 162 CD---------QNLYNLANRGMDHDLMPWLRDHHIPLMAYSPLGDG-----------GPAGTRVMV-NNTEVK------K 214
Cdd:cd19146 177 RAhgltqfvvyQGHWSAAFRDFERDILPMCEAEGMALAPWGVLGQGqfrteeefkrrGRSGRKGGPqTEKERKvsekleK 256
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233716732 215 VAARHHASAQQVMLAWCVRDGN-TLAIPQSANPEHLVQDFHSGSLELDEHDFAALDSAFP 273
Cdd:cd19146 257 VAEEKGTAITSVALAYVMHKAPyVFPIVGGRKVEHLKGNIEALGISLSDEEIQEIEDAYP 316
|
|
| |
