|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
22-283 |
2.57e-63 |
|
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: 200.14 E-value: 2.57e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 22 VSRLGIGISRAACSGRHAAEQRRELGLALVRRALELGVNFLDTTDYnYSPDraaCANVLIRDAFSPYQPNLVIATSIGLI 101
Cdd:cd19088 1 VSRLGYGAMRLTGPGIWGPPADREEAIAVLRRALELGVNFIDTADS-YGPD---VNERLIAEALHPYPDDVVIATKGGLV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 102 RD-DRNGIRAATGAELRWLVNEKLRQLRLDRLDLVILRLGETLPPHGESlavrFDALAELREEGLIRHLGLSNADDRHLS 180
Cdd:cd19088 77 RTgPGWWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQ----LGALAELQDEGLIRHIGLSNVTVAQIE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 181 EALQIAPVVAVQNLFHFGHQRDVALLRRCEKHNIAYIPFLPLGCTGVT-ACTPLARIALRHHTTVDQIALRWLLSVSPVT 259
Cdd:cd19088 153 EARAIVRIVSVQNRYNLANRDDEGVLDYCEAAGIAFIPWFPLGGGDLAqPGGLLAEVAARLGATPAQVALAWLLARSPVM 232
|
250 260
....*....|....*....|....
gi 1028513208 260 IVAPQIGSVSRLEELVLCRDLPLT 283
Cdd:cd19088 233 LPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
18-290 |
1.28e-57 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 186.33 E-value: 1.28e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 18 GELAVSRLGIGISRAACSGRHAAEQRRELGLALVRRALELGVNFLDTTDYnYSPDraaCANVLIRDAFSPYQPNLVIATS 97
Cdd:PRK10376 13 GGRSVNRLGYGAMQLAGPGVFGPPKDRDAAIAVLREAVALGVNHIDTSDF-YGPH---VTNQLIREALHPYPDDLTIVTK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 98 IGLIRDDRNG-IRAATGAELRWLVNEKLRQLRLDRLDLVILRL-GETLPPHGESLAVRFDALAELREEGLIRHLGLSNAD 175
Cdd:PRK10376 89 VGARRGEDGSwLPAFSPAELRRAVHDNLRNLGLDVLDVVNLRLmGDGHGPAEGSIEEPLTVLAELQRQGLVRHIGLSNVT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 176 DRHLSEALQIAPVVAVQNLFHFGHQRDVALLRRCEKHNIAYIPFLPLGctGVTA--CTPLARIALRHHTTVDQIALRWLL 253
Cdd:PRK10376 169 PTQVAEARKIAEIVCVQNHYNLAHRADDALIDALARDGIAYVPFFPLG--GFTPlqSSTLSDVAASLGATPMQVALAWLL 246
|
250 260 270
....*....|....*....|....*....|....*..
gi 1028513208 254 SVSPVTIVAPQIGSVSRLEELVLCRDLPLTAEDMADL 290
Cdd:PRK10376 247 QRSPNILLIPGTSSVAHLRENLAAAELVLSEEVLAEL 283
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
20-290 |
1.64e-40 |
|
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: 143.01 E-value: 1.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 20 LAVSRLGIGISRAACSGRHAAEQRrelGLALVRRALELGVNFLDTTDyNYSPDRAacaNVLIRDAFSPYQPN-LVIATSI 98
Cdd:COG0667 11 LKVSRLGLGTMTFGGPWGGVDEAE---AIAILDAALDAGINFFDTAD-VYGPGRS---EELLGEALKGRPRDdVVIATKV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 99 GLIRDDRNGIRAATGAELRWLVNEKLRQLRLDRLDLVILRLGETLPPHGESLAvrfdALAELREEGLIRHLGLSNADDRH 178
Cdd:COG0667 84 GRRMGPGPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLG----ALDELVREGKIRYIGVSNYSAEQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 179 LSEALQIA----PVVAVQNLFHFGHQR-DVALLRRCEKHNIAYIPFLPLG------------------------------ 223
Cdd:COG0667 160 LRRALAIAeglpPIVAVQNEYSLLDRSaEEELLPAARELGVGVLAYSPLAgglltgkyrrgatfpegdraatnfvqgylt 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1028513208 224 CTGVTACTPLARIALRHHTTVDQIALRWLLSVSPVTIVAPQIGSVSRLEELVLCRDLPLTAEDMADL 290
Cdd:COG0667 240 ERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADLELSAEDLAAL 306
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
19-290 |
3.30e-37 |
|
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381310 [Multi-domain] Cd Length: 296 Bit Score: 133.81 E-value: 3.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 19 ELAVSRLGIGIsrAACSGRHAAEQRRELGLALVRRALELGVNFLDTTDyNYSPDRAacaNVLIRDAFSPYQPNLVIATSI 98
Cdd:cd19084 1 DLKVSRIGLGT--WAIGGTWWGEVDDQESIEAIKAAIDLGINFFDTAP-VYGFGHS---EEILGKALKGRRDDVVIATKC 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 99 GLIRD-DRNGIRAATGAELRWLVNEKLRQLRLDRLDLVILRLGETLPPHGESLAvrfdALAELREEGLIRHLGLSNADDR 177
Cdd:cd19084 75 GLRWDgGKGVTKDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAE----ALEKLKKEGKIRYIGVSNFSVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 178 HLSEALQIAPVVAVQ---NLFHFGHQRDvaLLRRCEKHNIAYIPFLPLG---CTG------------------------- 226
Cdd:cd19084 151 QLEEARKYGPIVSLQppySMLEREIEEE--LLPYCRENGIGVLPYGPLAqglLTGkykkeptfppddrrsrfpffrgenf 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1028513208 227 --VTACTP-LARIALRHHTTVDQIALRWLLSVSPVTIVAPQIGSVSRLEELVLCRDLPLTAEDMADL 290
Cdd:cd19084 229 ekNLEIVDkLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDWELTEEELKEI 295
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
20-290 |
2.26e-32 |
|
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: 121.19 E-value: 2.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 20 LAVSRLGIGisraaCSGRHAAEQR---RELGLALVRRALELGVNFLDTTDYnYSPDraacAN-VLIRDAFSPYQPNLVIA 95
Cdd:cd19078 2 LEVSAIGLG-----CMGMSHGYGPppdKEEMIELIRKAVELGITFFDTAEV-YGPY----TNeELVGEALKPFRDQVVIA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 96 TSIG----------LIRDDR-NGIRAAtgaelrwlVNEKLRQLRLDRLDLVIL-RLGETLPPhgESLAvrfDALAELREE 163
Cdd:cd19078 72 TKFGfkidggkpgpLGLDSRpEHIRKA--------VEGSLKRLQTDYIDLYYQhRVDPNVPI--EEVA---GTMKELIKE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 164 GLIRHLGLSNADDRHLSEALQIAPVVAVQNLFHFGHqRDV--ALLRRCEKHNIAYIPFLPLGC----------------- 224
Cdd:cd19078 139 GKIRHWGLSEAGVETIRRAHAVCPVTAVQSEYSMMW-REPekEVLPTLEELGIGFVPFSPLGKgfltgkidentkfdegd 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 225 --TGVTACTP------------LARIALRHHTTVDQIALRWLLSVSPVTIVAPQIGSVSRLEELVLCRDLPLTAEDMADL 290
Cdd:cd19078 218 drASLPRFTPealeanqalvdlLKEFAEEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAADIELTPEELREI 297
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
25-290 |
3.96e-32 |
|
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: 120.11 E-value: 3.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 25 LGIGisrAACSGRHAAEQRRELGLALVRRALELGVNFLDTTD-YNYSPDRAACANVLIRDAFspYQPNLVIAT----SIG 99
Cdd:pfam00248 1 IGLG---TWQLGGGWGPISKEEALEALRAALEAGINFIDTAEvYGDGKSEELLGEALKDYPV--KRDKVVIATkvpdGDG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 100 LIRDD--RNGIRAAtgaelrwlVNEKLRQLRLDRLDLVIL-RLGETLPPhgesLAVrFDALAELREEGLIRHLGLSNADD 176
Cdd:pfam00248 76 PWPSGgsKENIRKS--------LEESLKRLGTDYIDLYYLhWPDPDTPI----EET-WDALEELKKEGKIRAIGVSNFDA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 177 RHLSEALQ--IAPVVAVQNLFHFGHQRDVA-LLRRCEKHNIAYIPFLPLG----------------------CTGVTACT 231
Cdd:pfam00248 143 EQIEKALTkgKIPIVAVQVEYNLLRRRQEEeLLEYCKKNGIPLIAYSPLGgglltgkytrdpdkgpgerrrlLKKGTPLN 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1028513208 232 -----PLARIALRHHTTVDQIALRWLLSVSPVTIVAPQIGSVSRLEELVLCRDLPLTAEDMADL 290
Cdd:pfam00248 223 lealeALEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARI 286
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
23-275 |
8.17e-32 |
|
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: 117.62 E-value: 8.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 23 SRLGIGISRAacsGRHAAEQRRElglALVRRALELGVNFLDTTDyNYSPDRAacaNVLIRDAFSPYQP--NLVIATSIGL 100
Cdd:cd06660 1 SRLGLGTMTF---GGDGDEEEAF---ALLDAALEAGGNFFDTAD-VYGDGRS---ERLLGRWLKGRGNrdDVVIATKGGH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 101 IRDDRNGIRAATGAELRWLVNEKLRQLRLDRLDLVIL-RLGETLPPhGESLavrfDALAELREEGLIRHLGLSNADDRHL 179
Cdd:cd06660 71 PPGGDPSRSRLSPEHIRRDLEESLRRLGTDYIDLYYLhRDDPSTPV-EETL----EALNELVREGKIRYIGVSNWSAERL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 180 SEALQIA------PVVAVQNLFHFGHQR--DVALLRRCEKHNIAYIPFLPLGCtGVTactplarialrhhttvdQIALRW 251
Cdd:cd06660 146 AEALAYAkahglpGFAAVQPQYSLLDRSpmEEELLDWAEENGLPLLAYSPLAR-GPA-----------------QLALAW 207
|
250 260
....*....|....*....|....
gi 1028513208 252 LLSVSPVTIVAPQIGSVSRLEELV 275
Cdd:cd06660 208 LLSQPFVTVPIVGARSPEQLEENL 231
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
21-290 |
1.11e-29 |
|
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: 113.09 E-value: 1.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 21 AVSRLGIGiSRAACSGRHAAEQRRELGLALVRRALELGVNFLDTTdYNYSpdrAACANVLIRDAFSPY-QPNLVIATSI- 98
Cdd:cd19072 3 EVPVLGLG-TWGIGGGMSKDYSDDKKAIEALRYAIELGINLIDTA-EMYG---GGHAEELVGKAIKGFdREDLFITTKVs 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 99 --GLIRDDRngIRAAtgaelrwlvNEKLRQLRLDRLDLVILR-------LGETLpphgeslavrfDALAELREEGLIRHL 169
Cdd:cd19072 78 pdHLKYDDV--IKAA---------KESLKRLGTDYIDLYLIHwpnpsipIEETL-----------RAMEELVEEGKIRYI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 170 GLSNADDRHLSEALQI---APVVAVQ---NLFHFGHQRDvaLLRRCEKHNIAYIPFLPLGCTGVTACTP---LARIALRH 240
Cdd:cd19072 136 GVSNFSLEELEEAQSYlkkGPIVANQveyNLFDREEESG--LLPYCQKNGIAIIAYSPLEKGKLSNAKGsplLDEIAKKY 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1028513208 241 HTTVDQIALRWLLSvSPVTIVAPQIGSVSRLEELVLCRDLPLTAEDMADL 290
Cdd:cd19072 214 GKTPAQIALNWLIS-KPNVIAIPKASNIEHLEENAGALGWELSEEDLQRL 262
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
20-290 |
7.07e-29 |
|
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor. Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381302 [Multi-domain] Cd Length: 303 Bit Score: 111.92 E-value: 7.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 20 LAVSRLGIGisraaCSGRHAA--EQRRELGLALVRRALELGVNFLDTTDYnYSPDRaacaN-VLIRDAFSPYQPNLVIAT 96
Cdd:cd19076 10 LEVSALGLG-----CMGMSAFygPADEEESIATLHRALELGVTFLDTADM-YGPGT----NeELLGKALKDRRDEVVIAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 97 SIGLIRDDRNGIRAATG--AELRWLVNEKLRQLRLDRLDLVILRLGETLPPHGESLAvrfdALAELREEGLIRHLGLSNA 174
Cdd:cd19076 80 KFGIVRDPGSGFRGVDGrpEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVG----AMAELVEEGKVRYIGLSEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 175 DDRHLSEALQIAPVVAVQ---NLFhfghQRDV--ALLRRCEKHNIAYIPFLPLG---CTGVTACT--------------- 231
Cdd:cd19076 156 SADTIRRAHAVHPITAVQseySLW----TRDIedEVLPTCRELGIGFVAYSPLGrgfLTGAIKSPedlpeddfrrnnprf 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1028513208 232 -------------PLARIALRHHTTVDQIALRWLLSVSPVTIVAPQIGSVSRLEELVLCRDLPLTAEDMADL 290
Cdd:cd19076 232 qgenfdknlklveKLEAIAAEKGCTPAQLALAWVLAQGDDIVPIPGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
49-291 |
2.71e-26 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 103.98 E-value: 2.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 49 ALVRRALELGVNFLDTtdynyspdraACA--N-VLIRDAfspyqpnlvIATSiGLIRDD-------------RNGIRAAt 112
Cdd:COG0656 22 AAVRTALEAGYRHIDT----------AAMygNeEGVGEA---------IAAS-GVPREElfvttkvwndnhgYDDTLAA- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 113 gaelrwlVNEKLRQLRLDRLDLVIL------RLGETLpphgeslavrfDALAELREEGLIRHLGLSNADDRHLSEALQIA 186
Cdd:COG0656 81 -------FEESLERLGLDYLDLYLIhwpgpgPYVETW-----------RALEELYEEGLIRAIGVSNFDPEHLEELLAET 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 187 PV--VAVQNLFHFGHQRDvALLRRCEKHNIAYIPFLPLGCTGVTACTPLARIALRHHTTVDQIALRWLLSVSPVTIvaPQ 264
Cdd:COG0656 143 GVkpAVNQVELHPYLQQR-ELLAFCREHGIVVEAYSPLGRGKLLDDPVLAEIAEKHGKTPAQVVLRWHLQRGVVVI--PK 219
|
250 260
....*....|....*....|....*..
gi 1028513208 265 IGSVSRLEELVLCRDLPLTAEDMADLA 291
Cdd:COG0656 220 SVTPERIRENLDAFDFELSDEDMAAID 246
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
21-290 |
3.29e-26 |
|
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: 103.87 E-value: 3.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 21 AVSRLGIGISRAACSGRHAAEQRRELglalvRRALELGVNFLDTTDyNYSPDRAacaNVLIRDAFSPYQPNLVIATSIGL 100
Cdd:cd19138 10 KVPALGQGTWYMGEDPAKRAQEIEAL-----RAGIDLGMTLIDTAE-MYGDGGS---EELVGEAIRGRRDKVFLVSKVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 101 IRDDRNGIRAATGAELRWLvneklrqlRLDRLDLVIL------RLGETLpphgeslavrfDALAELREEGLIRHLGLSNA 174
Cdd:cd19138 81 SNASRQGTVRACERSLRRL--------GTDYLDLYLLhwrggvPLAETV-----------AAMEELKKEGKIRAWGVSNF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 175 DDRHLSEALQIA---PVVAVQNLFHFGHqRDVA--LLRRCEKHNIAYIPFLPLGCTGVTAC-----TPLARIALRHHTTV 244
Cdd:cd19138 142 DTDDMEELWAVPgggNCAANQVLYNLGS-RGIEydLLPWCREHGVPVMAYSPLAQGGLLRRgllenPTLKEIAARHGATP 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1028513208 245 DQIALRWLLSvSPVTIVAPQIGSVSRLEELVLCRDLPLTAEDMADL 290
Cdd:cd19138 221 AQVALAWVLR-DGNVIAIPKSGSPEHARENAAAADLELTEEDLAEL 265
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
20-275 |
8.95e-26 |
|
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: 101.79 E-value: 8.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 20 LAVSRLGIGisraacsGRHAAEQRRELGLALVRRALELGVNFLDT-TDYNYSPDRaacanvlIRDAFSPYQPNLVIATSI 98
Cdd:cd19100 9 LKVSRLGFG-------GGPLGRLSQEEAAAIIRRALDLGINYFDTaPSYGDSEEK-------IGKALKGRRDKVFLATKT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 99 GliRDDRNGIRAAtgaelrwlVNEKLRQLRLDRLDLVILR-------LGETLPPHGeslAvrFDALAELREEGLIRHLGL 171
Cdd:cd19100 75 G--ARDYEGAKRD--------LERSLKRLGTDYIDLYQLHavdteedLDQVFGPGG---A--LEALLEAKEEGKIRFIGI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 172 SNADDRHLSEALQIAPVVAVQ---NLFHFGHQRDV-ALLRRCEKHNIayipflplgctGVTACTPLARIALRHHTTVD-Q 246
Cdd:cd19100 140 SGHSPEVLLRALETGEFDVVLfpiNPAGDHIDSFReELLPLAREKGV-----------GVIAMKVLAGGRLLSGDPLDpE 208
|
250 260
....*....|....*....|....*....
gi 1028513208 247 IALRWLLSVSPVTIVAPQIGSVSRLEELV 275
Cdd:cd19100 209 QALRYALSLPPVDVVIVGMDSPEELDENL 237
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
22-275 |
2.31e-25 |
|
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: 101.01 E-value: 2.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 22 VSRLGIG---ISRAACSGRHAAEqrrelGLALVRRALELGVNFLDTTDyNYSpdrAACANVLIRDAFSPYQPNLVIATSI 98
Cdd:cd19086 3 VSEIGFGtwgLGGDWWGDVDDAE-----AIRALRAALDLGINFFDTAD-VYG---DGHSERLLGKALKGRRDKVVIATKF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 99 GLIRDDRNGIRAATGAE-LRWLVNEKLRQLRLDRLDLVILrlgetlppHGESLAVR-----FDALAELREEGLIRHLGLS 172
Cdd:cd19086 74 GNRFDGGPERPQDFSPEyIREAVEASLKRLGTDYIDLYQL--------HNPPDEVLdndelFEALEKLKQEGKIRAYGVS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 173 NADDRHLSEALQIAPVVAVQ---NLFhfgHQRDVA-LLRRCEKHNIayipflplgctGVTACTPLA------RIAlrhht 242
Cdd:cd19086 146 VGDPEEALAALRRGGIDVVQviyNLL---DQRPEEeLFPLAEEHGV-----------GVIARVPLAsglltgKLA----- 206
|
250 260 270
....*....|....*....|....*....|...
gi 1028513208 243 tvdQIALRWLLSVSPVTIVAPQIGSVSRLEELV 275
Cdd:cd19086 207 ---QAALRFILSHPAVSTVIPGARSPEQVEENA 236
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
19-290 |
2.98e-25 |
|
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: 102.11 E-value: 2.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 19 ELAVSRLGIGISraACSGRHA-AEQRRELGLALVRRALELGVNFLDTTDYnYSPDRAacaNVLIRDAFSPYQPN-LVIAT 96
Cdd:cd19083 8 DIDVNPIGLGTN--AVGGHNLyPNLDEEEGKDLVREALDNGVNLLDTAFI-YGLGRS---EELVGEVLKEYNRNeVVIAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 97 SiGLIRDDRNGIRAATGAE-LRWLVNEKLRQLRLDRLDLVILRLgetlPPHGESLAVRFDALAELREEGLIRHLGLSNAD 175
Cdd:cd19083 82 K-GAHKFGGDGSVLNNSPEfLRSAVEKSLKRLNTDYIDLYYIHF----PDGETPKAEAVGALQELKDEGKIRAIGVSNFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 176 DRHLSEALQIAPVVAVQ---NLFhfghQRDV--ALLRRCEKHNIAYIPFLPLGC---TG--------------------- 226
Cdd:cd19083 157 LEQLKEANKDGYVDVLQgeyNLL----QREAeeDILPYCVENNISFIPYFPLASgllAGkytkdtkfpdndlrndkplfk 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1028513208 227 -------VTACTPLARIALRHHTTVDQIALRWLLSVSPVTIVAPQIGSVSRLEELVLCRDLPLTAEDMADL 290
Cdd:cd19083 233 gerfsenLDKVDKLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKALDVTLTEEEIAFI 303
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
50-291 |
1.33e-24 |
|
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: 99.09 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 50 LVRRALELGVNFLDT-TDYNyspDRAACANVlIRDAFSPyQPNLVIATSIGLIRDDRNGIRAAtgaelrwlVNEKLRQLR 128
Cdd:cd19071 19 AVLAALEAGYRHIDTaAAYG---NEAEVGEA-IRESGVP-REELFITTKLWPTDHGYERVREA--------LEESLKDLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 129 LDRLDLVIL---RLGETLPPHGESLAVrFDALAELREEGLIRHLGLSNADDRHLSEALQ---IAPVVaVQNLFHFGHQRD 202
Cdd:cd19071 86 LDYLDLYLIhwpVPGKEGGSKEARLET-WRALEELVDEGLVRSIGVSNFNVEHLEELLAaarIKPAV-NQIELHPYLQQK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 203 vALLRRCEKHNIAYIPFLPLGCTGVT--ACTPLARIALRHHTTVDQIALRWLLSVSpvTIVAPQIGSVSRLEELVLCRDL 280
Cdd:cd19071 164 -ELVEFCKEHGIVVQAYSPLGRGRRPllDDPVLKEIAKKYGKTPAQVLLRWALQRG--VVVIPKSSNPERIKENLDVFDF 240
|
250
....*....|.
gi 1028513208 281 PLTAEDMADLA 291
Cdd:cd19071 241 ELSEEDMAAID 251
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
48-288 |
1.52e-23 |
|
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: 96.19 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 48 LALVRRALELGVNFLDTTD-YNyspDRAACANVLIrdAFSPYQPNLVIATSIGLIRDDRNGIRAAtgaelrwlVNEKLRQ 126
Cdd:cd19073 17 ANAVKEALELGYRHIDTAEiYN---NEAEVGEAIA--ESGVPREDLFITTKVWRDHLRPEDLKKS--------VDRSLEK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 127 LRLDRLDLVILRLgetlPPHGESLAVRFDALAELREEGLIRHLGLSNADDRHLSEALQIAPV--VAVQNLFH-FGHQRDv 203
Cdd:cd19073 84 LGTDYVDLLLIHW----PNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPLpiAVNQVEFHpFLYQAE- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 204 aLLRRCEKHNIAYIPFLPLGCTGVTACTPLARIALRHHTTVDQIALRWLLSVSPVTIvaPQIGSVSRLEELVLCRDLPLT 283
Cdd:cd19073 159 -LLEYCRENDIVITAYSPLARGEVLRDPVIQEIAEKYDKTPAQVALRWLVQKGIVVI--PKASSEDHLKENLAIFDWELT 235
|
....*
gi 1028513208 284 AEDMA 288
Cdd:cd19073 236 SEDVA 240
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
22-290 |
2.61e-23 |
|
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: 96.50 E-value: 2.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 22 VSRLGIGISRAACSGRHAAEQRRELgLALVRRALELGVNFLDTTD-YN--YSPDraacanvLIRDAFSPYQPNLVIATSI 98
Cdd:cd19085 1 VSRLGLGCWQFGGGYWWGDQDDEES-IATIHAALDAGINFFDTAEaYGdgHSEE-------VLGKALKGRRDDVVIATKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 99 GLIRDDRNGIRAAtgaelrwlVNEKLRQLRLDRLDLVILRLgetlPPHGESLAVRFDALAELREEGLIRHLGLSNADDRH 178
Cdd:cd19085 73 SPDNLTPEDVRKS--------CERSLKRLGTDYIDLYQIHW----PSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 179 LSEALQIAPVVAVQ---NLFhfghQRDV--ALLRRCEKHNIAYIPFLPLG---CTGVTACTP------------------ 232
Cdd:cd19085 141 LEEALDAGRIDSNQlpyNLL----WRAIeyEILPFCREHGIGVLAYSPLAqglLTGKFSSAEdfppgdartrlfrhfepg 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1028513208 233 -----------LARIALRHHTTVDQIALRWLLSVSPVT--IVAPQigSVSRLEELVLCRDLPLTAEDMADL 290
Cdd:cd19085 217 aeeetfealekLKEIADELGVTMAQLALAWVLQQPGVTsvIVGAR--NPEQLEENAAAVDLELSPSVLERL 285
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
20-290 |
9.61e-23 |
|
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: 95.34 E-value: 9.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 20 LAVSRLGIGisraaC-----SGRHAAEQRRELGLALVRRALELGVNFLDTTDYnYSpdrAACANVLIRDAFSPYQP--NL 92
Cdd:cd19079 10 LKVSRLCLG-----CmsfgdPKWRPWVLDEEESRPIIKRALDLGINFFDTANV-YS---GGASEEILGRALKEFAPrdEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 93 VIATSIGL-IRDDRNGiRAATGAELRWLVNEKLRQLRLDRLDLVILrlgetlppHgeslavRFD----------ALAELR 161
Cdd:cd19079 81 VIATKVYFpMGDGPNG-RGLSRKHIMAEVDASLKRLGTDYIDLYQI--------H------RWDyetpieetleALHDVV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 162 EEGLIRHLGLSNADDRHLSEALQIA------PVVAVQ---NLFHFGHQRDVALLrrCEKHNIAYIPFLPLG---CTG--- 226
Cdd:cd19079 146 KSGKVRYIGASSMYAWQFAKALHLAekngwtKFVSMQnhyNLLYREEEREMIPL--CEEEGIGVIPWSPLArgrLARpwg 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 227 -------VTACTP-----------------LARIALRHHTTVDQIALRWLLSVSPVTivAPQIG--SVSRLEELVLCRDL 280
Cdd:cd19079 224 dtterrrSTTDTAklkydyfteadkeivdrVEEVAKERGVSMAQVALAWLLSKPGVT--APIVGatKLEHLEDAVAALDI 301
|
330
....*....|
gi 1028513208 281 PLTAEDMADL 290
Cdd:cd19079 302 KLSEEEIKYL 311
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
48-291 |
1.25e-22 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 95.05 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 48 LALVRRALELGVNFLDTtdynyspdrAAC-----ANVLIRDAFSPYQPNLVIATSIGLIRDDRNGIRAATGAE-LRWLVN 121
Cdd:cd19102 29 IAAIRAALDLGINWIDT---------AAVyglghSEEVVGRALKGLRDRPIVATKCGLLWDEEGRIRRSLKPAsIRAECE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 122 EKLRQLRLDRLDLVILRLgetlPPHGESLAVRFDALAELREEGLIRHLGLSNADDRHLSEALQIAPVVAVQN---LFHFG 198
Cdd:cd19102 100 ASLRRLGVDVIDLYQIHW----PDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQAIHPIASLQPpysLLRRG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 199 HQRDValLRRCEKHNIAYIPFLPLG---CTGvtACTP--------------------------------LARIALRHHTT 243
Cdd:cd19102 176 IEAEI--LPFCAEHGIGVIVYSPMQsglLTG--KMTPervaslpaddwrrrspffqepnlarnlalvdaLRPIAERHGRT 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1028513208 244 VDQIALRWLLSVSPVTIVAPQIGSVSRLEELVLCRDLPLTAEDMADLA 291
Cdd:cd19102 252 VAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAADLRLTPEELAEIE 299
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
116-291 |
3.90e-22 |
|
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: 92.71 E-value: 3.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 116 LRWLVNEKLRQLRLDRLDLVILRLgetlPPHGESLAVRFDALAELREEGLIRHLGLSNADDRHLSEALQI--APVVAVQN 193
Cdd:cd19140 80 FLASVEESLRKLRTDYVDLLLLHW----PNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELseAPLFTNQV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 194 LFHFGH-QRDValLRRCEKHNIAYIPFLPLGCTGVTACTPLARIALRHHTTVDQIALRWLLSVSPVtIVAPQIGSVSRLE 272
Cdd:cd19140 156 EYHPYLdQRKL--LDAAREHGIALTAYSPLARGEVLKDPVLQEIGRKHGKTPAQVALRWLLQQEGV-AAIPKATNPERLE 232
|
170
....*....|....*....
gi 1028513208 273 ELVLCRDLPLTAEDMADLA 291
Cdd:cd19140 233 ENLDIFDFTLSDEEMARIA 251
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
51-290 |
4.45e-21 |
|
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: 89.98 E-value: 4.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 51 VRRALELGVNFLDTTDYNYSPDRAACAnvlIRDAFSPyQPNLVIATSIGLIRDDrngIRAAtgaelrwlVNEKLRQLRLD 130
Cdd:cd19120 31 VKLALKAGFRHIDTAEMYGNEKEVGEA---LKESGVP-REDLFITTKVSPGIKD---PREA--------LRKSLAKLGVD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 131 RLDLVILRLGETLPPHGESLAVRFDALAELREEGLIRHLGLSNADDRHLSEALQIAPVV-AV-QNLFH-FGHQRDVALLR 207
Cdd:cd19120 96 YVDLYLIHSPFFAKEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAKIKpAVnQIEFHpYLYPQQPALLE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 208 RCEKHNI---AYIPFLPLgctGVTACTP----LARIALRHHTTVDQIALRWLLS--VSPVTIVapqiGSVSRLEELVLCR 278
Cdd:cd19120 176 YCREHGIvvsAYSPLSPL---TRDAGGPldpvLEKIAEKYGVTPAQVLLRWALQkgIVVVTTS----SKEERMKEYLEAF 248
|
250
....*....|..
gi 1028513208 279 DLPLTAEDMADL 290
Cdd:cd19120 249 DFELTEEEVEEI 260
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
49-288 |
1.15e-20 |
|
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: 89.64 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 49 ALVRRALELGVNFLDTTD-YNYspdraACANVLIRDAFSPYQPNLVIATSIGLIRDDRNG----------IRAATGAE-L 116
Cdd:cd19149 37 RTIHAALDLGINLIDTAPaYGF-----GHSEEIVGKAIKGRRDKVVLATKCGLRWDREGGsfffvrdgvtVYKNLSPEsI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 117 RWLVNEKLRQLRLDRLDLVILRLGETLPPHGESLAvrfdALAELREEGLIRHLGLSNADDRHLSEALQIAPVVAVQ---N 193
Cdd:cd19149 112 REEVEQSLKRLGTDYIDLYQTHWQDVETPIEETME----ALEELKRQGKIRAIGASNVSVEQIKEYVKAGQLDIIQekyS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 194 LFHFGHQRDVALLrrCEKHNIAYIPFLPLG----------------------------------CTGVTACTPLARialR 239
Cdd:cd19149 188 MLDRGIEKELLPY--CKKNNIAFQAYSPLEqglltgkitpdrefdagdarsgipwfspenrekvLALLEKWKPLCE---K 262
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1028513208 240 HHTTVDQIALRWLLSVSPVTIVAPQIGSVSRLEELVLCRDLPLTAEDMA 288
Cdd:cd19149 263 YGCTLAQLVIAWTLAQPGITSALCGARKPEQAEENAKAGDIRLSAEDIA 311
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
20-290 |
3.99e-20 |
|
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: 88.04 E-value: 3.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 20 LAVSRLGIGISR--AACSGRHAAeqrrelglALVRRALELGVNFLDTTDYnYSPDRAACAN----VLI---------RDa 84
Cdd:cd19081 7 LSVSPLCLGTMVfgWTADEETSF--------ALLDAFVDAGGNFIDTADV-YSAWVPGNAGgeseTIIgrwlksrgkRD- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 85 fspyqpNLVIATSIGL-IRDDRNG-----IRAAtgaelrwlVNEKLRQLRLDRLDLVILRLGETLPPHGESLAvrfdALA 158
Cdd:cd19081 77 ------RVVIATKVGFpMGPNGPGlsrkhIRRA--------VEASLRRLQTDYIDLYQAHWDDPATPLEETLG----ALN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 159 ELREEGLIRHLGLSNADDRHLSEALQIA------PVVAVQ---NLFHFGH-QRDVALLrrCEKHNIAYIPFLPLG---CT 225
Cdd:cd19081 139 DLIRQGKVRYIGASNYSAWRLQEALELSrqhglpRYVSLQpeyNLVDRESfEGELLPL--CREEGIGVIPYSPLAggfLT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 226 GV---TACTP-----------------------LARIALRHHTTVDQIALRWLLSVSPVTivAPQIG--SVSRLEELVLC 277
Cdd:cd19081 217 GKyrsEADLPgstrrgeaakrylnerglrildaLDEVAAEHGATPAQVALAWLLARPGVT--APIAGarTVEQLEDLLAA 294
|
330
....*....|...
gi 1028513208 278 RDLPLTAEDMADL 290
Cdd:cd19081 295 AGLRLTDEEVARL 307
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
19-291 |
9.86e-20 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 87.95 E-value: 9.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 19 ELAVSRLGIGISRAACSGRHAAEqrrelglALVRRALELGVNFLDTTdYNYSPDRAAcanvlIRDAFSPYQPNLVIATSI 98
Cdd:COG1453 10 GLEVSVLGFGGMRLPRKDEEEAE-------ALIRRAIDNGINYIDTA-RGYGDSEEF-----LGKALKGPRDKVILATKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 99 glirddrnGIRAATGAELRWLVNEKLRQLRLDRLDLVIL---RLGETLPPHGESLAVrFDALAELREEGLIRHLGLSNAD 175
Cdd:COG1453 77 --------PPWVRDPEDMRKDLEESLKRLQTDYIDLYLIhglNTEEDLEKVLKPGGA-LEALEKAKAEGKIRHIGFSTHG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 176 DrhLSEALQIA---PVVAVQ---NLFHFGHQRDVALLRRCEKHNIAYIPFLPLGctG---VTACTPLARIALRHHTTVDQ 246
Cdd:COG1453 148 S--LEVIKEAIdtgDFDFVQlqyNYLDQDNQAGEEALEAAAEKGIGVIIMKPLK--GgrlANPPEKLVELLCPPLSPAEW 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1028513208 247 iALRWLLSVSPVTIVAPQIGSVSRLEE--LVLCRDLPLTAEDMADLA 291
Cdd:COG1453 224 -ALRFLLSHPEVTTVLSGMSTPEQLDEnlKTADNLEPLTEEELAILE 269
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
20-273 |
1.23e-19 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 85.71 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 20 LAVSRLGIGisrAACSGRHAAEqrrelglaLVRRALELGVNFLDT-TDYNYSPDRAACANVL---IRDafspyqpNLVIA 95
Cdd:cd19105 11 LKVSRLGFG---GGGLPRESPE--------LLRRALDLGINYFDTaEGYGNGNSEEIIGEALkglRRD-------KVFLA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 96 TSIglirddRNGIRAATGAELRWLVNEKLRQLRLDRLDLVILRLGETLPPHGESLAVRfDALAELREEGLIRHLGLSNAD 175
Cdd:cd19105 73 TKA------SPRLDKKDKAELLKSVEESLKRLQTDYIDIYQLHGVDTPEERLLNEELL-EALEKLKKEGKVRFIGFSTHD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 176 DRH--LSEALQIAPVVAVQ---NLFHFGHQRDvALLRRCEKHNIayipflplgctGVTACTPLA-----RIALRHHT--- 242
Cdd:cd19105 146 NMAevLQAAIESGWFDVIMvayNFLNQPAELE-EALAAAAEKGI-----------GVVAMKTLAggylqPALLSVLKakg 213
|
250 260 270
....*....|....*....|....*....|..
gi 1028513208 243 -TVDQIALRWLLSVSPVTIVAPQIGSVSRLEE 273
Cdd:cd19105 214 fSLPQAALKWVLSNPRVDTVVPGMRNFAELEE 245
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
122-291 |
6.94e-19 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 83.56 E-value: 6.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 122 EKLRQLRLDRLDLVILRLGEtlPPHGESLAVRFDALAELREEGLIRHLGLSNADDRHLSEALQI---APVVAVQNLFH-- 196
Cdd:cd19139 79 ESLEKLRTDYVDLTLIHWPS--PNDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVvgaGAIATNQIELSpy 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 197 FGHQRDVALlrrCEKHNIAYIPFLPLGCTGVTACTPLARIALRHHTTVDQIALRWLLSVSpvTIVAPQIGSVSRLEELVL 276
Cdd:cd19139 157 LQNRKLVAH---CKQHGIHVTSYMTLAYGKVLDDPVLAAIAERHGATPAQIALAWAMARG--YAVIPSSTKREHLRSNLL 231
|
170
....*....|....*
gi 1028513208 277 CRDLPLTAEDMADLA 291
Cdd:cd19139 232 ALDLTLDADDMAAIA 246
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
23-273 |
4.53e-18 |
|
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: 81.51 E-value: 4.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 23 SRLGIGISRAacsGRHAAEQRRELGLALVRRALELGVNFLDTT-DYNYSPDR--AACANvLIRDafspyqpNLVIATSIG 99
Cdd:cd19095 1 SVLGLGTSGI---GRVWGVPSEAEAARLLNTALDLGINLIDTApAYGRSEERlgRALAG-LRRD-------DLFIATKVG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 100 LIRDDRNGIRAATGAELRWLVNEKLRQLRLDRLDLVILrlgetlppHGESLAVR----FDALAELREEGLIRHLGLSNaD 175
Cdd:cd19095 70 THGEGGRDRKDFSPAAIRASIERSLRRLGTDYIDLLQL--------HGPSDDELtgevLETLEDLKAAGKVRYIGVSG-D 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 176 DRHLSEALQIAPVVAVQNLFHFGHQRDVALLRRCEKHNIAYI--------------PFLPLGCTGVTACTPLARIALrhh 241
Cdd:cd19095 141 GEELEAAIASGVFDVVQLPYNVLDREEEELLPLAAEAGLGVIvnrplangrlrrrvRRRPLYADYARRPEFAAEIGG--- 217
|
250 260 270
....*....|....*....|....*....|..
gi 1028513208 242 TTVDQIALRWLLSVSPVTIVAPQIGSVSRLEE 273
Cdd:cd19095 218 ATWAQAALRFVLSHPGVSSAIVGTTNPEHLEE 249
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
43-287 |
9.77e-18 |
|
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: 80.69 E-value: 9.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 43 RRELGLALVRRALELGVNFLDTTDYnYSpdrAACANVLIRDAFSPY-QPNLVIATSI---GLIRDDRngIRAATGAelrw 118
Cdd:cd19137 24 RDEEMVELLKTAIELGYTHIDTAEM-YG---GGHTEELVGKAIKDFpREDLFIVTKVwptNLRYDDL--LRSLQNS---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 119 lvnekLRQLRLDRLDLVILRLgetlPPHGESLAVRFDALAELREEGLIRHLGLSNADDRHLSEALQIA--PVVAVQ---N 193
Cdd:cd19137 94 -----LRRLDTDYIDLYLIHW----PNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSqtPIVCNQvkyN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 194 LFHFGHQRDvALLRRCEKHNIAYIPFLPLGCTGVTACTPLARIALRHHTTVDQIALRWLLSvSPVTIVAPQIGSVSRLEE 273
Cdd:cd19137 165 LEDRDPERD-GLLEYCQKNGITVVAYSPLRRGLEKTNRTLEEIAKNYGKTIAQIALAWLIQ-KPNVVAIPKAGRVEHLKE 242
|
250
....*....|....
gi 1028513208 274 LVLCRDLPLTAEDM 287
Cdd:cd19137 243 NLKATEIKLSEEEM 256
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
122-290 |
2.16e-17 |
|
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: 79.68 E-value: 2.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 122 EKLRQLRLDRLDLVILRLgeTLPPHG-----ESLAVRFDALAELREEGLIRHLGLSNADDRHLSEALQ---IAPVVaVQN 193
Cdd:cd19135 91 ASLKRLGVDYLDLYLLHW--PDCPSSgknvkETRAETWRALEELYDEGLCRAIGVSNFLIEHLEQLLEdcsVVPHV-NQV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 194 LFHFgHQRDVALLRRCEKHNIAYIPFLPLGCTGVTACTPLARIALRHHTTVDQIALRWLLSVSPVTIvaPQIGSVSRLEE 273
Cdd:cd19135 168 EFHP-FQNPVELIEYCRDNNIVFEGYCPLAKGKALEEPTVTELAKKYQKTPAQILIRWSIQNGVVTI--PKSTKEERIKE 244
|
170
....*....|....*..
gi 1028513208 274 LVLCRDLPLTAEDMADL 290
Cdd:cd19135 245 NCQVFDFSLSEEDMATL 261
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
45-261 |
3.14e-17 |
|
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: 80.04 E-value: 3.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 45 ELGLALVRRALELGVNFLDTTDYnYSPDRA------ACANVLIRDAFspyqpnlVIATSIGLIRDDRNGI-RAATGAELR 117
Cdd:cd19148 25 KEAIETIHKALDLGINLIDTAPV-YGFGLSeeivgkALKEYGKRDRV-------VIATKVGLEWDEGGEVvRNSSPARIR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 118 WLVNEKLRQLRLDRLDLVILRLGETLPPHGESLAvrfdALAELREEGLIRHLGLSNADDRHLSEALQIAPVVAVQ---NL 194
Cdd:cd19148 97 KEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAE----ALKELLDEGKIRAIGVSNFSPEQMETFRKVAPLHTVQppyNL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 195 FHFGHQRDValLRRCEKHNIAYIPFLPLgCTG--------------------------------VTACTPLARIALRHH- 241
Cdd:cd19148 173 FEREIEKDV--LPYARKHNIVTLAYGAL-CRGllsgkmtkdtkfegddlrrtdpkfqeprfsqyLAAVEELDKLAQERYg 249
|
250 260
....*....|....*....|
gi 1028513208 242 TTVDQIALRWLLSVSPVTIV 261
Cdd:cd19148 250 KSVIHLAVRWLLDQPGVSIA 269
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-291 |
4.01e-17 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 80.00 E-value: 4.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 19 ELAVSRLGIGisrAACSGRHAAEQRRELGLALVRRALELGVNFLDTT-DYNyspdrAACANVLIRDAFSPYQPNLVIATS 97
Cdd:cd19104 9 GLKVSELTFG---GGGIGGLMGRTTREEQIAAVRRALDLGINFFDTApSYG-----DGKSEENLGRALKGLPAGPYITTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 98 IGLIRDDRNGIraatGAELRWLVNEKLRQLRLDRLDLVIL--RLG-ETLPPHGESLAVR--------FDALAELREEGLI 166
Cdd:cd19104 81 VRLDPDDLGDI----GGQIERSVEKSLKRLKRDSVDLLQLhnRIGdERDKPVGGTLSTTdvlglggvADAFERLRSEGKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 167 RHLGLSNADD-RHLSEALQIAPVVAVQ---NLFH----------FGHQRDVALLRRCEKHNIAYIPFLPLG----CTGV- 227
Cdd:cd19104 157 RFIGITGLGNpPAIRELLDSGKFDAVQvyyNLLNpsaaearprgWSAQDYGGIIDAAAEHGVGVMGIRVLAagalTTSLd 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 228 -------TACTPLAR----------IALRHHTTVDQIALRWLLSVSPVTIVAPQIGSVSRLEELVLCRDL-PLTAEDMAD 289
Cdd:cd19104 237 rgreappTSDSDVAIdfrraaafraLAREWGETLAQLAHRFALSNPGVSTVLVGVKNREELEEAVAAEAAgPLPAENLAR 316
|
..
gi 1028513208 290 LA 291
Cdd:cd19104 317 LE 318
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
17-286 |
7.08e-17 |
|
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: 78.75 E-value: 7.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 17 AGELAVSRLGIGISRAACSGRHAAEqrrelGLALVRRALELGVNFLDTTDY--NYSPD----RAACANVLIRDafspyqp 90
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADWGESAEE-----LLSLIEAALELGITTFDHADIygGGKCEelfgEALALNPGLRE------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 91 NLVIATSIGLIRDDRNGIRAA-----TGAELRWLVNEKLRQLRLDRLDLVILRLGETLPpHGESLAvrfDALAELREEGL 165
Cdd:cd19092 69 KIEIQTKCGIRLGDDPRPGRIkhydtSKEHILASVEGSLKRLGTDYLDLLLLHRPDPLM-DPEEVA---EAFDELVKSGK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 166 IRHLGLSNADDRHLsEALQIA---PVVAVQ---NLFHFGHQRDvALLRRCEKHNIAYIPFLPLG----CTGVTACTP--- 232
Cdd:cd19092 145 VRYFGVSNFTPSQI-ELLQSYldqPLVTNQielSLLHTEAIDD-GTLDYCQLLDITPMAWSPLGggrlFGGFDERFQrlr 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1028513208 233 --LARIALRHHTTVDQIALRWLLSvSPVTIVaPQIGS--VSRLEELVLCRDLPLTAED 286
Cdd:cd19092 223 aaLEELAEEYGVTIEAIALAWLLR-HPARIQ-PILGTtnPERIRSAVKALDIELTREE 278
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
120-291 |
1.70e-16 |
|
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: 77.29 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 120 VNEKLRQLRLDRLDLVIL------RLGETLPPHGESLAVRFDALAELREEGLIRHLGLSNADDRHLSEALQIAPVV-AV- 191
Cdd:cd19136 82 CLGSLERLGTDYLDLYLIhwpgvqGLKPSDPRNAELRRESWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYCEVPpAVn 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 192 QNLFH-FGHQRDvaLLRRCEKHNIAYIPFLPLGCTGVTACT--PLARIALRHHTTVDQIALRWLLSVSpvTIVAPQIGSV 268
Cdd:cd19136 162 QVEFHpHLVQKE--LLKFCKDHGIHLQAYSSLGSGDLRLLEdpTVLAIAKKYGRTPAQVLLRWALQQG--IGVIPKSTNP 237
|
170 180
....*....|....*....|...
gi 1028513208 269 SRLEELVLCRDLPLTAEDMADLA 291
Cdd:cd19136 238 ERIAENIKVFDFELSEEDMAELN 260
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
23-275 |
4.93e-16 |
|
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: 76.05 E-value: 4.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 23 SRLGIGisrAACSGRHAAEQRRELGLALVRRALELGVNFLDT-TDYNYSPDRaacanvlIRDAFSPYQPN-LVIATSIGL 100
Cdd:cd19090 1 SALGLG---TAGLGGVFGGVDDDEAVATIRAALDLGINYIDTaPAYGDSEER-------LGLALAELPREpLVLSTKVGR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 101 IRDDRNGIraaTGAELRWLVNEKLRQLRLDRLDLVILRLGETLPPHGE-SLAVRFDALAELREEGLIRHLGLSNADDRHL 179
Cdd:cd19090 71 LPEDTADY---SADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDIlAPGGALEALLELKEEGLIKHIGLGGGPPDLL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 180 SEALQIAPVVAVqnLFHFGH---QRDVA--LLRRCEKHNIAYIPFLPLGCTGVTACTP--------------------LA 234
Cdd:cd19090 148 RRAIETGDFDVV--LTANRYtllDQSAAdeLLPAAARHGVGVINASPLGMGLLAGRPPervrytyrwlspelldrakrLY 225
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1028513208 235 RIALRHHTTVDQIALRWLLSVSPVTIVAPQIGSVSRLEELV 275
Cdd:cd19090 226 ELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNV 266
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
22-290 |
6.50e-16 |
|
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: 76.33 E-value: 6.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 22 VSRLG---IGISraACSGRHAAEQRRelgLALVRRALELGVNFLDTTD-YNYSPD---RAACANVLIRDafspyqpNLVI 94
Cdd:cd19144 13 VPALGfgaMGLS--AFYGPPKPDEER---FAVLDAAFELGCTFWDTADiYGDSEEligRWFKQNPGKRE-------KIFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 95 ATSIGLIRDDRNGIRAATGAE--LRWLVNEKLRQLRLDRLDLVIL-RLGETLPphgesLAVRFDALAELREEGLIRHLGL 171
Cdd:cd19144 81 ATKFGIEKNVETGEYSVDGSPeyVKKACETSLKRLGVDYIDLYYQhRVDGKTP-----IEKTVAAMAELVQEGKIKHIGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 172 SNADDRHLSEALQIAPVVAVQ---NLFHFGHQR-DVALLRRCEKHNIAYIPFLPLG---CTG------------------ 226
Cdd:cd19144 156 SECSAETLRRAHAVHPIAAVQieySPFSLDIERpEIGVLDTCRELGVAIVAYSPLGrgfLTGairspddfeegdfrrmap 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1028513208 227 ----------VTACTPLARIALRHHTTVDQIALRWLLSVSPVTIVAPQIGSVSRLEELVLCRDLPLTAEDMADL 290
Cdd:cd19144 236 rfqaenfpknLELVDKIKAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLGALKVKLTEEEEKEI 309
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
22-290 |
1.30e-15 |
|
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: 75.34 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 22 VSRLGIGI----SRAacSGRHAAEQRRELgLALVRRALELGVNFLDTTD-YNYSPDRAACAnVLIRDafSPYQPNLVIAT 96
Cdd:cd19093 2 VSPLGLGTwqwgDRL--WWGYGEYGDEDL-QAAFDAALEAGVNLFDTAEvYGTGRSERLLG-RFLKE--LGDRDEVVIAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 97 SI-GLIRddRNGIRAATGAelrwlVNEKLRQLRLDRLDLVILRLGetlPPHGESLAVRFDALAELREEGLIRHLGLSNAD 175
Cdd:cd19093 76 KFaPLPW--RLTRRSVVKA-----LKASLERLGLDSIDLYQLHWP---GPWYSQIEALMDGLADAVEEGLVRAVGVSNYS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 176 DRHLSEALQI-----APVVAVQNLFHFGHqRDVA---LLRRCEKHNIAYIPFLPLG---CTGV-TACTP----------- 232
Cdd:cd19093 146 ADQLRRAHKAlkergVPLASNQVEYSLLY-RDPEqngLLPACDELGITLIAYSPLAqglLTGKySPENPppggrrrlfgr 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 233 ------------LARIALRHHTTVDQIALRWLLSVSPVTIvaPQIGSVSRLEELVLCRDLPLTAEDMADL 290
Cdd:cd19093 225 knlekvqplldaLEEIAEKYGKTPAQVALNWLIAKGVVPI--PGAKNAEQAEENAGALGWRLSEEEVAEL 292
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
122-288 |
1.50e-15 |
|
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: 74.40 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 122 EKLRQLRLDRLDLVILRLgetlpPHGESLAVRFDALAELREEGLIRHLGLSNADDRHLSEALQIAPVVAVQNLFHFgHQR 201
Cdd:cd19126 88 ESLDRLGLDYVDLYLIHW-----PGKDKFIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHADVVPAVNQVEF-HPY 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 202 DV--ALLRRCEKHNIAYIPFLPLGCTGVTACTPLARIALRHHTTVDQIALRWLLSVSPVTIvaPQIGSVSRLEELVLCRD 279
Cdd:cd19126 162 LTqkELRGYCKSKGIVVEAWSPLGQGGLLSNPVLAAIGEKYGKSAAQVVLRWDIQHGVVTI--PKSVHASRIKENADIFD 239
|
....*....
gi 1028513208 280 LPLTAEDMA 288
Cdd:cd19126 240 FELSEDDMT 248
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
122-291 |
1.07e-14 |
|
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: 72.02 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 122 EKLRQLRLDRLDLVILRLgetlPPHGESLAVR-FDALAELREEGLIRHLGLSNADDRHLSEALQIAPVVAVQN---LFHF 197
Cdd:cd19131 88 ESLRKLGLDYVDLYLIHW----PVPAQDKYVEtWKALIELKKEGRVKSIGVSNFTIEHLQRLIDETGVVPVVNqieLHPR 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 198 GHQRdvALLRRCEKHNIAYIPFLPLGCTGVTACTPLARIALRHHTTVDQIALRWLLSVSpvTIVAPQIGSVSRLEELVLC 277
Cdd:cd19131 164 FQQR--ELRAFHAKHGIQTESWSPLGQGGLLSDPVIGEIAEKHGKTPAQVVIRWHLQNG--LVVIPKSVTPSRIAENFDV 239
|
170
....*....|....
gi 1028513208 278 RDLPLTAEDMADLA 291
Cdd:cd19131 240 FDFELDADDMQAIA 253
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
18-290 |
1.17e-14 |
|
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: 72.66 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 18 GELAVSRLGIGISRAacSGRHAAEQRRElGLALVRRALELGVNFLDTTDYnYSPDRAAcANV-LIRDAFSPYQPN---LV 93
Cdd:cd19077 1 NGKLVGPIGLGLMGL--TWRPNPTPDEE-AFETMKAALDAGSNLWNGGEF-YGPPDPH-ANLkLLARFFRKYPEYadkVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 94 IATSIGLIRDDrnGIRAATGAELRWLVNEKLRQLR-LDRLDLVIL-RLGETLPPhgeslAVRFDALAELREEGLIRHLGL 171
Cdd:cd19077 76 LSVKGGLDPDT--LRPDGSPEAVRKSIENILRALGgTKKIDIFEPaRVDPNVPI-----EETIKALKELVKEGKIRGIGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 172 SNADDRHLSEALQIAPVVAVQNLFHFGhQRDVA---LLRRCEKHNIAYIPFLPLG---CTG------------------- 226
Cdd:cd19077 149 SEVSAETIRRAHAVHPIAAVEVEYSLF-SREIEengVLETCAELGIPIIAYSPLGrglLTGriksladipegdfrrhldr 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1028513208 227 ------------VTActpLARIALRHHTTVDQIALRWLLSVSPVTIVA-PQIGSVSRLEELVLCRDLPLTAEDMADL 290
Cdd:cd19077 228 fngenfeknlklVDA---LQELAEKKGCTPAQLALAWILAQSGPKIIPiPGSTTLERVEENLKAANVELTDEELKEI 301
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
47-291 |
1.44e-14 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381380 [Multi-domain] Cd Length: 303 Bit Score: 72.44 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 47 GLALVRRALELGVNFLDTTdYNYSPDRAacanvlIRDAFSPY-------QPNLVIATSIGLIRDDRNGIRAAtgaelrwl 119
Cdd:cd19154 27 GITAVRTALKAGYRLIDTA-FLYQNEEA------IGEALAELleegvvkREDLFITTKLWTHEHAPEDVEEA-------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 120 VNEKLRQLRLDRLDLVILRL--------GETLPP-HGESLAVRFD------ALAELREEGLIRHLGLSNADDRHLSEALQ 184
Cdd:cd19154 92 LRESLKKLQLEYVDLYLIHApaafkddeGESGTMeNGMSIHDAVDvedvwrGMEKVYDEGLTKAIGVSNFNNDQIQRILD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 185 IA--PVVAVQNLFH--FGHQRDVALlrrCEKHNIAYIPFLPLGCTGVTACTP---------------LARIALRHHTTVD 245
Cdd:cd19154 172 NArvKPHNNQVECHlyFPQKELVEF---CKKHNISVTSYATLGSPGRANFTKstgvspapnllqdpiVKAIAEKHGKTPA 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1028513208 246 QIALRWLLSVSPVTIvaPQIGSVSRLEELVLCRDLPLTAEDMADLA 291
Cdd:cd19154 249 QVLLRYLLQRGIAVI--PKSATPSRIKENFNIFDFSLSEEDMATLE 292
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
23-274 |
2.10e-14 |
|
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: 71.44 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 23 SRLGIGISRAACSGRHAAEQrrELGLALVRRALELGVNFLDTTdYNYSPDRA--ACANVLI---RDAFspyqpnlVIATS 97
Cdd:cd19096 1 SVLGFGTMRLPESDDDSIDE--EKAIEMIRYAIDAGINYFDTA-YGYGGGKSeeILGEALKegpREKF-------YLATK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 98 IGLIRDDrngiraaTGAELRWLVNEKLRQLRLDRLDLVILrlgetlppHG------ESLAVRFDALA---ELREEGLIRH 168
Cdd:cd19096 71 LPPWSVK-------SAEDFRRILEESLKRLGVDYIDFYLL--------HGlnspewLEKARKGGLLEfleKAKKEGLIRH 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 169 LGLS---NADDrhLSEALQIAPVVAVQ---NLFHFGHQRDVALLRRCEKHNIAYIPFLPLGcTGVTACTP--LARIALRH 240
Cdd:cd19096 136 IGFSfhdSPEL--LKEILDSYDFDFVQlqyNYLDQENQAGRPGIEYAAKKGMGVIIMEPLK-GGGLANNPpeALAILCGA 212
|
250 260 270
....*....|....*....|....*....|....
gi 1028513208 241 HTTVDQIALRWLLSVSPVTIVapqIGSVSRLEEL 274
Cdd:cd19096 213 PLSPAEWALRFLLSHPEVTTV---LSGMSTPEQL 243
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
122-291 |
3.08e-14 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 70.82 E-value: 3.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 122 EKLRQLRLDRLDLvilrlgeTL-----PPHGESLAVRFDALAELREEGLIRHLGLSNADDRHLSEALQI--APVVAVQNL 194
Cdd:PRK11172 81 ESLQKLRTDYVDL-------TLihwpsPNDEVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQAIAAvgAENIATNQI 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 195 FHFGHQRDVALLRRCEKHNIAYIPFLPLGCTGVTACTPLARIALRHHTTVDQIALRWLL----SVSPvtivapqigSVSR 270
Cdd:PRK11172 154 ELSPYLQNRKVVAFAKEHGIHVTSYMTLAYGKVLKDPVIARIAAKHNATPAQVILAWAMqlgySVIP---------SSTK 224
|
170 180
....*....|....*....|....
gi 1028513208 271 LEEL---VLCRDLPLTAEDMADLA 291
Cdd:PRK11172 225 RENLasnLLAQDLQLDAEDMAAIA 248
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
122-288 |
3.48e-14 |
|
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: 71.01 E-value: 3.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 122 EKLRQLRLDRLDLVILRLgetlpPHGESLAVRFDALAELREEGLIRHLGLSNADDRHLSEAL---QIAPVVAVQNLFHFG 198
Cdd:cd19156 88 ESLEKLGLDYVDLYLIHW-----PVKGKFKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLkscKVAPMVNQIELHPLL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 199 HQRDvaLLRRCEKHNIAYIPFLPLGCTGVTACTPLARIALRHHTTVDQIALRWLLSVSPVTIvaPQIGSVSRLEELVLCR 278
Cdd:cd19156 163 TQEP--LRKFCKEKNIAVEAWSPLGQGKLLSNPVLKAIGKKYGKSAAQVIIRWDIQHGIITI--PKSVHEERIQENFDVF 238
|
170
....*....|
gi 1028513208 279 DLPLTAEDMA 288
Cdd:cd19156 239 DFELTAEEIR 248
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
50-290 |
4.09e-14 |
|
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: 71.11 E-value: 4.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 50 LVRRALELGVNFLDTTDYnYSPDRAacaNVLIRDAFSPYQPNLVIATSIGL-IRDDRNGIRAATGAELRwLVNEKLRQLR 128
Cdd:cd19091 44 LVDIALDAGINFFDTADV-YSEGES---EEILGKALKGRRDDVLIATKVRGrMGEGPNDVGLSRHHIIR-AVEASLKRLG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 129 LDRLDLVILRLGETLPPHGESLAvrfdALAELREEGLIRHLGLSNADDRHLSEALQIA------PVVAVQ---NLFhfgh 199
Cdd:cd19091 119 TDYIDLYQLHGFDALTPLEETLR----ALDDLVRQGKVRYIGVSNFSAWQIMKALGISerrglaRFVALQayySLL---- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 200 QRDV--ALLRRCEKHNIAYIPFLPLG---CTG-VTACTP----------------------------LARIALRHHTTVD 245
Cdd:cd19091 191 GRDLehELMPLALDQGVGLLVWSPLAgglLSGkYRRGQPapegsrlrrtgfdfppvdrergydvvdaLREIAKETGATPA 270
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1028513208 246 QIALRWLLSVSPVTIVApqIG--SVSRLEELVLCRDLPLTAEDMADL 290
Cdd:cd19091 271 QVALAWLLSRPTVSSVI--IGarNEEQLEDNLGAAGLSLTPEEIARL 315
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
53-289 |
4.23e-14 |
|
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: 71.44 E-value: 4.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 53 RALELGVNFLDTTDyNY----SPDRAACANVLI---------RDafspyqpNLVIATSI----GLIRDDRNGIRAATGAE 115
Cdd:cd19094 26 YAFDEGVNFIDTAE-MYpvppSPETQGRTEEIIgswlkkkgnRD-------KVVLATKVagpgEGITWPRGGGTRLDREN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 116 LRWLVNEKLRQLRLDRLDLV----------ILRLGETLPPHGESLAVRF----DALAELREEGLIRHLGLSNADDRHLSE 181
Cdd:cd19094 98 IREAVEGSLKRLGTDYIDLYqlhwpdrytpLFGGGYYTEPSEEEDSVSFeeqlEALGELVKAGKIRHIGLSNETPWGVMK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 182 ALQIA------PVVAVQNLFHFGHQR-DVALLRRCEKHNIAYIPFLPLG---CTG------------------------- 226
Cdd:cd19094 178 FLELAeqlglpRIVSIQNPYSLLNRNfEEGLAEACHRENVGLLAYSPLAggvLTGkyldgaarpeggrlnlfpgymaryr 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1028513208 227 ----VTACTPLARIALRHHTTVDQIALRWLLSVSPV--TIvapqIG--SVSRLEELVLCRDLPLTAEDMAD 289
Cdd:cd19094 258 spqaLEAVAEYVKLARKHGLSPAQLALAWVRSRPFVtsTI----IGatTLEQLKENIDAFDVPLSDELLAE 324
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
20-290 |
5.28e-14 |
|
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381371 [Multi-domain] Cd Length: 304 Bit Score: 70.92 E-value: 5.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 20 LAVSRLGIGisraaC---SGRHAAEQRRELGLALVRRALELGVNFLDTTDYnYSPDraacAN-VLIRDAF-SPYQPNLVI 94
Cdd:cd19145 10 LEVSAQGLG-----CmglSGDYGAPKPEEEGIALIHHAFNSGVTFLDTSDI-YGPN----TNeVLLGKALkDGPREKVQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 95 ATSIGlIRDDRNGIRAATG--AELRWLVNEKLRQLRLDRLDLV-ILRLGETLPphgesLAVRFDALAELREEGLIRHLGL 171
Cdd:cd19145 80 ATKFG-IHEIGGSGVEVRGdpAYVRAACEASLKRLDVDYIDLYyQHRIDTTVP-----IEITMGELKKLVEEGKIKYIGL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 172 SNADDRHLSEALQIAPVVAVQ---NLFhfghQRDVA--LLRRCEKHNIAYIPFLPLGcTGVTACTP-------------- 232
Cdd:cd19145 154 SEASADTIRRAHAVHPITAVQlewSLW----TRDIEeeIIPTCRELGIGIVPYSPLG-RGFFAGKAkleellensdvrks 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 233 ------------------LARIALRHHTTVDQIALRWLL----SVSPVtivaPQIGSVSRLEELVLCRDLPLTAEDMADL 290
Cdd:cd19145 229 hprfqgenleknkvlyerVEALAKKKGCTPAQLALAWVLhqgeDVVPI----PGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
124-291 |
8.80e-14 |
|
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: 70.13 E-value: 8.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 124 LRQLRLDRLDL------VILRLGETLPPHGES--------LAVRFDALAELREEGLIRHLGLSNADDRHLSEAL---QIA 186
Cdd:cd19123 96 LADLQLDYLDLylmhwpVALKKGVGFPESGEDllslspipLEDTWRAMEELVDKGLCRHIGVSNFSVKKLEDLLataRIK 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 187 PVVAVQNLFHFGHQRDvaLLRRCEKHNIAYIPFLPLGCTGVTACTP------------LARIALRHHTTVDQIALRWLLS 254
Cdd:cd19123 176 PAVNQVELHPYLQQPE--LLAFCRDNGIHLTAYSPLGSGDRPAAMKaegepvlledpvINKIAEKHGASPAQVLIAWAIQ 253
|
170 180 190
....*....|....*....|....*....|....*..
gi 1028513208 255 VSpvTIVAPQIGSVSRLEELVLCRDLPLTAEDMADLA 291
Cdd:cd19123 254 RG--TVVIPKSVNPERIQQNLEAAEVELDASDMATIA 288
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
47-291 |
1.31e-13 |
|
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: 68.84 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 47 GLALVRRALELGVNFLDTTdYNYSPDRAAcaNVLIRDAFSPYQpNLVIATSIgliRDDRNGIRAATGAelrwlVNEKLRQ 126
Cdd:cd19132 22 GVEAVVAALQAGYRLLDTA-FNYENEGAV--GEAVRRSGVPRE-ELFVTTKL---PGRHHGYEEALRT-----IEESLYR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 127 LRLDRLDLVILRLgetlPPHGESLAVR-FDALAELREEGLIRHLGLSNADDRHLSEALQ---IAPVVAvQNLFHFGHQRD 202
Cdd:cd19132 90 LGLDYVDLYLIHW----PNPSRDLYVEaWQALIEAREEGLVRSIGVSNFLPEHLDRLIDetgVTPAVN-QIELHPYFPQA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 203 vALLRRCEKHNIAYIPFLPLG-CTGVTACTPLARIALRHHTTVDQIALRWL--LSVSPVtivaPQIGSVSRLEELVLCRD 279
Cdd:cd19132 165 -EQRAYHREHGIVTQSWSPLGrGSGLLDEPVIKAIAEKHGKTPAQVVLRWHvqLGVVPI----PKSANPERQRENLAIFD 239
|
250
....*....|..
gi 1028513208 280 LPLTAEDMADLA 291
Cdd:cd19132 240 FELSDEDMAAIA 251
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
105-290 |
7.56e-13 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 67.23 E-value: 7.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 105 RNGIRAATGAELRWLVNEKLRQLRLDRLDLVILrlgetlppHGESLAVR-----FDALAELREEGLIRHLGLSNADDRHL 179
Cdd:cd19101 79 DPGELTMTRAYVEAAIDRSLKRLGVDRLDLVQF--------HWWDYSDPgyldaAKHLAELQEEGKIRHLGLTNFDTERL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 180 SEALQI-APVVAVQNLFHFGHQR-DVALLRRCEKHNIAYIPFLPLG-------------CTGVTACTP------------ 232
Cdd:cd19101 151 REILDAgVPIVSNQVQYSLLDRRpENGMAALCEDHGIKLLAYGTLAggllsekylgvpePTGPALETRslqkyklmidew 230
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1028513208 233 ------------LARIALRHHTTVDQIALRWLLSvspvtivAPQIGSV-------SRLEELVLCRDLPLTAEDMADL 290
Cdd:cd19101 231 ggwdlfqellrtLKAIADKHGVSIANVAVRWVLD-------QPGVAGVivgarnsEHIDDNVRAFSFRLDDEDRAAI 300
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
124-287 |
9.42e-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: 67.13 E-value: 9.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 124 LRQLRLDRLDLVILR---------LGETLPPHGE----------SLAVRFDALAELREEGLIRHLGLSNAD---DRHLSE 181
Cdd:cd19112 93 LKKLQLDYLDLYLVHfpvatkhtgVGTTGSALGEdgvldidvtiSLETTWHAMEKLVSAGLVRSIGISNYDiflTRDCLA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 182 ALQIAPVVAvQNLFHFGHQRDvALLRRCEKHNIAYIPFLPLGCT-------GVTACTP---LARIALRHHTTVDQIALRW 251
Cdd:cd19112 173 YSKIKPAVN-QIETHPYFQRD-SLVKFCQKHGISVTAHTPLGGAaanaewfGSVSPLDdpvLKDLAKKYGKSAAQIVLRW 250
|
170 180 190
....*....|....*....|....*....|....*.
gi 1028513208 252 llSVSPVTIVAPQIGSVSRLEELVLCRDLPLTAEDM 287
Cdd:cd19112 251 --GIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDM 284
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
121-288 |
1.31e-12 |
|
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: 66.26 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 121 NEKLRQLRLDRLDLVILRLgetlpPHGESLAVRFDALAELREEGLIRHLGLSNADDRHLSEALQIAPVVAVQNLFHFgHQ 200
Cdd:cd19157 88 EASLERLGLDYLDLYLIHW-----PVKGKYKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAEIVPMVNQVEF-HP 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 201 RDV--ALLRRCEKHNIAYIPFLPLGCTGVTACTPLARIALRHHTTVDQIALRWLLSVSPVTIvaPQIGSVSRLEELVLCR 278
Cdd:cd19157 162 RLTqkELRDYCKKQGIQLEAWSPLMQGQLLDNPVLKEIAEKYNKSVAQVILRWDLQNGVVTI--PKSIKEHRIIENADVF 239
|
170
....*....|
gi 1028513208 279 DLPLTAEDMA 288
Cdd:cd19157 240 DFELSQEDMD 249
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
124-287 |
1.89e-12 |
|
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: 66.25 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 124 LRQLRLDRLDLVIL------RLGETLPPHGESLAVRFD---------ALAELREEGLIRHLGLSNADDRHLSEALQIA-- 186
Cdd:cd19106 92 LKDLQLDYLDLYLIhwpyafERGDNPFPKNPDGTIRYDsthyketwkAMEKLVDKGLVKAIGLSNFNSRQIDDILSVAri 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 187 -PVV-AVQNLFHFGHQRdvaLLRRCEKHNIAYIPFLPLGCTGVTACTP----------LARIALRHHTTVDQIALRWLLS 254
Cdd:cd19106 172 kPAVlQVECHPYLAQNE---LIAHCKARGLVVTAYSPLGSPDRPWAKPdepvlleepkVKALAKKYNKSPAQILLRWQVQ 248
|
170 180 190
....*....|....*....|....*....|...
gi 1028513208 255 VSPVTIvaPQIGSVSRLEELVLCRDLPLTAEDM 287
Cdd:cd19106 249 RGVVVI--PKSVTPSRIKQNIQVFDFTLSPEEM 279
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
20-261 |
4.58e-12 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 65.42 E-value: 4.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 20 LAVSRLGIGISRAACSGRHAAEQRRelglaLVRRALELGVNFLDTTDyNYSP-----------DRAACANVLIRDafspy 88
Cdd:cd19099 1 LTLSSLGLGTYRGDSDDETDEEYRE-----ALKAALDSGINVIDTAI-NYRGgrserligkalRELIEKGGIKRD----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 89 qpNLVIATSIGLIRDD----------------RNGIRAATGAE---------LRWLVNEKLRQLRLDRLDLVILRLGET- 142
Cdd:cd19099 70 --EVVIVTKAGYIPGDgdeplrplkyleeklgRGLIDVADSAGlrhcispayLEDQIERSLKRLGLDTIDLYLLHNPEEq 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 143 LPPHGES-----LAVRFDALAELREEGLIRHLGLSN--------ADDRHLS-EALQIAPVVAVQNLFHF----------- 197
Cdd:cd19099 148 LLELGEEefydrLEEAFEALEEAVAEGKIRYYGISTwdgfrappALPGHLSlEKLVAAAEEVGGDNHHFkviqlplnlle 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1028513208 198 ---------GHQRDVALLRRCEKHNIAYI---PFLPLGCTGVTActPLARIALRHHTTVDQIALRWLLSVSPVTIV 261
Cdd:cd19099 228 pealtekntVKGEALSLLEAAKELGLGVIasrPLNQGQLLGELR--LADLLALPGGATLAQRALQFARSTPGVDSA 301
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
122-290 |
5.17e-12 |
|
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a founding member of aldo-keto reductase family 2 member E4 (AKR2E4). It is a NADP-dependent oxidoreductase with high 3-dehydroecdysone reductase activity. It may play a role in the regulation of molting and has lower activity with phenylglyoxal and isatin (in vitro). This family also includes 3-dehydroecdysone 3b-reductase from Spodoptera littoralis and Trichoplusia ni, DL-glyceraldehyde reductase from Drosophila melanogaster, aldo-keto reductase from Bombyx mori, which correspond to aldo-keto reductase family 2 member E1, E2, E3 and E5 (AKR2E1/2/3/5), respectively.
Pssm-ID: 381342 [Multi-domain] Cd Length: 292 Bit Score: 65.00 E-value: 5.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 122 EKLRQLRLDRLDLVILRLGETLPPHGESLA------VRFD------ALAELREEGLIRHLGLSNADDRHLSEALQ---IA 186
Cdd:cd19116 94 ESLKRLGLDYVDLYLIHWPVAFKENNDSESngdgslSDIDyletwrGMEDLVKLGLTRSIGVSNFNSEQINRLLSncnIK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 187 PVVaVQNLFHFGHQRDvALLRRCEKHNIAYIPFLPLG--------CTGVTACTP-LARIALRHHTTVDQIALRWLLSVSP 257
Cdd:cd19116 174 PAV-NQIEVHPTLTQE-KLVAYCQSNGIVVMAYSPFGrlvprgqtNPPPRLDDPtLVAIAKKYGKTTAQIVLRYLIDRGV 251
|
170 180 190
....*....|....*....|....*....|...
gi 1028513208 258 VTIvaPQIGSVSRLEELVLCRDLPLTAEDMADL 290
Cdd:cd19116 252 VPI--PKSSNKKRIKENIDIFDFQLTPEEVAAL 282
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
51-290 |
3.80e-11 |
|
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381381 [Multi-domain] Cd Length: 307 Bit Score: 62.54 E-value: 3.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 51 VRRALELGVNFLDTTdYNYSpDRAACANVLIR--DAFSPYQPNLVIATSIglirdDRNGIRAAtgaELRWLVNEKLRQLR 128
Cdd:cd19155 31 VDTALEAGYRHIDTA-YVYR-NEAAIGNVLKKwiDSGKVKREELFIVTKL-----PPGGNRRE---KVEKFLLKSLEKLQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 129 LDRLDLVILRL-----------------GETLPPHGESLAVRFDALAELREEGLIRHLGLSNADDRHLSEALQIAPVVAV 191
Cdd:cd19155 101 LDYVDLYLIHFpvgslskeddsgkldptGEHKQDYTTDLLDIWKAMEAQVDQGLTRSIGLSNFNREQMARILKNARIKPA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 192 QN---LFHFGHQRDvaLLRRCEKHNIAYIPFLPLGCTGVTACTP-----------------LARIALRHHTTVDQIALRW 251
Cdd:cd19155 181 NLqveLHVYLQQKD--LVDFCSTHSITVTAYAPLGSPGAAHFSPgtgspsgsspdllqdpvVKAIAERHGKSPAQVLLRW 258
|
250 260 270
....*....|....*....|....*....|....*....
gi 1028513208 252 LLSVSPVTIvaPQIGSVSRLEELVLCRDLPLTAEDMADL 290
Cdd:cd19155 259 LMQRGVVVI--PKSTNAARIKENFQVFDFELTEADMAKL 295
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
124-291 |
4.06e-11 |
|
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: 61.82 E-value: 4.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 124 LRQLRLDRLDLVILRlgetlPPHGESLAVrFDALAELREEGLIRHLGLSNADDRHLSEAL---QIAPVVAvQNLFHFGHQ 200
Cdd:cd19133 90 LKRLGLDYLDLYLIH-----QPFGDVYGA-WRAMEELYKEGKIRAIGVSNFYPDRLVDLIlhnEVKPAVN-QIETHPFNQ 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 201 RdVALLRRCEKHNIAYIPFLPL--GCTGVTACTPLARIALRHHTTVDQIALRWLLSVSPVTIvaPQIGSVSRLEELVLCR 278
Cdd:cd19133 163 Q-IEAVEFLKKYGVQIEAWGPFaeGRNNLFENPVLTEIAEKYGKSVAQVILRWLIQRGIVVI--PKSVRPERIAENFDIF 239
|
170
....*....|...
gi 1028513208 279 DLPLTAEDMADLA 291
Cdd:cd19133 240 DFELSDEDMEAIA 252
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
122-287 |
4.53e-11 |
|
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: 62.16 E-value: 4.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 122 EKLRQLRLDRLDLVIL------RLGETLPPH---------GESLAVRFDALAELREEGLIRHLGLSNADDRHLSEALQIA 186
Cdd:cd19128 83 ITLQDLQLEYLDLFLIhwplafDMDTDGDPRddnqiqslsKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLNYC 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 187 PVVAVQNLF--HFGHQRDvALLRRCEKHNIAYIPFLPLG------CTGVTACTPLARIALRHHTTVDQIALRWLLSVSPV 258
Cdd:cd19128 163 KIKPFMNQIecHPYFQND-KLIKFCIENNIHVTAYRPLGgsygdgNLTFLNDSELKALATKYNTTPPQVIIAWHLQKWPK 241
|
170 180 190
....*....|....*....|....*....|
gi 1028513208 259 T-IVAPQIGSVSRLEELVLCRDLPLTAEDM 287
Cdd:cd19128 242 NySVIPKSANKSRCQQNFDINDLALTKEDM 271
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
120-291 |
4.81e-11 |
|
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: 61.98 E-value: 4.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 120 VNEKLRQLRLDRLDL------VILRLGETLPPHGESLAVRFD----ALAELREEGLIRHLGLSNADDRHLSEALQIAPVV 189
Cdd:cd19125 91 LEKTLKDLQLDYLDLylihwpVRLKKGAHMPEPEEVLPPDIPstwkAMEKLVDSGKVRAIGVSNFSVKKLEDLLAVARVP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 190 -AV-QNLFHFGHQRDVaLLRRCEKHNIAYIPFLPLGCTGvtacTPLARIALRHHTTVD-----------QIALRWLLSVS 256
Cdd:cd19125 171 pAVnQVECHPGWQQDK-LHEFCKSKGIHLSAYSPLGSPG----TTWVKKNVLKDPIVTkvaeklgktpaQVALRWGLQRG 245
|
170 180 190
....*....|....*....|....*....|....*
gi 1028513208 257 pvTIVAPQIGSVSRLEELVLCRDLPLTAEDMADLA 291
Cdd:cd19125 246 --TSVLPKSTNEERIKENIDVFDWSIPEEDFAKFS 278
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
122-290 |
2.55e-10 |
|
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: 59.82 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 122 EKLRQLRLDRLDLVIL--------RLGETLPPHGESLAVR-FDALAELREEGLIRHLGLSNADDRHLSEALQIApVVAVQ 192
Cdd:cd19111 86 KSLENLKLPYVDLYLIhhpcgfvnKKDKGERELASSDVTSvWRAMEALVSEGKVKSIGLSNFNPRQINKILAYA-KVKPS 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 193 NL---FH-FGHQRDvaLLRRCEKHNIAYIPFLPLGCTG---VTACTPLA---------RIALRHHTTVDQIALRWLLSVS 256
Cdd:cd19111 165 NLqleCHaYLQQRE--LRKFCNKKNIVVTAYAPLGSPGranQSLWPDQPdlledptvlAIAKELDKTPAQVLLRFVLQRG 242
|
170 180 190
....*....|....*....|....*....|....
gi 1028513208 257 pvTIVAPQIGSVSRLEELVLCRDLPLTAEDMADL 290
Cdd:cd19111 243 --TGVLPKSTNKERIEENFEVFDFELTEEHFKKL 274
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
124-290 |
1.65e-09 |
|
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: 57.66 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 124 LRQLRLDRLDLVIL----------------RLGETLPPHGESLAVrFDALAELREEGLIRHLGLSNADDRHLSE-----A 182
Cdd:cd19110 88 LKALKLNYLDLYLIhwpmgfkpgepdlpldRSGMVIPSDTDFLDT-WEAMEDLVIEGLVKNIGVSNFNHEQLERllnkpG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 183 LQIAPVVAVQNLFHFGHQRDvaLLRRCEKHNIAYIPFLPLG--CTGVTAC--TPLARIALRHHTTVDQIALRWLLSVSpv 258
Cdd:cd19110 167 LRVKPVTNQIECHPYLTQKK--LISFCQSRNVSVTAYRPLGgsCEGVDLIddPVIQRIAKKHGKSPAQILIRFQIQRN-- 242
|
170 180 190
....*....|....*....|....*....|..
gi 1028513208 259 TIVAPQIGSVSRLEELVLCRDLPLTAEDMADL 290
Cdd:cd19110 243 VIVIPKSVTPSRIKENIQVFDFELTEHDMDNL 274
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
45-275 |
1.76e-09 |
|
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: 57.60 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 45 ELGLALVRRALELGVNFLDTTDyNYSpdrAACANVLIRDAFSPYQ-PNLVIATSiglirddrngIRAATGAE-------- 115
Cdd:cd19074 22 EDAKACVRKAYDLGINFFDTAD-VYA---AGQAEEVLGKALKGWPrESYVISTK----------VFWPTGPGpndrglsr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 116 --LRWLVNEKLRQLRLDRLDLVILR-------LGETLpphgeslavrfDALAELREEGLIRHLGLSNADDRHLSEALQIA 186
Cdd:cd19074 88 khIFESIHASLKRLQLDYVDIYYCHrydpetpLEETV-----------RAMDDLIRQGKILYWGTSEWSAEQIAEAHDLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 187 ------PVVAVQNLFH-FGHQRDVALLRRCEKHNIAYIPFLPLGC---TG------------------------------ 226
Cdd:cd19074 157 rqfgliPPVVEQPQYNmLWREIEEEVIPLCEKNGIGLVVWSPLAQgllTGkyrdgipppsrsratdednrdkkrrlltde 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1028513208 227 -VTACTPLARIALRHHTTVDQIALRWLLSVSPVTivAPQIGSvSRLEELV 275
Cdd:cd19074 237 nLEKVKKLKPIADELGLTLAQLALAWCLRNPAVS--SAIIGA-SRPEQLE 283
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
51-291 |
3.90e-09 |
|
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: 56.07 E-value: 3.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 51 VRRALELGVNFLDTTDYnYSPD----RAACANVLIRDafspyqpNLVIATSIGLIRDDRNGIRAATGaelrwlvnEKLRQ 126
Cdd:cd19130 29 VATALEVGYRHIDTAAI-YGNEegvgAAIAASGIPRD-------ELFVTTKLWNDRHDGDEPAAAFA--------ESLAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 127 LRLDRLDLVILRLgeTLPPHGESLAVrFDALAELREEGLIRHLGLSNADDRHLSEALQIAPVVAVQN---LFHFGHQRDV 203
Cdd:cd19130 93 LGLDQVDLYLVHW--PTPAAGNYVHT-WEAMIELRAAGRTRSIGVSNFLPPHLERIVAATGVVPAVNqieLHPAYQQRTI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 204 AllRRCEKHNIAYIPFLPLGCTGVTACTPLARIALRHHTTVDQIALRWLLSVSPVtiVAPQIGSVSRLEELVLCRDLPLT 283
Cdd:cd19130 170 R--DWAQAHDVKIEAWSPLGQGKLLGDPPVGAIAAAHGKTPAQIVLRWHLQKGHV--VFPKSVRRERMEDNLDVFDFDLT 245
|
....*...
gi 1028513208 284 AEDMADLA 291
Cdd:cd19130 246 DTEIAAID 253
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
44-290 |
4.01e-09 |
|
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: 56.43 E-value: 4.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 44 RELGLALVRRALELGVNFLDTTDyNYSPDRaacANVLIRDAFSPYQPNLVIATSIGLIRDDRNGIRaatGAELRWLVN-- 121
Cdd:cd19087 29 EETSFAIMDRALDAGINFFDTAD-VYGGGR---SEEIIGRWIAGRRDDIVLATKVFGPMGDDPNDR---GLSRRHIRRav 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 122 -EKLRQLRLDRLDLVIL-------RLGETLpphgeslavrfDALAELREEGLIRHLGLSN------ADDRHLSEALQIAP 187
Cdd:cd19087 102 eASLRRLQTDYIDLYQMhhfdrdtPLEETL-----------RALDDLVRQGKIRYIGVSNfaawqiAKAQGIAARRGLLR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 188 VVAVQNLFHF-GHQRDVALLRRCEKHNIAYIPFLPLG----------------CTGVTACTPLARIALRHHTTVDQ---- 246
Cdd:cd19087 171 FVSEQPMYNLlKRQAELEILPAARAYGLGVIPYSPLAgglltgkygkgkrpesGRLVERARYQARYGLEEYRDIAErfea 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1028513208 247 -----------IALRWLLSVSPVTivAPQIG--SVSRLEELVLCRDLPLTAEDMADL 290
Cdd:cd19087 251 laaeagltpasLALAWVLSHPAVT--SPIIGprTLEQLEDSLAALEITLTPELLAEI 305
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
49-195 |
6.66e-09 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 55.61 E-value: 6.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 49 ALVRRALELGVNFLDT-TDYNYSPDRaacanvlIRDAFSPYQpNLVIATSIGLIRDDRNGIRAATGAElrwlVNEKLRQL 127
Cdd:cd19097 30 KILEYALKAGINTLDTaPAYGDSEKV-------LGKFLKRLD-KFKIITKLPPLKEDKKEDEAAIEAS----VEASLKRL 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1028513208 128 RLDRLDLVILRLGETLPPHGESLavrFDALAELREEGLIRHLGLSNADDRHLSEALQIAPVVAVQ---NLF 195
Cdd:cd19097 98 KVDSLDGLLLHNPDDLLKHGGKL---VEALLELKKEGLIRKIGVSVYSPEELEKALESFKIDIIQlpfNIL 165
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
122-254 |
1.34e-08 |
|
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: 54.58 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 122 EKLRQLRLDRLDL------VILRLGETLPPHGESLAVRFD------ALAELREEGLIRHLGLSNADDRHLSEALQIA--P 187
Cdd:cd19124 90 KSLRNLQLEYVDLylihwpVSLKPGKFSFPIEEEDFLPFDikgvweAMEECQRLGLTKAIGVSNFSCKKLQELLSFAtiP 169
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1028513208 188 VVAVQNLFHFGHQ----RDVallrrCEKHNIAYIPFLPLGCTG-------VTACTPLARIALRHHTTVDQIALRWLLS 254
Cdd:cd19124 170 PAVNQVEMNPAWQqkklREF-----CKANGIHVTAYSPLGAPGtkwgsnaVMESDVLKEIAAAKGKTVAQVSLRWVYE 242
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
124-290 |
1.47e-08 |
|
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: 54.48 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 124 LRQLRLDRLDLVILRLgeTLPPHGESLAVrFDALAELREEGLIRHLGLSNADDRHLSEALQIAPVVAVQNLFHFGHQRDV 203
Cdd:cd19134 91 LERLGLDYVDLYLIHW--PAGREGKYVDS-WGGLMKLREEGLARSIGVSNFTAEHLENLIDLTFFTPAVNQIELHPLLNQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 204 ALLRRCE-KHNIAYIPFLPLGCTGVTACTPLARIALRHHTTVDQIALRWLLSVSPVTIvaPQIGSVSRLEELVLCRDLPL 282
Cdd:cd19134 168 AELRKVNaQHGIVTQAYSPLGVGRLLDNPAVTAIAAAHGRTPAQVLLRWSLQLGNVVI--SRSSNPERIASNLDVFDFEL 245
|
....*...
gi 1028513208 283 TAEDMADL 290
Cdd:cd19134 246 TADHMDAL 253
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
122-291 |
3.49e-08 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 53.54 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 122 EKLRQLRLDRLDLVILRLgetlP-PHGESLAVRFDALAELREEGLIRHLGLSNADDRHLSEALQ---IAPVVAVQNLFHF 197
Cdd:PRK11565 91 ESLKKLQLDYVDLYLMHW----PvPAIDHYVEAWKGMIELQKEGLIKSIGVCNFQIHHLQRLIDetgVTPVINQIELHPL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 198 GHQRDVALLRrcEKHNIAYIPFLPL--GCTGVTACTPLARIALRHHTTVDQIALRWLLSVSPVTIvaPQIGSVSRLEELV 275
Cdd:PRK11565 167 MQQRQLHAWN--ATHKIQTESWSPLaqGGKGVFDQKVIRDLADKYGKTPAQIVIRWHLDSGLVVI--PKSVTPSRIAENF 242
|
170
....*....|....*.
gi 1028513208 276 LCRDLPLTAEDMADLA 291
Cdd:PRK11565 243 DVFDFRLDKDELGEIA 258
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
20-172 |
4.38e-08 |
|
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: 53.32 E-value: 4.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 20 LAVSRLGIGISRAACSGRHAAEQRrelGLALVRRALELGVNFLDTTDYnYSPDRA------ACANVlIRDAFspyqpnlV 93
Cdd:cd19163 11 LKVSKLGFGASPLGGVFGPVDEEE---AIRTVHEALDSGINYIDTAPW-YGQGRSetvlgkALKGI-PRDSY-------Y 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 94 IATSIGLIRDDRNGIRAATGAELRWLVNEKLRQLRLDRLDLVILR-----------LGETLPphgeslavrfdALAELRE 162
Cdd:cd19163 79 LATKVGRYGLDPDKMFDFSAERITKSVEESLKRLGLDYIDIIQVHdiefapsldqiLNETLP-----------ALQKLKE 147
|
170
....*....|
gi 1028513208 163 EGLIRHLGLS 172
Cdd:cd19163 148 EGKVRFIGIT 157
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
124-290 |
4.45e-08 |
|
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes 3-oxo-5-beta-steroid 4-dehydrogenase (EC 1.3.1.3) from Homo sapiens (AKR1D1), Rattus norvegicus (liver, AKR1D2), and Oryctolagus cuniculus (AKR1D3). 3-oxo-5-beta-steroid 4-dehydrogenase, also called delta(4)-3-ketosteroid 5-beta-reductase (EC 1.3.99.6), or delta(4)-3-oxosteroid 5-beta-reductase, or 5-beta-reductase, efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites.
Pssm-ID: 381335 [Multi-domain] Cd Length: 308 Bit Score: 53.26 E-value: 4.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 124 LRQLRLDRLDLVILRL------GETLPPHGESLAVRFD---------ALAELREEGLIRHLGLSNADDRHLS-----EAL 183
Cdd:cd19109 92 LKVLQLDYVDLYIIEMpmafkpGDEIYPRDENGKWLYHktnlcatweALEACKDAGLVKSIGVSNFNRRQLElilnkPGL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 184 QIAPVV-AVQNLFHFGHQRdvaLLRRCEKHNIAYIPFLPLGCTGV-----TACTP------LARIALRHHTTVDQIALRW 251
Cdd:cd19109 172 KHKPVSnQVECHPYFTQPK---LLEFCQQHDIVIVAYSPLGTCRDpiwvnVSSPPlledplLNSIGKKYNKTAAQVVLRF 248
|
170 180 190
....*....|....*....|....*....|....*....
gi 1028513208 252 LLSVSPVTIvaPQIGSVSRLEELVLCRDLPLTAEDMADL 290
Cdd:cd19109 249 NIQRGVVVI--PKSFNPERIKENFQIFDFSLTEEEMKDI 285
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
44-275 |
1.04e-07 |
|
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: 52.17 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 44 RELGLALVRRALELGVNFLDTT-DYNYSPDRAACANVL--------IRDafspyqpNLVIATSIGLIRDDRNGIRAATGA 114
Cdd:cd19082 16 EEEAFALLDAFVELGGNFIDTArVYGDWVERGASERVIgewlksrgNRD-------KVVIATKGGHPDLEDMSRSRLSPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 115 ELRWLVNEKLRQLRLDRLDLVIL-RLGETLPPhGESLavrfDALAELREEGLIRHLGLSN-ADDRhLSEALQIA------ 186
Cdd:cd19082 89 DIRADLEESLERLGTDYIDLYFLhRDDPSVPV-GEIV----DTLNELVRAGKIRAFGASNwSTER-IAEANAYAkahglp 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 187 PVVAVQNLFHFGHQR------------DVALLRRCEKHNIAYIPFLPLG--------CTGVTACTPLAR----------- 235
Cdd:cd19082 163 GFAASSPQWSLARPNeppwpgptlvamDEEMRAWHEENQLPVFAYSSQArgffskraAGGAEDDSELRRvyyseenferl 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1028513208 236 -----IALRHHTTVDQIALRWLLSVSP--VTIVAPQigSVSRLEELV 275
Cdd:cd19082 243 erakeLAEEKGVSPTQIALAYVLNQPFptVPIIGPR--TPEQLRDSL 287
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
22-172 |
3.70e-07 |
|
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: 50.35 E-value: 3.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 22 VSRLGIGisrAACSGRHAAEQRRELGLA-LVRRALELGVNFLDTTDYnYSPDRAACANVL--IRDAF--SPYQpnlvIAT 96
Cdd:cd19164 13 LPPLIFG---AATFSYQYTTDPESIPPVdIVRRALELGIRAFDTSPY-YGPSEIILGRALkaLRDEFprDTYF----IIT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 97 SIGLIRDD-----RNGIRAAtgaelrwlVNEKLRQLRLDRLDLVILRLGETLPPHGESLAVRfdALAELREEGLIRHLGL 171
Cdd:cd19164 85 KVGRYGPDdfdysPEWIRAS--------VERSLRRLHTDYLDLVYLHDVEFVADEEVLEALK--ELFKLKDEGKIRNVGI 154
|
.
gi 1028513208 172 S 172
Cdd:cd19164 155 S 155
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
44-273 |
6.44e-07 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 49.64 E-value: 6.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 44 RELGLALVRRALELGVNFLDTTDyNYS----PDRAACANVLI---------RDAfspyqpnLVIATSIG---LIRDDRNG 107
Cdd:cd19752 16 EETSFAILDRYVAAGGNFLDTAN-NYAfwteGGVGGESERLIgrwlkdrgnRDD-------VVIATKVGagpRDPDGGPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 108 IRAATGAE-LRWLVNEKLRQLRLDRLDLVILRLGETLPPHGESLavrfDALAELREEGLIRHLGLSNADDRHLSEALQIA 186
Cdd:cd19752 88 SPEGLSAEtIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETL----EAFNELVKAGKVRAIGASNFAAWRLERARQIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 187 ------PVVAVQNLF---------HFGHQRDVA--LLRRCEKHN----IAYIPFLPlGCTGVTA---------------C 230
Cdd:cd19752 164 rqqgwaEFSAIQQRHsylrprpgaDFGVQRIVTdeLLDYASSRPdltlLAYSPLLS-GAYTRPDrplpeqydgpdsdarL 242
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1028513208 231 TPLARIALRHHTTVDQIALRWLLSVSPVTIVAPQIGSVSRLEE 273
Cdd:cd19752 243 AVLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEE 285
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
26-202 |
7.92e-06 |
|
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: 46.37 E-value: 7.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 26 GIGISRAACSGRHAAEQRRELGLALVRRALELGVNFLDTTDYnYSPDRaacANVLIRDAFSPYQ---PNLVIATSIGLIR 102
Cdd:cd19153 14 PVGLGTAALGGVYGDGLEQDEAVAIVAEAFAAGINHFDTSPY-YGAES---SEAVLGKALAALQvprSSYTVATKVGRYR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 103 DD-----RNGIRAAtgaelrwlVNEKLRQLRLDRLDLVILR----------LGETLPphgeslavrfdALAELREEGLIR 167
Cdd:cd19153 90 DSefdysAERVRAS--------VATSLERLHTTYLDVVYLHdiefvdydtlVDEALP-----------ALRTLKDEGVIK 150
|
170 180 190
....*....|....*....|....*....|....*...
gi 1028513208 168 HLGLSNADDRHLSEALQ---IAPVVAVQNLFHFGHQRD 202
Cdd:cd19153 151 RIGIAGYPLDTLTRATRrcsPGSLDAVLSYCHLTLQDA 188
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
49-290 |
3.47e-05 |
|
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: 44.52 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 49 ALVRRALELGVNFLDTTDyNYSpdrAACANVLIRDAFSPYQPNLVIATSIGLirDDRNGIRAATGAE---LRWLVNEKLR 125
Cdd:cd19080 35 AMFDAYVEAGGNFIDTAN-NYT---NGTSERLLGEFIAGNRDRIVLATKYTM--NRRPGDPNAGGNHrknLRRSVEASLR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 126 QLRLDRLDLVILRLGETLPPHGESLavrfDALAELREEGLIRHLGLSN------------ADDRHLSealqiaPVVAVQN 193
Cdd:cd19080 109 RLQTDYIDLLYVHAWDFTTPVEEVM----RALDDLVRAGKVLYVGISDtpawvvarantlAELRGWS------PFVALQI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 194 LFHFGhQRDVA--LLRRCEKHNIAYIPFLPLG------------------CTGVTACTP------------LARIALRHH 241
Cdd:cd19080 179 EYSLL-ERTPEreLLPMARALGLGVTPWSPLGgglltgkyqrgeegrageAKGVTVGFGklternwaivdvVAAVAEELG 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1028513208 242 TTVDQIALRWLLSVSPVTIvaPQIGS--VSRLEELVLCRDLPLTAEDMADL 290
Cdd:cd19080 258 RSAAQVALAWVRQKPGVVI--PIIGArtLEQLKDNLGALDLTLSPEQLARL 306
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
49-290 |
4.15e-05 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 44.60 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 49 ALVRRALELGVNFLDTTDyNYSPDRAACAN---VLIRDAFSPYQPNLVIATSIGLirdDRNGIRAATGAELRWL---VNE 122
Cdd:PRK09912 47 AILRKAFDLGITHFDLAN-NYGPPPGSAEEnfgRLLREDFAAYRDELIISTKAGY---DMWPGPYGSGGSRKYLlasLDQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 123 KLRQLRLDRLDLVIL-RLGETLPPhgESLAvrfDALAELREEGLIRHLGLSN---ADDRHLSEALQ--IAPVVAVQNLFH 196
Cdd:PRK09912 123 SLKRMGLEYVDIFYShRVDENTPM--EETA---SALAHAVQSGKALYVGISSyspERTQKMVELLRewKIPLLIHQPSYN 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 197 FGHQ--RDVALLRRCEKHNIAYIPFLPLG---CTG------------------VTACTP-------------LARIALRH 240
Cdd:PRK09912 198 LLNRwvDKSGLLDTLQNNGVGCIAFTPLAqglLTGkylngipqdsrmhregnkVRGLTPkmlteanlnslrlLNEMAQQR 277
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1028513208 241 HTTVDQIALRWLLSVSPVTIVAPQIGSVSRLEELVLC-RDLPLTAEDMADL 290
Cdd:PRK09912 278 GQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQAlNNLTFSTEELAQI 328
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
124-251 |
6.89e-05 |
|
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: 43.60 E-value: 6.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 124 LRQLRLDRLDLVILRL------GETLPPHGESLAVRFD----------ALAELREEGLIRHLGLSNAD---DRHLSEALQ 184
Cdd:cd19129 90 LKRLQLDYLDLYLIHTpfafqpGDEQDPRDANGNVIYDdgvtlldtwrAMERLVDEGRCKAIGLSDVSlekLREIFEAAR 169
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 185 IAPVVaVQNLFHFGHQrDVALLRRCEKHNIAYIPFLPLGCT---GVTACTPLARIALRHHTTVDQIALRW 251
Cdd:cd19129 170 IKPAV-VQVESHPYLP-EWELLDFCKNHGIVLQAFAPLGHGmepKLLEDPVITAIARRVNKTPAQVLLAW 237
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
121-267 |
8.13e-05 |
|
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: 43.17 E-value: 8.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 121 NEKLRQLRLDRLDLVILRLGETLPPHGE--------------------SLAVRFDALAELREEGLIRHLGLSNADDRHLS 180
Cdd:cd19118 89 DDTLKELGLDYLDLYLIHWPVAFKPTGDlnpltavptnggevdldlsvSLVDTWKAMVELKKTGKVKSIGVSNFSIDHLQ 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 181 ---EALQIAPVVaVQNLFHFGHQRDvALLRRCEKHNI---AYIPF------LPLgctgVTACTPLARIALRHHTTVDQIA 248
Cdd:cd19118 169 aiiEETGVVPAV-NQIEAHPLLLQD-ELVDYCKSKNIhitAYSPLgnnlagLPL----LVQHPEVKAIAAKLGKTPAQVL 242
|
170 180
....*....|....*....|...
gi 1028513208 249 LRWLL----SVSPVTIVAPQIGS 267
Cdd:cd19118 243 IAWGIqrghSVIPKSVTPSRIRS 265
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
120-290 |
3.37e-04 |
|
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar proteins; Saccharomyces cerevisiae Ara1p (EC 1.1.1.117), also called D-arabinose 1-dehydrogenase (NAD(P)(+)), is a founding members of aldo-keto reductase family 3 member C1 (AKR3C1). It catalyzes the oxidation of D-arabinose, L-xylose, L-fucose, and L-galactose in the presence of NADP(+).
Pssm-ID: 381345 [Multi-domain] Cd Length: 294 Bit Score: 41.33 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 120 VNEKLRQLRLDRLDLVILR-----------LGETLPPHGESLAVRFDA----------LAELREEGLIRHLGLSNADDRH 178
Cdd:cd19119 92 LDESLKALGLDYVDLLLVHwpvcfekdsddSGKPFTPVNDDGKTRYAAsgdhittykqLEKIYLDGRAKAIGVSNYSIVY 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 179 LSEALQIAPVVAVQNLFHFgH----QRDvaLLRRCEKHNIAYIPFLPLGCTGVTAC-TPLA-RIALRHHTTVDQIALRWl 252
Cdd:cd19119 172 LERLIKECKVVPAVNQVEL-HphlpQMD--LRDFCFKHGILVTAYSPLGSHGAPNLkNPLVkKIAEKYNVSTGDILISY- 247
|
170 180 190
....*....|....*....|....*....|....*...
gi 1028513208 253 lSVSPVTIVAPQIGSVSRLEELVlcRDLPLTAEDMADL 290
Cdd:cd19119 248 -HVRQGVIVLPKSLKPVRIVSNG--KIVSLTKEDLQKL 282
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
49-223 |
3.87e-04 |
|
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: 41.39 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 49 ALVRRALELGVNFLDTTdYNYSPDRAacaNVLIRDAFSPyQPNLVIATSI------GLIRDdrnGIRAAtgaelrwlVNE 122
Cdd:cd19075 24 ELLDAFLERGHTEIDTA-RVYPDGTS---EELLGELGLG-ERGFKIDTKAnpgvggGLSPE---NVRKQ--------LET 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 123 KLRQLRLDRLDLVILRLgetlPPHGESLAVRFDALAELREEGLIRHLGLSNADDRHLSEALQIA-------PVV--AVQN 193
Cdd:cd19075 88 SLKRLKVDKVDVFYLHA----PDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICkengwvlPTVyqGMYN 163
|
170 180 190
....*....|....*....|....*....|....*
gi 1028513208 194 LFHfghqRDV-----ALLRrceKHNIAYIPFLPLG 223
Cdd:cd19075 164 AIT----RQVetelfPCLR---KLGIRFYAYSPLA 191
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
156-291 |
2.07e-03 |
|
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent D-xylose reductase (XR) from Pichia stipites, Kluyveromyces lactis, Pachysolen tannophilus, Candida tropicalis, and Candida tenuis, Gre3p from Saccharomyces cerevisiae, XR from Candida tropicalis, Pichia guilliermondii, Debaryomyces hansenli, and Debaryomyces nepalensis, which correspond to aldo-keto reductase family 2 member B1-B10 (AKR2B1-10), respectively. XR (EC1.1.1.307) catalyzes the NAD(P)H dependent reduction of xylose to xylitol.
Pssm-ID: 381339 [Multi-domain] Cd Length: 310 Bit Score: 38.97 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 156 ALAELREEGLIRHLGLSN---ADDRHLSEALQIAPvvAVQNLFHFGHQRDVALLRRCEKHNI---AYIPFLP-----LGC 224
Cdd:cd19113 148 ALEKLVDAGKIKSIGVSNfpgALILDLLRGATIKP--AVLQIEHHPYLQQPKLIEYAQKAGItitAYSSFGPqsfveLNQ 225
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90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1028513208 225 TGVTACTPL------ARIALRHHTTVDQIALRWllSVSPVTIVAPQIGSVSRLEELVLCRDLPLTAEDMADLA 291
Cdd:cd19113 226 GRALNTPTLfehdtiKSIAAKHNKTPAQVLLRW--ATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIA 296
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| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
23-191 |
2.82e-03 |
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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: 38.49 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 23 SRLGIGisrAACSGRHAAEQRRElGLALVRRALELGVNFLDTtdynySPDRAACANVLIRDAFSPYQP--NLVIATSIGL 100
Cdd:cd19162 1 PRLGLG---AASLGNLARAGEDE-AAATLDAAWDAGIRYFDT-----APLYGLGLSERRLGAALARHPraEYVVSTKVGR 71
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 101 IRDDRNGIRAA--------TGAELRWLVNEKLRQLRLDRLDLVILrlgETLPPH-GESLAVRFDALAELREEGLIRHLGL 171
Cdd:cd19162 72 LLEPGAAGRPAgadrrfdfSADGIRRSIEASLERLGLDRLDLVFL---HDPDRHlLQALTDAFPALEELRAEGVVGAIGV 148
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170 180
....*....|....*....|
gi 1028513208 172 SNADDRHLSEALQIAPVVAV 191
Cdd:cd19162 149 GVTDWAALLRAARRADVDVV 168
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| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
124-217 |
8.18e-03 |
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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: 37.31 E-value: 8.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028513208 124 LRQLRLDRLDLVILR-LGETLppHGESLAVR---------FDALAELREEGLIRHLGLSNADDRHLSEALQIAPV---VA 190
Cdd:cd19161 113 LQRLGLNRIDILYVHdIGVYT--HGDRKERHhfaqlmsggFKALEELKKAGVIKAFGLGVNEVQICLEALDEADLdcfLL 190
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90 100
....*....|....*....|....*..
gi 1028513208 191 VQNLFHFGHQRDVALLRRCEKHNIAYI 217
Cdd:cd19161 191 AGRYSLLDQSAEEEFLPRCEQRGTSLV 217
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