|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
1-286 |
0e+00 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 596.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 1 MSSNTFTLGTKSVNRLGYGAMQLAGPGVFGPPRDRHVAITVLREALALGVNHIDTSDFYGPHVTNQIIREALYPYSDDLT 80
Cdd:PRK10376 5 MSSGTFTLGGRSVNRLGYGAMQLAGPGVFGPPKDRDAAIAVLREAVALGVNHIDTSDFYGPHVTNQLIREALHPYPDDLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 81 IVTKIGARRGEDASWLPAFSPAELQKAVHDNLRNLGLDVLDVVNLRvMMGDGHGPAEGSIEASLTVLAEMQQQGLVKHIG 160
Cdd:PRK10376 85 IVTKVGARRGEDGSWLPAFSPAELRRAVHDNLRNLGLDVLDVVNLR-LMGDGHGPAEGSIEEPLTVLAELQRQGLVRHIG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 161 LSNVTPTQVAEARKIAEIVCVQNEYNIAHRADDAMIDALAHDGIAYVPFFPLGGFTPLQSSTLSDVAASLGATPMQVALA 240
Cdd:PRK10376 164 LSNVTPTQVAEARKIAEIVCVQNHYNLAHRADDALIDALARDGIAYVPFFPLGGFTPLQSSTLSDVAASLGATPMQVALA 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 16129367 241 WLLQRSPNILLIPGTSSVAHLRENMAAEKLHLSEEVLSTLDGISRE 286
Cdd:PRK10376 244 WLLQRSPNILLIPGTSSVAHLRENLAAAELVLSEEVLAELDGIARE 289
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
13-273 |
1.26e-142 |
|
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: 401.21 E-value: 1.26e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 13 VNRLGYGAMQLAGPGVFGPPRDRHVAITVLREALALGVNHIDTSDFYGPHVTNQIIREALYPYSDDLTIVTKIGARRGED 92
Cdd:cd19088 1 VSRLGYGAMRLTGPGIWGPPADREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHPYPDDVVIATKGGLVRTGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 93 ASWLPAFSPAELQKAVHDNLRNLGLDVLDVVNLRVMMgdghgpAEGSIEASLTVLAEMQQQGLVKHIGLSNVTPTQVAEA 172
Cdd:cd19088 81 GWWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRID------PKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 173 RKIAEIVCVQNEYNIAHRADDAMIDALAHDGIAYVPFFPLGGFTPLQSSTLSD-VAASLGATPMQVALAWLLQRSPNILL 251
Cdd:cd19088 155 RAIVRIVSVQNRYNLANRDDEGVLDYCEAAGIAFIPWFPLGGGDLAQPGGLLAeVAARLGATPAQVALAWLLARSPVMLP 234
|
250 260
....*....|....*....|..
gi 16129367 252 IPGTSSVAHLRENMAAEKLHLS 273
Cdd:cd19088 235 IPGTSSVEHLEENLAAAGLRLS 256
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
12-286 |
6.56e-76 |
|
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: 233.92 E-value: 6.56e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 12 SVNRLGYGAMQLAGPgvFGPPrDRHVAITVLREALALGVNHIDTSDFYGPHVTNQIIREALYPYS-DDLTIVTKIGARRG 90
Cdd:COG0667 12 KVSRLGLGTMTFGGP--WGGV-DEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALKGRPrDDVVIATKVGRRMG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 91 EDAsWLPAFSPAELQKAVHDNLRNLGLDVLDVVNLrvmmgdgHGP-AEGSIEASLTVLAEMQQQGLVKHIGLSNVTPTQV 169
Cdd:COG0667 89 PGP-NGRGLSREHIRRAVEASLRRLGTDYIDLYQL-------HRPdPDTPIEETLGALDELVREGKIRYIGVSNYSAEQL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 170 AEARKIAE----IVCVQNEYNIAHR-ADDAMIDALAHDGIAYVPFFPLGG----------------------FTPLQSS- 221
Cdd:COG0667 161 RRALAIAEglppIVAVQNEYSLLDRsAEEELLPAARELGVGVLAYSPLAGglltgkyrrgatfpegdraatnFVQGYLTe 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129367 222 -------TLSDVAASLGATPMQVALAWLLQRSPNILLIPGTSSVAHLRENMAAEKLHLSEEVLSTLDGISRE 286
Cdd:COG0667 241 rnlalvdALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADLELSAEDLAALDAALAA 312
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
7-280 |
6.10e-56 |
|
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: 182.42 E-value: 6.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 7 TLGTK--SVNRLGYGAMQLAGpgvFGPPRDRHVAITVLREALALGVNHIDTSDFYGPHVTNQIIREALYPYSDDLTIVTK 84
Cdd:cd19076 4 KLGTQglEVSALGLGCMGMSA---FYGPADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKDRRDEVVIATK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 85 IGARRGEDASWLPAF-SPAELQKAVHDNLRNLGLDVLDVVNLRVMmgDGHGPAEGSIEAsltvLAEMQQQGLVKHIGLSN 163
Cdd:cd19076 81 FGIVRDPGSGFRGVDgRPEYVRAACEASLKRLGTDVIDLYYQHRV--DPNVPIEETVGA----MAELVEEGKVRYIGLSE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 164 VTPTQVAEARKIAEIVCVQNEYNIAHR-ADDAMIDALAHDGIAYVPFFPLG-GFT--PLQSS------------------ 221
Cdd:cd19076 155 ASADTIRRAHAVHPITAVQSEYSLWTRdIEDEVLPTCRELGIGFVAYSPLGrGFLtgAIKSPedlpeddfrrnnprfqge 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129367 222 ----------TLSDVAASLGATPMQVALAWLLQRSPNILLIPGTSSVAHLRENMAAEKLHLSEEVLSTL 280
Cdd:cd19076 235 nfdknlklveKLEAIAAEKGCTPAQLALAWVLAQGDDIVPIPGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
16-283 |
3.14e-55 |
|
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: 180.20 E-value: 3.14e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 16 LGYGAMQLAGPGVFGPPRDrhvAITVLREALALGVNHIDTSDFYGPHVTNQIIREALYPYS---DDLTIVTKIGARrgeD 92
Cdd:pfam00248 1 IGLGTWQLGGGWGPISKEE---ALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPvkrDKVVIATKVPDG---D 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 93 ASWLPAFSPAELQKAVHDNLRNLGLDVLDVVNLrvmmgdgHGP-AEGSIEASLTVLAEMQQQGLVKHIGLSNVTPTQVAE 171
Cdd:pfam00248 75 GPWPSGGSKENIRKSLEESLKRLGTDYIDLYYL-------HWPdPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 172 ARKIAE--IVCVQNEYNIA-HRADDAMIDALAHDGIAYVPFFPLGG---------------------FTPLQSS------ 221
Cdd:pfam00248 148 ALTKGKipIVAVQVEYNLLrRRQEEELLEYCKKNGIPLIAYSPLGGglltgkytrdpdkgpgerrrlLKKGTPLnleale 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129367 222 TLSDVAASLGATPMQVALAWLLQRSPNILLIPGTSSVAHLRENMAAEKLHLSEEVLSTLDGI 283
Cdd:pfam00248 228 ALEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDEL 289
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
15-266 |
3.25e-55 |
|
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: 178.10 E-value: 3.25e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 15 RLGYGAMQlagpgvFGPPRDRHVAITVLREALALGVNHIDTSDFYGPHVTNQIIREAL--YPYSDDLTIVTKIGARRGED 92
Cdd:cd06660 2 RLGLGTMT------FGGDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLkgRGNRDDVVIATKGGHPPGGD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 93 ASWlPAFSPAELQKAVHDNLRNLGLDVLDVVNLrvmmgdgHGPAEG-SIEASLTVLAEMQQQGLVKHIGLSNVTPTQVAE 171
Cdd:cd06660 76 PSR-SRLSPEHIRRDLEESLRRLGTDYIDLYYL-------HRDDPStPVEETLEALNELVREGKIRYIGVSNWSAERLAE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 172 ARKIA------EIVCVQNEYNIAHR--ADDAMIDALAHDGIAYVPFFPLGGftplqsstlsdvaaslGatPMQVALAWLL 243
Cdd:cd06660 148 ALAYAkahglpGFAAVQPQYSLLDRspMEEELLDWAEENGLPLLAYSPLAR----------------G--PAQLALAWLL 209
|
250 260
....*....|....*....|...
gi 16129367 244 QRSPNILLIPGTSSVAHLRENMA 266
Cdd:cd06660 210 SQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
11-281 |
2.44e-53 |
|
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase. Escherichia coli YeaE may act as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381298 [Multi-domain] Cd Length: 263 Bit Score: 174.34 E-value: 2.44e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 11 KSVNRLGYGAMQLAGpGVFGPPRDRHVAITVLREALALGVNHIDTSDFYGPHVTNQIIREALYPYS-DDLTIVTKIgarr 89
Cdd:cd19072 2 EEVPVLGLGTWGIGG-GMSKDYSDDKKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAIKGFDrEDLFITTKV---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 90 gedasWLPAFSPAELQKAVHDNLRNLGLDVLDVVNLrvmmgdgHGP-AEGSIEASLTVLAEMQQQGLVKHIGLSNVTPTQ 168
Cdd:cd19072 77 -----SPDHLKYDDVIKAAKESLKRLGTDYIDLYLI-------HWPnPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 169 VAEARKI---AEIVCVQNEYNIAHR-ADDAMIDALAHDGIAYVPFFPLG-GFTPL--QSSTLSDVAASLGATPMQVALAW 241
Cdd:cd19072 145 LEEAQSYlkkGPIVANQVEYNLFDReEESGLLPYCQKNGIAIIAYSPLEkGKLSNakGSPLLDEIAKKYGKTPAQIALNW 224
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 16129367 242 LLQRsPNILLIPGTSSVAHLRENMAAEKLHLSEEVLSTLD 281
Cdd:cd19072 225 LISK-PNVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
13-281 |
1.03e-52 |
|
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: 173.96 E-value: 1.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 13 VNRLGYGAMQLAGPgvFGPPRDRHVAITVLREALALGVNHIDTSDFYGPHVTNQIIREALYPYSDDLTIVTKIGARRGED 92
Cdd:cd19078 4 VSAIGLGCMGMSHG--YGPPPDKEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKPFRDQVVIATKFGFKIDGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 93 ASWLPAF--SPAELQKAVHDNLRNLGLDVLDVVNL-RVmmgDGHGPaegsIEASLTVLAEMQQQGLVKHIGLSNVTPTQV 169
Cdd:cd19078 82 KPGPLGLdsRPEHIRKAVEGSLKRLQTDYIDLYYQhRV---DPNVP----IEEVAGTMKELIKEGKIRHWGLSEAGVETI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 170 AEARKIAEIVCVQNEYNIAHR-ADDAMIDALAHDGIAYVPFFPLG-GF--------TPLQSST----------------- 222
Cdd:cd19078 155 RRAHAVCPVTAVQSEYSMMWRePEKEVLPTLEELGIGFVPFSPLGkGFltgkidenTKFDEGDdraslprftpealeanq 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129367 223 -----LSDVAASLGATPMQVALAWLLQRSPNILLIPGTSSVAHLRENMAAEKLHLSEEVLSTLD 281
Cdd:cd19078 235 alvdlLKEFAEEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAADIELTPEELREIE 298
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
13-281 |
1.61e-50 |
|
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381310 [Multi-domain] Cd Length: 296 Bit Score: 168.09 E-value: 1.61e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 13 VNRLGYGAMQLaGPGVFGPPrDRHVAITVLREALALGVNHIDTSDFYGPHVTNQIIREALYPYSDDLTIVTKIGARRGED 92
Cdd:cd19084 4 VSRIGLGTWAI-GGTWWGEV-DDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKGRRDDVVIATKCGLRWDGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 93 ASWLPAFSPAELQKAVHDNLRNLGLDVLDVVNLrvmmgdgHGPAEG-SIEASLTVLAEMQQQGLVKHIGLSNVTPTQVAE 171
Cdd:cd19084 82 KGVTKDLSPESIRKEVEQSLRRLQTDYIDLYQI-------HWPDPNtPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 172 ARKIAEIVCVQNEYNIAHR-ADDAMIDALAHDGIAYVPFFPLGG------FTPLQS------------------------ 220
Cdd:cd19084 155 ARKYGPIVSLQPPYSMLEReIEEELLPYCRENGIGVLPYGPLAQglltgkYKKEPTfppddrrsrfpffrgenfeknlei 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129367 221 -STLSDVAASLGATPMQVALAWLLQRSPNILLIPGTSSVAHLRENMAAEKLHLSEEVLSTLD 281
Cdd:cd19084 235 vDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDWELTEEELKEID 296
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
13-286 |
5.08e-50 |
|
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: 166.61 E-value: 5.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 13 VNRLGYGAMQLAGpGVFGPPRDRHVAITVLREALALGVNHIDTSDFYGPHVTNQIIREALYPYSDDLTIVTKIgarrged 92
Cdd:cd19085 1 VSRLGLGCWQFGG-GYWWGDQDDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKGRRDDVVIATKV------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 93 asWLPAFSPAELQKAVHDNLRNLGLDVLDVVNLrvmmgdgHGPAEG-SIEASLTVLAEMQQQGLVKHIGLSNVTPTQVAE 171
Cdd:cd19085 73 --SPDNLTPEDVRKSCERSLKRLGTDYIDLYQI-------HWPSSDvPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 172 ARKIAEIVCVQNEYNIAHRA-DDAMIDALAHDGIAYVPFFPL------GGFTPLQSST---------------------- 222
Cdd:cd19085 144 ALDAGRIDSNQLPYNLLWRAiEYEILPFCREHGIGVLAYSPLaqglltGKFSSAEDFPpgdartrlfrhfepgaeeetfe 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129367 223 ----LSDVAASLGATPMQVALAWLLQRsPNI-LLIPGTSSVAHLRENMAAEKLHLSEEVLSTLDGISRE 286
Cdd:cd19085 224 alekLKEIADELGVTMAQLALAWVLQQ-PGVtSVIVGARNPEQLEENAAAVDLELSPSVLERLDEISDP 291
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
12-267 |
1.41e-47 |
|
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: 158.79 E-value: 1.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 12 SVNRLGYGAMQLAGPgvFGPPRDRHVAITVLREALALGVNHIDTSDFYGPHVTNQIIREALYPYSDDLTIVTKIGARRGE 91
Cdd:cd19086 2 EVSEIGFGTWGLGGD--WWGDVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKGRRDKVVIATKFGNRFDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 92 DASWLPAFSPAELQKAVHDNLRNLGLDVLDVVNLrvmmgdgHGP--AEGSIEASLTVLAEMQQQGLVKHIGLSNVTPTQV 169
Cdd:cd19086 80 GPERPQDFSPEYIREAVEASLKRLGTDYIDLYQL-------HNPpdEVLDNDELFEALEKLKQEGKIRAYGVSVGDPEEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 170 AEARKIAEIVCVQNEYNIAH-RADDAMIDALAHDGIAYVpffplgGFTPLQSSTLSDVAAslgatpmQVALAWLLQRSPN 248
Cdd:cd19086 153 LAALRRGGIDVVQVIYNLLDqRPEEELFPLAEEHGVGVI------ARVPLASGLLTGKLA-------QAALRFILSHPAV 219
|
250
....*....|....*....
gi 16129367 249 ILLIPGTSSVAHLRENMAA 267
Cdd:cd19086 220 STVIPGARSPEQVEENAAA 238
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
27-285 |
5.77e-47 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 157.91 E-value: 5.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 27 GVFGPPRDrhVAITVLREALALGVNHIDTSDFYGphvtN-----QIIREALYPySDDLTIVTKIgarrgedasWLPAFSP 101
Cdd:COG0656 11 GTWQLPGE--EAAAAVRTALEAGYRHIDTAAMYG----NeegvgEAIAASGVP-REELFVTTKV---------WNDNHGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 102 AELQKAVHDNLRNLGLDVLDVVNLrvmmgdgHGPAEGSIEASLTVLAEMQQQGLVKHIGLSNVTPTQVAEARKIAEIVCV 181
Cdd:COG0656 75 DDTLAAFEESLERLGLDYLDLYLI-------HWPGPGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETGVKPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 182 --QNEYNIAHRADDaMIDALAHDGIAYVPFFPLGGFTPLQSSTLSDVAASLGATPMQVALAWLLQRspNILLIPGTSSVA 259
Cdd:COG0656 148 vnQVELHPYLQQRE-LLAFCREHGIVVEAYSPLGRGKLLDDPVLAEIAEKHGKTPAQVVLRWHLQR--GVVVIPKSVTPE 224
|
250 260
....*....|....*....|....*.
gi 16129367 260 HLRENMAAEKLHLSEEVLSTLDGISR 285
Cdd:COG0656 225 RIRENLDAFDFELSDEDMAAIDALDR 250
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
21-281 |
1.21e-42 |
|
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: 146.47 E-value: 1.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 21 MQLAGPGVFGPPRDRhvAITVLREALALGVNHIDTSDFYGphvtNQ-----IIREALYPySDDLTIVTKIgarrgedasW 95
Cdd:cd19071 1 MPLIGLGTYKLKPEE--TAEAVLAALEAGYRHIDTAAAYG----NEaevgeAIRESGVP-REELFITTKL---------W 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 96 LPAFSPAELQKAVHDNLRNLGLDVLDVVNLRVMMGDGHGPAEGSIEASLTVLAEMQQQGLVKHIGLSNVTPTQVAEARKI 175
Cdd:cd19071 65 PTDHGYERVREALEESLKDLGLDYLDLYLIHWPVPGKEGGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 176 AEI--VCVQNEYNIAHRaDDAMIDALAHDGIAYVPFFPLGG--FTPLQSSTLSDVAASLGATPMQVALAWLLQRspNILL 251
Cdd:cd19071 145 ARIkpAVNQIELHPYLQ-QKELVEFCKEHGIVVQAYSPLGRgrRPLLDDPVLKEIAKKYGKTPAQVLLRWALQR--GVVV 221
|
250 260 270
....*....|....*....|....*....|
gi 16129367 252 IPGTSSVAHLRENMAAEKLHLSEEVLSTLD 281
Cdd:cd19071 222 IPKSSNPERIKENLDVFDFELSEEDMAAID 251
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
29-281 |
3.67e-40 |
|
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: 139.71 E-value: 3.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 29 FGPPRDRH-VAITVLREALALGVNHIDTSDFYGPH-VTNQIIREALYPySDDLTIVTKIgarrgedasWLPAFSPAELQK 106
Cdd:cd19073 6 LGTWQLRGdDCANAVKEALELGYRHIDTAEIYNNEaEVGEAIAESGVP-REDLFITTKV---------WRDHLRPEDLKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 107 AVHDNLRNLGLDVLDVVNLrvmmgdgHGPA-EGSIEASLTVLAEMQQQGLVKHIGLSNVTPTQVAEARKIAE--IVCVQN 183
Cdd:cd19073 76 SVDRSLEKLGTDYVDLLLI-------HWPNpTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPlpIAVNQV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 184 EYNIAHRADDaMIDALAHDGIAYVPFFPLGGFTPLQSSTLSDVAASLGATPMQVALAWLLQRspNILLIPGTSSVAHLRE 263
Cdd:cd19073 149 EFHPFLYQAE-LLEYCRENDIVITAYSPLARGEVLRDPVIQEIAEKYDKTPAQVALRWLVQK--GIVVIPKASSEDHLKE 225
|
250
....*....|....*...
gi 16129367 264 NMAAEKLHLSEEVLSTLD 281
Cdd:cd19073 226 NLAIFDWELTSEDVAKID 243
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
15-283 |
1.05e-39 |
|
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: 138.93 E-value: 1.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 15 RLGYGAMQLAGpgvfgpprdrHVAITVLREALALGVNHIDTSDFYGphvtN-----QIIREALYPySDDLTIVTKIgarr 89
Cdd:cd19140 10 ALGLGTYPLTG----------EECTRAVEHALELGYRHIDTAQMYG----NeaqvgEAIAASGVP-RDELFLTTKV---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 90 gedasWLPAFSPAELQKAVHDNLRNLGLDVLDVVNLrvmmgdgHGP-AEGSIEASLTVLAEMQQQGLVKHIGLSNVTPTQ 168
Cdd:cd19140 71 -----WPDNYSPDDFLASVEESLRKLRTDYVDLLLL-------HWPnKDVPLAETLGALNEAQEAGLARHIGVSNFTVAL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 169 VAEARKIAE--IVCVQNEYNIAHRaDDAMIDALAHDGIAYVPFFPLGGFTPLQSSTLSDVAASLGATPMQVALAWLLQrS 246
Cdd:cd19140 139 LREAVELSEapLFTNQVEYHPYLD-QRKLLDAAREHGIALTAYSPLARGEVLKDPVLQEIGRKHGKTPAQVALRWLLQ-Q 216
|
250 260 270
....*....|....*....|....*....|....*..
gi 16129367 247 PNILLIPGTSSVAHLRENMAAEKLHLSEEVLSTLDGI 283
Cdd:cd19140 217 EGVAAIPKATNPERLEENLDIFDFTLSDEEMARIAAL 253
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
12-281 |
2.43e-39 |
|
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: 139.27 E-value: 2.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 12 SVNRLGYGAMqlagpgVFGPPRDRHVAITVLREALALGVNHIDTSDFYGPHVTN-------QIIREALYPYS--DDLTIV 82
Cdd:cd19081 8 SVSPLCLGTM------VFGWTADEETSFALLDAFVDAGGNFIDTADVYSAWVPGnaggeseTIIGRWLKSRGkrDRVVIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 83 TKIGARRGEDAswlPAFSPAELQKAVHDNLRNLGLDVLDVVNLrvmmgdgHGP-AEGSIEASLTVLAEMQQQGLVKHIGL 161
Cdd:cd19081 82 TKVGFPMGPNG---PGLSRKHIRRAVEASLRRLQTDYIDLYQA-------HWDdPATPLEETLGALNDLIRQGKVRYIGA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 162 SNVTPTQVAEARKIAE------IVCVQNEYNIAHRA--DDAMIDALAHDGIAYVPFFPL-GGF--------TPLQSS--- 221
Cdd:cd19081 152 SNYSAWRLQEALELSRqhglprYVSLQPEYNLVDREsfEGELLPLCREEGIGVIPYSPLaGGFltgkyrseADLPGStrr 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129367 222 -----------------TLSDVAASLGATPMQVALAWLLQRSPNILLIPGTSSVAHLRENMAAEKLHLSEEVLSTLD 281
Cdd:cd19081 232 geaakrylnerglrildALDEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAGLRLTDEEVARLD 308
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-283 |
3.38e-39 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 138.96 E-value: 3.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 15 RLGYGAMQLAGPGVFGP--PRDRHVAITVLREALALGVNHIDTSDFYGPHVTNQIIREALYPYSDDLTIVTKIGARRGED 92
Cdd:cd19102 3 TIGLGTWAIGGGGWGGGwgPQDDRDSIAAIRAALDLGINWIDTAAVYGLGHSEEVVGRALKGLRDRPIVATKCGLLWDEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 93 ASWLPAFSPAELQKAVHDNLRNLGLDVLDVVNLrvmmgdgHGPA-EGSIEASLTVLAEMQQQGLVKHIGLSNVTPTQVAE 171
Cdd:cd19102 83 GRIRRSLKPASIRAECEASLRRLGVDVIDLYQI-------HWPDpDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 172 ARKIAEIVCVQNEYNIAHRADDAMI-DALAHDGIAYVPFFPL------GGFTPLQSSTLSD------------------- 225
Cdd:cd19102 156 CQAIHPIASLQPPYSLLRRGIEAEIlPFCAEHGIGVIVYSPMqsglltGKMTPERVASLPAddwrrrspffqepnlarnl 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129367 226 --------VAASLGATPMQVALAWLLQRsPNIL-LIPGTSSVAHLRENMAAEKLHLSEEVLSTLDGI 283
Cdd:cd19102 236 alvdalrpIAERHGRTVAQLAIAWVLRR-PEVTsAIVGARRPDQIDETVGAADLRLTPEELAEIEAL 301
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
5-281 |
3.64e-39 |
|
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: 137.77 E-value: 3.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 5 TFTLGT-KSVNRLGYGAMQLaGPGvfgpPRDRHVAITVLREALALGVNHIDTSDFYGPHVTNQIIREALYPYSDDLTIVT 83
Cdd:cd19138 2 TVTLPDgTKVPALGQGTWYM-GED----PAKRAQEIEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIRGRRDKVFLVS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 84 KIgarrgedaswLPA-FSPAELQKAVHDNLRNLGLDVLDVVNLrvmmgdgHGPAEGSIEASLTVLAEMQQQGLVKHIGLS 162
Cdd:cd19138 77 KV----------LPSnASRQGTVRACERSLRRLGTDYLDLYLL-------HWRGGVPLAETVAAMEELKKEGKIRAWGVS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 163 NVTPTQVAEARKIA---EIVCVQNEYNIAHRA-DDAMIDALAHDGIAYVPFFPL--GGFTP---LQSSTLSDVAASLGAT 233
Cdd:cd19138 140 NFDTDDMEELWAVPgggNCAANQVLYNLGSRGiEYDLLPWCREHGVPVMAYSPLaqGGLLRrglLENPTLKEIAARHGAT 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 16129367 234 PMQVALAWLLqRSPNILLIPGTSSVAHLRENMAAEKLHLSEEVLSTLD 281
Cdd:cd19138 220 PAQVALAWVL-RDGNVIAIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
13-283 |
3.65e-39 |
|
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: 139.09 E-value: 3.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 13 VNRLGYGAMQLAGPGVFgPPRDRHVAITVLREALALGVNHIDTSDFYGPHVTNQIIREALYPYS-DDLTIVTKIGARRGE 91
Cdd:cd19083 11 VNPIGLGTNAVGGHNLY-PNLDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLKEYNrNEVVIATKGAHKFGG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 92 DASWLPAfSPAELQKAVHDNLRNLGLDVLDVvnLRVMMGDGHGPAEGSIEAsltvLAEMQQQGLVKHIGLSNVTPTQVAE 171
Cdd:cd19083 90 DGSVLNN-SPEFLRSAVEKSLKRLNTDYIDL--YYIHFPDGETPKAEAVGA----LQELKDEGKIRAIGVSNFSLEQLKE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 172 ARKIAEIVCVQNEYNIAHR-ADDAMIDALAHDGIAYVPFFPL------GGFTP--------LQSST-------------- 222
Cdd:cd19083 163 ANKDGYVDVLQGEYNLLQReAEEDILPYCVENNISFIPYFPLasgllaGKYTKdtkfpdndLRNDKplfkgerfsenldk 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129367 223 ---LSDVAASLGATPMQVALAWLLQRSPNILLIPGTSSVAHLRENMAAEKLHLSEEVLSTLDGI 283
Cdd:cd19083 243 vdkLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
5-275 |
4.26e-38 |
|
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: 136.42 E-value: 4.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 5 TFTLGTK--SVNRLGYGAMQLAGpgVFGPPRDRHVAITVLREALALGVNHIDTSDFYGPHvTNQIIR-EALYP-YSDDLT 80
Cdd:cd19144 3 TRTLGRNgpSVPALGFGAMGLSA--FYGPPKPDEERFAVLDAAFELGCTFWDTADIYGDS-EELIGRwFKQNPgKREKIF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 81 IVTKIGARR-GEDASWLPAFSPAELQKAVHDNLRNLGLDVLDVVNL-RVmmgDGHGPaegsIEASLTVLAEMQQQGLVKH 158
Cdd:cd19144 80 LATKFGIEKnVETGEYSVDGSPEYVKKACETSLKRLGVDYIDLYYQhRV---DGKTP----IEKTVAAMAELVQEGKIKH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 159 IGLSNVTPTQVAEARKIAEIVCVQNEYNI----AHRADDAMIDALAHDGIAYVPFFPLG-GF-TPLQSS----------- 221
Cdd:cd19144 153 IGLSECSAETLRRAHAVHPIAAVQIEYSPfsldIERPEIGVLDTCRELGVAIVAYSPLGrGFlTGAIRSpddfeegdfrr 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129367 222 ------------------TLSDVAASLGATPMQVALAWLLQRSPNILLIPGTSSVAHLRENMAAEKLHLSEE 275
Cdd:cd19144 233 maprfqaenfpknlelvdKIKAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLGALKVKLTEE 304
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
38-281 |
4.61e-38 |
|
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: 135.01 E-value: 4.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 38 AITVLREALALGVNHIDTSDFYGPHVTNQIIREA-LYPYSDDLTIVTKIgarrgedasWLPAFSPAELQKAVHDNLRNLG 116
Cdd:cd19137 28 MVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAiKDFPREDLFIVTKV---------WPTNLRYDDLLRSLQNSLRRLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 117 LDVLDVVNLrvmmgdgHGP-AEGSIEASLTVLAEMQQQGLVKHIGLSNVTPTQVAEARKIAE--IVCVQNEYNIAHR--A 191
Cdd:cd19137 99 TDYIDLYLI-------HWPnPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQtpIVCNQVKYNLEDRdpE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 192 DDAMIDALAHDGIAYVPFFPLGGFTPLQSSTLSDVAASLGATPMQVALAWLLQRsPNILLIPGTSSVAHLRENMAAEKLH 271
Cdd:cd19137 172 RDGLLEYCQKNGITVVAYSPLRRGLEKTNRTLEEIAKNYGKTIAQIALAWLIQK-PNVVAIPKAGRVEHLKENLKATEIK 250
|
250
....*....|
gi 16129367 272 LSEEVLSTLD 281
Cdd:cd19137 251 LSEEEMKLLD 260
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
13-283 |
1.09e-35 |
|
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: 130.38 E-value: 1.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 13 VNRLGYGAMqlagpgVFGPPRDRHVAITVLREALALGVNHIDTSDFY-------GPHVTNQIIREAL--YPYSDDLTIVT 83
Cdd:cd19094 1 VSEICLGTM------TWGEQNTEAEAHEQLDYAFDEGVNFIDTAEMYpvppspeTQGRTEEIIGSWLkkKGNRDKVVLAT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 84 KIgARRGEDASWL----PAFSPAELQKAVHDNLRNLGLDVLDVVNL-----RVMMGDGHG-------PAEGSIEASLTVL 147
Cdd:cd19094 75 KV-AGPGEGITWPrgggTRLDRENIREAVEGSLKRLGTDYIDLYQLhwpdrYTPLFGGGYytepseeEDSVSFEEQLEAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 148 AEMQQQGLVKHIGLSNVTP------TQVAEARKIAEIVCVQNEYNIAHRADD-AMIDALAHDGIAYVPFFPLGG------ 214
Cdd:cd19094 154 GELVKAGKIRHIGLSNETPwgvmkfLELAEQLGLPRIVSIQNPYSLLNRNFEeGLAEACHRENVGLLAYSPLAGgvltgk 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 215 -------------------FTPLQSST-------LSDVAASLGATPMQVALAWLLQRSPNILLIPGTSSVAHLRENMAAE 268
Cdd:cd19094 234 yldgaarpeggrlnlfpgyMARYRSPQaleavaeYVKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLKENIDAF 313
|
330
....*....|....*
gi 16129367 269 KLHLSEEVLSTLDGI 283
Cdd:cd19094 314 DVPLSDELLAEIDAV 328
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
13-281 |
1.33e-35 |
|
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: 129.27 E-value: 1.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 13 VNRLGYGAMQLAGPGV-FGPPRDRHVAITVLREALALGVNHIDTSDFYGPHVTNQIIREAL--YPYSDDLTIVTKigarr 89
Cdd:cd19093 2 VSPLGLGTWQWGDRLWwGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLkeLGDRDEVVIATK----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 90 gedasWLPA---FSPAELQKAVHDNLRNLGLDVLDVVNLrvmmgdgHGPAE--GSIEASLTVLAEMQQQGLVKHIGLSNV 164
Cdd:cd19093 77 -----FAPLpwrLTRRSVVKALKASLERLGLDSIDLYQL-------HWPGPwySQIEALMDGLADAVEEGLVRAVGVSNY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 165 TPTQVAEARKI-----AEIVCVQNEYNIAHRA--DDAMIDALAHDGIAYVPFFPLG------------------------ 213
Cdd:cd19093 145 SADQLRRAHKAlkergVPLASNQVEYSLLYRDpeQNGLLPACDELGITLIAYSPLAqglltgkyspenpppggrrrlfgr 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129367 214 ----GFTPLQSsTLSDVAASLGATPMQVALAWLLQRspNILLIPGTSSVAHLRENMAAEKLHLSEEVLSTLD 281
Cdd:cd19093 225 knleKVQPLLD-ALEEIAEKYGKTPAQVALNWLIAK--GVVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
15-267 |
2.54e-35 |
|
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: 127.35 E-value: 2.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 15 RLGYGAMqlaGPGVFGPPRDRHVAITVLREALALGVNHIDTSDFYGPhvTNQIIREAL-YPYSDDLTIVTKIGARRGEDA 93
Cdd:cd19095 2 VLGLGTS---GIGRVWGVPSEAEAARLLNTALDLGINLIDTAPAYGR--SEERLGRALaGLRRDDLFIATKVGTHGEGGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 94 SWlPAFSPAELQKAVHDNLRNLGLDVLDVVNLrvmmgdgHGPAEGSI-EASLTVLAEMQQQGLVKHIGLSNVTPTqVAEA 172
Cdd:cd19095 77 DR-KDFSPAAIRASIERSLRRLGTDYIDLLQL-------HGPSDDELtGEVLETLEDLKAAGKVRYIGVSGDGEE-LEAA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 173 RKIAEIVCVQNEYNIAHRADDAMIDALAHDGIA-----------YVPFFPLGGFTPLQSSTLSDVAASLGATPMQVALAW 241
Cdd:cd19095 148 IASGVFDVVQLPYNVLDREEEELLPLAAEAGLGvivnrplangrLRRRVRRRPLYADYARRPEFAAEIGGATWAQAALRF 227
|
250 260
....*....|....*....|....*.
gi 16129367 242 LLQRSPNILLIPGTSSVAHLRENMAA 267
Cdd:cd19095 228 VLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
13-281 |
3.38e-35 |
|
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381305 [Multi-domain] Cd Length: 312 Bit Score: 128.47 E-value: 3.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 13 VNRLGYGAMQLAGPGVFGPPRDRHVAITVLREALALGVNHIDTSDFYGPHVTNQIIREAL--YPYSDDLTIVTKIGARRG 90
Cdd:cd19079 12 VSRLCLGCMSFGDPKWRPWVLDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALkeFAPRDEVVIATKVYFPMG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 91 EDASwLPAFSPAELQKAVHDNLRNLGLDVLDVVNLRVMmgDGHGPaegsIEASLTVLAEMQQQGLVKHIGLSNVTPTQVA 170
Cdd:cd19079 92 DGPN-GRGLSRKHIMAEVDASLKRLGTDYIDLYQIHRW--DYETP----IEETLEALHDVVKSGKVRYIGASSMYAWQFA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 171 EARKIAEI------VCVQNEYNIAHRADD-AMIDALAHDGIAYVPFFPL-GGF--------TPLQSSTLSD--------- 225
Cdd:cd19079 165 KALHLAEKngwtkfVSMQNHYNLLYREEErEMIPLCEEEGIGVIPWSPLaRGRlarpwgdtTERRRSTTDTaklkydyft 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129367 226 ------------VAASLGATPMQVALAWLLQRSPNILLIPGTSSVAHLRENMAAEKLHLSEEVLSTLD 281
Cdd:cd19079 245 eadkeivdrveeVAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAALDIKLSEEEIKYLE 312
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
12-275 |
3.56e-33 |
|
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: 122.66 E-value: 3.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 12 SVNRLGYGAMQLAGPGVfgpprDRHVAITVLREALALGVNHIDTSDFYGPHVTNQIIREALY---PYSDDLTIVTKIGAR 88
Cdd:cd19092 5 EVSRLVLGCMRLADWGE-----SAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALAlnpGLREKIEIQTKCGIR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 89 RGED-ASWLPA---FSPAELQKAVHDNLRNLGLDVLDVVNLrvmmgdgHGP-----AEGSIEAsltvLAEMQQQGLVKHI 159
Cdd:cd19092 80 LGDDpRPGRIKhydTSKEHILASVEGSLKRLGTDYLDLLLL-------HRPdplmdPEEVAEA----FDELVKSGKVRYF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 160 GLSNVTPTQVA--EARKIAEIVCVQNEYNIAHRA--DDAMIDALAHDGIAYVPFFPLGG---FTPLQSST------LSDV 226
Cdd:cd19092 149 GVSNFTPSQIEllQSYLDQPLVTNQIELSLLHTEaiDDGTLDYCQLLDITPMAWSPLGGgrlFGGFDERFqrlraaLEEL 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 16129367 227 AASLGATPMQVALAWLLQRSPNILLIPGTSSVAHLRENMAAEKLHLSEE 275
Cdd:cd19092 229 AEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALDIELTRE 277
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
9-281 |
2.35e-32 |
|
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: 120.81 E-value: 2.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 9 GTKSVNRLGYGAMQLAGPGvfgPPRDRHVAITVLREALALGVNHIDTSDFYG---PHVTNQIIREAL--YP-YSDDLTIV 82
Cdd:cd19077 1 NGKLVGPIGLGLMGLTWRP---NPTPDEEAFETMKAALDAGSNLWNGGEFYGppdPHANLKLLARFFrkYPeYADKVVLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 83 TKIGARRGEDAswlPAFSPAELQKAVHDNLRNLG-LDVLDVVNL-RVmmgDGHGPaegsIEASLTVLAEMQQQGLVKHIG 160
Cdd:cd19077 78 VKGGLDPDTLR---PDGSPEAVRKSIENILRALGgTKKIDIFEPaRV---DPNVP----IEETIKALKELVKEGKIRGIG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 161 LSNVTPTQVAEARKIAEIVCVQNEYNIAHR--ADDAMIDALAHDGIAYVPFFPLG-GFTPLQSSTLSDV----------- 226
Cdd:cd19077 148 LSEVSAETIRRAHAVHPIAAVEVEYSLFSReiEENGVLETCAELGIPIIAYSPLGrGLLTGRIKSLADIpegdfrrhldr 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129367 227 -------------------AASLGATPMQVALAWLLQRS-PNILLIPGTSSVAHLRENMAAEKLHLSEEVLSTLD 281
Cdd:cd19077 228 fngenfeknlklvdalqelAEKKGCTPAQLALAWILAQSgPKIIPIPGSTTLERVEENLKAANVELTDEELKEIN 302
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
13-285 |
5.78e-32 |
|
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: 119.98 E-value: 5.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 13 VNRLGYGAMQlagpgvFGPPRDRHVAITVLREALALGVNHIDTSDFYGPHVTNQIIREALYPYSDDLTIVTKIGARRGED 92
Cdd:cd19087 13 VSRLCLGTMN------FGGRTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAGRRDDIVLATKVFGPMGDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 93 AsWLPAFSPAELQKAVHDNLRNLGLDVLDVVNLRvmmgdgHGPAEGSIEASLTVLAEMQQQGLVKHIGLSNVTPTQVAEA 172
Cdd:cd19087 87 P-NDRGLSRRHIRRAVEASLRRLQTDYIDLYQMH------HFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQIAKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 173 RKIAE------IVCVQNEYNIAHR-ADDAMIDALAHDGIAYVPFFPLGG------FTPLQSST----------------- 222
Cdd:cd19087 160 QGIAArrgllrFVSEQPMYNLLKRqAELEILPAARAYGLGVIPYSPLAGglltgkYGKGKRPEsgrlveraryqarygle 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129367 223 --------LSDVAASLGATPMQVALAWLLQR----SPnillIPGTSSVAHLRENMAAEKLHLSEEVLSTLDGISR 285
Cdd:cd19087 240 eyrdiaerFEALAAEAGLTPASLALAWVLSHpavtSP----IIGPRTLEQLEDSLAALEITLTPELLAEIDELFP 310
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
25-281 |
7.16e-32 |
|
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: 118.22 E-value: 7.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 25 GPGVFGPPRDrhVAITVLREALALGVNHIDTSDFYGPHV-TNQIIREALYPySDDLTIVTKIgarrgedasWLPAFSPAE 103
Cdd:cd19139 5 GLGTFRLKDD--VVIDSVRTALELGYRHIDTAQIYDNEAaVGQAIAESGVP-RDELFITTKI---------WIDNLSKDK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 104 LQKAVHDNLRNLGLDVLDVVNLRVMMGDGHGPAEGSIEAsltvLAEMQQQGLVKHIGLSNVTPTQVAEARKI---AEIVC 180
Cdd:cd19139 73 LLPSLEESLEKLRTDYVDLTLIHWPSPNDEVPVEEYIGA----LAEAKEQGLTRHIGVSNFTIALLDEAIAVvgaGAIAT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 181 VQNEYNiAHRADDAMIDALAHDGIAYVPFFPLGGFTPLQSSTLSDVAASLGATPMQVALAWLLQRspNILLIPGTSSVAH 260
Cdd:cd19139 149 NQIELS-PYLQNRKLVAHCKQHGIHVTSYMTLAYGKVLDDPVLAAIAERHGATPAQIALAWAMAR--GYAVIPSSTKREH 225
|
250 260
....*....|....*....|.
gi 16129367 261 LRENMAAEKLHLSEEVLSTLD 281
Cdd:cd19139 226 LRSNLLALDLTLDADDMAAIA 246
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
13-284 |
7.77e-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: 120.03 E-value: 7.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 13 VNRLGYGAMQLAGPGVFGPPR---DRHVAITVLREALALGVNHIDTSDFYGPHVTNQIIREALYPYSDDLTIVTKIGARR 89
Cdd:cd19091 13 VSELALGTMTFGGGGGFFGAWggvDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKGRRDDVLIATKVRGRM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 90 GEDASWLPAfSPAELQKAVHDNLRNLGLDVLDVVNLrvmmgdgHGP-AEGSIEASLTVLAEMQQQGLVKHIGLSNVTPTQ 168
Cdd:cd19091 93 GEGPNDVGL-SRHHIIRAVEASLKRLGTDYIDLYQL-------HGFdALTPLEETLRALDDLVRQGKVRYIGVSNFSAWQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 169 VAEARKIAE------IVCVQNEYNIAHR-ADDAMIDALAHDGIAYVPFFPLGG------FTPLQSS-------------- 221
Cdd:cd19091 165 IMKALGISErrglarFVALQAYYSLLGRdLEHELMPLALDQGVGLLVWSPLAGgllsgkYRRGQPApegsrlrrtgfdfp 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129367 222 ------------TLSDVAASLGATPMQVALAWLLQRSPNILLIPGTSSVAHLRENMAAEKLHLSEEVLSTLDGIS 284
Cdd:cd19091 245 pvdrergydvvdALREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGAAGLSLTPEEIARLDKVS 319
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
8-280 |
1.12e-31 |
|
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: 119.07 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 8 LGTK--SVNRLGYGAMQLAGpgVFGPPRDRHVAITVLREALALGVNHIDTSDFYGPHVTNQIIREALY-PYSDDLTIVTK 84
Cdd:cd19145 5 LGSQglEVSAQGLGCMGLSG--DYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALKdGPREKVQLATK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 85 IGARRGEDASWLPAFSPAELQKAVHDNLRNLGLDVLDV-----VNLRVmmgdghgpaegSIEASLTVLAEMQQQGLVKHI 159
Cdd:cd19145 83 FGIHEIGGSGVEVRGDPAYVRAACEASLKRLDVDYIDLyyqhrIDTTV-----------PIEITMGELKKLVEEGKIKYI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 160 GLSNVTPTQVAEARKIAEIVCVQNEYNIAHR-ADDAMIDALAHDGIAYVPFFPLG-GF----TPLQSS------------ 221
Cdd:cd19145 152 GLSEASADTIRRAHAVHPITAVQLEWSLWTRdIEEEIIPTCRELGIGIVPYSPLGrGFfagkAKLEELlensdvrkshpr 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129367 222 --------------TLSDVAASLGATPMQVALAWLLQRSPNILLIPGTSSVAHLRENMAAEKLHLSEEVLSTL 280
Cdd:cd19145 232 fqgenleknkvlyeRVEALAKKKGCTPAQLALAWVLHQGEDVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-267 |
1.18e-31 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 117.69 E-value: 1.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 13 VNRLGYGAMQLAGPgvfgpprdrhvAITVLREALALGVNHIDTSDFYGPHVTNQIIREALYPYS-DDLTIVTKIGARRGE 91
Cdd:cd19105 13 VSRLGFGGGGLPRE-----------SPELLRRALDLGINYFDTAEGYGNGNSEEIIGEALKGLRrDKVFLATKASPRLDK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 92 DaswlpafSPAELQKAVHDNLRNLGLDVLDVVNL-RVMMGDGHGPAEGSIEAsltvLAEMQQQGLVKHIGLS--NVTPTQ 168
Cdd:cd19105 82 K-------DKAELLKSVEESLKRLQTDYIDIYQLhGVDTPEERLLNEELLEA----LEKLKKEGKVRFIGFSthDNMAEV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 169 VAEARKIAEIVCVQNEYNIAHRADDAM--IDALAHDGIAYVPFFPLGGFTPLQSSTLSDVAAslGATPMQVALAWLLQRs 246
Cdd:cd19105 151 LQAAIESGWFDVIMVAYNFLNQPAELEeaLAAAAEKGIGVVAMKTLAGGYLQPALLSVLKAK--GFSLPQAALKWVLSN- 227
|
250 260
....*....|....*....|..
gi 16129367 247 PNI-LLIPGTSSVAHLRENMAA 267
Cdd:cd19105 228 PRVdTVVPGMRNFAELEENLAA 249
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-266 |
1.16e-28 |
|
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: 109.49 E-value: 1.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 13 VNRLGYGAMQLagpgvfgPPRDRHVAITVLREALALGVNHIDTSDFYGphVTNQIIREALYPYSDDLTIVTKIGARRGED 92
Cdd:cd19100 11 VSRLGFGGGPL-------GRLSQEEAAAIIRRALDLGINYFDTAPSYG--DSEEKIGKALKGRRDKVFLATKTGARDYEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 93 AswlpafspaelQKAVHDNLRNLGLDVLDVVNL----------RVMMGDGhgpaegSIEAsltvLAEMQQQGLVKHIGLS 162
Cdd:cd19100 82 A-----------KRDLERSLKRLGTDYIDLYQLhavdteedldQVFGPGG------ALEA----LLEAKEEGKIRFIGIS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 163 NVTPTQVAEARKIAEIVCVQNEYNIAHRADDAMIDAL---AHD-GIAYVPFFPLGGfTPLQSSTLSDVAAslgatpmqvA 238
Cdd:cd19100 141 GHSPEVLLRALETGEFDVVLFPINPAGDHIDSFREELlplAREkGVGVIAMKVLAG-GRLLSGDPLDPEQ---------A 210
|
250 260
....*....|....*....|....*...
gi 16129367 239 LAWLLQRSPNILLIPGTSSVAHLRENMA 266
Cdd:cd19100 211 LRYALSLPPVDVVIVGMDSPEELDENLA 238
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-267 |
1.55e-28 |
|
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: 110.50 E-value: 1.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 15 RLGYGAMQlagpgvFGPPRDRHVAITVLREALALGVNHIDTSDFYGPHVTN-------QIIREALYPYS--DDLTIVTKI 85
Cdd:cd19752 2 ELCLGTMY------FGTRTDEETSFAILDRYVAAGGNFLDTANNYAFWTEGgvggeseRLIGRWLKDRGnrDDVVIATKV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 86 GARRGEDASWLPAF---SPAELQKAVHDNLRNLGLDVLDVVNLRVMmgDGHGPAEGSIEAsltvLAEMQQQGLVKHIGLS 162
Cdd:cd19752 76 GAGPRDPDGGPESPeglSAETIEQEIDKSLRRLGTDYIDLYYAHVD--DRDTPLEETLEA----FNELVKAGKVRAIGAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 163 NVTPTQVAEARKIA------EIVCVQNEYNI---AHRADDAMIDALAHDGIAYV---PFFPLGGFTPLQS---------- 220
Cdd:cd19752 150 NFAAWRLERARQIArqqgwaEFSAIQQRHSYlrpRPGADFGVQRIVTDELLDYAssrPDLTLLAYSPLLSgaytrpdrpl 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 221 -------------STLSDVAASLGATPMQVALAWLLQRSPNILLIPGTSSVAHLRENMAA 267
Cdd:cd19752 230 peqydgpdsdarlAVLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAA 289
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
12-286 |
2.50e-27 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 106.65 E-value: 2.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 12 SVNRLGYGAMQLAGpgvfgpprdrHVAITVLREALALGVNHIDTSDFYGPHV-TNQIIREALYPySDDLTIVTKIgarrg 90
Cdd:PRK11172 2 SIPAFGLGTFRLKD----------QVVIDSVKTALELGYRAIDTAQIYDNEAaVGQAIAESGVP-RDELFITTKI----- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 91 edasWLPAFSPAELQKAVHDNLRNLGLDVLDVVNLrvmmgdgHGPAEG---SIEASLTVLAEMQQQGLVKHIGLSNVTpt 167
Cdd:PRK11172 66 ----WIDNLAKDKLIPSLKESLQKLRTDYVDLTLI-------HWPSPNdevSVEEFMQALLEAKKQGLTREIGISNFT-- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 168 qVAEARKIAEIVCVQNeynIAHRA--------DDAMIDALAHDGIAYVPFFPLGGFTPLQSSTLSDVAASLGATPMQVAL 239
Cdd:PRK11172 133 -IALMKQAIAAVGAEN---IATNQielspylqNRKVVAFAKEHGIHVTSYMTLAYGKVLKDPVIARIAAKHNATPAQVIL 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 16129367 240 AWLLQRspNILLIPGTSSVAHLRENMAAEKLHLSEE---VLSTLDGISRE 286
Cdd:PRK11172 209 AWAMQL--GYSVIPSSTKRENLASNLLAQDLQLDAEdmaAIAALDRNGRL 256
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
16-283 |
4.66e-26 |
|
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: 103.10 E-value: 4.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 16 LGYGAMQLagpgvfgppRDRHVAITVLREALALGVNHIDTSDFYG--PHVTNqIIREALYPYS---DDLTIVTKIGAR-R 89
Cdd:cd19136 4 LGLGTFRL---------RGEEEVRQAVDAALKAGYRLIDTASVYRneADIGK-ALRDLLPKYGlsrEDIFITSKLAPKdQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 90 GEDASwlpafspaelQKAVHDNLRNLGLDVLD--------VVNLRVmmgDGHGPAEGSIEaSLTVLAEMQQQGLVKHIGL 161
Cdd:cd19136 74 GYEKA----------RAACLGSLERLGTDYLDlylihwpgVQGLKP---SDPRNAELRRE-SWRALEDLYKEGKLRAIGV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 162 SNVTPTQVAEARKIAEIVC--VQNEYNiAHRADDAMIDALAHDGIAYVPFFPLGGFTP--LQSSTLSDVAASLGATPMQV 237
Cdd:cd19136 140 SNYTVRHLEELLKYCEVPPavNQVEFH-PHLVQKELLKFCKDHGIHLQAYSSLGSGDLrlLEDPTVLAIAKKYGRTPAQV 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 16129367 238 ALAWLLQRspNILLIPGTSSVAHLRENMAAEKLHLSEEVLSTLDGI 283
Cdd:cd19136 219 LLRWALQQ--GIGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
13-286 |
1.74e-25 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 103.75 E-value: 1.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 13 VNRLGYGAMQLagpgvfgPPRDRHVAITVLREALALGVNHIDTSDFYgpHVTNQIIREALYPYSDDLTIVTKIgarrged 92
Cdd:COG1453 13 VSVLGFGGMRL-------PRKDEEEAEALIRRAIDNGINYIDTARGY--GDSEEFLGKALKGPRDKVILATKL------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 93 ASWLPafSPAELQKAVHDNLRNLGLDVLDV-----VNL-----RVMMGDGhgpaegsieaSLTVLAEMQQQGLVKHIGLS 162
Cdd:COG1453 77 PPWVR--DPEDMRKDLEESLKRLQTDYIDLylihgLNTeedleKVLKPGG----------ALEALEKAKAEGKIRHIGFS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 163 NVTPTQVaeARKIAE---IVCVQNEYNIA---HRADDAMIDALAHDGIayvPFF---PL-GGFTPLQSSTLSDVAASlGA 232
Cdd:COG1453 145 THGSLEV--IKEAIDtgdFDFVQLQYNYLdqdNQAGEEALEAAAEKGI---GVIimkPLkGGRLANPPEKLVELLCP-PL 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 16129367 233 TPMQVALAWLLQRsPNI-LLIPGTSSVAHLRENMA-AEKLH-LSEEVLSTLDGISRE 286
Cdd:COG1453 219 SPAEWALRFLLSH-PEVtTVLSGMSTPEQLDENLKtADNLEpLTEEELAILERLAEE 274
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
15-267 |
7.57e-25 |
|
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: 99.94 E-value: 7.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 15 RLGYGAMQLagPGVFGPPRDRHVAITVLREALALGVNHIDTSDFYGPHVTNQIIREAL--YPySDDLTIVTKIGARRGEd 92
Cdd:cd19096 2 VLGFGTMRL--PESDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALkeGP-REKFYLATKLPPWSVK- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 93 aswlpafSPAELQKAVHDNLRNLGLDVLDVVNLRVMMGDGHgPAEGSIEASLTVLAEMQQQGLVKHIGLSNVTPTQVaea 172
Cdd:cd19096 78 -------SAEDFRRILEESLKRLGVDYIDFYLLHGLNSPEW-LEKARKGGLLEFLEKAKKEGLIRHIGFSFHDSPEL--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 173 rkIAEIV------CVQNEYNIAHRADDAMIDAL--AHD-GIAYVPFFPL-GGFTPLQSSTLSDVAASLGATPMQVALAWL 242
Cdd:cd19096 147 --LKEILdsydfdFVQLQYNYLDQENQAGRPGIeyAAKkGMGVIIMEPLkGGGLANNPPEALAILCGAPLSPAEWALRFL 224
|
250 260
....*....|....*....|....*.
gi 16129367 243 LqRSPNIL-LIPGTSSVAHLRENMAA 267
Cdd:cd19096 225 L-SHPEVTtVLSGMSTPEQLDENIAA 249
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
15-267 |
2.06e-24 |
|
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: 99.55 E-value: 2.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 15 RLGYGAMqlagpgVFGPPRDRHVAITVLREALALGVNHIDT----SDFYGPHVTNQIIREAL--YPYSDDLTIVTKiGAR 88
Cdd:cd19082 2 RIVLGTA------DFGTRIDEEEAFALLDAFVELGGNFIDTarvyGDWVERGASERVIGEWLksRGNRDKVVIATK-GGH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 89 RGEDASWLPAFSPAELQKAVHDNLRNLGLDVLDVV-----NLRVmmgdghgPAEGSIEasltVLAEMQQQGLVKHIGLSN 163
Cdd:cd19082 75 PDLEDMSRSRLSPEDIRADLEESLERLGTDYIDLYflhrdDPSV-------PVGEIVD----TLNELVRAGKIRAFGASN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 164 VTPTQVAEARKIAE------IVCVQNEYNIAHR------------ADDAMIDALAHDGIAYVPFFPLGG--FTPLQSSTL 223
Cdd:cd19082 144 WSTERIAEANAYAKahglpgFAASSPQWSLARPneppwpgptlvaMDEEMRAWHEENQLPVFAYSSQARgfFSKRAAGGA 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129367 224 SD----------------------VAASLGATPMQVALAWLLQRSPNILLIPGTSSVAHLRENMAA 267
Cdd:cd19082 224 EDdselrrvyyseenferlerakeLAEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAA 289
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
13-276 |
2.73e-24 |
|
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: 99.20 E-value: 2.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 13 VNRLGYGAMqlagpGVFGPPRDRHVAITVLREALALGVNHIDTSDFYGPHVTNQIIREALYPYS-DDLTIVTKIGARRGE 91
Cdd:cd19074 4 VSELSLGTW-----LTFGGQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALKGWPrESYVISTKVFWPTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 92 daswlpafSPAE-------LQKAVHDNLRNLGLDVLDVVNLrvmmgdgHGP-AEGSIEASLTVLAEMQQQGLVKHIGLSN 163
Cdd:cd19074 79 --------GPNDrglsrkhIFESIHASLKRLQLDYVDIYYC-------HRYdPETPLEETVRAMDDLIRQGKILYWGTSE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 164 VTPTQVAEARKIAE------IVCVQNEYNIAHR-ADDAMIDALAHDGIAYVPFFPL--GGFT-------PLQSST----- 222
Cdd:cd19074 144 WSAEQIAEAHDLARqfglipPVVEQPQYNMLWReIEEEVIPLCEKNGIGLVVWSPLaqGLLTgkyrdgiPPPSRSratde 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129367 223 --------------------LSDVAASLGATPMQVALAWLLQRSPNILLIPGTSSVAHLRENMAAEKLHLSEEV 276
Cdd:cd19074 224 dnrdkkrrlltdenlekvkkLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKASGVKLSPEV 297
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
18-283 |
4.44e-24 |
|
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: 98.78 E-value: 4.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 18 YGAMQLAGPGVFGPPRDRHVAITVLREAlalGVNHIDTSDFYGPHVTNQIIREALYPYSDdLTIVTKIGARRGedaswlP 97
Cdd:cd19075 5 LGTMTFGSQGRFTTAEAAAELLDAFLER---GHTEIDTARVYPDGTSEELLGELGLGERG-FKIDTKANPGVG------G 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 98 AFSPAELQKAVHDNLRNLGLDVLDVVNLrvmmgdgHGPAEG-SIEASLTVLAEMQQQGLVKHIGLSNVTPTQVAEarkIA 176
Cdd:cd19075 75 GLSPENVRKQLETSLKRLKVDKVDVFYL-------HAPDRStPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAE---IV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 177 EIvCVQN----------EYN-IAHRADDAMIDALAHDGIAYVPFFPL-GGF---TPLQSST------------------- 222
Cdd:cd19075 145 EI-CKENgwvlptvyqgMYNaITRQVETELFPCLRKLGIRFYAYSPLaGGFltgKYKYSEDkagggrfdpnnalgklyrd 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 223 -------------LSDVAASLGATPMQVALAWL-----LQRSPNILLIPGTSSVAHLRENMAA-EKLHLSEEVLSTLDGI 283
Cdd:cd19075 224 rywkpsyfealekVEEAAEKEGISLAEAALRWLyhhsaLDGEKGDGVILGASSLEQLEENLAAlEKGPLPEEVVKAIDEA 303
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
13-281 |
6.11e-24 |
|
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: 98.50 E-value: 6.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 13 VNRLGYGAMQLAGpGVFGPPRDRHVAITVLREALALGVNHIDTSDFYGPHVTNQIIREALYPYSDDLTIVTKIGAR--RG 90
Cdd:cd19149 11 ASVIGLGTWAIGG-GPWWGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKGRRDKVVLATKCGLRwdRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 91 EDASWLPA--------FSPAELQKAVHDNLRNLGLDVLDVVNLrvmmgdgHGPA-EGSIEASLTVLAEMQQQGLVKHIGL 161
Cdd:cd19149 90 GGSFFFVRdgvtvyknLSPESIREEVEQSLKRLGTDYIDLYQT-------HWQDvETPIEETMEALEELKRQGKIRAIGA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 162 SNVTPTQVAEARKIAEIVCVQNEYNIAHRA-DDAMIDALAHDGIAYVPFFPL------GGFTP---------------LQ 219
Cdd:cd19149 163 SNVSVEQIKEYVKAGQLDIIQEKYSMLDRGiEKELLPYCKKNNIAFQAYSPLeqglltGKITPdrefdagdarsgipwFS 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129367 220 SSTLSDVAASL----------GATPMQVALAWLLQRSPNILLIPGTSSVAHLRENMAAEKLHLSEEVLSTLD 281
Cdd:cd19149 243 PENREKVLALLekwkplcekyGCTLAQLVIAWTLAQPGITSALCGARKPEQAEENAKAGDIRLSAEDIATMR 314
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
6-281 |
5.46e-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: 95.75 E-value: 5.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 6 FTLGTKS--VNRLGYGAMQLAGPGVFGPPRDRhvAITVLREALALGVNHIDTSDFYGPHVTNQIIREALYPYSDDLTIVT 83
Cdd:cd19080 1 RLLGRSGlrVSPLALGTMTFGTEWGWGADREE--ARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAGNRDRIVLAT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 84 K-IGARRGEDaswlPAF---SPAELQKAVHDNLRNLGLDVLDVvnLRVMMGDGHGPaegsIEASLTVLAEMQQQGLVKHI 159
Cdd:cd19080 79 KyTMNRRPGD----PNAggnHRKNLRRSVEASLRRLQTDYIDL--LYVHAWDFTTP----VEEVMRALDDLVRAGKVLYV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 160 GLSNVTPTQVAEARKIAE------IVCVQNEYNIAHRADDAMIDALA-HDGIAYVPFFPLGG------------------ 214
Cdd:cd19080 149 GISDTPAWVVARANTLAElrgwspFVALQIEYSLLERTPERELLPMArALGLGVTPWSPLGGglltgkyqrgeegragea 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129367 215 -FTPLQSSTLSD-----------VAASLGATPMQVALAWLLQRSPNILLIPGTSSVAHLRENMAAEKLHLSEEVLSTLD 281
Cdd:cd19080 229 kGVTVGFGKLTErnwaivdvvaaVAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDLTLSPEQLARLD 307
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
29-277 |
3.24e-22 |
|
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: 93.86 E-value: 3.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 29 FGPPRDRHVAITVLREALALGVNHIDTSDFYGP------HVTNQIIREALYPYSDDLTIVTKIGARR--GEDASWLpafS 100
Cdd:cd19089 22 FGDYTSPEEARELLRTAFDLGITHFDLANNYGPppgsaeENFGRILKRDLRPYRDELVISTKAGYGMwpGPYGDGG---S 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 101 PAELQKAVHDNLRNLGLDVLDVVNLRVMmgDGHGPaegsIEASLTVLAEMQQQGLVKHIGLSNVTPTQVAEARKI----- 175
Cdd:cd19089 99 RKYLLASLDQSLKRMGLDYVDIFYHHRY--DPDTP----LEETMTALADAVRSGKALYVGISNYPGAKARRAIALlrelg 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 176 AEIVCVQNEYNIAHR-ADDAMIDALAHDGIAYVPFFPL-----------------------GGFTPLQSS--------TL 223
Cdd:cd19089 173 VPLIIHQPRYSLLDRwAEDGLLEVLEEAGIGFIAFSPLaqglltdkylngippdsrraaesKFLTEEALTpekleqlrKL 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 16129367 224 SDVAASLGATPMQVALAWLLqRSPNI--LLIpGTSSVAHLRENMAAEK-LHLSEEVL 277
Cdd:cd19089 253 NKIAAKRGQSLAQLALSWVL-RDPRVtsVLI-GASSPSQLEDNVAALKnLDFSEEEL 307
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
21-281 |
3.77e-22 |
|
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: 92.64 E-value: 3.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 21 MQLAGPGVFGPPRDRHVAITVLrEALALGVNHIDTSDFYGphvtN-----QIIREALYPySDDLTIVTKIgarrgedasW 95
Cdd:cd19133 9 MPILGFGVFQIPDPEECERAVL-EAIKAGYRLIDTAAAYG----NeeavgRAIKKSGIP-REELFITTKL---------W 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 96 LPAFSPAELQKAVHDNLRNLGLDVLDVVNLRVMMGDGHGpaegsieaSLTVLAEMQQQGLVKHIGLSNVTPTQVAEARKI 175
Cdd:cd19133 74 IQDAGYEKAKKAFERSLKRLGLDYLDLYLIHQPFGDVYG--------AWRAMEELYKEGKIRAIGVSNFYPDRLVDLILH 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 176 AEIVCVQN--EYNIAHRADDAmIDALAHDGIAYVPFFPLGGFTP--LQSSTLSDVAASLGATPMQVALAWLLQRspNILL 251
Cdd:cd19133 146 NEVKPAVNqiETHPFNQQIEA-VEFLKKYGVQIEAWGPFAEGRNnlFENPVLTEIAEKYGKSVAQVILRWLIQR--GIVV 222
|
250 260 270
....*....|....*....|....*....|...
gi 16129367 252 IPGTSSVAHLRENMAAEKLHLSEE---VLSTLD 281
Cdd:cd19133 223 IPKSVRPERIAENFDIFDFELSDEdmeAIAALD 255
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
15-277 |
4.84e-22 |
|
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH) and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. The family also includes L-galactose dehydrogenase (L-galDH) and D-arabinose 1-dehydrogenase (ARA2). L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381316 [Multi-domain] Cd Length: 278 Bit Score: 92.62 E-value: 4.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 15 RLGYGAMQLAGpgVFGPPRDRHvAITVLREALALGVNHIDTSDFYGP------HVTNQIIREALYpysddltIVTKIGAR 88
Cdd:cd19090 2 ALGLGTAGLGG--VFGGVDDDE-AVATIRAALDLGINYIDTAPAYGDseerlgLALAELPREPLV-------LSTKVGRL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 89 RGEDASwlpaFSPAELQKAVHDNLRNLGLDVLDVVNL----RVMMGDGHGPAeGSIEAsltvLAEMQQQGLVKHIGLSnV 164
Cdd:cd19090 72 PEDTAD----YSADRVRRSVEESLERLGRDRIDLLMIhdpeRVPWVDILAPG-GALEA----LLELKEEGLIKHIGLG-G 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 165 TPTQVAeARKIAE----IVCVQNEYN-IAHRADDAMIDALAHDGIAYV---PF---FPLGGFTPLQSSTLSDVAASLGAT 233
Cdd:cd19090 142 GPPDLL-RRAIETgdfdVVLTANRYTlLDQSAADELLPAAARHGVGVInasPLgmgLLAGRPPERVRYTYRWLSPELLDR 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 16129367 234 -------------PM-QVALAWLLqRSPNI-LLIPGTSSVAHLRENMAAEKLHLSEEVL 277
Cdd:cd19090 221 akrlyelcdehgvPLpALALRFLL-RDPRIsTVLVGASSPEELEQNVAAAEGPLPEELW 278
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
21-283 |
1.06e-21 |
|
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: 91.34 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 21 MQLAGPGVFGPPRDRHvAITVLREALALGVNHIDTSDFYGPHVT-NQIIREALYPySDDLTIVTK-----IGARRGEDAs 94
Cdd:cd19126 9 MPWLGLGVFQTPDGDE-TERAVQTALENGYRSIDTAAIYKNEEGvGEAIRESGVP-REELFVTTKlwnddQRARRTEDA- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 95 wlpafspaelqkaVHDNLRNLGLDVLDVVNLrvmmgdgHGPAEGSIEASLTVLAEMQQQGLVKHIGLSNVTPTQVAEARK 174
Cdd:cd19126 86 -------------FQESLDRLGLDYVDLYLI-------HWPGKDKFIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 175 IAEIVCVQNEYNIAHR-ADDAMIDALAHDGIAYVPFFPLGGFTPLQSSTLSDVAASLGATPMQVALAWLLQRSpnILLIP 253
Cdd:cd19126 146 HADVVPAVNQVEFHPYlTQKELRGYCKSKGIVVEAWSPLGQGGLLSNPVLAAIGEKYGKSAAQVVLRWDIQHG--VVTIP 223
|
250 260 270
....*....|....*....|....*....|
gi 16129367 254 GTSSVAHLRENMAAEKLHLSEEVLSTLDGI 283
Cdd:cd19126 224 KSVHASRIKENADIFDFELSEDDMTAIDAL 253
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
22-283 |
4.54e-21 |
|
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: 89.74 E-value: 4.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 22 QLaGPGVFGPPRDrhVAITVLREALALGVNHIDTSDFYGPHV-TNQIIREALYPySDDLTIVTKI-GARRGEDASwlpaf 99
Cdd:cd19131 12 QL-GLGVWQVSND--EAASAVREALEVGYRSIDTAAIYGNEEgVGKAIRASGVP-REELFITTKLwNSDQGYDST----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 100 spaelQKAVHDNLRNLGLDVLDVVNLRVMMgdghgPAEGSIEASLTVLAEMQQQGLVKHIGLSNVTPTQVAEARKIAEIV 179
Cdd:cd19131 83 -----LRAFDESLRKLGLDYVDLYLIHWPV-----PAQDKYVETWKALIELKKEGRVKSIGVSNFTIEHLQRLIDETGVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 180 CVQNEYNIAHRADDAMIDAL-AHDGIAYVPFFPLGGFTPLQSSTLSDVAASLGATPMQVALAWLLQRspNILLIPGTSSV 258
Cdd:cd19131 153 PVVNQIELHPRFQQRELRAFhAKHGIQTESWSPLGQGGLLSDPVIGEIAEKHGKTPAQVVIRWHLQN--GLVVIPKSVTP 230
|
250 260
....*....|....*....|....*
gi 16129367 259 AHLRENMAAEKLHLSEEVLSTLDGI 283
Cdd:cd19131 231 SRIAENFDVFDFELDADDMQAIAGL 255
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
1-285 |
6.67e-21 |
|
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: 90.16 E-value: 6.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 1 MSSNTFTLGTKsVNRLGYGAMQlAGPGVFGPprdrhvaitVLREALALGVNHIDTSDFYG-----------PHVTNQIIR 69
Cdd:cd19123 1 MKTLPLSNGDL-IPALGLGTWK-SKPGEVGQ---------AVKQALEAGYRHIDCAAIYGneaeigaalaeVFKEGKVKR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 70 EalypysdDLTIVTKIgarrgedasWLPAFSPAELQKAVHDNLRNLGLDVLDV------VNLRVMMG------DGHGPAE 137
Cdd:cd19123 70 E-------DLWITSKL---------WNNSHAPEDVLPALEKTLADLQLDYLDLylmhwpVALKKGVGfpesgeDLLSLSP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 138 GSIEASLTVLAEMQQQGLVKHIGLSNVTPTQVAEARKIAEIVCVQNEYNI-AHRADDAMIDALAHDGIAYVPFFPLGGFT 216
Cdd:cd19123 134 IPLEDTWRAMEELVDKGLCRHIGVSNFSVKKLEDLLATARIKPAVNQVELhPYLQQPELLAFCRDNGIHLTAYSPLGSGD 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 217 P------------LQSSTLSDVAASLGATPMQVALAWLLQRspNILLIPGTSSVAHLRENMAAEKLHLSEEVLSTLDGIS 284
Cdd:cd19123 214 RpaamkaegepvlLEDPVINKIAEKHGASPAQVLIAWAIQR--GTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALD 291
|
.
gi 16129367 285 R 285
Cdd:cd19123 292 R 292
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
20-286 |
1.50e-19 |
|
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a founding member of aldo-keto reductase family 2 member E4 (AKR2E4). It is a NADP-dependent oxidoreductase with high 3-dehydroecdysone reductase activity. It may play a role in the regulation of molting and has lower activity with phenylglyoxal and isatin (in vitro). This family also includes 3-dehydroecdysone 3b-reductase from Spodoptera littoralis and Trichoplusia ni, DL-glyceraldehyde reductase from Drosophila melanogaster, aldo-keto reductase from Bombyx mori, which correspond to aldo-keto reductase family 2 member E1, E2, E3 and E5 (AKR2E1/2/3/5), respectively.
Pssm-ID: 381342 [Multi-domain] Cd Length: 292 Bit Score: 86.18 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 20 AMQLAGPGVFGPPRDRHVAITVlREALALGVNHIDTSDFYG-PHVTNQIIREALYP---YSDDLTIVTKIgarrgedasW 95
Cdd:cd19116 10 EIPAIALGTWKLKDDEGVRQAV-KHAIEAGYRHIDTAYLYGnEAEVGEAIREKIAEgvvKREDLFITTKL---------W 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 96 LPAFSPAELQKAVHDNLRNLGLDVLDVVNLRVMMG-------DGHGPAEGSIEASLTVLAEMQQ---QGLVKHIGLSNVT 165
Cdd:cd19116 80 NSYHEREQVEPALRESLKRLGLDYVDLYLIHWPVAfkenndsESNGDGSLSDIDYLETWRGMEDlvkLGLTRSIGVSNFN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 166 PTQVAEARKIAEI--VCVQNEYNIAHRADDaMIDALAHDGI---AYVPF------FPLGGFTPLQSSTLSDVAASLGATP 234
Cdd:cd19116 160 SEQINRLLSNCNIkpAVNQIEVHPTLTQEK-LVAYCQSNGIvvmAYSPFgrlvprGQTNPPPRLDDPTLVAIAKKYGKTT 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 16129367 235 MQVALAWLLQRspNILLIPGTSSVAHLRENMAAEKLHLSEEVLSTLDGISRE 286
Cdd:cd19116 239 AQIVLRYLIDR--GVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTN 288
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
42-278 |
2.56e-19 |
|
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2).
Pssm-ID: 381377 [Multi-domain] Cd Length: 309 Bit Score: 85.92 E-value: 2.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 42 LREALALGVNHIDTSDFYGPHVTN------QIIREALYPYSDDLTIVTKIGARR--GEDASWlpaFSPAELQKAVHDNLR 113
Cdd:cd19151 36 LRRAFDLGITHFDLANNYGPPPGSaeenfgRILKEDLKPYRDELIISTKAGYTMwpGPYGDW---GSKKYLIASLDQSLK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 114 NLGLDVLDVVNlrvmmgdGHGP-AEGSIEASLTVLAEMQQQGLVKHIGLSNVTPTQVAEARKIAE---IVCV--QNEYNI 187
Cdd:cd19151 113 RMGLDYVDIFY-------HHRPdPETPLEETMGALDQIVRQGKALYVGISNYPPEEAREAAAILKdlgTPCLihQPKYSM 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 188 AHRA-DDAMIDALAHDGIAYVPFFPLGG--------------------FTPLQSST-----------LSDVAASLGATPM 235
Cdd:cd19151 186 FNRWvEEGLLDVLEEEGIGCIAFSPLAQglltdrylngipedsraakgSSFLKPEQiteeklakvrrLNEIAQARGQKLA 265
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 16129367 236 QVALAWLLQRSPNILLIPGTSSVAHLRENMAA-EKLHLSEEVLS 278
Cdd:cd19151 266 QMALAWVLRNKRVTSVLIGASKPSQIEDAVGAlDNREFSEEELA 309
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
11-191 |
9.50e-19 |
|
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: 84.28 E-value: 9.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 11 KSVNRLGYGAMQLAGpGVFGPPRDRHvAITVLREALALGVNHIDTSDFYGPHVTNQIIREAL--YPYSDDLTIVTKIGAR 88
Cdd:cd19148 2 LPVSRIALGTWAIGG-WMWGGTDEKE-AIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALkeYGKRDRVVIATKVGLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 89 RGEDASWLPAFSPAELQKAVHDNLRNLGLDVLDVVNLrvmmgdgHGPAEGS-IEASLTVLAEMQQQGLVKHIGLSNVTPT 167
Cdd:cd19148 80 WDEGGEVVRNSSPARIRKEVEDSLRRLQTDYIDLYQV-------HWPDPLVpIEETAEALKELLDEGKIRAIGVSNFSPE 152
|
170 180
....*....|....*....|....
gi 16129367 168 QVAEARKIAEIVCVQNEYNIAHRA 191
Cdd:cd19148 153 QMETFRKVAPLHTVQPPYNLFERE 176
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
15-275 |
1.20e-18 |
|
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: 83.34 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 15 RLGYGAMQLagpgvfgPPRDrhvAITVLREALALGVNHIDTSDFYGPH-----VTNQIIREALYPySDDLTIVTKIgarr 89
Cdd:cd19128 3 RLGFGTYKI-------TESE---SKEAVKNAIKAGYRHIDCAYYYGNEafigiAFSEIFKDGGVK-REDLFITSKL---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 90 gedasWLPAFSPAELQKAVHDNLRNLGLDVLDVV----NLRVMMGDGHGPAEGSIEASLT------VLAEMQQ---QGLV 156
Cdd:cd19128 68 -----WPTMHQPENVKEQLLITLQDLQLEYLDLFlihwPLAFDMDTDGDPRDDNQIQSLSkkpledTWRAMEQcvdEKLT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 157 KHIGLSNVTPTQVAEARKIAEIVCVQNEYNIA-HRADDAMIDALAHDGIAYVPFFPLGG------FTPLQSSTLSDVAAS 229
Cdd:cd19128 143 KNIGVSNYSTKLLTDLLNYCKIKPFMNQIECHpYFQNDKLIKFCIENNIHVTAYRPLGGsygdgnLTFLNDSELKALATK 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 16129367 230 LGATPMQVALAWLLQRSP-NILLIPGTSSVAHLRENMAAEKLHLSEE 275
Cdd:cd19128 223 YNTTPPQVIIAWHLQKWPkNYSVIPKSANKSRCQQNFDINDLALTKE 269
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
49-284 |
1.28e-18 |
|
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: 83.14 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 49 GVNHIDTSDFYG-PHVTNQIIREALYPySDDLTIVTKIgarrgedasWLPAFSPAELQKAVHDNLRNLGLDVLDVVnlrv 127
Cdd:cd19135 39 GYRHIDTAKRYGcEELLGKAIKESGVP-REDLFLTTKL---------WPSDYGYESTKQAFEASLKRLGVDYLDLY---- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 128 MMgdgHGPAEGS--------IEASLTVLAEMQQQGLVKHIGLSNVTPTQVAEARKIAEIV--CVQNEYNIAHRaDDAMID 197
Cdd:cd19135 105 LL---HWPDCPSsgknvketRAETWRALEELYDEGLCRAIGVSNFLIEHLEQLLEDCSVVphVNQVEFHPFQN-PVELIE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 198 ALAHDGIAYVPFFPLGGFTPLQSSTLSDVAASLGATPMQVALAWLLQRspNILLIPGTSSVAHLRENMAAEKLHLSEEVL 277
Cdd:cd19135 181 YCRDNNIVFEGYCPLAKGKALEEPTVTELAKKYQKTPAQILIRWSIQN--GVVTIPKSTKEERIKENCQVFDFSLSEEDM 258
|
....*..
gi 16129367 278 STLDGIS 284
Cdd:cd19135 259 ATLDSLH 265
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
6-286 |
1.81e-18 |
|
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: 83.16 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 6 FTLGT-KSVNRLGYGAMQlAGPGVFGpprdrhvaiTVLREALALGVNHIDTSDFYGphvtNQI-----IREALYP---YS 76
Cdd:cd19125 3 FKLNTgAKIPAVGLGTWQ-ADPGVVG---------NAVKTAIKEGYRHIDCAAIYG----NEKeigkaLKKLFEDgvvKR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 77 DDLTIVTKIgarrgedasWLPAFSPAELQKAVHDNLRNLGLDVLD--VVNLRVMMGDG-HGPAEG-----SIEAsltVLA 148
Cdd:cd19125 69 EDLFITSKL---------WCTDHAPEDVPPALEKTLKDLQLDYLDlyLIHWPVRLKKGaHMPEPEevlppDIPS---TWK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 149 EMQQ---QGLVKHIGLSNVTPTQVAEARKIAEI---VCvQNEYNIAHRaDDAMIDALAHDGI---AYVPF-FPLGGFTP- 217
Cdd:cd19125 137 AMEKlvdSGKVRAIGVSNFSVKKLEDLLAVARVppaVN-QVECHPGWQ-QDKLHEFCKSKGIhlsAYSPLgSPGTTWVKk 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129367 218 --LQSSTLSDVAASLGATPMQVALAWLLQRSPNILliPGTSSVAHLRENMAAEKLHLSEEVLSTLDGISRE 286
Cdd:cd19125 215 nvLKDPIVTKVAEKLGKTPAQVALRWGLQRGTSVL--PKSTNEERIKENIDVFDWSIPEEDFAKFSSIEQQ 283
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
15-275 |
6.09e-18 |
|
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis NADPH-dependent conjugated polyketone reductase C2 (CPR), and similar proteins; Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase (EC 1.1.1.190/EC 1.1.1.191) and Candida parapsilosis NADPH-dependent CPR (EC 1.1.1.358/EC 1.1.1.168) are founding members of aldo-keto reductase family 3 member C2 (AKR3C2) and C3 (AKR3C3), respectively. Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase catalyzes the conversion from (Indol-3-yl)ethanol to (indol-3-yl)acetaldehyde in a NAD/NADP-dependent manner. CPR, also called 2-dehydropantolactone reductase, or 2-dehydropantolactone reductase (A-specific), or ketopantoyl-lactone reductase, acts as a NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. It reduces ketopantoyl lactone and isatin.
Pssm-ID: 381346 [Multi-domain] Cd Length: 269 Bit Score: 81.12 E-value: 6.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 15 RLGYGAmqlaGPGVFGPPR---DRHVAITVLrEALALGVNHIDTSDFYGPHV-TNQIIREALYPYSDdLTIVTKIGaRRG 90
Cdd:cd19120 6 AIAFGT----GTAWYKSGDddiQRDLVDSVK-LALKAGFRHIDTAEMYGNEKeVGEALKESGVPRED-LFITTKVS-PGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 91 EDAswlpafspaelQKAVHDNLRNLGLDVLDVVNLrvmmgdgHGP--AEGSIEASLTVLAEMQQ---QGLVKHIGLSNVT 165
Cdd:cd19120 79 KDP-----------REALRKSLAKLGVDYVDLYLI-------HSPffAKEGGPTLAEAWAELEAlkdAGLVRSIGVSNFR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 166 PTQVAEARKIAEI--VCVQNEYN--IAHRaDDAMIDALAHDGI---AYVPFFPLGGFT--PLQSsTLSDVAASLGATPMQ 236
Cdd:cd19120 141 IEDLEELLDTAKIkpAVNQIEFHpyLYPQ-QPALLEYCREHGIvvsAYSPLSPLTRDAggPLDP-VLEKIAEKYGVTPAQ 218
|
250 260 270
....*....|....*....|....*....|....*....
gi 16129367 237 VALAWLLQRspNILLIPGTSSVAHLRENMAAEKLHLSEE 275
Cdd:cd19120 219 VLLRWALQK--GIVVVTTSSKEERMKEYLEAFDFELTEE 255
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
29-278 |
1.51e-17 |
|
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
Pssm-ID: 381376 [Multi-domain] Cd Length: 309 Bit Score: 80.96 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 29 FGPPRDRHVAITVLREALALGVNHIDTSDFYGPHV----TN--QIIREALYPYSDDLTIVTKIGARR--GEDASWlpaFS 100
Cdd:cd19150 23 FGDDTPLETQRAILRTAFDLGITHFDLANNYGPPPgsaeENfgRILREDFAGYRDELIISTKAGYDMwpGPYGEW---GS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 101 PAELQKAVHDNLRNLGLDVLDVV-NLRVmmgDGHGPAEGSIEAsltvLAEMQQQGLVKHIGLSNVTPTQVAEARKIAE-- 177
Cdd:cd19150 100 RKYLLASLDQSLKRMGLDYVDIFySHRF---DPDTPLEETMGA----LDHAVRSGKALYVGISSYSPERTREAAAILRel 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 178 ---IVCVQNEYNIAHR--ADDAMIDALAHDGIAYVPFFPL----------------------GGFTP--LQSSTLSDV-- 226
Cdd:cd19150 173 gtpLLIHQPSYNMLNRwvEESGLLDTLQELGVGCIAFTPLaqglltdkylngipegsraskeRSLSPkmLTEANLNSIra 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 16129367 227 ----AASLGATPMQVALAWLLQRSPNILLIPGTSSVAHLRENMAA-EKLHLSEEVLS 278
Cdd:cd19150 253 lneiAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGAlDNLTFSADELA 309
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
21-283 |
2.24e-17 |
|
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: 79.74 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 21 MQLAGPGVFGPPRDRHVAITVlREALALGVNHIDTSDFYG-PHVTNQIIREALYPySDDLTIVTKI-GARRGEDASwLPA 98
Cdd:cd19157 10 MPWLGLGVFKVEEGSEVVNAV-KTALKNGYRSIDTAAIYGnEEGVGKGIKESGIP-REELFITSKVwNADQGYDST-LKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 99 FSpaelqkavhDNLRNLGLDVLDVVNLrvmmgdgHGPAEGSIEASLTVLAEMQQQGLVKHIGLSNVTPTQVAEARKIAEI 178
Cdd:cd19157 87 FE---------ASLERLGLDYLDLYLI-------HWPVKGKYKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAEI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 179 VCVQNEYNIAHRAD-DAMIDALAHDGIAYVPFFPLGGFTPLQSSTLSDVAASLGATPMQVALAWLLQRspNILLIPGTSS 257
Cdd:cd19157 151 VPMVNQVEFHPRLTqKELRDYCKKQGIQLEAWSPLMQGQLLDNPVLKEIAEKYNKSVAQVILRWDLQN--GVVTIPKSIK 228
|
250 260
....*....|....*....|....*.
gi 16129367 258 VAHLRENMAAEKLHLSEEVLSTLDGI 283
Cdd:cd19157 229 EHRIIENADVFDFELSQEDMDKIDAL 254
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
40-281 |
3.12e-17 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 80.42 E-value: 3.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 40 TVLREALALGVNHIDTSDFYGPHVTN------QIIREALYPYSDDLTIVTKIGARRgedasWLPAF----SPAELQKAVH 109
Cdd:PRK09912 47 AILRKAFDLGITHFDLANNYGPPPGSaeenfgRLLREDFAAYRDELIISTKAGYDM-----WPGPYgsggSRKYLLASLD 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 110 DNLRNLGLDVLDVV-NLRVmmgDGHGPAEGSIEAsltvLAEMQQQGLVKHIGLSNVTPtqvAEARKIAE--------IVC 180
Cdd:PRK09912 122 QSLKRMGLEYVDIFySHRV---DENTPMEETASA----LAHAVQSGKALYVGISSYSP---ERTQKMVEllrewkipLLI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 181 VQNEYNIAHRADD--AMIDALAHDGIAYVPFFPLG--------------------------GFTP-------LQS-STLS 224
Cdd:PRK09912 192 HQPSYNLLNRWVDksGLLDTLQNNGVGCIAFTPLAqglltgkylngipqdsrmhregnkvrGLTPkmlteanLNSlRLLN 271
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 16129367 225 DVAASLGATPMQVALAWLLQRSPNILLIPGTSSVAHLRENMAA-EKLHLSEEVLSTLD 281
Cdd:PRK09912 272 EMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQAlNNLTFSTEELAQID 329
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
13-285 |
3.71e-16 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 77.20 E-value: 3.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 13 VNRLGYGAMqlagpgVFGPPRDRHVAITVLREALALGVNHIDTSDFYG--PHVTNQIIREAlYPYS--------DDLTIV 82
Cdd:PRK10625 13 VSTLGLGTM------TFGEQNSEADAHAQLDYAVAQGINLIDVAEMYPvpPRPETQGLTET-YIGNwlakrgsrEKLIIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 83 TKI-GARRGEDASWLP--AFSPAELQKAVHDNLRNLGLDVLDVVNLrvmmgdgHGP------------------AEGSIE 141
Cdd:PRK10625 86 SKVsGPSRNNDKGIRPnqALDRKNIREALHDSLKRLQTDYLDLYQV-------HWPqrptncfgklgyswtdsaPAVSLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 142 ASLTVLAEMQQQGLVKHIGLSNVTP------TQVAEARKIAEIVCVQNEYNIAHRA-DDAMIDALAHDGIAYVPFFPLgG 214
Cdd:PRK10625 159 ETLDALAEQQRAGKIRYIGVSNETAfgvmryLHLAEKHDLPRIVTIQNPYSLLNRSfEVGLAEVSQYEGVELLAYSCL-A 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 215 FTPLQSSTLS-------------------------------DVAASLGATPMQVALAWLLQRSPNILLIPGTSSVAHLRE 263
Cdd:PRK10625 238 FGTLTGKYLNgakpagarntlfsrftrysgeqtqkavaayvDIAKRHGLDPAQMALAFVRRQPFVASTLLGATTMEQLKT 317
|
330 340
....*....|....*....|..
gi 16129367 264 NMAAEKLHLSEEVLSTLDGISR 285
Cdd:PRK10625 318 NIESLHLTLSEEVLAEIEAVHQ 339
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
16-283 |
4.03e-16 |
|
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: 76.30 E-value: 4.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 16 LGYGAMQlAGPGvfgpprdrHVAITVLrEALALGVNHIDTSDFYG-PHVTNQIIREALYPYS----DDLTIVTKIgarrg 90
Cdd:cd19118 10 IGLGTWQ-AEPG--------EVGAAVK-IALKAGYRHLDLAKVYQnQHEVGQALKELLKEEPgvkrEDLFITSKL----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 91 edasWLPAFSPAELQKAVHDNLRNLGLDVLDV------VNLR------VMMGDGHGPAEGSIEASLTVLA------EMQQ 152
Cdd:cd19118 75 ----WNNSHRPEYVEPALDDTLKELGLDYLDLylihwpVAFKptgdlnPLTAVPTNGGEVDLDLSVSLVDtwkamvELKK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 153 QGLVKHIGLSNVTPTQVAEARKIAEIVCVQNEYNiAHR--ADDAMIDALAHDGIAYVPFFPLGGFT---PL--QSSTLSD 225
Cdd:cd19118 151 TGKVKSIGVSNFSIDHLQAIIEETGVVPAVNQIE-AHPllLQDELVDYCKSKNIHITAYSPLGNNLaglPLlvQHPEVKA 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 16129367 226 VAASLGATPMQVALAWLLQRSPNIllIPGTSSVAHLRENMaaEKLHLSEEVLSTLDGI 283
Cdd:cd19118 230 IAAKLGKTPAQVLIAWGIQRGHSV--IPKSVTPSRIRSNF--EQVELSDDEFNAVTAL 283
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
17-285 |
4.70e-16 |
|
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: 76.68 E-value: 4.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 17 GYGAMQLAGPGVfgpprdrhvaITVLREALALGVNHIDTSDFY-GPHVTNQIIREALYPYS---DDLTIVTKIgarrged 92
Cdd:cd19154 16 GLGTWQSKGAEG----------ITAVRTALKAGYRLIDTAFLYqNEEAIGEALAELLEEGVvkrEDLFITTKL------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 93 asWLPAFSPAELQKAVHDNLRNLGLDVLDV-----------VNLRVMMGDGHGPAEGSIEAsLTVLAEMQQ---QGLVKH 158
Cdd:cd19154 79 --WTHEHAPEDVEEALRESLKKLQLEYVDLylihapaafkdDEGESGTMENGMSIHDAVDV-EDVWRGMEKvydEGLTKA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 159 IGLSNVTPTQVAEARKIAEI--VCVQNEYNIaHRADDAMIDALAHDGIAYVPFFPLG---------------GFTPLQSS 221
Cdd:cd19154 156 IGVSNFNNDQIQRILDNARVkpHNNQVECHL-YFPQKELVEFCKKHNISVTSYATLGspgranftkstgvspAPNLLQDP 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129367 222 TLSDVAASLGATPMQVALAWLLQRSpnILLIPGTSSVAHLRENMAAEKLHLSEEVLSTLDGISR 285
Cdd:cd19154 235 IVKAIAEKHGKTPAQVLLRYLLQRG--IAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEK 296
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
8-281 |
8.15e-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: 381329 [Multi-domain] Cd Length: 299 Bit Score: 75.83 E-value: 8.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 8 LGTKSvnrlgYGAMQLAGPGVFGpprdRHVAITVLR----EALALGVNHIDTSDFYGPHVTNQIIREALYPYS-DDLTIV 82
Cdd:cd19103 9 LGTWS-----WGSGGAGGDQVFG----NHLDEDTLKavfdKAMAAGLNLWDTAAVYGMGASEKILGEFLKRYPrEDYIIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 83 TK---IGARRGEDAswlpafspaeLQKAVHDNLRNLGLDVLDVVNLrvmmgdgHGPAEgsIEASLTVLAEMQQQGLVKHI 159
Cdd:cd19103 80 TKftpQIAGQSADP----------VADMLEGSLARLGTDYIDIYWI-------HNPAD--VERWTPELIPLLKSGKVKHV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 160 GLSNVTPTQVAEARKIAE-----IVCVQNEYNIAHRA--DDAMIDALAHDGIAYVPF-----------------FPLGG- 214
Cdd:cd19103 141 GVSNHNLAEIKRANEILAkagvsLSAVQNHYSLLYRSseEAGILDYCKENGITFFAYmvleqgalsgkydtkhpLPEGSg 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129367 215 ----FTPLQ------SSTLSDVAASLGATPMQVALAWllQRSPNILLIPGTSSVAHLRENMAAEKLHLSEEVLSTLD 281
Cdd:cd19103 221 raetYNPLLpqleelTAVMAEIGAKHGASIAQVAIAW--AIAKGTTPIIGVTKPHHVEDAARAASITLTDDEIKELE 295
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-283 |
1.11e-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: 75.76 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 13 VNRLGYGAMQLAGpgVFGPPrDRHVAITVLREALALGVNHIDTSDFYGPHVTNQIIREALYPYSDDLTIVTKIGARRGED 92
Cdd:cd19104 12 VSELTFGGGGIGG--LMGRT-TREEQIAAVRRALDLGINFFDTAPSYGDGKSEENLGRALKGLPAGPYITTKVRLDPDDL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 93 ASwlpafSPAELQKAVHDNLRNLGLDVLDVVNL--RVMMGDGHGP-AEGSIEASL------TVLAEMQQQGLVKHIGLsn 163
Cdd:cd19104 89 GD-----IGGQIERSVEKSLKRLKRDSVDLLQLhnRIGDERDKPVgGTLSTTDVLglggvaDAFERLRSEGKIRFIGI-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 164 vtpTQVAEARKIAEIV------CVQNEYNI--------------AHRADDAMIDALAHD-GIAYVPFFPLGGFT------ 216
Cdd:cd19104 162 ---TGLGNPPAIRELLdsgkfdAVQVYYNLlnpsaaearprgwsAQDYGGIIDAAAEHGvGVMGIRVLAAGALTtsldrg 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 217 PLQSST--------------LSDVAASLGATPMQVALAWLLQrSPNI-LLIPGTSSVAHLRENMAAEKL-HLSEEVLSTL 280
Cdd:cd19104 239 REAPPTsdsdvaidfrraaaFRALAREWGETLAQLAHRFALS-NPGVsTVLVGVKNREELEEAVAAEAAgPLPAENLARL 317
|
...
gi 16129367 281 DGI 283
Cdd:cd19104 318 EAL 320
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
38-269 |
1.31e-15 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 74.87 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 38 AITVLREALALGVNHIDTSDFYGphVTNQIIREALyPYSDDLTIVTKIGArrgedASWLPAFSPAELQKAVHDNLRNLGL 117
Cdd:cd19097 28 AKKILEYALKAGINTLDTAPAYG--DSEKVLGKFL-KRLDKFKIITKLPP-----LKEDKKEDEAAIEASVEASLKRLKV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 118 DVLDVVNLrvmmgdgHGPAE-----GSIEASLTvlaEMQQQGLVKHIGLSNVTPTQVAEARKIAEIVCVQNEYNIA-HRA 191
Cdd:cd19097 100 DSLDGLLL-------HNPDDllkhgGKLVEALL---ELKKEGLIRKIGVSVYSPEELEKALESFKIDIIQLPFNILdQRF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 192 DDA-MIDALAHDGIA-YV------------PFFPLGGFTPLQS--STLSDVAASLGATPMQVALAWLLQRSPNILLIPGT 255
Cdd:cd19097 170 LKSgLLAKLKKKGIEiHArsvflqglllmePDKLPAKFAPAKPllKKLHELAKKLGLSPLELALGFVLSLPEIDKIVVGV 249
|
250
....*....|....
gi 16129367 256 SSVAHLRENMAAEK 269
Cdd:cd19097 250 DSLEQLKEIIAAFK 263
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
21-285 |
3.56e-15 |
|
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: 74.10 E-value: 3.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 21 MQLAGPGVF-GPPRDRHVAITVlreALALGVNHIDTSDFYGphvTNQIIREALYPYSD-------DLTIVTK---IGARr 89
Cdd:cd19155 12 MPVVGLGTWqSSPEEIETAVDT---ALEAGYRHIDTAYVYR---NEAAIGNVLKKWIDsgkvkreELFIVTKlppGGNR- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 90 gedaswlpafsPAELQKAVHDNLRNLGLDVLDV--VNLRVMM-----GDGHGPAEGSIE-------ASLTVLAEMQ-QQG 154
Cdd:cd19155 85 -----------REKVEKFLLKSLEKLQLDYVDLylIHFPVGSlskedDSGKLDPTGEHKqdyttdlLDIWKAMEAQvDQG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 155 LVKHIGLSNVTPTQVAEARKIAEI--VCVQNEYNIAHRADDaMIDALAHDGIAYVPFFPLGG-----------------F 215
Cdd:cd19155 154 LTRSIGLSNFNREQMARILKNARIkpANLQVELHVYLQQKD-LVDFCSTHSITVTAYAPLGSpgaahfspgtgspsgssP 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 216 TPLQSSTLSDVAASLGATPMQVALAWLLQRspNILLIPGTSSVAHLRENMAAEKLHLSEEVLSTLDGISR 285
Cdd:cd19155 233 DLLQDPVVKAIAERHGKSPAQVLLRWLMQR--GVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDK 300
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
15-283 |
6.94e-15 |
|
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: 72.94 E-value: 6.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 15 RLGYGAMQLagpgvfgppRDRHVAITVLREALALGVNHIDTSDFYGPHVT-NQIIREALYPySDDLTIVTKI-GARRGED 92
Cdd:cd19156 11 RLGLGVWRV---------QDGAEAENAVKWAIEAGYRHIDTAAIYKNEEGvGQGIRESGVP-REEVFVTTKLwNSDQGYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 93 aSWLPAFSpaelqkavhDNLRNLGLDVLDVVNLrvmmgdgHGPAEGSIEASLTVLAEMQQQGLVKHIGLSNVTPTQVAEA 172
Cdd:cd19156 81 -STLAAFE---------ESLEKLGLDYVDLYLI-------HWPVKGKFKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEEL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 173 RKIAEIVCVQNEYNIaH--RADDAMIDALAHDGIAYVPFFPLGGFTPLQSSTLSDVAASLGATPMQVALAWLLQRspNIL 250
Cdd:cd19156 144 LKSCKVAPMVNQIEL-HplLTQEPLRKFCKEKNIAVEAWSPLGQGKLLSNPVLKAIGKKYGKSAAQVIIRWDIQH--GII 220
|
250 260 270
....*....|....*....|....*....|...
gi 16129367 251 LIPGTSSVAHLRENMAAEKLHLSEEVLSTLDGI 283
Cdd:cd19156 221 TIPKSVHEERIQENFDVFDFELTAEEIRQIDGL 253
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
13-162 |
7.08e-15 |
|
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+).
Pssm-ID: 381389 [Multi-domain] Cd Length: 293 Bit Score: 72.97 E-value: 7.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 13 VNRLGYGAMQLAGpgVFGPPRDRHvAITVLREALALGVNHIDTSDFYGPHVTNQIIREALYPYS-DDLTIVTKIGaRRGE 91
Cdd:cd19163 13 VSKLGFGASPLGG--VFGPVDEEE-AIRTVHEALDSGINYIDTAPWYGQGRSETVLGKALKGIPrDSYYLATKVG-RYGL 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129367 92 DASWLPAFSPAELQKAVHDNLRNLGLDVLDVVNLrvmmgdgHGPAEGS-----IEASLTVLAEMQQQGLVKHIGLS 162
Cdd:cd19163 89 DPDKMFDFSAERITKSVEESLKRLGLDYIDIIQV-------HDIEFAPsldqiLNETLPALQKLKEEGKVRFIGIT 157
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
15-285 |
8.06e-15 |
|
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: 72.30 E-value: 8.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 15 RLGYGAMQLAGpgvfgpprdrHVAITVLREALALGVNHIDTSDFYGPHVT-NQIIREALYPySDDLTIVTKIGAR--RGE 91
Cdd:cd19132 9 AIGFGTYPLKG----------DEGVEAVVAALQAGYRLLDTAFNYENEGAvGEAVRRSGVP-REELFVTTKLPGRhhGYE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 92 DAswlpafspaelQKAVHDNLRNLGLDVLDVVNLrvmmgdgH--GPAEGSIEASLTVLAEMQQQGLVKHIGLSNVTPTQV 169
Cdd:cd19132 78 EA-----------LRTIEESLYRLGLDYVDLYLI-------HwpNPSRDLYVEAWQALIEAREEGLVRSIGVSNFLPEHL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 170 aeaRKIAEIVCV-----QNEYNiAHRADDAMIDALAHDGIAYVPFFPLG-GFTPLQSSTLSDVAASLGATPMQVALAWLL 243
Cdd:cd19132 140 ---DRLIDETGVtpavnQIELH-PYFPQAEQRAYHREHGIVTQSWSPLGrGSGLLDEPVIKAIAEKHGKTPAQVVLRWHV 215
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 16129367 244 QRspNILLIPGTSSVAHLRENMAAEKLHLSEEVLSTLDGISR 285
Cdd:cd19132 216 QL--GVVPIPKSANPERQRENLAIFDFELSDEDMAAIAALDR 255
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-283 |
9.93e-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: 381327 [Multi-domain] Cd Length: 304 Bit Score: 72.63 E-value: 9.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 15 RLGYGAMQLAGPGvfGPPRDRHVAITVLREALALGVNHIDTSDFYGPhvTNQIIREAL------YPYSDDLTIVTKIGAR 88
Cdd:cd19101 4 RVINGMWQLSGGH--GGIRDEDAAVRAMAAYVDAGLTTFDCADIYGP--AEELIGEFRkrlrreRDAADDVQIHTKWVPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 89 RGEDAswlpaFSPAELQKAVHDNLRNLGLDVLDVV-----NLRVmmgdghgpaEGSIEASLTvLAEMQQQGLVKHIGLSN 163
Cdd:cd19101 80 PGELT-----MTRAYVEAAIDRSLKRLGVDRLDLVqfhwwDYSD---------PGYLDAAKH-LAELQEEGKIRHLGLTN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 164 VTPTQVAEA-RKIAEIVCVQNEYN-IAHRADDAMIDALAHDGIAYVPFFPL----------------------------- 212
Cdd:cd19101 145 FDTERLREIlDAGVPIVSNQVQYSlLDRRPENGMAALCEDHGIKLLAYGTLaggllsekylgvpeptgpaletrslqkyk 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 213 ------GGFTPLQS--STLSDVAASLGATPMQVALAWLLQRspnilliPGTSSV-------AHLRENMAAEKLHLSEEVL 277
Cdd:cd19101 225 lmidewGGWDLFQEllRTLKAIADKHGVSIANVAVRWVLDQ-------PGVAGVivgarnsEHIDDNVRAFSFRLDDEDR 297
|
....*.
gi 16129367 278 STLDGI 283
Cdd:cd19101 298 AAIDAV 303
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
12-267 |
1.07e-14 |
|
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: 72.57 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 12 SVNRLGYGAMQLAGpgVFGPPRDRHVAITVLREALALGVNHIDTSDFYGPHVTNQIIREAL----YPySDDLTIVTKIGa 87
Cdd:cd19153 11 NVSPVGLGTAALGG--VYGDGLEQDEAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALaalqVP-RSSYTVATKVG- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 88 rRGEDASWlpAFSPAELQKAVHDNLRNLGLDVLDVVNLR-VMMGDghgpAEGSIEASLTVLAEMQQQGLVKHIGLSNV-- 164
Cdd:cd19153 87 -RYRDSEF--DYSAERVRASVATSLERLHTTYLDVVYLHdIEFVD----YDTLVDEALPALRTLKDEGVIKRIGIAGYpl 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 165 -TPTQVAEARKIAEIVCVQNeYNIAHRADDAMIDALAH----DGIAYVPFFPLG----------GFTPLQS--------- 220
Cdd:cd19153 160 dTLTRATRRCSPGSLDAVLS-YCHLTLQDARLESDAPGlvrgAGPHVINASPLSmglltsqgppPWHPASGelrhyaaaa 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 16129367 221 -STLSDVAASLGATPMQVALAWLLQRSPNILlipGTSSVAHLRENMAA 267
Cdd:cd19153 239 dAVCASVEASLPDLALQYSLAAHAGVGTVLL---GPSSLAQLRSMLAA 283
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
21-283 |
1.37e-14 |
|
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) is a founding member of the aldo-keto reductase family 5 member B1 (AKR5B1). M6DH (EC 1.1.1.218), also called naloxone reductase, oxidizes the C-6 hydroxy group of morphine and codeine.
Pssm-ID: 381353 [Multi-domain] Cd Length: 268 Bit Score: 72.05 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 21 MQLAGPGVFGPPRDRhvAITVLREALALGVNHIDTSDFYGPHV-TNQIIREALYPYSDdLTIVTKIgarrgedasWLPAF 99
Cdd:cd19127 9 MPALGLGVFQTPPEE--TADAVATALADGYRLIDTAAAYGNEReVGEGIRRSGVDRSD-IFVTTKL---------WISDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 100 SPAELQKAVHDNLRNLGLDVLDVVNLrvmmgdgHGPAEGSIE---ASLTVLAEMQQQGLVKHIGLSNVTPTQVAEARKIA 176
Cdd:cd19127 77 GYDKALRGFDASLRRLGLDYVDLYLL-------HWPVPNDFDrtiQAYKALEKLLAEGRVRAIGVSNFTPEHLERLIDAT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 177 EIVCVQNEYNI-AHRADDAMIDALAHDGIAYVPFFPLGGFT------------PLQSSTLSDVAASLGATPMQVALAWLL 243
Cdd:cd19127 150 TVVPAVNQVELhPYFSQKDLRAFHRRLGIVTQAWSPIGGVMrygasgptgpgdVLQDPTITGLAEKYGKTPAQIVLRWHL 229
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 16129367 244 QRspNILLIPGTSSVAHLRENMAAEKLHLSEEVLSTLDGI 283
Cdd:cd19127 230 QN--GVSAIPKSVHPERIAENIDIFDFALSAEDMAAIDAL 267
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
12-283 |
2.94e-14 |
|
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: 70.71 E-value: 2.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 12 SVNRLGYGAMQLagpgvfgPPRDRHVAITvlrEALALGVNHIDTSDFYGphvTNQIIREALYPYS---DDLTIVTKIGAR 88
Cdd:cd19130 9 SIPQLGYGVFKV-------PPADTQRAVA---TALEVGYRHIDTAAIYG---NEEGVGAAIAASGiprDELFVTTKLWND 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 89 RGEdaswlpafsPAELQKAVHDNLRNLGLDVLDVVNLRVMMgdghgPAEGSIEASLTVLAEMQQQGLVKHIGLSNVTPTQ 168
Cdd:cd19130 76 RHD---------GDEPAAAFAESLAKLGLDQVDLYLVHWPT-----PAAGNYVHTWEAMIELRAAGRTRSIGVSNFLPPH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 169 VAEARKIAEIVCVQNEYNIAHR-ADDAMIDALAHDGIAYVPFFPLGGFTPLQSSTLSDVAASLGATPMQVALAWLLQRSP 247
Cdd:cd19130 142 LERIVAATGVVPAVNQIELHPAyQQRTIRDWAQAHDVKIEAWSPLGQGKLLGDPPVGAIAAAHGKTPAQIVLRWHLQKGH 221
|
250 260 270
....*....|....*....|....*....|....*.
gi 16129367 248 NIllIPGTSSVAHLRENMAAEKLHLSEEVLSTLDGI 283
Cdd:cd19130 222 VV--FPKSVRRERMEDNLDVFDFDLTDTEIAAIDAL 255
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
13-283 |
6.37e-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: 70.70 E-value: 6.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 13 VNRLGYGAMQlagpgVFGPPRDRHVAITVLREALALGVNHIDTSDFYG----PHVTNQIIREALYPYSDdLTIVTKI--G 86
Cdd:cd19143 13 VSALSFGSWV-----TFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYAngqsEEIMGQAIKELGWPRSD-YVVSTKIfwG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 87 ARRGEDASwlPAFSPAELQKAVHDNLRNLGLDVLDVVNLrvmmgdgHGP-AEGSIEAslTVLA--EMQQQGLVKHIGLSN 163
Cdd:cd19143 87 GGGPPPND--RGLSRKHIVEGTKASLKRLQLDYVDLVFC-------HRPdPATPIEE--TVRAmnDLIDQGKAFYWGTSE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 164 VTPTQVAEARKIAEI------VCVQNEYNIAHRaddamiDALAHDgiaYVPFFPLGG-----FTPLQSSTLS-------- 224
Cdd:cd19143 156 WSAQQIEEAHEIADRlglippVMEQPQYNLFHR------ERVEVE---YAPLYEKYGlgtttWSPLASGLLTgkynngip 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 225 --------------------------------DVAASLGATPMQVALAWLLqRSPNI-LLIPGTSSVAHLRENMAAEKL- 270
Cdd:cd19143 227 egsrlalpgyewlkdrkeelgqekiekvrklkPIAEELGCSLAQLAIAWCL-KNPNVsTVITGATKVEQLEENLKALEVl 305
|
330
....*....|....
gi 16129367 271 -HLSEEVLSTLDGI 283
Cdd:cd19143 306 pKLTPEVMEKIEAI 319
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
21-285 |
8.66e-14 |
|
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: 69.83 E-value: 8.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 21 MQLAGPGVFGPPRDrhVAITVLREALALGVNHIDTSDFYGphvTNQIIREALYPYSD-------DLTIVTKIgarrgeda 93
Cdd:cd19111 4 MPVIGLGTYQSPPE--EVRAAVDYALFVGYRHIDTALSYQ---NEKAIGEALKWWLKngklkreEVFITTKL-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 94 sWLPAFSPAELQKAVHDNLRNLGLDVLDVVNLRVMMG---DGHGPAEGSIEASLT-VLAEMQQQ---GLVKHIGLSNVTP 166
Cdd:cd19111 71 -PPVYLEFKDTEKSLEKSLENLKLPYVDLYLIHHPCGfvnKKDKGERELASSDVTsVWRAMEALvseGKVKSIGLSNFNP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 167 TQVAEARKIAEIVC--VQNEYNIAHRADDAMIDALAHDgIAYVPFFPLGG------------FTPLQSSTLSDVAASLGA 232
Cdd:cd19111 150 RQINKILAYAKVKPsnLQLECHAYLQQRELRKFCNKKN-IVVTAYAPLGSpgranqslwpdqPDLLEDPTVLAIAKELDK 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 16129367 233 TPMQVALAWLLQRspNILLIPGTSSVAHLRENMAAEKLHLSEEVLSTLDGISR 285
Cdd:cd19111 229 TPAQVLLRFVLQR--GTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDR 279
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
45-286 |
2.09e-13 |
|
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: 68.95 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 45 ALALGVNHIDTSDFYG--PHVtNQIIREALYPYS----DDLTIVTKIgarrgedasWLPAFSPAELQKAVHDNLRNLGLD 118
Cdd:cd19106 29 ALDAGYRHIDCAAVYGneQEV-GEALKEKVGPGKavprEDLFVTSKL---------WNTKHHPEDVEPALRKTLKDLQLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 119 VLDVVNLRVMMGDGHG----P--AEGSIEASLT-------VLAEMQQQGLVKHIGLSNVTPTQVAEARKIAEI--VCVQN 183
Cdd:cd19106 99 YLDLYLIHWPYAFERGdnpfPknPDGTIRYDSThyketwkAMEKLVDKGLVKAIGLSNFNSRQIDDILSVARIkpAVLQV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 184 EYNiAHRADDAMIDALAHDGIAYVPFFPLGG----------FTPLQSSTLSDVAASLGATPMQVALAWLLQRSpnILLIP 253
Cdd:cd19106 179 ECH-PYLAQNELIAHCKARGLVVTAYSPLGSpdrpwakpdePVLLEEPKVKALAKKYNKSPAQILLRWQVQRG--VVVIP 255
|
250 260 270
....*....|....*....|....*....|...
gi 16129367 254 GTSSVAHLRENMAAEKLHLSEEVLSTLDGISRE 286
Cdd:cd19106 256 KSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRN 288
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
15-280 |
2.20e-13 |
|
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: 68.92 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 15 RLGYGAMQLAGPGVFGpprdRHVAITVLREALALGVNHIDTSDFYGPHVTNQIIREALYPYS-DDLTIVTKIGARRGEDA 93
Cdd:cd19162 2 RLGLGAASLGNLARAG----EDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALARHPrAEYVVSTKVGRLLEPGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 94 SWLPA-------FSPAELQKAVHDNLRNLGLDVLDVvnlrVMMGDGHGPAEGSIEASLTVLAEMQQQGLVKHIGlsnVTP 166
Cdd:cd19162 78 AGRPAgadrrfdFSADGIRRSIEASLERLGLDRLDL----VFLHDPDRHLLQALTDAFPALEELRAEGVVGAIG---VGV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 167 TQVAEARKIAEI-----VCVQNEYNIA-HRADDAMIDALAHDGIAYV---PF--------------FPLGGFTP---LQS 220
Cdd:cd19162 151 TDWAALLRAARRadvdvVMVAGRYTLLdRRAATELLPLCAAKGVAVVaagVFnsgilatddpagdrYDYRPATPevlARA 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129367 221 STLSDVAASLGATPMQVALAWLLqRSPNIL-LIPGTSSVAHLRENMAAEKLHLSEEVLSTL 280
Cdd:cd19162 231 RRLAAVCRRYGVPLPAAALQFPL-RHPAVAsVVVGAASPAELRDNLALLRTPIPAEFWAEL 290
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
21-285 |
4.25e-13 |
|
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: 68.28 E-value: 4.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 21 MQLAGPGVFgpPRDRHVAITVLREALALGVNHIDTSDFYGphvTNQIIREALYPYSD-------DLTIVTKIGarrGEDA 93
Cdd:cd19112 11 MPVIGLGVW--RMEPGEIKELILNAIKIGYRHFDCAADYK---NEKEVGEALAEAFKtglvkreDLFITTKLW---NSDH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 94 SWLPafspaelqKAVHDNLRNLGLDVLDVVNLRVMMGDGH------GPAEG-----------SIEASLTVLAEMQQQGLV 156
Cdd:cd19112 83 GHVI--------EACKDSLKKLQLDYLDLYLVHFPVATKHtgvgttGSALGedgvldidvtiSLETTWHAMEKLVSAGLV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 157 KHIGLSNVTPTQVAEARKIAEI--VCVQNEYNIAHRADDAMIDALAHdGIAYVPFFPLGG----------FTPLQSSTLS 224
Cdd:cd19112 155 RSIGISNYDIFLTRDCLAYSKIkpAVNQIETHPYFQRDSLVKFCQKH-GISVTAHTPLGGaaanaewfgsVSPLDDPVLK 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129367 225 DVAASLGATPMQVALAWLLQRspNILLIPGTSSVAHLRENMAAEKLHLSEEVLSTLDGISR 285
Cdd:cd19112 234 DLAKKYGKSAAQIVLRWGIQR--NTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDR 292
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
21-283 |
4.58e-13 |
|
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: 67.68 E-value: 4.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 21 MQLAGPGVFGPPRDRHVAITVLREALALGVNHIDTSDFYGphvTNQIIREA--------LYPYSDDLTIVTKIGARRGED 92
Cdd:cd19124 5 MPVIGMGTASDPPSPEDIKAAVLEAIEVGYRHFDTAAAYG---TEEALGEAlaealrlgLVKSRDELFVTSKLWCSDAHP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 93 ASWLPAfspaeLQKAvhdnLRNLGLDVLD--VVNLRVMMGDG---HGPAEG-----SIEASLTVLAEMQQQGLVKHIGLS 162
Cdd:cd19124 82 DLVLPA-----LKKS----LRNLQLEYVDlyLIHWPVSLKPGkfsFPIEEEdflpfDIKGVWEAMEECQRLGLTKAIGVS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 163 NVTPTQVAEARKIAEI--VCVQNEYNIAHRADDaMIDALAHDGIAYVPFFPLGGF-TP------LQSSTLSDVAASLGAT 233
Cdd:cd19124 153 NFSCKKLQELLSFATIppAVNQVEMNPAWQQKK-LREFCKANGIHVTAYSPLGAPgTKwgsnavMESDVLKEIAAAKGKT 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 16129367 234 PMQVALAWLLQRSpnILLIPGTSSVAHLRENMAAEKLHLSEEVLSTLDGI 283
Cdd:cd19124 232 VAQVSLRWVYEQG--VSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
49-275 |
1.67e-12 |
|
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: 66.68 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 49 GVNHIDTSDFYGPHVTNQIIRE--ALYPYSDDLTIVTK--IGARRGED---ASWLPAFSPAELQKAVHDNLRNLGLDVLD 121
Cdd:cd19146 48 GGNFIDTANNYQGEESERWVGEwmASRGNRDEMVLATKytTGYRRGGPikiKSNYQGNHAKSLRLSVEASLKKLQTSYID 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 122 VvnLRVMMGDghgpAEGSIEASLTVLAEMQQQGLVKHIGLSNvTPTQV-------AEARKIAEIVCVQNEYNIAHRADDA 194
Cdd:cd19146 128 I--LYVHWWD----YTTSIPELMQSLNHLVAAGKVLYLGVSD-TPAWVvskanayARAHGLTQFVVYQGHWSAAFRDFER 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 195 MIDALA-HDGIAYVPFFPLGG------------------FTPLQ------SSTLSDVAASLGATPMQVALAWLLQRSPNI 249
Cdd:cd19146 201 DILPMCeAEGMALAPWGVLGQgqfrteeefkrrgrsgrkGGPQTekerkvSEKLEKVAEEKGTAITSVALAYVMHKAPYV 280
|
250 260
....*....|....*....|....*.
gi 16129367 250 LLIPGTSSVAHLRENMAAEKLHLSEE 275
Cdd:cd19146 281 FPIVGGRKVEHLKGNIEALGISLSDE 306
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
23-162 |
3.40e-12 |
|
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: 65.38 E-value: 3.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 23 LAGPGVFGP-----PRDRHVAiTVLREALALGVNHIDTSDFYGPHVTnqIIREAL------YPySDDLTIVTKIGARRGE 91
Cdd:cd19164 17 IFGAATFSYqyttdPESIPPV-DIVRRALELGIRAFDTSPYYGPSEI--ILGRALkalrdeFP-RDTYFIITKVGRYGPD 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129367 92 DASwlpaFSPAELQKAVHDNLRNLGLDVLDVvnlrVMMGDGHGPAEGSIEASLTVLAEMQQQGLVKHIGLS 162
Cdd:cd19164 93 DFD----YSPEWIRASVERSLRRLHTDYLDL----VYLHDVEFVADEEVLEALKELFKLKDEGKIRNVGIS 155
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
45-283 |
9.53e-12 |
|
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: 63.72 E-value: 9.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 45 ALALGVNHIDTSDFYGPHV-TNQIIREALYPySDDLTIVTKIG-ARRGEDASwlpafspaelQKAVHDNLRNLGLDVLDV 122
Cdd:cd19134 33 ALEAGYRLIDTAAAYGNEAaVGRAIAASGIP-RGELFVTTKLAtPDQGFTAS----------QAACRASLERLGLDYVDL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 123 VNLrvmmgdgH--GPAEGSIEASLTVLAEMQQQGLVKHIGLSNVTPTQVAEARKIAEIVCVQNEYNIAHR-ADDAMIDAL 199
Cdd:cd19134 102 YLI-------HwpAGREGKYVDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLTFFTPAVNQIELHPLlNQAELRKVN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 200 AHDGIAYVPFFPLGGFTPLQSSTLSDVAASLGATPMQVALAWLLQRSpnILLIPGTSSVAHLRENMAAEKLHLSEEVLST 279
Cdd:cd19134 175 AQHGIVTQAYSPLGVGRLLDNPAVTAIAAAHGRTPAQVLLRWSLQLG--NVVISRSSNPERIASNLDVFDFELTADHMDA 252
|
....
gi 16129367 280 LDGI 283
Cdd:cd19134 253 LDGL 256
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
17-264 |
9.81e-12 |
|
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: 64.02 E-value: 9.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 17 GYGAMQLAGPGVFGPprDRHVAITVLREALALGVNHIDTSDFY-GPHVTNQIIREALYP---YSDDLTIVTKIgarrged 92
Cdd:cd19129 2 GSGAIPALGFGTLIP--DPSATRNAVKAALEAGFRHFDCAERYrNEAEVGEAMQEVFKAgkiRREDLFVTTKL------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 93 asWLPAFSPAELQKAVHDNLRNLGLDVLDVVNLRVMM----GDGHGP--AEGSI--EASLTVL------AEMQQQGLVKH 158
Cdd:cd19129 73 --WNTNHRPERVKPAFEASLKRLQLDYLDLYLIHTPFafqpGDEQDPrdANGNViyDDGVTLLdtwramERLVDEGRCKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 159 IGLSNVTPTQVAEARKIAEI--VCVQNEYNIAHRADDaMIDALAHDGIAYVPFFPLG-GFTP--LQSSTLSDVAASLGAT 233
Cdd:cd19129 151 IGLSDVSLEKLREIFEAARIkpAVVQVESHPYLPEWE-LLDFCKNHGIVLQAFAPLGhGMEPklLEDPVITAIARRVNKT 229
|
250 260 270
....*....|....*....|....*....|.
gi 16129367 234 PMQVALAWLLQRSPNILLIPGTSSvaHLREN 264
Cdd:cd19129 230 PAQVLLAWAIQRGTALLTTSKTPS--RIREN 258
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
33-266 |
1.59e-11 |
|
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: 63.49 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 33 RDRHVAITVLREALALGVNHIDTSDFYGphvtNQI--------IREALYPYS---DDLTIVTKIGARRGEDASWLPA--- 98
Cdd:cd19099 18 ETDEEYREALKAALDSGINVIDTAINYR----GGRserligkaLRELIEKGGikrDEVVIVTKAGYIPGDGDEPLRPlky 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 99 ---------------------FSPAELQKAVHDNLRNLGLDVLDVVNL----RVMMGDGHGPAEGSIEASLTVLAEMQQQ 153
Cdd:cd19099 94 leeklgrglidvadsaglrhcISPAYLEDQIERSLKRLGLDTIDLYLLhnpeEQLLELGEEEFYDRLEEAFEALEEAVAE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 154 GLVKHIGLSNVTPTQV----------AEARKIAEIVC--------VQNEYNIAHRADDAM-----------IDALAHDGI 204
Cdd:cd19099 174 GKIRYYGISTWDGFRAppalpghlslEKLVAAAEEVGgdnhhfkvIQLPLNLLEPEALTEkntvkgealslLEAAKELGL 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129367 205 AYVPFFPLGGFTPLQSSTLSDVAA-SLGATPMQVALAWLLQRSPNILLIPGTSSVAHLRENMA 266
Cdd:cd19099 254 GVIASRPLNQGQLLGELRLADLLAlPGGATLAQRALQFARSTPGVDSALVGMRRPEHVDENLA 316
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
7-281 |
2.84e-11 |
|
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: 62.92 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 7 TLGTKsVNRLGYGAMQLAGP-GVFGPPRDRHVAITVLREALALGVNHIDTSDFYGPHVTNQIIRE--ALYPYSDDLTIVT 83
Cdd:cd19147 5 TAGIR-VSPLILGAMSIGDAwSGFMGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEwmKSRKNRDQIVIAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 84 KIGA--RRGEDASWLPAFSPAELQKAVH----DNLRNLGLDVLDVvnLRVMMGDghgpAEGSIEASLTVLAEMQQQGLVK 157
Cdd:cd19147 84 KFTTdyKAYEVGKGKAVNYCGNHKRSLHvsvrDSLRKLQTDWIDI--LYVHWWD----YTTSIEEVMDSLHILVQQGKVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 158 HIGLSNvTPTQV-------AEARKIAEIVCVQNEYNIAHRADDAMIDALA-HDGIAYVPFFPLGG--F------------ 215
Cdd:cd19147 158 YLGVSD-TPAWVvsaanyyATAHGKTPFSVYQGRWNVLNRDFERDIIPMArHFGMALAPWDVLGGgkFqskkaveerkkn 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 216 -------------TPLQ---SSTLSDVAASLGATPMQ-VALAWLLQRSPNILLIPGTSSVAHLRENMAAEKLHLSEEVLS 278
Cdd:cd19147 237 geglrsfvggteqTPEEvkiSEALEKVAEEHGTESVTaIALAYVRSKAPNVFPLVGGRKIEHLKDNIEALSIKLTPEEIE 316
|
...
gi 16129367 279 TLD 281
Cdd:cd19147 317 YLE 319
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
13-283 |
1.13e-10 |
|
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: 61.33 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 13 VNRLGYGAMQlagpgVFGPPRDRHVAITVLREALALGVNHIDTSD-FYGPHVTNQ---IIREALYPYSdDLTIVTKIGAR 88
Cdd:cd19142 13 VSNVGLGTWS-----TFSTAISEEQAEEIVTLAYENGINYFDTSDaFTSGQAETElgrILKKKGWKRS-SYIVSTKIYWS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 89 RGEDASWLpafSPAELQKAVHDNLRNLGLDVLDVVNLRVMmgDGHGPAEGSIEAsltvLAEMQQQGLVKHIGLSNVTPTQ 168
Cdd:cd19142 87 YGSEERGL---SRKHIIESVRASLRRLQLDYIDIVIIHKA--DPMCPMEEVVRA----MSYLIDNGLIMYWGTSRWSPVE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 169 VAEARKIAEI------VCVQNEYNIAHRadDAM---IDALAH-----------------DGIAYVPFFPLGGFTPLQSST 222
Cdd:cd19142 158 IMEAFSIARQfncptpICEQSEYHMFCR--EKMelyMPELYNkvgvglitwsplslgldPGISEETRRLVTKLSFKSSKY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 223 ----------------------LSDVAASLGATPMQVALAWLLQRSP-NILLIpGTSSVAHLRENMAAEKLH--LSEEVL 277
Cdd:cd19142 236 kvgsdgngiheetrrashklreLSLIAERLGCDLTQLLIAWSLKNENvQCVLI-GASSLEQLYSQLNSLQLLpkLNSAVM 314
|
....*.
gi 16129367 278 STLDGI 283
Cdd:cd19142 315 EELERI 320
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
13-283 |
1.88e-10 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 60.56 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 13 VNRLGYGAMQLAGpgVFGPPRdRHVAITVLREALALGVNHIDTSDFYGPHVTNQIIREALYPYS---DDLTIVTKIGaRR 89
Cdd:PLN02587 11 VSSVGFGASPLGS--VFGPVS-EEDAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKALGiprEKYVVSTKCG-RY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 90 GEDASwlpaFSPAELQKAVHDNLRNLGLDVLDVVNLrvmmgdgHGPAEGS----IEASLTVLAEMQQQGLVKHIGLS--- 162
Cdd:PLN02587 87 GEGFD----FSAERVTKSVDESLARLQLDYVDILHC-------HDIEFGSldqiVNETIPALQKLKESGKVRFIGITglp 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 163 ---------NVTPTQVaearkiaEIVCVQNEYNIAHRADDAMIDALAHDGIAYVPFFPL--GGFT----------PLQSS 221
Cdd:PLN02587 156 laiftyvldRVPPGTV-------DVILSYCHYSLNDSSLEDLLPYLKSKGVGVISASPLamGLLTengppewhpaPPELK 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 222 TLSDVAASL----GATPMQVALAWLLQRSPNILLIPGTSSVAHLRENMAA----EKLHLSEEVLSTLDGI 283
Cdd:PLN02587 229 SACAAAATHckekGKNISKLALQYSLSNKDISTTLVGMNSVQQVEENVAAatelETSGIDEELLSEVEAI 298
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
42-285 |
3.85e-10 |
|
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) from Mus musculus (liver, AKR1E1) and Homo sapiens (AKR1E2). 1,5-anhydro-D-fructose reductase), also called AF reductase, or aldo-keto reductase family 1 member C-like protein 2 (AKR1CL2), catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. AKR1E2 is a testis aldo-keto reductase (tAKR), which is also known as testis-specific protein (TSP), or LoopADR.
Pssm-ID: 381336 [Multi-domain] Cd Length: 301 Bit Score: 59.59 E-value: 3.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 42 LREALALGVNHIDTSDFYgpHVTNQI-------IREALYPySDDLTIVTKIgarrgedasWLPAFSPAELQKAVHDNLRN 114
Cdd:cd19110 23 VKVAIDAGYRHFDCAYLY--HNESEVgagirekIKEGVVR-REDLFIVSKL---------WCTCHKKSLVKTACTRSLKA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 115 LGLDVLDVVNLRVMMG----------DGHG---PAEGSIEASLTVLAEMQQQGLVKHIGLSNVTPTQVAEA--RKIAEIV 179
Cdd:cd19110 91 LKLNYLDLYLIHWPMGfkpgepdlplDRSGmviPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLERLlnKPGLRVK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 180 CVQNEYNI-AHRADDAMIDALAHDGIAYVPFFPLGG----FTPLQSSTLSDVAASLGATPMQVALAWLLQRspNILLIPG 254
Cdd:cd19110 171 PVTNQIEChPYLTQKKLISFCQSRNVSVTAYRPLGGscegVDLIDDPVIQRIAKKHGKSPAQILIRFQIQR--NVIVIPK 248
|
250 260 270
....*....|....*....|....*....|.
gi 16129367 255 TSSVAHLRENMAAEKLHLSEEVLSTLDGISR 285
Cdd:cd19110 249 SVTPSRIKENIQVFDFELTEHDMDNLLSLDR 279
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
2-286 |
7.80e-10 |
|
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: 58.28 E-value: 7.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 2 SSNTFTLGT-KSVNRLGYGAMQLAgpgvfgPPRDRHVAITVLREalalGVNHIDTSDFYG-PHVTNQIIREALYPYSDdL 79
Cdd:cd19117 2 SSKTFKLNTgAEIPAVGLGTWQSK------PNEVAKAVEAALKA----GYRHIDTAAIYGnEEEVGQGIKDSGVPREE-I 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 80 TIVTKIgarrgeDASWlpafsPAELQKAVHDNLRNLGLDVLDvvnLRVMmgdgHGPA-------------EGSIEASLT- 145
Cdd:cd19117 71 FITTKL------WCTW-----HRRVEEALDQSLKKLGLDYVD---LYLM----HWPVpldpdgndflfkkDDGTKDHEPd 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 146 -----VLAEMQQ---QGLVKHIGLSNVTPTQVAE--ARKIAEIVCVQNEYNI-AHRADDAMIDALAHDGIAYVPFFPLGG 214
Cdd:cd19117 133 wdfikTWELMQKlpaTGKVKAIGVSNFSIKNLEKllASPSAKIVPAVNQIELhPLLPQPKLVDFCKSKGIHATAYSPLGS 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129367 215 F-TPL-QSSTLSDVAASLGATPMQVALAWLLQRspNILLIPGTSSVAHLRENMaaEKLHLSEEVLSTLDGISRE 286
Cdd:cd19117 213 TnAPLlKEPVIIKIAKKHGKTPAQVIISWGLQR--GYSVLPKSVTPSRIESNF--KLFTLSDEEFKEIDELHKE 282
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
45-285 |
1.56e-08 |
|
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase (AR, EC 1.1.1.21) from Homo sapiens (AKR1B1), Oryctolagus cuniculus (kidney, AKR1B2), Mus musculus (AKR1B3), Rattus norvegicus (lens, AKR1B4), Bos taurus (lens/testis, AKR1B5), and Sus scrofa (lens, AKR1B6), aldose reductase-related protein 1 (ALD1, EC1.1.1.21) from Mus musculus (AKR1B7), Rattus norvegicus (AKR1B14), and Homo sapiens (AKR1B15), Mus musculus fibroblast growth factor induced protein (FR-1 or AKR1B8, EC 1.1.1.21), Cricetulus griseus aldose reductase-related protein 2 (ALD2 or AKR1B9, EC 1.1.1.21), aldose reductase-like from Homo sapiens (ARL-1 or AKR1B10) and Rattus norvegicus (AKR1B13), aldo-keto reductase from Gallus domesticus (eye, tongue, esophagus, AKR1B12), and Oryctolagus cuniculus AR-like protein (3beta-HSD, AKR1B19). AR, also called aldehyde reductase, catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. ALD1 reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. It may play a role in the metabolism of xenobiotic aromatic aldehydes. FR-1, also called aldose reductase-related protein 2, or fibroblast growth factor-regulated protein (FGFRP), is induced by fibroblast growth factor-1. It may play a role in the regulation of the cell cycle. FR-1 belongs to the NADPH-dependent aldo-keto reductase family. ALD2 is an inducible aldo-keto reductase with a preference for aliphatic substrates. It can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. ARL-1, also called aldose reductase-like, or aldose reductase-related protein (ARP), or small intestine reductase, or SI reductase, acts as all-trans-retinaldehyde reductase that can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). It may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. AKR1B15, also called estradiol 17-beta-dehydrogenase AKR1B15, is a mitochondrial aldo-keto reductase that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. It has a strong selectivity towards NADP(H). AKR1B19 is aldose reductase-like that may show 3-beta-hydroxysteroid dehydrogenase (3beta-HSD) activity.
Pssm-ID: 381333 [Multi-domain] Cd Length: 307 Bit Score: 54.73 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 45 ALALGVNHIDTSDFY------GPHVTNQIIREALYpySDDLTIVTKIgarrgedasWLPAFSPAELQKAVHDNLRNLGLD 118
Cdd:cd19107 26 AIDAGYRHIDCAYVYqnenevGEAIQEKIKEQVVK--REDLFIVSKL---------WCTFHEKGLVKGACQKTLSDLKLD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 119 VLDVVNLRVMMG----------DGHG---PAEGSIEASLTVLAEMQQQGLVKHIGLSNVTPTQVAEarkiaeivcVQNEY 185
Cdd:cd19107 95 YLDLYLIHWPTGfkpgkelfplDESGnviPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIER---------ILNKP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 186 NIAHR------------ADDAMIDALAHDGIAYVPFFPLGG-----FTPLQSSTLSD-----VAASLGATPMQVALAWLL 243
Cdd:cd19107 166 GLKYKpavnqiechpylTQEKLIQYCQSKGIVVTAYSPLGSpdrpwAKPEDPSLLEDpkikeIAAKHNKTTAQVLIRFPI 245
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 16129367 244 QRspNILLIPGTSSVAHLRENMAAEKLHLSEEVLSTLDGISR 285
Cdd:cd19107 246 QR--NLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNR 285
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
38-281 |
2.06e-08 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 53.92 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 38 AITVLREALALGVNHIDTSDFYGPHV-TNQIIREALYPySDDLTIVTKIGARRGEDAswlpafspaelQKAVHDNLRNLG 116
Cdd:PRK11565 30 VITAIHKALEVGYRSIDTAAIYKNEEgVGKALKEASVA-REELFITTKLWNDDHKRP-----------REALEESLKKLQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 117 LDVLDvvnLRVMmgdgHGP--AEGSIEASLTVLAEMQQQGLVKHIGLSNVTPTQVaeARKIAE--IVCVQNEYNIAHRAD 192
Cdd:PRK11565 98 LDYVD---LYLM----HWPvpAIDHYVEAWKGMIELQKEGLIKSIGVCNFQIHHL--QRLIDEtgVTPVINQIELHPLMQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 193 DAMIDAL-AHDGIAYVPFFPL--GGFTPLQSSTLSDVAASLGATPMQVALAWLLQRSpnILLIPGTSSVAHLRENMAA-- 267
Cdd:PRK11565 169 QRQLHAWnATHKIQTESWSPLaqGGKGVFDQKVIRDLADKYGKTPAQIVIRWHLDSG--LVVIPKSVTPSRIAENFDVfd 246
|
250
....*....|....*..
gi 16129367 268 ---EKLHLSEevLSTLD 281
Cdd:PRK11565 247 frlDKDELGE--IAKLD 261
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
29-283 |
5.15e-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: 53.07 E-value: 5.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 29 FGPPRDRHVAITVLREALALGVNHIDTSDFYGP----HVTNQIIREALYPYSDdLTIVTKIgaRRGEDASWLPAFSPAEL 104
Cdd:cd19160 26 FGSQISDETAEDLLTVAYEHGVNLFDTAEVYAAgkaeRTLGNILKSKGWRRSS-YVVTTKI--YWGGQAETERGLSRKHI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 105 QKAVHDNLRNLGLDVLDVVNLRVMmgDGHGPAEGSIEASLTVLaemqQQGLVKHIGLSNVTPTQVAEARKIAE------I 178
Cdd:cd19160 103 IEGLRGSLDRLQLEYVDIVFANRS--DPNSPMEEIVRAMTYVI----NQGMAMYWGTSRWSAMEIMEAYSVARqfnlipP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 179 VCVQNEYNIAHRAD-DAMIDALAHD-GIAYVPFFPLG---------------------GFTPLQSSTLSD---------- 225
Cdd:cd19160 177 VCEQAEYHLFQREKvEMQLPELYHKiGVGSVTWSPLAcglitgkydgrvpdtcraavkGYQWLKEKVQSEegkkqqakvk 256
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129367 226 ----VAASLGATPMQVALAWLLQRSPNILLIPGTSSVAHLRENMAAEKL--HLSEEVLSTLDGI 283
Cdd:cd19160 257 elhpIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGSIQVlsQLTPQTVMEIDAL 320
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
135-285 |
2.38e-07 |
|
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose reductase xyl1 (XR, EC 1.1.1.307) is a founding member of aldo-keto reductase family 2 member D1 (AKR2D1). It catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol in a NAD(P)H dependent manner.
Pssm-ID: 381341 [Multi-domain] Cd Length: 311 Bit Score: 51.27 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 135 PAEGSIEASLTVLAEMQQQGLVKHIGLSNVTPTQVAEARKIAEI--VCVQNEYNiAHRADDAMIDALAHDGI---AYVPF 209
Cdd:cd19115 138 FSNAPIQETWTAMEKLVDKGLARSIGVSNFSAQLLMDLLRYARIrpATLQIEHH-PYLTQPRLVKYAQKEGIavtAYSSF 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 210 FPLG----------GFTPL-QSSTLSDVAASLGATPMQVALAWLLQRspNILLIPGTSSVAHLRENMAAEKLHLSEEVLS 278
Cdd:cd19115 217 GPQSfleldlpgakDTPPLfEHDVIKSIAEKHGKTPAQVLLRWATQR--GIAVIPKSNNPKRLAQNLDVTGFDLEAEEIK 294
|
....*..
gi 16129367 279 TLDGISR 285
Cdd:cd19115 295 AISALDI 301
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
41-281 |
8.05e-07 |
|
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.
Pssm-ID: 381340 [Multi-domain] Cd Length: 302 Bit Score: 49.48 E-value: 8.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 41 VLREALALGVNHIDTSDFYGPHV-----TNQIIREALYPySDDLTIVTKIgarrgedasWLPAFSPAELQKAVHDNLRNL 115
Cdd:cd19114 22 VIYNAIKVGYRLIDGALLYGNEAevgrgIRKAIQEGLVK-REDLFIVTKL---------WNNFHGKDHVREAFDRQLKDY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 116 GLDVLDV-----------VNLRVMM--GDGHG-----PAEGS-IEASLTVLAEMQQQGLVKHIGLSNVTPTQVAEARKIA 176
Cdd:cd19114 92 GLDYIDLylihfpipaayVDPAENYpfLWKDKelkkfPLEQSpMQECWREMEKLVDAGLVRNIGIANFNVQLILDLLTYA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 177 EI--VCVQNEYNiAHRADDAMIDALAHDGI---AYVPFFP---------LGGFTPL-QSSTLSDVAASLGATPMQVALAW 241
Cdd:cd19114 172 KIkpAVLQIEHH-PYLQQKRLIDWAKKQGIqitAYSSFGNavytkvtkhLKHFTNLlEHPVVKKLADKHKRDTGQVLLRW 250
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 16129367 242 LLQRspNILLIPGTSSVAHLRENMAAEKLHLSEEVLSTLD 281
Cdd:cd19114 251 AVQR--NITVIPKSVNVERMKTNLDITSYKLDEEDMEALY 288
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
25-275 |
9.89e-07 |
|
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: 49.16 E-value: 9.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 25 GPGVFGPPRDRHVAITVLREALALGVNHIDTSDFYgpHVTNQI---IREALYPYSD----DLTIVTKIgarrgedasWLP 97
Cdd:cd19122 13 GFGTFANEGAKGETYAAVTKALDVGYRHLDCAWFY--LNEDEVgdaVRDFLKENPSvkreDLFICTKV---------WNH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 98 AFSPAELQKAVHDNLRNLGLDVLDVV----NLRVMMGDGHGPAEGS-----IEASLT--------VLAEMQQQGLVKHIG 160
Cdd:cd19122 82 LHEPEDVKWSIDNSLKNLKLDYIDLFlvhwPIAAEKNDQRSPKLGPdgkyvILKDLTenpeptwrAMEEIYESGKAKAIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 161 LSNVTPTQVAEARKIAEIVCVQNEYNI-AHRADDAMIDALAHDGIAYVPFFPLGGFTPLQSS--------TLSDVAASLG 231
Cdd:cd19122 162 VSNWTIPGLKKLLSFAKVKPHVNQIEIhPFLPNEELVDYCFSNDILPEAYSPLGSQNQVPSTgervsenpTLNEVAEKGG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 16129367 232 ATPMQVALAWLLQRSpnILLIPGTSSVAHLRENMaaEKLHLSEE 275
Cdd:cd19122 242 YSLAQVLIAWGLRRG--YVVLPKSSTPSRIESNF--KSIELSDE 281
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
141-280 |
1.63e-06 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 48.49 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 141 EASLTVLAEMQQQGLvkHIGLSNVTPTQVAEARKIAEIV--------CVQNEYNI-----------AHRADDAMI--DAL 199
Cdd:cd19098 143 ADVLAALAELKAEGV--KIGLSLSGPQQAETLRRALEIEidgarlfdSVQATWNLleqsagealeeAHEAGMGVIvkEAL 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 200 AHDGIAYVPffPLGGFTPLqSSTLSDVAASLGATPMQVALAWLLQRSPNILLIPGTSSVAHLRENMAAEKLHLSEEVLST 279
Cdd:cd19098 221 ANGRLTDRN--PSPELAPL-MAVLKAVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRALDVSLDLELLAA 297
|
.
gi 16129367 280 L 280
Cdd:cd19098 298 L 298
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
147-286 |
1.22e-05 |
|
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: 45.90 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 147 LAEMQQQGLVKHIGLSNVTPTQVAEARKIAEI--VCVQNEYNiAHRADDAMIDALAHDGI---AYVPFFP---------- 211
Cdd:cd19113 149 LEKLVDAGKIKSIGVSNFPGALILDLLRGATIkpAVLQIEHH-PYLQQPKLIEYAQKAGItitAYSSFGPqsfvelnqgr 227
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129367 212 -LGGFTPLQSSTLSDVAASLGATPMQVALAWLLQRspNILLIPGTSSVAHLRENMAAEKLHLSEEVLSTLDGISRE 286
Cdd:cd19113 228 aLNTPTLFEHDTIKSIAAKHNKTPAQVLLRWATQR--GIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIG 301
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
45-285 |
2.46e-05 |
|
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: 44.91 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 45 ALALGVNHIDTSDFYG--PHVtNQIIREALYPYS---DDLTIVTKIgarrgedasWLPAFSPAELQKAVHDNLRNLGLDV 119
Cdd:cd19108 36 AIDAGFRHIDSAYLYQneEEV-GQAIRSKIADGTvkrEDIFYTSKL---------WCTFHRPELVRPALEKSLKKLQLDY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 120 LD--VVNLRVMM--GDGHGPAEGS---------IEASLTVLAEMQQQGLVKHIGLSNVTPTQVaeaRKIA-------EIV 179
Cdd:cd19108 106 VDlyLIHFPVALkpGEELFPKDENgklifdtvdLCATWEAMEKCKDAGLAKSIGVSNFNRRQL---EMILnkpglkyKPV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 180 CVQNEYNIaHRADDAMIDALAHDGIAYVPFFPLGGFTP-----------LQSSTLSDVAASLGATPMQVALAWLLQRSpn 248
Cdd:cd19108 183 CNQVECHP-YLNQSKLLDFCKSKDIVLVAYSALGSQRDkewvdqnspvlLEDPVLCALAKKHKRTPALIALRYQLQRG-- 259
|
250 260 270
....*....|....*....|....*....|....*..
gi 16129367 249 ILLIPGTSSVAHLRENMAAEKLHLSEEVLSTLDGISR 285
Cdd:cd19108 260 VVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNR 296
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
38-207 |
1.35e-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: 42.70 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 38 AITVLREALALGVNHIDTSDFYGPHVTNQIIREALYPY-SDDLTIVTKIG-----ARRGE--DASW----LP-----AFS 100
Cdd:cd19161 22 ADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKpRDEFVLSTKVGrllkpAREGSvpDPNGfvdpLPfeivyDYS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 101 PAELQKAVHDNLRNLGLDVLDVVNL----RVMMGDGHGPA------EGSIEAsltvLAEMQQQGLVKHIGLSnVTPTQV- 169
Cdd:cd19161 102 YDGIMRSFEDSLQRLGLNRIDILYVhdigVYTHGDRKERHhfaqlmSGGFKA----LEELKKAGVIKAFGLG-VNEVQIc 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16129367 170 AEARKIAEIVC--VQNEYNI-AHRADDAMIDALAHDGIAYV 207
Cdd:cd19161 177 LEALDEADLDCflLAGRYSLlDQSAEEEFLPRCEQRGTSLV 217
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
14-267 |
2.47e-04 |
|
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381378 [Multi-domain] Cd Length: 308 Bit Score: 41.83 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 14 NRLGYGAMQLAGPGVFGPPRDrhvAITVLREALALGVNHIDTSDFYGPHVTNQIIREALYPYS-DDLTIVTKIG----AR 88
Cdd:cd19152 1 PKLGFGTAPLGNLYEAVSDEE---AKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELGrEDYVISTKVGrllvPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 89 RGEDASWLPAF------------SPAELQKAVHDNLRNLGLDVLDVVNLrvmmgdgHGPAEGSIEASLTV---------- 146
Cdd:cd19152 78 QEVEPTFEPGFwnplpfdavfdySYDGILRSIEDSLQRLGLSRIDLLSI-------HDPDEDLAGAESDEhfaqaikgaf 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129367 147 --LAEMQQQGLVKHIGL-SNvtptQVAEARKIAE-----IVCVQNEYNI-AHRADDAMIDALAHDGIAYV---------- 207
Cdd:cd19152 151 raLEELREEGVIKAIGLgVN----DWEVILRILEeadldWVMLAGRYTLlDHSAARELLPECEKRGVKVVnagpfnsgfl 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129367 208 ---PFFPLGGFTPL------QSSTLSDVAASLGATPMQVALAWLLQRSPNILLIPGTSSVAHLRENMAA 267
Cdd:cd19152 227 aggDNFDYYEYGPAppeliaRRDRIEALCEQHGVSLAAAALQFALAPPAVASVAPGASSPERVEENVAL 295
|
|
| |
