|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
23-278 |
1.75e-168 |
|
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: 466.69 E-value: 1.75e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 23 VHRLGYGAMQLTGPGIWGPPKDRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHPYAKGVVVATKAGLVRTGP 102
Cdd:cd19088 1 VSRLGYGAMRLTGPGIWGPPADREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHPYPDDVVIATKGGLVRTGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 103 NEWHPVGAPKYLRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSEVSVEEIQRARKVVDI 182
Cdd:cd19088 81 GWWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAIVRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 183 VSVQNRYNLTDRVHEKVLDYCEKENLGFIPWFPLATGGLAKPGSTLDSVAKQHDATPAQIALSWLLARSPVMLPIPGTSS 262
Cdd:cd19088 161 VSVQNRYNLANRDDEGVLDYCEAAGIAFIPWFPLGGGDLAQPGGLLAEVAARLGATPAQVALAWLLARSPVMLPIPGTSS 240
|
250
....*....|....*.
gi 1485949817 263 VKHLEENLAGAEVKLT 278
Cdd:cd19088 241 VEHLEENLAAAGLRLS 256
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
16-287 |
1.60e-115 |
|
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: 335.22 E-value: 1.60e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 16 KLG-GDLPVHRLGYGAMQLTGPgiWGPPkDRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHPYA-KGVVVAT 93
Cdd:COG0667 5 RLGrSGLKVSRLGLGTMTFGGP--WGGV-DEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALKGRPrDDVVIAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 94 KAGLVRtGPNEWHPVGAPKYLRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSEVSVEEI 173
Cdd:COG0667 82 KVGRRM-GPGPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSAEQL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 174 QRARKV----VDIVSVQNRYNLTDRVHEK-VLDYCEKENLGFIPWFPLATGGLA---KPGST------------------ 227
Cdd:COG0667 161 RRALAIaeglPPIVAVQNEYSLLDRSAEEeLLPAARELGVGVLAYSPLAGGLLTgkyRRGATfpegdraatnfvqgylte 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1485949817 228 --------LDSVAKQHDATPAQIALSWLLARSPVMLPIPGTSSVKHLEENLAGAEVKLTKDELAAVDA 287
Cdd:COG0667 241 rnlalvdaLRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADLELSAEDLAALDA 308
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
8-290 |
5.16e-104 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 304.97 E-value: 5.16e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 8 PAEKSGTFKLGGdLPVHRLGYGAMQLTGPGIWGPPKDRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHPYAK 87
Cdd:PRK10376 3 TIMSSGTFTLGG-RSVNRLGYGAMQLAGPGVFGPPKDRDAAIAVLREAVALGVNHIDTSDFYGPHVTNQLIREALHPYPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 88 GVVVATKAGLVRTGPNEWHPVGAPKYLRQQLEMSLRRLKLERIDLYQLhRI--DPKVPVEESLGE----LKALQKEGKIR 161
Cdd:PRK10376 82 DLTIVTKVGARRGEDGSWLPAFSPAELRRAVHDNLRNLGLDVLDVVNL-RLmgDGHGPAEGSIEEpltvLAELQRQGLVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 162 HIGLSEVSVEEIQRARKVVDIVSVQNRYNLTDRVHEKVLDYCEKENLGFIPWFPLatGGLAkP--GSTLDSVAKQHDATP 239
Cdd:PRK10376 161 HIGLSNVTPTQVAEARKIAEIVCVQNHYNLAHRADDALIDALARDGIAYVPFFPL--GGFT-PlqSSTLSDVAASLGATP 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1485949817 240 AQIALSWLLARSPVMLPIPGTSSVKHLEENLAGAEVKLTKDELAAVDAQAS 290
Cdd:PRK10376 238 MQVALAWLLQRSPNILLIPGTSSVAHLRENLAAAELVLSEEVLAELDGIAR 288
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
20-286 |
5.29e-97 |
|
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: 287.59 E-value: 5.29e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 20 DLPVHRLGYGAMQLTGPgiWGPPKDRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHPYAKGVVVATKAGlVR 99
Cdd:cd19078 1 GLEVSAIGLGCMGMSHG--YGPPPDKEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKPFRDQVVIATKFG-FK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 100 TGPNEWHPVG---APKYLRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSEVSVEEIQRA 176
Cdd:cd19078 78 IDGGKPGPLGldsRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETIRRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 177 RKVVDIVSVQNRYNLTDRVHEK-VLDYCEKENLGFIPWFPLATGGLA---KPGSTLDS---------------------- 230
Cdd:cd19078 158 HAVCPVTAVQSEYSMMWREPEKeVLPTLEELGIGFVPFSPLGKGFLTgkiDENTKFDEgddraslprftpealeanqalv 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1485949817 231 -----VAKQHDATPAQIALSWLLARSPVMLPIPGTSSVKHLEENLAGAEVKLTKDELAAVD 286
Cdd:cd19078 238 dllkeFAEEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAADIELTPEELREIE 298
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
20-286 |
4.21e-92 |
|
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: 274.79 E-value: 4.21e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 20 DLPVHRLGYGAMQLtGPGIWGPpKDRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHPYAKGVVVATKAGLVR 99
Cdd:cd19084 1 DLKVSRIGLGTWAI-GGTWWGE-VDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKGRRDDVVIATKCGLRW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 100 TGPNEWHPVGAPKYLRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSEVSVEEIQRARKV 179
Cdd:cd19084 79 DGGKGVTKDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEARKY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 180 VDIVSVQNRYNLTDRVHEK-VLDYCEKENLGFIPWFPLATGGLA---KPGST---------------------------L 228
Cdd:cd19084 159 GPIVSLQPPYSMLEREIEEeLLPYCRENGIGVLPYGPLAQGLLTgkyKKEPTfppddrrsrfpffrgenfeknleivdkL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1485949817 229 DSVAKQHDATPAQIALSWLLARSPVMLPIPGTSSVKHLEENLAGAEVKLTKDELAAVD 286
Cdd:cd19084 239 KEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDWELTEEELKEID 296
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
16-284 |
1.02e-89 |
|
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: 269.09 E-value: 1.02e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 16 KLGGDLP-VHRLGYGAMQLTGpgIWGPPkDRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHPYAKGVVVATK 94
Cdd:cd19076 4 KLGTQGLeVSALGLGCMGMSA--FYGPA-DEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKDRRDEVVIATK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 95 AGLVRTGPNEWHPV-GAPKYLRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSEVSVEEI 173
Cdd:cd19076 81 FGIVRDPGSGFRGVdGRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLSEASADTI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 174 QRARKVVDIVSVQNRYNLTDR-VHEKVLDYCEKENLGFIPWFPLA----TGGLAKPG----------------------- 225
Cdd:cd19076 161 RRAHAVHPITAVQSEYSLWTRdIEDEVLPTCRELGIGFVAYSPLGrgflTGAIKSPEdlpeddfrrnnprfqgenfdknl 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1485949817 226 ---STLDSVAKQHDATPAQIALSWLLARSPVMLPIPGTSSVKHLEENLAGAEVKLTKDELAA 284
Cdd:cd19076 241 klvEKLEAIAAEKGCTPAQLALAWVLAQGDDIVPIPGTKRIKYLEENVGALDVVLTPEELAE 302
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
26-287 |
1.89e-88 |
|
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain regulatory domains - these are reported to have oxidoreductase activity.
Pssm-ID: 425554 [Multi-domain] Cd Length: 290 Bit Score: 265.33 E-value: 1.89e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 26 LGYGAMQLTGPgiWGPPkDRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEAL---HPYAKGVVVATKaglVRTGP 102
Cdd:pfam00248 1 IGLGTWQLGGG--WGPI-SKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALkdyPVKRDKVVIATK---VPDGD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 103 NEWHPVGAPKYLRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSEVSVEEIQRAR--KVV 180
Cdd:pfam00248 75 GPWPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALtkGKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 181 DIVSVQNRYN-LTDRVHEKVLDYCEKENLGFIPWFPLATGGLAK---------PGS-----------------TLDSVAK 233
Cdd:pfam00248 155 PIVAVQVEYNlLRRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGkytrdpdkgPGErrrllkkgtplnlealeALEEIAK 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1485949817 234 QHDATPAQIALSWLLARSPVMLPIPGTSSVKHLEENLAGAEVKLTKDELAAVDA 287
Cdd:pfam00248 235 EHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDE 288
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
25-271 |
1.86e-83 |
|
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: 250.51 E-value: 1.86e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 25 RLGYGAMQltgpgiWGPPKDRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHPYAK--GVVVATKAGLVRTGP 102
Cdd:cd06660 2 RLGLGTMT------FGGDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRGNrdDVVIATKGGHPPGGD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 103 NEWHPVGaPKYLRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSEVSVEEIQRARKVVD- 181
Cdd:cd06660 76 PSRSRLS-PEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKa 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 182 -----IVSVQNRYNLTDR--VHEKVLDYCEKENLGFIPWFPLATGglakpgstldsvakqhdatPAQIALSWLLARSPVM 254
Cdd:cd06660 155 hglpgFAAVQPQYSLLDRspMEEELLDWAEENGLPLLAYSPLARG-------------------PAQLALAWLLSQPFVT 215
|
250
....*....|....*..
gi 1485949817 255 LPIPGTSSVKHLEENLA 271
Cdd:cd06660 216 VPIVGARSPEQLEENLA 232
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
23-286 |
4.14e-79 |
|
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: 240.59 E-value: 4.14e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 23 VHRLGYGAMQLtGPGIWGPPKDRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHPYAK-GVVVATKAglvrtg 101
Cdd:cd19072 4 VPVLGLGTWGI-GGGMSKDYSDDKKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAIKGFDReDLFITTKV------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 102 pNEWHpvGAPKYLRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSEVSVEEIQRARKVVD 181
Cdd:cd19072 77 -SPDH--LKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 182 ---IVSVQNRYNLTDRVHEK-VLDYCEKENLGFIPWFPLATGGL--AKPGSTLDSVAKQHDATPAQIALSWLLARsPVML 255
Cdd:cd19072 154 kgpIVANQVEYNLFDREEESgLLPYCQKNGIAIIAYSPLEKGKLsnAKGSPLLDEIAKKYGKTPAQIALNWLISK-PNVI 232
|
250 260 270
....*....|....*....|....*....|.
gi 1485949817 256 PIPGTSSVKHLEENLAGAEVKLTKDELAAVD 286
Cdd:cd19072 233 AIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
16-284 |
1.21e-73 |
|
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: 228.24 E-value: 1.21e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 16 KLGG-DLPVHRLGYGAMQLTGPGIWGPPKDRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHPYAK--GVVVA 92
Cdd:cd19079 4 RLGNsGLKVSRLCLGCMSFGDPKWRPWVLDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEFAPrdEVVIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 93 TKAGL-VRTGPNewhPVG-APKYLRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSEVSV 170
Cdd:cd19079 84 TKVYFpMGDGPN---GRGlSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGASSMYA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 171 EEIQRARKVVDI------VSVQNRYNLTDRVHEK-VLDYCEKENLGFIPWFPLATGGLAKPGST---------------- 227
Cdd:cd19079 161 WQFAKALHLAEKngwtkfVSMQNHYNLLYREEEReMIPLCEEEGIGVIPWSPLARGRLARPWGDtterrrsttdtaklky 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 228 -------------LDSVAKQHDATPAQIALSWLLARSPVMLPIPGTSSVKHLEENLAGAEVKLTKDELAA 284
Cdd:cd19079 241 dyfteadkeivdrVEEVAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAALDIKLSEEEIKY 310
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
21-271 |
4.12e-72 |
|
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: 221.97 E-value: 4.12e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 21 LPVHRLGYGAMQLTGPgiWGPPKDRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHPYAKGVVVATKAGLVRT 100
Cdd:cd19086 1 LEVSEIGFGTWGLGGD--WWGDVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKGRRDKVVIATKFGNRFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 101 GPNEWHPVGAPKYLRQQLEMSLRRLKLERIDLYQLHRIDPKV-PVEESLGELKALQKEGKIRHIGLSEVSVEEIQRARKV 179
Cdd:cd19086 79 GGPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLHNPPDEVlDNDELFEALEKLKQEGKIRAYGVSVGDPEEALAALRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 180 VDIVSVQNRYNLTD-RVHEKVLDYCEKENLGFIPWFPLATGGLAKpgstldsvakqhdaTPAQIALSWLLARSPVMLPIP 258
Cdd:cd19086 159 GGIDVVQVIYNLLDqRPEEELFPLAEEHGVGVIARVPLASGLLTG--------------KLAQAALRFILSHPAVSTVIP 224
|
250
....*....|...
gi 1485949817 259 GTSSVKHLEENLA 271
Cdd:cd19086 225 GARSPEQVEENAA 237
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
14-287 |
3.75e-70 |
|
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: 219.21 E-value: 3.75e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 14 TFKLG-GDLPVHRLGYGAMQLTGPGIWgPPKDRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHPYAKG-VVV 91
Cdd:cd19083 1 KVKLGkSDIDVNPIGLGTNAVGGHNLY-PNLDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLKEYNRNeVVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 92 ATKAGLvRTGPNEWHPVGAPKYLRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSEVSVE 171
Cdd:cd19083 80 ATKGAH-KFGGDGSVLNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFSLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 172 EIQRARKVVDIVSVQNRYNLTDRVHEK-VLDYCEKENLGFIPWFPLATGGLA---------------------------- 222
Cdd:cd19083 159 QLKEANKDGYVDVLQGEYNLLQREAEEdILPYCVENNISFIPYFPLASGLLAgkytkdtkfpdndlrndkplfkgerfse 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1485949817 223 --KPGSTLDSVAKQHDATPAQIALSWLLARSPVMLPIPGTSSVKHLEENLAGAEVKLTKDELAAVDA 287
Cdd:cd19083 239 nlDKVDKLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDA 305
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
16-286 |
5.24e-70 |
|
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: 219.01 E-value: 5.24e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 16 KLGG-DLPVHRLGYGAMQLtgpgiwGPPKDRAEAVRVLRRALELGVDFIDTADSYGPYV-------SEEIIAEALHpyAK 87
Cdd:cd19081 1 PLGRtGLSVSPLCLGTMVF------GWTADEETSFALLDAFVDAGGNFIDTADVYSAWVpgnaggeSETIIGRWLK--SR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 88 G----VVVATKAGLvRTGPNewHPVGAPKYLRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHI 163
Cdd:cd19081 73 GkrdrVVIATKVGF-PMGPN--GPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 164 GLSEVSVEEIQRARKVVD------IVSVQNRYNLTDRVH-EK-VLDYCEKENLGFIPWFPLATGGL-------AKPGS-- 226
Cdd:cd19081 150 GASNYSAWRLQEALELSRqhglprYVSLQPEYNLVDRESfEGeLLPLCREEGIGVIPYSPLAGGFLtgkyrseADLPGst 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1485949817 227 -------------------TLDSVAKQHDATPAQIALSWLLARSPVMLPIPGTSSVKHLEENLAGAEVKLTKDELAAVD 286
Cdd:cd19081 230 rrgeaakrylnerglrildALDEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAGLRLTDEEVARLD 308
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
14-285 |
3.57e-68 |
|
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: 214.61 E-value: 3.57e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 14 TFKLGGDLP-VHRLGYGAMQLTGpgIWGPPKDRAEAVRVLRRALELGVDFIDTADSYGPyvSEEIIAE--ALHP-YAKGV 89
Cdd:cd19144 3 TRTLGRNGPsVPALGFGAMGLSA--FYGPPKPDEERFAVLDAAFELGCTFWDTADIYGD--SEELIGRwfKQNPgKREKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 90 VVATKAGLVRTGPNEWHPV-GAPKYLRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSEV 168
Cdd:cd19144 79 FLATKFGIEKNVETGEYSVdGSPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLSEC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 169 SVEEIQRARKVVDIVSVQNRYN--LTD--RVHEKVLDYCEKENLGFIPWFPLATGGLA---------KPG---------- 225
Cdd:cd19144 159 SAETLRRAHAVHPIAAVQIEYSpfSLDieRPEIGVLDTCRELGVAIVAYSPLGRGFLTgairspddfEEGdfrrmaprfq 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1485949817 226 -----------STLDSVAKQHDATPAQIALSWLLARSPVMLPIPGTSSVKHLEENLAGAEVKLTKDELAAV 285
Cdd:cd19144 239 aenfpknlelvDKIKAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLGALKVKLTEEEEKEI 309
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
19-286 |
1.66e-67 |
|
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: 212.10 E-value: 1.66e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 19 GDLPVHRLGYGAMQLTGpgiWGPPKDRAEAVRVLRRALELGVDFIDTADSYG---PYVSEEIIAEAL--HP-YAKGVVVA 92
Cdd:cd19077 1 NGKLVGPIGLGLMGLTW---RPNPTPDEEAFETMKAALDAGSNLWNGGEFYGppdPHANLKLLARFFrkYPeYADKVVLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 93 TKAGLVRTGpneWHPVGAPKYLRQQLEMSLRRLK-LERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSEVSVE 171
Cdd:cd19077 78 VKGGLDPDT---LRPDGSPEAVRKSIENILRALGgTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 172 EIQRARKVVDIVSVQNRYNL--TDRVHEKVLDYCEKENLGFIPWFPLA----TGGLAKPG-------------------- 225
Cdd:cd19077 155 TIRRAHAVHPIAAVEVEYSLfsREIEENGVLETCAELGIPIIAYSPLGrgllTGRIKSLAdipegdfrrhldrfngenfe 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1485949817 226 ------STLDSVAKQHDATPAQIALSWLLARS-PVMLPIPGTSSVKHLEENLAGAEVKLTKDELAAVD 286
Cdd:cd19077 235 knlklvDALQELAEKKGCTPAQLALAWILAQSgPKIIPIPGSTTLERVEENLKAANVELTDEELKEIN 302
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
23-287 |
2.03e-67 |
|
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: 211.68 E-value: 2.03e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 23 VHRLGYGAMQLtGPGIWGPPKDRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHPYAKGVVVATKAGLVRTGP 102
Cdd:cd19085 1 VSRLGLGCWQF-GGGYWWGDQDDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKGRRDDVVIATKVSPDNLTP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 103 NEwhpvgapkyLRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSEVSVEEIQRARKVVDI 182
Cdd:cd19085 80 ED---------VRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 183 VSVQNRYNLTDRVHEK-VLDYCEKENLGFIPWFPLATGGLA----------------------KPG------STLDSV-- 231
Cdd:cd19085 151 DSNQLPYNLLWRAIEYeILPFCREHGIGVLAYSPLAQGLLTgkfssaedfppgdartrlfrhfEPGaeeetfEALEKLke 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1485949817 232 -AKQHDATPAQIALSWLLARSPVMLPIPGTSSVKHLEENLAGAEVKLTKDELAAVDA 287
Cdd:cd19085 231 iADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVDLELSPSVLERLDE 287
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
25-287 |
6.33e-67 |
|
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: 210.61 E-value: 6.33e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 25 RLGYGAMQLTGPGIWGP--PKDRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHPYAKGVVVATKAGLVRTGP 102
Cdd:cd19102 3 TIGLGTWAIGGGGWGGGwgPQDDRDSIAAIRAALDLGINWIDTAAVYGLGHSEEVVGRALKGLRDRPIVATKCGLLWDEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 103 NEWHPVGAPKYLRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSEVSVEEIQRARKVVDI 182
Cdd:cd19102 83 GRIRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQAIHPI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 183 VSVQNRYNLTDRVHEK-VLDYCEKENLGFIPWFPLATGGL------------------------AKPG--------STLD 229
Cdd:cd19102 163 ASLQPPYSLLRRGIEAeILPFCAEHGIGVIVYSPMQSGLLtgkmtpervaslpaddwrrrspffQEPNlarnlalvDALR 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1485949817 230 SVAKQHDATPAQIALSWLLARSPVMLPIPGTSSVKHLEENLAGAEVKLTKDELAAVDA 287
Cdd:cd19102 243 PIAERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAADLRLTPEELAEIEA 300
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
13-285 |
1.10e-65 |
|
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: 207.67 E-value: 1.10e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 13 GTFKLGGD-LPVHRLGYGAMQLTGpgIWGPPKDRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHPYAKGVV- 90
Cdd:cd19145 1 PRVKLGSQgLEVSAQGLGCMGLSG--DYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALKDGPREKVq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 91 VATKAGLVRTGPNEWHPVGAPKYLRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSEVSV 170
Cdd:cd19145 79 LATKFGIHEIGGSGVEVRGDPAYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSEASA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 171 EEIQRARKVVDIVSVQNRYNLTDR-VHEKVLDYCEKENLGFIPWFPLATGGLA-KP-------------------GSTLD 229
Cdd:cd19145 159 DTIRRAHAVHPITAVQLEWSLWTRdIEEEIIPTCRELGIGIVPYSPLGRGFFAgKAkleellensdvrkshprfqGENLE 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1485949817 230 ----------SVAKQHDATPAQIALSWLLARSPVMLPIPGTSSVKHLEENLAGAEVKLTKDELAAV 285
Cdd:cd19145 239 knkvlyerveALAKKKGCTPAQLALAWVLHQGEDVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
16-287 |
7.22e-63 |
|
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: 200.96 E-value: 7.22e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 16 KLG-GDLPVHRLGYGAMQLTGpGIWGPPKDRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHPYAKGVVVATK 94
Cdd:cd19149 3 KLGkSGIEASVIGLGTWAIGG-GPWWGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKGRRDKVVLATK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 95 AGLV--RTGPNEWHPVG--------APKYLRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIG 164
Cdd:cd19149 82 CGLRwdREGGSFFFVRDgvtvyknlSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQGKIRAIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 165 LSEVSVEEIQRARKVVDIVSVQNRYNLTDRVHEK-VLDYCEKENLGFIPWFPLATG--------------GLAKPGSTLD 229
Cdd:cd19149 162 ASNVSVEQIKEYVKAGQLDIIQEKYSMLDRGIEKeLLPYCKKNNIAFQAYSPLEQGlltgkitpdrefdaGDARSGIPWF 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1485949817 230 S----------------VAKQHDATPAQIALSWLLARSPVMLPIPGTSSVKHLEENLAGAEVKLTKDELAAVDA 287
Cdd:cd19149 242 SpenrekvlallekwkpLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPEQAEENAKAGDIRLSAEDIATMRS 315
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
21-287 |
1.64e-62 |
|
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: 199.72 E-value: 1.64e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 21 LPVHRLGYGAMQltgpgiWGPPKDRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHPYAKGVVVATKAGlVRT 100
Cdd:cd19087 11 LKVSRLCLGTMN------FGGRTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAGRRDDIVLATKVF-GPM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 101 GPNEWHPVGAPKYLRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSE------VSVEEIQ 174
Cdd:cd19087 84 GDDPNDRGLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNfaawqiAKAQGIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 175 RARKVVDIVSVQNRYNLTDRVHE-KVLDYCEKENLGFIPWFPLATG---GLAKPGSTLDS-------------------- 230
Cdd:cd19087 164 ARRGLLRFVSEQPMYNLLKRQAElEILPAARAYGLGVIPYSPLAGGlltGKYGKGKRPESgrlveraryqarygleeyrd 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1485949817 231 -------VAKQHDATPAQIALSWLLARSPVMLPIPGTSSVKHLEENLAGAEVKLTKDELAAVDA 287
Cdd:cd19087 244 iaerfeaLAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEITLTPELLAEIDE 307
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
21-287 |
1.28e-61 |
|
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: 197.84 E-value: 1.28e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 21 LPVHRLGYGAMQLTG----PGIWGPpKDRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHPYAKGVVVATKAG 96
Cdd:cd19091 11 LKVSELALGTMTFGGgggfFGAWGG-VDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKGRRDDVLIATKVR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 97 LvRTG--PNEwhpVGAPKY-LRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSEVSVEEI 173
Cdd:cd19091 90 G-RMGegPND---VGLSRHhIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVRYIGVSNFSAWQI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 174 QRARKVVD------IVSVQNRYNLTDRVHE-KVLDYCEKENLGFIPWFPLATGGL---------AKPGS----------- 226
Cdd:cd19091 166 MKALGISErrglarFVALQAYYSLLGRDLEhELMPLALDQGVGLLVWSPLAGGLLsgkyrrgqpAPEGSrlrrtgfdfpp 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1485949817 227 -----------TLDSVAKQHDATPAQIALSWLLARSPVMLPIPGTSSVKHLEENLAGAEVKLTKDELAAVDA 287
Cdd:cd19091 246 vdrergydvvdALREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGAAGLSLTPEEIARLDK 317
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
18-281 |
1.13e-54 |
|
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: 178.90 E-value: 1.13e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 18 GGDLPVHRLGYGAMqltgpGIWGPPKDRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEAL--HP-YAKGVVVATK 94
Cdd:cd19092 1 PEGLEVSRLVLGCM-----RLADWGESAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALalNPgLREKIEIQTK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 95 AGLVRTGPNEWHPVG----APKYLRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSEVSV 170
Cdd:cd19092 76 CGIRLGDDPRPGRIKhydtSKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFTP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 171 EEIQRARKVVD--IVSVQNRYNL--TDRVHEKVLDYCEKENLGFIPWFPLATGGLAKPGS--------TLDSVAKQHDAT 238
Cdd:cd19092 156 SQIELLQSYLDqpLVTNQIELSLlhTEAIDDGTLDYCQLLDITPMAWSPLGGGRLFGGFDerfqrlraALEELAEEYGVT 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1485949817 239 PAQIALSWLLaRSPV-MLPIPGTSSVKHLEENLAGAEVKLTKDE 281
Cdd:cd19092 236 IEAIALAWLL-RHPArIQPILGTTNPERIRSAVKALDIELTREE 278
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
23-286 |
2.83e-53 |
|
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: 175.49 E-value: 2.83e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 23 VHRLGYGAMQLTGPGIWG-PPKDRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHPYAKG--VVVATK-AGL- 97
Cdd:cd19093 2 VSPLGLGTWQWGDRLWWGyGEYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELGDRdeVVIATKfAPLp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 98 VRTGPNewHPVGApkylrqqLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGE-LKALQKEGKIRHIGLSEVSVEEIQRA 176
Cdd:cd19093 82 WRLTRR--SVVKA-------LKASLERLGLDSIDLYQLHWPGPWYSQIEALMDgLADAVEEGLVRAVGVSNYSADQLRRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 177 RKV-----VDIVSVQNRYNLTDRVHEK--VLDYCEKENLGFIPWFPLATGGLA--------KPG---------------- 225
Cdd:cd19093 153 HKAlkergVPLASNQVEYSLLYRDPEQngLLPACDELGITLIAYSPLAQGLLTgkyspenpPPGgrrrlfgrknlekvqp 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1485949817 226 --STLDSVAKQHDATPAQIALSWLLARSPVmlPIPGTSSVKHLEENLAGAEVKLTKDELAAVD 286
Cdd:cd19093 233 llDALEEIAEKYGKTPAQVALNWLIAKGVV--PIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
14-286 |
2.96e-53 |
|
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: 174.36 E-value: 2.96e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 14 TFKLGGDLPVHRLGYGAMQLtGPGiwgpPKDRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHPYAKGVVVAT 93
Cdd:cd19138 2 TVTLPDGTKVPALGQGTWYM-GED----PAKRAQEIEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIRGRRDKVFLVS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 94 KAglvrtgpnewHPVGA-PKYLRQQLEMSLRRLKLERIDLYQLH-RIDpkVPVEESLGELKALQKEGKIRHIGLSEVSVE 171
Cdd:cd19138 77 KV----------LPSNAsRQGTVRACERSLRRLGTDYLDLYLLHwRGG--VPLAETVAAMEELKKEGKIRAWGVSNFDTD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 172 EIQRARKVVD---IVSVQNRYNLTDRVHE-KVLDYCEKENLGFIPWFPLATGGLAKPG----STLDSVAKQHDATPAQIA 243
Cdd:cd19138 145 DMEELWAVPGggnCAANQVLYNLGSRGIEyDLLPWCREHGVPVMAYSPLAQGGLLRRGllenPTLKEIAARHGATPAQVA 224
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1485949817 244 LSWLLaRSPVMLPIPGTSSVKHLEENLAGAEVKLTKDELAAVD 286
Cdd:cd19138 225 LAWVL-RDGNVIAIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
25-271 |
3.72e-53 |
|
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: 173.96 E-value: 3.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 25 RLGYGAMQlTGpGIWGPPkDRAEAVRVLRRALELGVDFIDTADSYGPyvSEEIIAEAL-HPYAKGVVVATKAGLVRTGPN 103
Cdd:cd19095 2 VLGLGTSG-IG-RVWGVP-SEAEAARLLNTALDLGINLIDTAPAYGR--SEERLGRALaGLRRDDLFIATKVGTHGEGGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 104 EWHPVgAPKYLRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSeVSVEEIQRARKVVDIV 183
Cdd:cd19095 77 DRKDF-SPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVS-GDGEELEAAIASGVFD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 184 SVQNRYNLTDRVHEKVLDYCEKENLGFIPWFPLATGGLAKPGSTLDSVAKQHDA----------TPAQIALSWLLARSPV 253
Cdd:cd19095 155 VVQLPYNVLDREEEELLPLAAEAGLGVIVNRPLANGRLRRRVRRRPLYADYARRpefaaeiggaTWAQAALRFVLSHPGV 234
|
250
....*....|....*...
gi 1485949817 254 MLPIPGTSSVKHLEENLA 271
Cdd:cd19095 235 SSAIVGTTNPEHLEENLA 252
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
18-287 |
5.83e-53 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 173.32 E-value: 5.83e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 18 GGDLPVhrLGYGAMQLTGpgiwgppkdrAEAVRVLRRALELGVDFIDTADSYGpyvSEEIIAEALHpyAKGV-----VVA 92
Cdd:COG0656 2 GVEIPA--LGLGTWQLPG----------EEAAAAVRTALEAGYRHIDTAAMYG---NEEGVGEAIA--ASGVpreelFVT 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 93 TKAglvrtgPNEWHpvgAPKYLRQQLEMSLRRLKLERIDLYQLHRidP-KVPVEESLGELKALQKEGKIRHIGLSEVSVE 171
Cdd:COG0656 65 TKV------WNDNH---GYDDTLAAFEESLERLGLDYLDLYLIHW--PgPGPYVETWRALEELYEEGLIRAIGVSNFDPE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 172 EIQRARKVVDIVSV--QNRYNLTDRvHEKVLDYCEKENLGFIPWFPLATGGLAKpGSTLDSVAKQHDATPAQIALSWLLA 249
Cdd:COG0656 134 HLEELLAETGVKPAvnQVELHPYLQ-QRELLAFCREHGIVVEAYSPLGRGKLLD-DPVLAEIAEKHGKTPAQVVLRWHLQ 211
|
250 260 270
....*....|....*....|....*....|....*...
gi 1485949817 250 RSpvMLPIPGTSSVKHLEENLAGAEVKLTKDELAAVDA 287
Cdd:COG0656 212 RG--VVVIPKSVTPERIRENLDAFDFELSDEDMAAIDA 247
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
21-280 |
7.02e-53 |
|
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: 174.32 E-value: 7.02e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 21 LPVHRLGYGAMQLTGPGIwgppkDRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHPYAK-GVVVATKA-GLV 98
Cdd:cd19074 2 LKVSELSLGTWLTFGGQV-----DDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALKGWPReSYVISTKVfWPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 99 RTGPNEWhpvG-APKYLRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSEVSVEEIQRAR 177
Cdd:cd19074 77 GPGPNDR---GlSRKHIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 178 KVVD------IVSVQNRYNLTDRVHE-KVLDYCEKENLGFIPWFPLATGGLA---KPGSTLDS----------------- 230
Cdd:cd19074 154 DLARqfglipPVVEQPQYNMLWREIEeEVIPLCEKNGIGLVVWSPLAQGLLTgkyRDGIPPPSrsratdednrdkkrrll 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1485949817 231 -------------VAKQHDATPAQIALSWLLARSPVMLPIPGTSSVKHLEENLAGAEVKLTKD 280
Cdd:cd19074 234 tdenlekvkklkpIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
20-287 |
2.51e-50 |
|
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: 168.25 E-value: 2.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 20 DLPVHRLGYGAMQLTGpGIWGPPkDRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHPYAK--GVVVATKAGL 97
Cdd:cd19148 1 DLPVSRIALGTWAIGG-WMWGGT-DEKEAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKEYGKrdRVVIATKVGL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 98 vrtgpnEWHPVG------APKYLRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSEVSVE 171
Cdd:cd19148 79 ------EWDEGGevvrnsSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSPE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 172 EIQRARKVVDIVSVQNRYNLTDRVHEK-VLDYCEKENLGFIPWFPLATG---GLAKPGST-------------------- 227
Cdd:cd19148 153 QMETFRKVAPLHTVQPPYNLFEREIEKdVLPYARKHNIVTLAYGALCRGllsGKMTKDTKfegddlrrtdpkfqeprfsq 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1485949817 228 -------LDSVAKQHDATP-AQIALSWLLARSPVMLPIPGTSSVKHLEENLAGAEVKLTKDELAAVDA 287
Cdd:cd19148 233 ylaaveeLDKLAQERYGKSvIHLAVRWLLDQPGVSIALWGARKPEQLDAVDEVFGWSLNDEDMKEIDA 300
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
16-287 |
2.99e-50 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 169.61 E-value: 2.99e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 16 KLG-GDLPVHRLGYGAMQLtgpgiwgPPKDRAEAVRVLRRALELGVDFIDTADSYGPyvSEEIIAEALHPYAKGVVVATK 94
Cdd:COG1453 5 RLGkTGLEVSVLGFGGMRL-------PRKDEEEAEALIRRAIDNGINYIDTARGYGD--SEEFLGKALKGPRDKVILATK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 95 -AGLVRTgpnewhpvgaPKYLRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGE------LKALQKEGKIRHIGLS- 166
Cdd:COG1453 76 lPPWVRD----------PEDMRKDLEESLKRLQTDYIDLYLIHGLNTEEDLEKVLKPggaleaLEKAKAEGKIRHIGFSt 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 167 EVSVEEIQRARKVVDIVSVQNRYNLTDRVH---EKVLDYCEKENLGFIPWFPLATGGLAKPGSTLDSVAKQhDATPAQIA 243
Cdd:COG1453 146 HGSLEVIKEAIDTGDFDFVQLQYNYLDQDNqagEEALEAAAEKGIGVIIMKPLKGGRLANPPEKLVELLCP-PLSPAEWA 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1485949817 244 LSWLLARSPVMLPIPGTSSVKHLEENLAGAE--VKLTKDELAAVDA 287
Cdd:COG1453 225 LRFLLSHPEVTTVLSGMSTPEQLDENLKTADnlEPLTEEELAILER 270
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
21-286 |
8.59e-50 |
|
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: 166.63 E-value: 8.59e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 21 LPVHRLGYGAMQLTGPgiWGPPKDRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHPYAKGVVVATKAGLVRT 100
Cdd:cd19080 8 LRVSPLALGTMTFGTE--WGWGADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAGNRDRIVLATKYTMNRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 101 GPNEWHPVGAPKYLRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSEV------SVEEIQ 174
Cdd:cd19080 86 PGDPNAGGNHRKNLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDTpawvvaRANTLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 175 RARKVVDIVSVQNRYNLTDR-VHEKVLDYCEKENLGFIPWFPLATG-----------------GLAKPGS---------- 226
Cdd:cd19080 166 ELRGWSPFVALQIEYSLLERtPERELLPMARALGLGVTPWSPLGGGlltgkyqrgeegrageaKGVTVGFgklternwai 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1485949817 227 --TLDSVAKQHDATPAQIALSWLLARSPVMLPIPGTSSVKHLEENLAGAEVKLTKDELAAVD 286
Cdd:cd19080 246 vdVVAAVAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDLTLSPEQLARLD 307
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
35-286 |
9.50e-48 |
|
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: 160.04 E-value: 9.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 35 GPGIWG------PPKDR-AEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHPYAK-GVVVATKAglvrtgpneWH 106
Cdd:cd19137 8 GLGTWGiggfltPDYSRdEEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKDFPReDLFIVTKV---------WP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 107 PVGAPKYLRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSEVSVEEIQRARKVV--DIVS 184
Cdd:cd19137 79 TNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSqtPIVC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 185 VQNRYNLTDRVHEK--VLDYCEKENLGFIPWFPLATgGLAKPGSTLDSVAKQHDATPAQIALSWLLARsPVMLPIPGTSS 262
Cdd:cd19137 159 NQVKYNLEDRDPERdgLLEYCQKNGITVVAYSPLRR-GLEKTNRTLEEIAKNYGKTIAQIALAWLIQK-PNVVAIPKAGR 236
|
250 260
....*....|....*....|....
gi 1485949817 263 VKHLEENLAGAEVKLTKDELAAVD 286
Cdd:cd19137 237 VEHLKENLKATEIKLSEEEMKLLD 260
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
23-287 |
1.00e-47 |
|
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: 161.96 E-value: 1.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 23 VHRLGYGAMQltgpgiWGPPKDRAEAVRVLRRALELGVDFIDTADSYgPY--------VSEEIIAEALHpyAKG----VV 90
Cdd:cd19094 1 VSEICLGTMT------WGEQNTEAEAHEQLDYAFDEGVNFIDTAEMY-PVppspetqgRTEEIIGSWLK--KKGnrdkVV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 91 VATK-AGlvRTGPNEWHPVGAPKYLRQQL----EMSLRRLKLERIDLYQLH---RIDP---------------KVPVEES 147
Cdd:cd19094 72 LATKvAG--PGEGITWPRGGGTRLDRENIreavEGSLKRLGTDYIDLYQLHwpdRYTPlfgggyytepseeedSVSFEEQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 148 LGELKALQKEGKIRHIGLSEvsvE---------EIQRARKVVDIVSVQNRYNLTDRVHEKVL-DYCEKENLGFIPWFPLA 217
Cdd:cd19094 150 LEALGELVKAGKIRHIGLSN---EtpwgvmkflELAEQLGLPRIVSIQNPYSLLNRNFEEGLaEACHRENVGLLAYSPLA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 218 TGGL---------AKPGSTLD----------------------SVAKQHDATPAQIALSWLLARSPVMLPIPGTSSVKHL 266
Cdd:cd19094 227 GGVLtgkyldgaaRPEGGRLNlfpgymaryrspqaleavaeyvKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQL 306
|
330 340
....*....|....*....|.
gi 1485949817 267 EENLAGAEVKLTKDELAAVDA 287
Cdd:cd19094 307 KENIDAFDVPLSDELLAEIDA 327
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
19-287 |
2.58e-47 |
|
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: 158.96 E-value: 2.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 19 GDLPVHRLGYGAMQLTGpgiwgppkdrAEAVRVLRRALELGVDFIDTADSYGpyvSEEIIAEAL--HPYAKG-VVVATKA 95
Cdd:cd19140 4 NGVRIPALGLGTYPLTG----------EECTRAVEHALELGYRHIDTAQMYG---NEAQVGEAIaaSGVPRDeLFLTTKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 96 glvrtgpneWHPVGAPKYLRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSEVSVEEIQR 175
Cdd:cd19140 71 ---------WPDNYSPDDFLASVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLRE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 176 ARKVV--DIVSVQNRYN-LTDRvhEKVLDYCEKENLGFIPWFPLATGGLAK-PgsTLDSVAKQHDATPAQIALSWLLARS 251
Cdd:cd19140 142 AVELSeaPLFTNQVEYHpYLDQ--RKLLDAAREHGIALTAYSPLARGEVLKdP--VLQEIGRKHGKTPAQVALRWLLQQE 217
|
250 260 270
....*....|....*....|....*....|....*.
gi 1485949817 252 PVMLpIPGTSSVKHLEENLAGAEVKLTKDELAAVDA 287
Cdd:cd19140 218 GVAA-IPKATNPERLEENLDIFDFTLSDEEMARIAA 252
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
25-274 |
4.10e-46 |
|
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: 156.94 E-value: 4.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 25 RLGYGAMQLtgpgiwGPPKDRAEAVRVLRRALELGVDFIDTADSYG----PYVSEEIIAEALHpyAKG----VVVATKAG 96
Cdd:cd19082 2 RIVLGTADF------GTRIDEEEAFALLDAFVELGGNFIDTARVYGdwveRGASERVIGEWLK--SRGnrdkVVIATKGG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 97 LvrtgPNEWHPVGA---PKYLRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSEVSVEEI 173
Cdd:cd19082 74 H----PDLEDMSRSrlsPEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNWSTERI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 174 QRARK------VVDIVSVQNRYNLTDRVHEKVLDYC------------EKENLGFIPWFPLATG---GLAKPGSTLDS-- 230
Cdd:cd19082 150 AEANAyakahgLPGFAASSPQWSLARPNEPPWPGPTlvamdeemrawhEENQLPVFAYSSQARGffsKRAAGGAEDDSel 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1485949817 231 ------------------VAKQHDATPAQIALSWLLARSPVMLPIPGTSSVKHLEENLAGAE 274
Cdd:cd19082 230 rrvyyseenferlerakeLAEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAAAD 291
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
25-274 |
1.87e-45 |
|
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: 153.87 E-value: 1.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 25 RLGYGAMQLtgPGIWGPPKDRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEAL-HPYAKGVVVATKAGlvrtgpn 103
Cdd:cd19096 2 VLGFGTMRL--PESDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALkEGPREKFYLATKLP------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 104 eWHPVGAPKYLRQQLEMSLRRLKLERIDLYQLH-----RIDPKVPVEESLGELKALQKEGKIRHIGLS-EVSVEEIQRAR 177
Cdd:cd19096 73 -PWSVKSAEDFRRILEESLKRLGVDYIDFYLLHglnspEWLEKARKGGLLEFLEKAKKEGLIRHIGFSfHDSPELLKEIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 178 KVVDIVSVQNRYNLTDRVH---EKVLDYCEKENLGFIPWFPLATGGLAKPGSTLDSVAKQHDATPAQIALSWLLARSPVM 254
Cdd:cd19096 152 DSYDFDFVQLQYNYLDQENqagRPGIEYAAKKGMGVIIMEPLKGGGLANNPPEALAILCGAPLSPAEWALRFLLSHPEVT 231
|
250 260
....*....|....*....|
gi 1485949817 255 LPIPGTSSVKHLEENLAGAE 274
Cdd:cd19096 232 TVLSGMSTPEQLDENIAAAD 251
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
26-286 |
5.76e-45 |
|
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: 152.43 E-value: 5.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 26 LGYGAMQLTGpgiwgppkdrAEAVRVLRRALELGVDFIDTADSYGpyvSEEIIAEALHPYAKG---VVVATKAglvrtgp 102
Cdd:cd19073 4 LGLGTWQLRG----------DDCANAVKEALELGYRHIDTAEIYN---NEAEVGEAIAESGVPredLFITTKV------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 103 neWHPVGAPKYLRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSEVSVEEIQRARKV--V 180
Cdd:cd19073 64 --WRDHLRPEDLKKSVDRSLEKLGTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDIspL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 181 DIVSVQNRYNLTdRVHEKVLDYCEKENLGFIPWFPLATGGLAKpGSTLDSVAKQHDATPAQIALSWLLARSpvMLPIPGT 260
Cdd:cd19073 142 PIAVNQVEFHPF-LYQAELLEYCRENDIVITAYSPLARGEVLR-DPVIQEIAEKYDKTPAQVALRWLVQKG--IVVIPKA 217
|
250 260
....*....|....*....|....*.
gi 1485949817 261 SSVKHLEENLAGAEVKLTKDELAAVD 286
Cdd:cd19073 218 SSEDHLKENLAIFDWELTSEDVAKID 243
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-271 |
1.06e-44 |
|
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: 151.48 E-value: 1.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 16 KLG-GDLPVHRLGYGAMQLtgpgiwgPPKDRAEAVRVLRRALELGVDFIDTADSYGpyVSEEIIAEALHPYAKGVVVATK 94
Cdd:cd19100 3 RLGrTGLKVSRLGFGGGPL-------GRLSQEEAAAIIRRALDLGINYFDTAPSYG--DSEEKIGKALKGRRDKVFLATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 95 AGlvrtgpnEWHPVGApkylRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGE------LKALQKEGKIRHIGLSEV 168
Cdd:cd19100 74 TG-------ARDYEGA----KRDLERSLKRLGTDYIDLYQLHAVDTEEDLDQVFGPggaleaLLEAKEEGKIRFIGISGH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 169 SVEEIQRARKVVDIVSVQNRYNLTDRVH----EKVLDYCEKENLGFIPWFPLATGGLAKPgstldsvakqhDATPAQIAL 244
Cdd:cd19100 143 SPEVLLRALETGEFDVVLFPINPAGDHIdsfrEELLPLAREKGVGVIAMKVLAGGRLLSG-----------DPLDPEQAL 211
|
250 260
....*....|....*....|....*..
gi 1485949817 245 SWLLARSPVMLPIPGTSSVKHLEENLA 271
Cdd:cd19100 212 RYALSLPPVDVVIVGMDSPEELDENLA 238
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
37-283 |
2.23e-44 |
|
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo. Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2). It catalyzes the conversion of 3-hydroxybutanal (3-HB) to 1,3-butanediol (1,3-BDO) by using NADPH as a cofactor.
Pssm-ID: 381315 [Multi-domain] Cd Length: 308 Bit Score: 152.80 E-value: 2.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 37 GIW---GPPKDRAEAVRVLRRALELGVDFIDTADSYGPY--VSEEIIAEALH----PYAKGVVVATKAGLvRTGPNEWHP 107
Cdd:cd19089 17 GLWhnfGDYTSPEEARELLRTAFDLGITHFDLANNYGPPpgSAEENFGRILKrdlrPYRDELVISTKAGY-GMWPGPYGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 108 VGAPKYLRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSEVSVEEIQRARKV-----VDI 182
Cdd:cd19089 96 GGSRKYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPGAKARRAIALlrelgVPL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 183 VSVQNRYNLTDR-VHEKVLDYCEKENLGFIPWFPLATGGLA-------KPGS-----------------------TLDSV 231
Cdd:cd19089 176 IIHQPRYSLLDRwAEDGLLEVLEEAGIGFIAFSPLAQGLLTdkylngiPPDSrraaeskflteealtpekleqlrKLNKI 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1485949817 232 AKQHDATPAQIALSWLLARSPVMLPIPGTSSVKHLEENLAGAE-VKLTKDELA 283
Cdd:cd19089 256 AAKRGQSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAALKnLDFSEEELA 308
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-271 |
4.39e-44 |
|
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: 150.43 E-value: 4.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 16 KLGG-DLPVHRLGYGAMQLtgpgiwgppkdRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHPYA-KGVVVAT 93
Cdd:cd19105 5 TLGKtGLKVSRLGFGGGGL-----------PRESPELLRRALDLGINYFDTAEGYGNGNSEEIIGEALKGLRrDKVFLAT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 94 KAglvrtgpNEWHPVGAPKYLRQQLEMSLRRLKLERIDLYQLHRIDPKVP---VEESLGELKALQKEGKIRHIGLSEVSV 170
Cdd:cd19105 74 KA-------SPRLDKKDKAELLKSVEESLKRLQTDYIDIYQLHGVDTPEErllNEELLEALEKLKKEGKVRFIGFSTHDN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 171 EE--IQRA--RKVVDIVSVqnRYNLTDRVHE--KVLDYCEKENLGFIPWFPLATGGLAKPgstLDSVAKQHDATPAQIAL 244
Cdd:cd19105 147 MAevLQAAieSGWFDVIMV--AYNFLNQPAEleEALAAAAEKGIGVVAMKTLAGGYLQPA---LLSVLKAKGFSLPQAAL 221
|
250 260
....*....|....*....|....*..
gi 1485949817 245 SWLLARSPVMLPIPGTSSVKHLEENLA 271
Cdd:cd19105 222 KWVLSNPRVDTVVPGMRNFAELEENLA 248
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
25-274 |
9.41e-44 |
|
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: 150.56 E-value: 9.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 25 RLGYGAMQLtgpgiwGPPKDRAEAVRVLRRALELGVDFIDTADSYGPYV-------SEEIIAEALHpyAKG----VVVAT 93
Cdd:cd19752 2 ELCLGTMYF------GTRTDEETSFAILDRYVAAGGNFLDTANNYAFWTeggvggeSERLIGRWLK--DRGnrddVVIAT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 94 KAGLVRTGPNEWHPVG---APKYLRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSEVSV 170
Cdd:cd19752 74 KVGAGPRDPDGGPESPeglSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 171 EEIQRARKVV------DIVSVQNRYNLTDR-----------VHEKVLDYCEKE-NLGFIPWFPLATGGLAKPG------- 225
Cdd:cd19752 154 WRLERARQIArqqgwaEFSAIQQRHSYLRPrpgadfgvqriVTDELLDYASSRpDLTLLAYSPLLSGAYTRPDrplpeqy 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1485949817 226 ---------STLDSVAKQHDATPAQIALSWLLARSPVMLPIPGTSSVKHLEENLAGAE 274
Cdd:cd19752 234 dgpdsdarlAVLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAALD 291
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
25-286 |
6.55e-42 |
|
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. The family includes AKR1A/B/C/D/E/G/I, AKR2A/B/C/D/E, AKR3A/B/C/D/E/G, AKR4A/B/C, AKR5A/B/C/D/E/F/G/H, and similar proteins.
Pssm-ID: 381297 [Multi-domain] Cd Length: 251 Bit Score: 144.55 E-value: 6.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 25 RLGYGAMQLtgpgiwgppkDRAEAVRVLRRALELGVDFIDTADSYGpyvSEEIIAEALHpyAKGVV-----VATKAglvr 99
Cdd:cd19071 3 LIGLGTYKL----------KPEETAEAVLAALEAGYRHIDTAAAYG---NEAEVGEAIR--ESGVPreelfITTKL---- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 100 tgpneWHPVGAPKYLRQQLEMSLRRLKLERIDLYQLH------RIDPKVPVEESLGELKALQKEGKIRHIGLSEVSVEEI 173
Cdd:cd19071 64 -----WPTDHGYERVREALEESLKDLGLDYLDLYLIHwpvpgkEGGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 174 QRARKVVDI--VSVQNRYN--LTDRvheKVLDYCEKENLGFIPWFPLATGG---LAKPgsTLDSVAKQHDATPAQIALSW 246
Cdd:cd19071 139 EELLAAARIkpAVNQIELHpyLQQK---ELVEFCKEHGIVVQAYSPLGRGRrplLDDP--VLKEIAKKYGKTPAQVLLRW 213
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1485949817 247 LLARSpvMLPIPGTSSVKHLEENLAGAEVKLTKDELAAVD 286
Cdd:cd19071 214 ALQRG--VVVIPKSSNPERIKENLDVFDFELSEEDMAAID 251
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
22-287 |
9.61e-40 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 140.42 E-value: 9.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 22 PVHRLGYGAMQLTGPgiWGPPKDRAEAVRVLRRALELGVDFIDTADSYGPyvSEEIIAEALHPYAKG------VVVATKa 95
Cdd:cd19101 1 TISRVINGMWQLSGG--HGGIRDEDAAVRAMAAYVDAGLTTFDCADIYGP--AEELIGEFRKRLRRErdaaddVQIHTK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 96 glvrtgpneWHPVGA-----PKYLRQQLEMSLRRLKLERIDLYQLHRIDPKVP-VEESLGELKALQKEGKIRHIGLSEVS 169
Cdd:cd19101 76 ---------WVPDPGeltmtRAYVEAAIDRSLKRLGVDRLDLVQFHWWDYSDPgYLDAAKHLAELQEEGKIRHLGLTNFD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 170 VEEIQRA-RKVVDIVSVQNRYNLTD-RVHEKVLDYCEKENLGFIPWFPLATG-------GLAKPG--------------- 225
Cdd:cd19101 147 TERLREIlDAGVPIVSNQVQYSLLDrRPENGMAALCEDHGIKLLAYGTLAGGllsekylGVPEPTgpaletrslqkyklm 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1485949817 226 --------------STLDSVAKQHDATPAQIALSWLLARSPVMLPIPGTSSVKHLEENLAGAEVKLTKDELAAVDA 287
Cdd:cd19101 227 idewggwdlfqellRTLKAIADKHGVSIANVAVRWVLDQPGVAGVIVGARNSEHIDDNVRAFSFRLDDEDRAAIDA 302
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
25-277 |
1.38e-39 |
|
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: 139.61 E-value: 1.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 25 RLGYGAMQLTGpgIWGPPkDRAEAVRVLRRALELGVDFIDTADSYGPyvSEEIIAEAL-HPYAKGVVVATKAGLVRTGPN 103
Cdd:cd19090 2 ALGLGTAGLGG--VFGGV-DDDEAVATIRAALDLGINYIDTAPAYGD--SEERLGLALaELPREPLVLSTKVGRLPEDTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 104 EWhpvgAPKYLRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEE-----SLGELKALQKEGKIRHIGLSEVSVEEIQRA-- 176
Cdd:cd19090 77 DY----SADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDIlapggALEALLELKEEGLIKHIGLGGGPPDLLRRAie 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 177 RKVVDIVSVQNRYNLTDRVH-EKVLDYCEKENLGFIPWFPLATGGLAKPGS-------------------TLDSVAKQHD 236
Cdd:cd19090 153 TGDFDVVLTANRYTLLDQSAaDELLPAAARHGVGVINASPLGMGLLAGRPPervrytyrwlspelldrakRLYELCDEHG 232
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1485949817 237 ATPAQIALSWLLARSPVMLPIPGTSSVKHLEENLAGAEVKL 277
Cdd:cd19090 233 VPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAAEGPL 273
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
44-283 |
1.27e-38 |
|
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2).
Pssm-ID: 381377 [Multi-domain] Cd Length: 309 Bit Score: 137.92 E-value: 1.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 44 DRAEAVR-VLRRALELGVDFIDTADSYGPYV--SEE----IIAEALHPYAKGVVVATKAGLVR-TGP-NEWhpvGAPKYL 114
Cdd:cd19151 27 DRYENSRaMLRRAFDLGITHFDLANNYGPPPgsAEEnfgrILKEDLKPYRDELIISTKAGYTMwPGPyGDW---GSKKYL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 115 RQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSEVSVEEIQRARKVVDIVSV-----QNRY 189
Cdd:cd19151 104 IASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGISNYPPEEAREAAAILKDLGTpclihQPKY 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 190 NLTDR-VHEKVLDYCEKENLGFIPWFPLATGGL--------------AKPGS----------------TLDSVAKQHDAT 238
Cdd:cd19151 184 SMFNRwVEEGLLDVLEEEGIGCIAFSPLAQGLLtdrylngipedsraAKGSSflkpeqiteeklakvrRLNEIAQARGQK 263
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1485949817 239 PAQIALSWLLARSPVMLPIPGTSSVKHLEENLAG-AEVKLTKDELA 283
Cdd:cd19151 264 LAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGAlDNREFSEEELA 309
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
34-289 |
3.46e-37 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 133.61 E-value: 3.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 34 TGPGIWGPPKDRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHPYAK-GVVVATK--AGLVRTGPNewhPVga 110
Cdd:cd19103 20 GGDQVFGNHLDEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEFLKRYPReDYIISTKftPQIAGQSAD---PV-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 111 pkylRQQLEMSLRRLKLERIDLYQLHriDPkVPVEESLGELKALQKEGKIRHIGLSEVSVEEIQRARKV-----VDIVSV 185
Cdd:cd19103 95 ----ADMLEGSLARLGTDYIDIYWIH--NP-ADVERWTPELIPLLKSGKVKHVGVSNHNLAEIKRANEIlakagVSLSAV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 186 QNRYNLTDRVHEK--VLDYCEKENLGFIPWFPLATGGLAKPGST---------------------------LDSVAKQHD 236
Cdd:cd19103 168 QNHYSLLYRSSEEagILDYCKENGITFFAYMVLEQGALSGKYDTkhplpegsgraetynpllpqleeltavMAEIGAKHG 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1485949817 237 ATPAQIALSWLLARSpvMLPIPGTSSVKHLEENLAGAEVKLTKDELAAVDAQA 289
Cdd:cd19103 248 ASIAQVAIAWAIAKG--TTPIIGVTKPHHVEDAARAASITLTDDEIKELEQLA 298
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
28-287 |
5.53e-37 |
|
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: 133.45 E-value: 5.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 28 YGAMQLtgpGIWGPPKDRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHPyAKGVVVATKAglvrtgPNEWHP 107
Cdd:cd19075 5 LGTMTF---GSQGRFTTAEAAAELLDAFLERGHTEIDTARVYPDGTSEELLGELGLG-ERGFKIDTKA------NPGVGG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 108 VGAPKYLRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSEVSVEEIQRarkVVDIV---- 183
Cdd:cd19075 75 GLSPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAE---IVEICkeng 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 184 ----SV-QNRYNLTDRVHE-KVLDYCEKENLGFIPWFPLATGGLAKPGSTLDS--------------------------- 230
Cdd:cd19075 152 wvlpTVyQGMYNAITRQVEtELFPCLRKLGIRFYAYSPLAGGFLTGKYKYSEDkagggrfdpnnalgklyrdrywkpsyf 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1485949817 231 --------VAKQHDATPAQIALSWLLARSPVMLP-----IPGTSSVKHLEENLAGAEV-KLTKDELAAVDA 287
Cdd:cd19075 232 ealekveeAAEKEGISLAEAALRWLYHHSALDGEkgdgvILGASSLEQLEENLAALEKgPLPEEVVKAIDE 302
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
16-283 |
1.58e-36 |
|
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: 131.90 E-value: 1.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 16 KLGG-DLPVHRLGYGAMQLTGpgIWGPPkDRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALhpyaKGV----- 89
Cdd:cd19163 5 KLGKtGLKVSKLGFGASPLGG--VFGPV-DEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKAL----KGIprdsy 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 90 VVATKAGlvRTGPNEwhpvgaPKYL-------RQQLEMSLRRLKLERIDLYQLHRID--PKVP--VEESLGELKALQKEG 158
Cdd:cd19163 78 YLATKVG--RYGLDP------DKMFdfsaeriTKSVEESLKRLGLDYIDIIQVHDIEfaPSLDqiLNETLPALQKLKEEG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 159 KIRHIGLS----EVSVEEIQRARKVVDIVSVQNRYNLTDRVHEKVLDYCEKENLGFIPWFPLATGGLakpgsTLDSVAKQ 234
Cdd:cd19163 150 KVRFIGITgyplDVLKEVLERSPVKIDTVLSYCHYTLNDTSLLELLPFFKEKGVGVINASPLSMGLL-----TERGPPDW 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1485949817 235 HDATP--------------------AQIALSWLLARSPVMLPIPGTSSVKHLEENLAGAEVKLTKDELA 283
Cdd:cd19163 225 HPASPeikeacakaaaycksrgvdiSKLALQFALSNPDIATTLVGTASPENLRKNLEAAEEPLDAHLLA 293
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-287 |
1.14e-35 |
|
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: 130.46 E-value: 1.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 14 TFKLGG-DLPVHRLGYGAmqltG--PGIWGPpKDRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHPYAKGVV 90
Cdd:cd19104 2 YRRFGRtGLKVSELTFGG----GgiGGLMGR-TTREEQIAAVRRALDLGINFFDTAPSYGDGKSEENLGRALKGLPAGPY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 91 VATKAGLVRTGPNEwhpvgAPKYLRQQLEMSLRRLKLERIDLYQLH-RI--------DPKVPVEESLGE------LKALQ 155
Cdd:cd19104 77 ITTKVRLDPDDLGD-----IGGQIERSVEKSLKRLKRDSVDLLQLHnRIgderdkpvGGTLSTTDVLGLggvadaFERLR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 156 KEGKIRHIGLSEVSVEEIqrARKVVD---IVSVQNRYNLTD--------RVHE-----KVLDYCEKENLGFIPWFPLATG 219
Cdd:cd19104 152 SEGKIRFIGITGLGNPPA--IRELLDsgkFDAVQVYYNLLNpsaaearpRGWSaqdygGIIDAAAEHGVGVMGIRVLAAG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 220 GLAKPGST---------------------LDSVAKQHDATPAQIALSWLLARSPVMLPIPGTSSVKHLEENLAGAEV-KL 277
Cdd:cd19104 230 ALTTSLDRgreapptsdsdvaidfrraaaFRALAREWGETLAQLAHRFALSNPGVSTVLVGVKNREELEEAVAAEAAgPL 309
|
330
....*....|
gi 1485949817 278 TKDELAAVDA 287
Cdd:cd19104 310 PAENLARLEA 319
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
49-287 |
2.45e-34 |
|
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: 124.77 E-value: 2.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 49 VRVLRRALELGVDFIDTADSYGpyvSEEIIAEALHpyAKGV-----VVATKAGLVRTGPNEwhpvgapkyLRQQLEMSLR 123
Cdd:cd19139 17 IDSVRTALELGYRHIDTAQIYD---NEAAVGQAIA--ESGVprdelFITTKIWIDNLSKDK---------LLPSLEESLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 124 RLKLERIDLYQLH--RIDPKVPVEESLGELKALQKEGKIRHIGLSEVSVEEIQRARKVV---DIVS--------VQNRyn 190
Cdd:cd19139 83 KLRTDYVDLTLIHwpSPNDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVgagAIATnqielspyLQNR-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 191 ltdrvheKVLDYCEKENLGFIPWFPLATGGLAKpGSTLDSVAKQHDATPAQIALSWLLARSpvMLPIPGTSSVKHLEENL 270
Cdd:cd19139 161 -------KLVAHCKQHGIHVTSYMTLAYGKVLD-DPVLAAIAERHGATPAQIALAWAMARG--YAVIPSSTKREHLRSNL 230
|
250
....*....|....*..
gi 1485949817 271 AGAEVKLTKDELAAVDA 287
Cdd:cd19139 231 LALDLTLDADDMAAIAA 247
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
51-283 |
7.61e-34 |
|
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
Pssm-ID: 381376 [Multi-domain] Cd Length: 309 Bit Score: 125.26 E-value: 7.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 51 VLRRALELGVDFIDTADSYGP-YVSEE-----IIAEALHPYAKGVVVATKAGL-VRTGP-NEWhpvGAPKYLRQQLEMSL 122
Cdd:cd19150 35 ILRTAFDLGITHFDLANNYGPpPGSAEenfgrILREDFAGYRDELIISTKAGYdMWPGPyGEW---GSRKYLLASLDQSL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 123 RRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSEVSVEeiqRARKVVDIVSV--------QNRYNLTDR 194
Cdd:cd19150 112 KRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYSPE---RTREAAAILRElgtpllihQPSYNMLNR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 195 VHEK--VLDYCEKENLGFIPWFPLATGGL--------------AKPGS---------------TLDSVAKQHDATPAQIA 243
Cdd:cd19150 189 WVEEsgLLDTLQELGVGCIAFTPLAQGLLtdkylngipegsraSKERSlspkmlteanlnsirALNEIAQKRGQSLAQMA 268
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1485949817 244 LSWLLARSPVMLPIPGTSSVKHLEENLAGAE-VKLTKDELA 283
Cdd:cd19150 269 LAWVLRDGRVTSALIGASRPEQLEENVGALDnLTFSADELA 309
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
21-287 |
1.29e-31 |
|
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381369 [Multi-domain] Cd Length: 319 Bit Score: 119.62 E-value: 1.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 21 LPVHRLGYGAMqLTgpgiWGPPKDRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHPYA---KGVVVATKA-- 95
Cdd:cd19143 11 LKVSALSFGSW-VT----FGNQVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELGwprSDYVVSTKIfw 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 96 GLVRTGPNEwhpVG-APKYLRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSEVSVEEIQ 174
Cdd:cd19143 86 GGGGPPPND---RGlSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGTSEWSAQQIE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 175 RARKVVDIVSV------QNRYNLTDRvhEKV-LDY---CEKENLGFIPWFPLATGGL-------AKPGS----------- 226
Cdd:cd19143 163 EAHEIADRLGLippvmeQPQYNLFHR--ERVeVEYaplYEKYGLGTTTWSPLASGLLtgkynngIPEGSrlalpgyewlk 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1485949817 227 ---------------TLDSVAKQHDATPAQIALSWLLARSPVMLPIPGTSSVKHLEENLAGAEV--KLTKDELAAVDA 287
Cdd:cd19143 241 drkeelgqekiekvrKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEENLKALEVlpKLTPEVMEKIEA 318
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
51-286 |
2.60e-31 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 119.32 E-value: 2.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 51 VLRRALELGVDFIDTADSYGPY--VSEE----IIAEALHPYAKGVVVATKAGLvRTGPNEWHPVGAPKYLRQQLEMSLRR 124
Cdd:PRK09912 48 ILRKAFDLGITHFDLANNYGPPpgSAEEnfgrLLREDFAAYRDELIISTKAGY-DMWPGPYGSGGSRKYLLASLDQSLKR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 125 LKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSEVSVEEIQRARKV-----VDIVSVQNRYNLTDRVHEK- 198
Cdd:PRK09912 127 MGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPERTQKMVELlrewkIPLLIHQPSYNLLNRWVDKs 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 199 -VLDYCEKENLGFIPWFPLATG------------------------GLAKPGST---------LDSVAKQHDATPAQIAL 244
Cdd:PRK09912 207 gLLDTLQNNGVGCIAFTPLAQGlltgkylngipqdsrmhregnkvrGLTPKMLTeanlnslrlLNEMAQQRGQSMAQMAL 286
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1485949817 245 SWLLARSPVMLPIPGTSSVKHLEENLAG-AEVKLTKDELAAVD 286
Cdd:PRK09912 287 SWLLKDERVTSVLIGASRAEQLEENVQAlNNLTFSTEELAQID 329
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
21-271 |
3.58e-31 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 118.19 E-value: 3.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 21 LPVHRLGYGaMQLTGPGiwgpPKDRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHPYAKG-------VVVAT 93
Cdd:cd19099 1 LTLSSLGLG-TYRGDSD----DETDEEYREALKAALDSGINVIDTAINYRGGRSERLIGKALRELIEKggikrdeVVIVT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 94 KAGLV------RTGPNEWHPVGA------------------PKYLRQQLEMSLRRLKLERIDLYQLH-------RIDPKV 142
Cdd:cd19099 76 KAGYIpgdgdePLRPLKYLEEKLgrglidvadsaglrhcisPAYLEDQIERSLKRLGLDTIDLYLLHnpeeqllELGEEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 143 P---VEESLGELKALQKEGKIRHIGlseVSVEEIQRA----------RKVVDIV-----------SVQNRYNL------T 192
Cdd:cd19099 156 FydrLEEAFEALEEAVAEGKIRYYG---ISTWDGFRAppalpghlslEKLVAAAeevggdnhhfkVIQLPLNLlepealT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 193 DRVHEK-----VLDYCEKENLGFIPWFPLATGGLAKPGSTLDSVAKQHDATPAQIALSWLLARSPVMLPIPGTSSVKHLE 267
Cdd:cd19099 233 EKNTVKgealsLLEAAKELGLGVIASRPLNQGQLLGELRLADLLALPGGATLAQRALQFARSTPGVDSALVGMRRPEHVD 312
|
....
gi 1485949817 268 ENLA 271
Cdd:cd19099 313 ENLA 316
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
44-271 |
2.35e-28 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 109.54 E-value: 2.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 44 DRAEAVRVLRRALELGVDFIDTADSYGpyVSEEIIAEALHPYaKGVVVATKaglvrTGPNEWHPVGAPKYLRQQLEMSLR 123
Cdd:cd19097 24 SEKEAKKILEYALKAGINTLDTAPAYG--DSEKVLGKFLKRL-DKFKIITK-----LPPLKEDKKEDEAAIEASVEASLK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 124 RLKLERIDLYQLHRI-DPKVPVEESLGELKALQKEGKIRHIGLSEVSVEEIQRARKVVDIVSVQNRYNLTDR--VHEKVL 200
Cdd:cd19097 96 RLKVDSLDGLLLHNPdDLLKHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKALESFKIDIIQLPFNILDQrfLKSGLL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 201 DYCEKENLGFI------------------PWFPLATGGLAKpgstLDSVAKQHDATPAQIALSWLLARSPVMLPIPGTSS 262
Cdd:cd19097 176 AKLKKKGIEIHarsvflqglllmepdklpAKFAPAKPLLKK----LHELAKKLGLSPLELALGFVLSLPEIDKIVVGVDS 251
|
....*....
gi 1485949817 263 VKHLEENLA 271
Cdd:cd19097 252 LEQLKEIIA 260
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
22-287 |
4.31e-28 |
|
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: 109.68 E-value: 4.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 22 PVHRLGYG-AMQLTGPGIWGPPKDRaEAVRVLRRALELGVDFIDTADSYGpyvSEEIIAEALHP-YAKGVV------VAT 93
Cdd:cd19116 1 PTIKLNDGnEIPAIALGTWKLKDDE-GVRQAVKHAIEAGYRHIDTAYLYG---NEAEVGEAIREkIAEGVVkredlfITT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 94 KAglvrtgpneWHPVGAPKYLRQQLEMSLRRLKLERIDLYQLH----------------RIDPKVPVEESLGELKALQKE 157
Cdd:cd19116 77 KL---------WNSYHEREQVEPALRESLKRLGLDYVDLYLIHwpvafkenndsesngdGSLSDIDYLETWRGMEDLVKL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 158 GKIRHIGLSEVSVEEIQRARKVVDIVSVQNRY----NLTdrvHEKVLDYCEKENL---GFIPW-FPLATGGLAKP----G 225
Cdd:cd19116 148 GLTRSIGVSNFNSEQINRLLSNCNIKPAVNQIevhpTLT---QEKLVAYCQSNGIvvmAYSPFgRLVPRGQTNPPprldD 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1485949817 226 STLDSVAKQHDATPAQIALSWLLARSPVmlPIPGTSSVKHLEENLAGAEVKLTKDELAAVDA 287
Cdd:cd19116 225 PTLVAIAKKYGKTTAQIVLRYLIDRGVV--PIPKSSNKKRIKENIDIFDFQLTPEEVAALNS 284
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
44-287 |
1.46e-27 |
|
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins; Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis.
Pssm-ID: 381372 [Multi-domain] Cd Length: 326 Bit Score: 108.67 E-value: 1.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 44 DRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAE--ALHPYAKGVVVATK--AGLVRTGPNEW---HPVGAPKYLRQ 116
Cdd:cd19146 33 DKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEwmASRGNRDEMVLATKytTGYRRGGPIKIksnYQGNHAKSLRL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 117 QLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSE------VSVEEIQRARKVVDIVSVQNRYN 190
Cdd:cd19146 113 SVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSDtpawvvSKANAYARAHGLTQFVVYQGHWS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 191 LTDRVHEK-VLDYCEKENLGFIPWFPLATGGLA-----------------------KPGSTLDSVAKQHDATPAQIALSW 246
Cdd:cd19146 193 AAFRDFERdILPMCEAEGMALAPWGVLGQGQFRteeefkrrgrsgrkggpqtekerKVSEKLEKVAEEKGTAITSVALAY 272
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1485949817 247 LLARSPVMLPIPGTSSVKHLEENLAGAEVKLTKDELAAVDA 287
Cdd:cd19146 273 VMHKAPYVFPIVGGRKVEHLKGNIEALGISLSDEEIQEIED 313
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
31-286 |
1.48e-27 |
|
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: 107.97 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 31 MQLTGPGIW-GPPKDRAEAVRVlrrALELGVDFIDTADSYGpyvSEEIIAEALHPYAKGVVVATKAGLVRTgpnEWHPVG 109
Cdd:cd19111 4 MPVIGLGTYqSPPEEVRAAVDY---ALFVGYRHIDTALSYQ---NEKAIGEALKWWLKNGKLKREEVFITT---KLPPVY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 110 -APKYLRQQLEMSLRRLKLERIDLYQLH-------------RIDPKVPVEESLGELKALQKEGKIRHIGLSEVSVEEIQR 175
Cdd:cd19111 75 lEFKDTEKSLEKSLENLKLPYVDLYLIHhpcgfvnkkdkgeRELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 176 ARKV--VDIVSVQNRYNLTDRVHEKVlDYCEKENLGFIPWFPLATGGLA---KPGSTLD--------SVAKQHDATPAQI 242
Cdd:cd19111 155 ILAYakVKPSNLQLECHAYLQQRELR-KFCNKKNIVVTAYAPLGSPGRAnqsLWPDQPDlledptvlAIAKELDKTPAQV 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1485949817 243 ALSWLLARSPVmlPIPGTSSVKHLEENLAGAEVKLTKDELAAVD 286
Cdd:cd19111 234 LLRFVLQRGTG--VLPKSTNKERIEENFEVFDFELTEEHFKKLK 275
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
25-271 |
1.64e-27 |
|
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: 107.83 E-value: 1.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 25 RLGYGAMQLTGPGIWGppkdRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHPYAK-GVVVATKAGLVRTGPN 103
Cdd:cd19162 2 RLGLGAASLGNLARAG----EDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALARHPRaEYVVSTKVGRLLEPGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 104 EWHPVGAPKYL-------RQQLEMSLRRLKLERIDLYQLHRIDPK--VPVEESLGELKALQKEGKIRHIGLSEVSVEEIQ 174
Cdd:cd19162 78 AGRPAGADRRFdfsadgiRRSIEASLERLGLDRLDLVFLHDPDRHllQALTDAFPALEELRAEGVVGAIGVGVTDWAALL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 175 RA--RKVVDIVSVQNRYNLTDR-VHEKVLDYCEKENLGFIPWFPLATGGLAK---PGSTLDS----------------VA 232
Cdd:cd19162 158 RAarRADVDVVMVAGRYTLLDRrAATELLPLCAAKGVAVVAAGVFNSGILATddpAGDRYDYrpatpevlararrlaaVC 237
|
250 260 270
....*....|....*....|....*....|....*....
gi 1485949817 233 KQHDATPAQIALSWLLARSPVMLPIPGTSSVKHLEENLA 271
Cdd:cd19162 238 RRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLA 276
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
32-285 |
2.23e-27 |
|
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: 106.69 E-value: 2.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 32 QLtGPGIWGPPKDraEAVRVLRRALELGVDFIDTADSYGpyvSEEIIAEALHpyAKGV-----VVATKAglvrtgpneWH 106
Cdd:cd19131 12 QL-GLGVWQVSND--EAASAVREALEVGYRSIDTAAIYG---NEEGVGKAIR--ASGVpreelFITTKL---------WN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 107 PVGAPKYLRQQLEMSLRRLKLERIDLYQLH----RIDPKVpveESLGELKALQKEGKIRHIGLSEVSVEEIQRARKVVDI 182
Cdd:cd19131 75 SDQGYDSTLRAFDESLRKLGLDYVDLYLIHwpvpAQDKYV---ETWKALIELKKEGRVKSIGVSNFTIEHLQRLIDETGV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 183 VSVQNRYNLTDRVHEKVL-DYCEKENLGFIPWFPLATGG-LAKPgsTLDSVAKQHDATPAQIALSWLLARSPVMlpIPGT 260
Cdd:cd19131 152 VPVVNQIELHPRFQQRELrAFHAKHGIQTESWSPLGQGGlLSDP--VIGEIAEKHGKTPAQVVIRWHLQNGLVV--IPKS 227
|
250 260
....*....|....*....|....*
gi 1485949817 261 SSVKHLEENLAGAEVKLTKDELAAV 285
Cdd:cd19131 228 VTPSRIAENFDVFDFELDADDMQAI 252
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
18-287 |
1.64e-26 |
|
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: 104.62 E-value: 1.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 18 GGDLPVhrLGYGamqlTGPGIWGPPKDRA--EAVRVLRRALELGVDFIDTADSYGpyvSEEIIAEALHPY---AKGVVVA 92
Cdd:cd19120 1 GSKIPA--IAFG----TGTAWYKSGDDDIqrDLVDSVKLALKAGFRHIDTAEMYG---NEKEVGEALKESgvpREDLFIT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 93 TKaglvrTGPNEWHPVGApkylrqqLEMSLRRLKLERIDLYQLH---RIDPKVP-VEESLGELKALQKEGKIRHIGLSEV 168
Cdd:cd19120 72 TK-----VSPGIKDPREA-------LRKSLAKLGVDYVDLYLIHspfFAKEGGPtLAEAWAELEALKDAGLVRSIGVSNF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 169 SVEEIQRARKVVDIVSVQNR-----YNLTDrvHEKVLDYCEKENL---GFIPWFPL--ATGGLAKPgsTLDSVAKQHDAT 238
Cdd:cd19120 140 RIEDLEELLDTAKIKPAVNQiefhpYLYPQ--QPALLEYCREHGIvvsAYSPLSPLtrDAGGPLDP--VLEKIAEKYGVT 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1485949817 239 PAQIALSWLLARSpvmlPIPGTSSVK--HLEENLAGAEVKLTKDELAAVDA 287
Cdd:cd19120 216 PAQVLLRWALQKG----IVVVTTSSKeeRMKEYLEAFDFELTEEEVEEIDK 262
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
14-287 |
3.04e-25 |
|
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: 102.11 E-value: 3.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 14 TFKLGGDLPVhrLGYGAMQLTGpgiwgppkdrAEAVRVLRRALELGVDFIDTADSYGpyvSEEIIAEALHPY-AKGVV-- 90
Cdd:cd19154 5 TLSNGVKMPL--IGLGTWQSKG----------AEGITAVRTALKAGYRLIDTAFLYQ---NEEAIGEALAELlEEGVVkr 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 91 ----VATKAGLVRTgpnewhpvgAPKYLRQQLEMSLRRLKLERIDLYQLH-------------------RIDPKVPVEES 147
Cdd:cd19154 70 edlfITTKLWTHEH---------APEDVEEALRESLKKLQLEYVDLYLIHapaafkddegesgtmengmSIHDAVDVEDV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 148 LGELKALQKEGKIRHIGLSEVSVEEIQRARKV--VDIVSVQNRYNLTDRVHEKVlDYCEKENLGFIPWFPLAT------- 218
Cdd:cd19154 141 WRGMEKVYDEGLTKAIGVSNFNNDQIQRILDNarVKPHNNQVECHLYFPQKELV-EFCKKHNISVTSYATLGSpgranft 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1485949817 219 --GGLAKPGSTLD-----SVAKQHDATPAQIALSWLLARSpvMLPIPGTSSVKHLEENLAGAEVKLTKDELAAVDA 287
Cdd:cd19154 220 ksTGVSPAPNLLQdpivkAIAEKHGKTPAQVLLRYLLQRG--IAVIPKSATPSRIKENFNIFDFSLSEEDMATLEE 293
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
18-287 |
4.28e-25 |
|
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: 100.42 E-value: 4.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 18 GGDLPvhRLGYGAMQLTGpgiwgppkdrAEAVRVLRRALELGVDFIDTADSYGpyvSEEIIAEALHpyAKGV-----VVA 92
Cdd:cd19132 4 GTQIP--AIGFGTYPLKG----------DEGVEAVVAALQAGYRLLDTAFNYE---NEGAVGEAVR--RSGVpreelFVT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 93 TKAglvrtgPNEWHPVGApkyLRQQLEMSLRRLKLERIDLYQLHRIDPKVPVE-ESLGELKALQKEGKIRHIGLSEVSVE 171
Cdd:cd19132 67 TKL------PGRHHGYEE---ALRTIEESLYRLGLDYVDLYLIHWPNPSRDLYvEAWQALIEAREEGLVRSIGVSNFLPE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 172 EIQRARKVVDIVSVQNRYNLtdrvH-----EKVLDYCEKENLGFIPWFPLATGGLAKPGSTLDSVAKQHDATPAQIALSW 246
Cdd:cd19132 138 HLDRLIDETGVTPAVNQIEL----HpyfpqAEQRAYHREHGIVTQSWSPLGRGSGLLDEPVIKAIAEKHGKTPAQVVLRW 213
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1485949817 247 LLARSpvMLPIPGTSSVKHLEENLAGAEVKLTKDELAAVDA 287
Cdd:cd19132 214 HVQLG--VVPIPKSANPERQRENLAIFDFELSDEDMAAIAA 252
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
52-287 |
2.01e-24 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 98.94 E-value: 2.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 52 LRRALELGVDFIDTADSYGpyvSEEIIAEALHpyAKGVV-----VATKAglvrtgpneWHPVGAPKYLRQQLEMSLRRLK 126
Cdd:PRK11172 22 VKTALELGYRAIDTAQIYD---NEAAVGQAIA--ESGVPrdelfITTKI---------WIDNLAKDKLIPSLKESLQKLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 127 LERIDLYQLHRIDPK--VPVEESLGELKALQKEGKIRHIGLSEVSVEEIQRARKVV---DIVS--------VQNRynltd 193
Cdd:PRK11172 88 TDYVDLTLIHWPSPNdeVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQAIAAVgaeNIATnqielspyLQNR----- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 194 rvheKVLDYCEKENLGFIPWFPLATGG-LAKPgsTLDSVAKQHDATPAQIALSWLLARSpvMLPIPGTSSVKHLEENLAG 272
Cdd:PRK11172 163 ----KVVAFAKEHGIHVTSYMTLAYGKvLKDP--VIARIAAKHNATPAQVILAWAMQLG--YSVIPSSTKRENLASNLLA 234
|
250
....*....|....*
gi 1485949817 273 AEVKLTKDELAAVDA 287
Cdd:PRK11172 235 QDLQLDAEDMAAIAA 249
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
26-287 |
3.86e-24 |
|
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: 98.09 E-value: 3.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 26 LGYGAMQLtgpgiwgppKDRAEAVRVLRRALELGVDFIDTADSYGpyvSEEIIAEAL---HPyakgvvvatKAGLVRT-- 100
Cdd:cd19136 4 LGLGTFRL---------RGEEEVRQAVDAALKAGYRLIDTASVYR---NEADIGKALrdlLP---------KYGLSREdi 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 101 ------GPNEWHPVGApkylRQQLEMSLRRLKLERIDLYQLH-----RIDPKVPVE-----ESLGELKALQKEGKIRHIG 164
Cdd:cd19136 63 fitsklAPKDQGYEKA----RAACLGSLERLGTDYLDLYLIHwpgvqGLKPSDPRNaelrrESWRALEDLYKEGKLRAIG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 165 LSEVSVEEIQRARKVVDIV-SV-QNRYNlTDRVHEKVLDYCEKENLGFIPWFPLATGGLAKPG-STLDSVAKQHDATPAQ 241
Cdd:cd19136 139 VSNYTVRHLEELLKYCEVPpAVnQVEFH-PHLVQKELLKFCKDHGIHLQAYSSLGSGDLRLLEdPTVLAIAKKYGRTPAQ 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1485949817 242 IALSWLLARSPVMlpIPGTSSVKHLEENLAGAEVKLTKDELAAVDA 287
Cdd:cd19136 218 VLLRWALQQGIGV--IPKSTNPERIAENIKVFDFELSEEDMAELNA 261
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
31-287 |
1.11e-23 |
|
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: 97.87 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 31 MQLTGPGIWGPPKdrAEAVRVLRRALELGVDFIDTADSYGpyvSEEIIAEAL-HPYAKGVVvaTKAGLVRTGpNEWHPVG 109
Cdd:cd19123 12 IPALGLGTWKSKP--GEVGQAVKQALEAGYRHIDCAAIYG---NEAEIGAALaEVFKEGKV--KREDLWITS-KLWNNSH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 110 APKYLRQQLEMSLRRLKLERIDLYQLH-------------------RIDPkVPVEESLGELKALQKEGKIRHIGLSEVSV 170
Cdd:cd19123 84 APEDVLPALEKTLADLQLDYLDLYLMHwpvalkkgvgfpesgedllSLSP-IPLEDTWRAMEELVDKGLCRHIGVSNFSV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 171 EEIQRARKVVDIVSVQNRYNLTDRVHE-KVLDYCEKENLGFIPWFPLATGG-------------LAKPgsTLDSVAKQHD 236
Cdd:cd19123 163 KKLEDLLATARIKPAVNQVELHPYLQQpELLAFCRDNGIHLTAYSPLGSGDrpaamkaegepvlLEDP--VINKIAEKHG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1485949817 237 ATPAQIALSWLLARSPVMlpIPGTSSVKHLEENLAGAEVKLTKDELAAVDA 287
Cdd:cd19123 241 ASPAQVLIAWAIQRGTVV--IPKSVNPERIQQNLEAAEVELDASDMATIAA 289
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
24-276 |
3.04e-23 |
|
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381378 [Multi-domain] Cd Length: 308 Bit Score: 96.52 E-value: 3.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 24 HRLGYGamqlTGP--GIWGPPKDrAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHPYAKG-VVVATKAGLVRT 100
Cdd:cd19152 1 PKLGFG----TAPlgNLYEAVSD-EEAKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELGREdYVISTKVGRLLV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 101 GPNEWHP---VGAPKYL-------------RQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESL-----------GELKA 153
Cdd:cd19152 76 PLQEVEPtfePGFWNPLpfdavfdysydgiLRSIEDSLQRLGLSRIDLLSIHDPDEDLAGAESDehfaqaikgafRALEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 154 LQKEGKIRHIGLSEVSVEEIQRARKVV--DIVSVQNRYNLTDRVHEK-VLDYCEKENLGFIPWFPLATGGLA-------K 223
Cdd:cd19152 156 LREEGVIKAIGLGVNDWEVILRILEEAdlDWVMLAGRYTLLDHSAAReLLPECEKRGVKVVNAGPFNSGFLAggdnfdyY 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1485949817 224 PGSTLD-----------SVAKQHDATPAQIALSWLLARSPVMLPIPGTSSVKHLEENLAGAEVK 276
Cdd:cd19152 236 EYGPAPpeliarrdrieALCEQHGVSLAAAALQFALAPPAVASVAPGASSPERVEENVALLATE 299
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
31-287 |
4.61e-22 |
|
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: 92.84 E-value: 4.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 31 MQLTGPGIWGPPKDRaEAVRVLRRALELGVDFIDTADSYGpyvSEEIIAEALhpyakgvvvatKAGLVrtgPNE------ 104
Cdd:cd19157 10 MPWLGLGVFKVEEGS-EVVNAVKTALKNGYRSIDTAAIYG---NEEGVGKGI-----------KESGI---PREelfits 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 105 --WHP-VGAPKYLrQQLEMSLRRLKLERIDLYQLHRidpkvPVEESLGE----LKALQKEGKIRHIGLSEVSVEEIQRAR 177
Cdd:cd19157 72 kvWNAdQGYDSTL-KAFEASLERLGLDYLDLYLIHW-----PVKGKYKEtwkaLEKLYKDGRVRAIGVSNFQVHHLEDLL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 178 KVVDIVSVQNRYNLTDR-VHEKVLDYCEKENLGFIPWFPLATGG-LAKPgsTLDSVAKQHDATPAQIALSWLLARSPVML 255
Cdd:cd19157 146 ADAEIVPMVNQVEFHPRlTQKELRDYCKKQGIQLEAWSPLMQGQlLDNP--VLKEIAEKYNKSVAQVILRWDLQNGVVTI 223
|
250 260 270
....*....|....*....|....*....|...
gi 1485949817 256 PipgTSSVKH-LEENLAGAEVKLTKDELAAVDA 287
Cdd:cd19157 224 P---KSIKEHrIIENADVFDFELSQEDMDKIDA 253
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
12-287 |
1.55e-21 |
|
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: 91.13 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 12 SGTFKLGGDLPvhRLGYGAMQLtgpgiwgPPKDRAEAVRVlrrALELGVDFIDTADSYGpyvSEEIIAEALHpyAKGV-- 89
Cdd:cd19130 1 SIVLNDGNSIP--QLGYGVFKV-------PPADTQRAVAT---ALEVGYRHIDTAAIYG---NEEGVGAAIA--ASGIpr 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 90 ---VVATKAGLVRTGPNEwhpvgapkyLRQQLEMSLRRLKLERIDLYQLHRIDPK----VPVEESLGELKAlqkEGKIRH 162
Cdd:cd19130 64 delFVTTKLWNDRHDGDE---------PAAAFAESLAKLGLDQVDLYLVHWPTPAagnyVHTWEAMIELRA---AGRTRS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 163 IGLSEVSVEEIQRARKVVDIVSVQNRYNLTDRVHEKVL-DYCEKENLGFIPWFPLATGGLAKpGSTLDSVAKQHDATPAQ 241
Cdd:cd19130 132 IGVSNFLPPHLERIVAATGVVPAVNQIELHPAYQQRTIrDWAQAHDVKIEAWSPLGQGKLLG-DPPVGAIAAAHGKTPAQ 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1485949817 242 IALSWLLARSPVMlpIPGTSSVKHLEENLAGAEVKLTKDELAAVDA 287
Cdd:cd19130 211 IVLRWHLQKGHVV--FPKSVRRERMEDNLDVFDFDLTDTEIAAIDA 254
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
18-287 |
5.96e-21 |
|
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: 89.56 E-value: 5.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 18 GGDLPVhrLGYGAMQLTGPgiwgppkdrAEAVRVLRRALELGVDFIDTADSYGpyvSEEIIAEALHpyAKGV-----VVA 92
Cdd:cd19133 6 GVEMPI--LGFGVFQIPDP---------EECERAVLEAIKAGYRLIDTAAAYG---NEEAVGRAIK--KSGIpreelFIT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 93 TKAGLVRTGPNewhpvGAPKylrqQLEMSLRRLKLERIDLYQLHRidPKVPVEESLGELKALQKEGKIRHIGLSEVSVEE 172
Cdd:cd19133 70 TKLWIQDAGYE-----KAKK----AFERSLKRLGLDYLDLYLIHQ--PFGDVYGAWRAMEELYKEGKIRAIGVSNFYPDR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 173 IQRARKVVDIVSVQNRYNLtdrvH-----EKVLDYCEKENLGFIPWFPLATG--GLAKpGSTLDSVAKQHDATPAQIALS 245
Cdd:cd19133 139 LVDLILHNEVKPAVNQIET----HpfnqqIEAVEFLKKYGVQIEAWGPFAEGrnNLFE-NPVLTEIAEKYGKSVAQVILR 213
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1485949817 246 WLLARSPVMlpIPGTSSVKHLEENLAGAEVKLTKDELAAVDA 287
Cdd:cd19133 214 WLIQRGIVV--IPKSVRPERIAENFDIFDFELSDEDMEAIAA 253
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
57-287 |
5.96e-21 |
|
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: 89.69 E-value: 5.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 57 ELGVDFIDTADSYGpyvSEEIIAEALHpyAKGV-----VVATKAglvrtgpneWHPVGAPKYLRQQLEMSLRRLKLERID 131
Cdd:cd19135 37 ECGYRHIDTAKRYG---CEELLGKAIK--ESGVpredlFLTTKL---------WPSDYGYESTKQAFEASLKRLGVDYLD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 132 LYQLHRIDPKVPV-------EESLGELKALQKEGKIRHIGLSEVSVEEIQRARKVVDIVSV--QNRYNLTDRvHEKVLDY 202
Cdd:cd19135 103 LYLLHWPDCPSSGknvketrAETWRALEELYDEGLCRAIGVSNFLIEHLEQLLEDCSVVPHvnQVEFHPFQN-PVELIEY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 203 CEKENLGFIPWFPLATG-GLAKPgsTLDSVAKQHDATPAQIALSWLLARSPVMlpIPGTSSVKHLEENLAGAEVKLTKDE 281
Cdd:cd19135 182 CRDNNIVFEGYCPLAKGkALEEP--TVTELAKKYQKTPAQILIRWSIQNGVVT--IPKSTKEERIKENCQVFDFSLSEED 257
|
....*.
gi 1485949817 282 LAAVDA 287
Cdd:cd19135 258 MATLDS 263
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
31-287 |
6.69e-21 |
|
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes prostaglandin F2-alpha synthase (PGFS) from Leishmania major (AKR5A1) and Trypanosoma brucei (AKR5A2). PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity for synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde. The AKR5G family of AKR includes Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase, which corresponds to aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381352 [Multi-domain] Cd Length: 254 Bit Score: 89.42 E-value: 6.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 31 MQLTGPGIWGPPKDRaEAVRVLRRALELGVDFIDTAdsyGPYVSEEIIAEALHpyAKGV-----VVATKAglvrtgpneW 105
Cdd:cd19126 9 MPWLGLGVFQTPDGD-ETERAVQTALENGYRSIDTA---AIYKNEEGVGEAIR--ESGVpreelFVTTKL---------W 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 106 HPVGAPKYLRQQLEMSLRRLKLERIDLYQLHRidpkvPVEESLGE----LKALQKEGKIRHIGLSEVSVEEIQRARKVVD 181
Cdd:cd19126 74 NDDQRARRTEDAFQESLDRLGLDYVDLYLIHW-----PGKDKFIDtwkaLEKLYASGKVKAIGVSNFQEHHLEELLAHAD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 182 IVSVQNRYNLTDR-VHEKVLDYCEKENLGFIPWFPLATGGLAKpGSTLDSVAKQHDATPAQIALSWLLARSPVMlpIPGT 260
Cdd:cd19126 149 VVPAVNQVEFHPYlTQKELRGYCKSKGIVVEAWSPLGQGGLLS-NPVLAAIGEKYGKSAAQVVLRWDIQHGVVT--IPKS 225
|
250 260
....*....|....*....|....*..
gi 1485949817 261 SSVKHLEENLAGAEVKLTKDELAAVDA 287
Cdd:cd19126 226 VHASRIKENADIFDFELSEDDMTAIDA 252
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
21-287 |
8.13e-21 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 90.68 E-value: 8.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 21 LPVHRLGYGAMQltgpgiWGPPKDRAEAVRVLRRALELGVDFIDTADSYgPY--------VSEEIIAEALHPYA--KGVV 90
Cdd:PRK10625 11 LEVSTLGLGTMT------FGEQNSEADAHAQLDYAVAQGINLIDVAEMY-PVpprpetqgLTETYIGNWLAKRGsrEKLI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 91 VATK-AGLVRTGPNEWHPVGA--PKYLRQQLEMSLRRLKLERIDLYQLH-----------------RIDPKVPVEESLGE 150
Cdd:PRK10625 84 IASKvSGPSRNNDKGIRPNQAldRKNIREALHDSLKRLQTDYLDLYQVHwpqrptncfgklgyswtDSAPAVSLLETLDA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 151 LKALQKEGKIRHIGLSEVSVEEIQRARKVVD------IVSVQNRYNLTDRVHEKVL-DYCEKENLGFIPWFPLATGGL-- 221
Cdd:PRK10625 164 LAEQQRAGKIRYIGVSNETAFGVMRYLHLAEkhdlprIVTIQNPYSLLNRSFEVGLaEVSQYEGVELLAYSCLAFGTLtg 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 222 -----AKPG---STLDS-------------------VAKQHDATPAQIALSWLLARSPVMLPIPGTSSVKHLEENLAGAE 274
Cdd:PRK10625 244 kylngAKPAgarNTLFSrftrysgeqtqkavaayvdIAKRHGLDPAQMALAFVRRQPFVASTLLGATTMEQLKTNIESLH 323
|
330
....*....|...
gi 1485949817 275 VKLTKDELAAVDA 287
Cdd:PRK10625 324 LTLSEEVLAEIEA 336
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
16-274 |
9.67e-20 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 87.14 E-value: 9.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 16 KLGGD-LPVHRLGYGAMQLTGpgIWGPPKdRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHPYA---KGVVV 91
Cdd:PLN02587 3 ELGSTgLKVSSVGFGASPLGS--VFGPVS-EEDAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKALGiprEKYVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 92 ATKAGLVRTGPNewhpVGAPKYLRqQLEMSLRRLKLERIDLYQLHRID----PKVpVEESLGELKALQKEGKIRHIGLSE 167
Cdd:PLN02587 80 STKCGRYGEGFD----FSAERVTK-SVDESLARLQLDYVDILHCHDIEfgslDQI-VNETIPALQKLKESGKVRFIGITG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 168 VSVE----EIQRARK-VVDIVSVQNRYNLTDRVHEKVLDYCEKENLGFIPWFPLATGGLAKPG---------------ST 227
Cdd:PLN02587 154 LPLAiftyVLDRVPPgTVDVILSYCHYSLNDSSLEDLLPYLKSKGVGVISASPLAMGLLTENGppewhpappelksacAA 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1485949817 228 LDSVAKQHDATPAQIALSWLLARSPVMLPIPGTSSVKHLEENLAGAE 274
Cdd:PLN02587 234 AATHCKEKGKNISKLALQYSLSNKDISTTLVGMNSVQQVEENVAAAT 280
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
42-286 |
1.41e-19 |
|
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; Phanerochaete chrysosporium ADD (EC1.1.1.91) is a founding member of aldo-keto reductase family 9 member A3. It is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). This family also includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381373 [Multi-domain] Cd Length: 319 Bit Score: 86.80 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 42 PKDRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAE--ALHPYAKGVVVATK------AGLVRTGPNEWHPVGAPKY 113
Cdd:cd19147 30 SMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEwmKSRKNRDQIVIATKfttdykAYEVGKGKAVNYCGNHKRS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 114 LRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSEV------SVEEIQRARKVVDIVSVQN 187
Cdd:cd19147 110 LHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDTpawvvsAANYYATAHGKTPFSVYQG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 188 RYNLTDRVHEK-VLDYCEKENLGFIPWFPLATGGLAKP-----------------------------GSTLDSVAKQH-D 236
Cdd:cd19147 190 RWNVLNRDFERdIIPMARHFGMALAPWDVLGGGKFQSKkaveerkkngeglrsfvggteqtpeevkiSEALEKVAEEHgT 269
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1485949817 237 ATPAQIALSWLLARSPVMLPIPGTSSVKHLEENLAGAEVKLTKDELAAVD 286
Cdd:cd19147 270 ESVTAIALAYVRSKAPNVFPLVGGRKIEHLKDNIEALSIKLTPEEIEYLE 319
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
25-285 |
2.69e-19 |
|
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: 85.27 E-value: 2.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 25 RLGYGAMQLtgpgiwgPPKDRAEAVRVlrrALELGVDFIDTADSYGpyvSEEIIAEALHPYAKGVVVATKAGLVRTgpNE 104
Cdd:cd19128 3 RLGFGTYKI-------TESESKEAVKN---AIKAGYRHIDCAYYYG---NEAFIGIAFSEIFKDGGVKREDLFITS--KL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 105 WHPVGAPKYLRQQLEMSLRRLKLERIDLYQLH-------------------RIDPKVPVEESLGELKALQKEGKIRHIGL 165
Cdd:cd19128 68 WPTMHQPENVKEQLLITLQDLQLEYLDLFLIHwplafdmdtdgdprddnqiQSLSKKPLEDTWRAMEQCVDEKLTKNIGV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 166 SEVSVEEIQRARKVVDIVSVQNRYNLTDRV-HEKVLDYCEKENLGFIPWFPL----ATGGLAKPG-STLDSVAKQHDATP 239
Cdd:cd19128 148 SNYSTKLLTDLLNYCKIKPFMNQIECHPYFqNDKLIKFCIENNIHVTAYRPLggsyGDGNLTFLNdSELKALATKYNTTP 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1485949817 240 AQIALSWLLARSPVMLP-IPGTSSVKHLEENLAGAEVKLTKDELAAV 285
Cdd:cd19128 228 PQVIIAWHLQKWPKNYSvIPKSANKSRCQQNFDINDLALTKEDMDAI 274
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
31-287 |
4.13e-19 |
|
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: 84.49 E-value: 4.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 31 MQLTGPGIWGPPkDRAEAVRVLRRALELGVDFIDTADSYGpyvSEEIIAEALHPYA---KGVVVATKAglvrtgpneWHP 107
Cdd:cd19156 9 MPRLGLGVWRVQ-DGAEAENAVKWAIEAGYRHIDTAAIYK---NEEGVGQGIRESGvprEEVFVTTKL---------WNS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 108 VGAPKYLRQQLEMSLRRLKLERIDLYQLHRidpkvPVE----ESLGELKALQKEGKIRHIGLSEVSVEEIQRARKVVDIV 183
Cdd:cd19156 76 DQGYESTLAAFEESLEKLGLDYVDLYLIHW-----PVKgkfkDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCKVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 184 SVQNRYNLTDRVHEKVL-DYCEKENLGFIPWFPLATGGLAKpGSTLDSVAKQHDATPAQIALSWLLARSPVMlpIPGTSS 262
Cdd:cd19156 151 PMVNQIELHPLLTQEPLrKFCKEKNIAVEAWSPLGQGKLLS-NPVLKAIGKKYGKSAAQVIIRWDIQHGIIT--IPKSVH 227
|
250 260
....*....|....*....|....*
gi 1485949817 263 VKHLEENLAGAEVKLTKDELAAVDA 287
Cdd:cd19156 228 EERIQENFDVFDFELTAEEIRQIDG 252
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
31-287 |
5.21e-19 |
|
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: 84.14 E-value: 5.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 31 MQLTGPGIWGPPKDRAEavRVLRRALELGVDFIDTADSYGpyvSEEIIAEALHpyAKGV-----VVATKAglvrtgpneW 105
Cdd:cd19134 11 MPVIGLGVGELSDDEAE--RSVSAALEAGYRLIDTAAAYG---NEAAVGRAIA--ASGIprgelFVTTKL---------A 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 106 HPVGAPKYLRQQLEMSLRRLKLERIDLYQLHRIDPKV-PVEESLGELKALQKEGKIRHIGLSEVSVEEIQRARKVVDIVS 184
Cdd:cd19134 75 TPDQGFTASQAACRASLERLGLDYVDLYLIHWPAGREgKYVDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLTFFTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 185 VQNRYNLTDRVHEKVL-DYCEKENLGFIPWFPLATGGLAKpGSTLDSVAKQHDATPAQIALSWLLARSPVMlpIPGTSSV 263
Cdd:cd19134 155 AVNQIELHPLLNQAELrKVNAQHGIVTQAYSPLGVGRLLD-NPAVTAIAAAHGRTPAQVLLRWSLQLGNVV--ISRSSNP 231
|
250 260
....*....|....*....|....
gi 1485949817 264 KHLEENLAGAEVKLTKDELAAVDA 287
Cdd:cd19134 232 ERIASNLDVFDFELTADHMDALDG 255
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
22-285 |
3.13e-18 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 82.43 E-value: 3.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 22 PVHRLGYGAM--QLtGPGIWGPPKDraEAVRVLRRALELGVDFIDTADSYGpyvSEEIIAEALHPYA---KGVVVATKAG 96
Cdd:PRK11565 5 TVIKLQDGNVmpQL-GLGVWQASNE--EVITAIHKALEVGYRSIDTAAIYK---NEEGVGKALKEASvarEELFITTKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 97 lvrtgpNEWHpvgapKYLRQQLEMSLRRLKLERIDLYQLH----RIDPKVpveESLGELKALQKEGKIRHIGLSEVSVEE 172
Cdd:PRK11565 79 ------NDDH-----KRPREALEESLKKLQLDYVDLYLMHwpvpAIDHYV---EAWKGMIELQKEGLIKSIGVCNFQIHH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 173 IQRARKVVDIVSVQNRYNLTDRVHEKVLD-YCEKENLGFIPWFPLATGGlakpGSTLDS-----VAKQHDATPAQIALSW 246
Cdd:PRK11565 145 LQRLIDETGVTPVINQIELHPLMQQRQLHaWNATHKIQTESWSPLAQGG----KGVFDQkvirdLADKYGKTPAQIVIRW 220
|
250 260 270
....*....|....*....|....*....|....*....
gi 1485949817 247 LLARSpvMLPIPGTSSVKHLEENLAGAEVKLTKDELAAV 285
Cdd:PRK11565 221 HLDSG--LVVIPKSVTPSRIAENFDVFDFRLDKDELGEI 257
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
18-287 |
3.25e-18 |
|
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) is a founding member of the aldo-keto reductase family 5 member B1 (AKR5B1). M6DH (EC 1.1.1.218), also called naloxone reductase, oxidizes the C-6 hydroxy group of morphine and codeine.
Pssm-ID: 381353 [Multi-domain] Cd Length: 268 Bit Score: 82.07 E-value: 3.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 18 GGDLPVhrLGYGAMQLtgpgiwgPPKDRAEAVRVlrrALELGVDFIDTADSYGpyvSEEIIAEALHpyAKGV-----VVA 92
Cdd:cd19127 6 GVEMPA--LGLGVFQT-------PPEETADAVAT---ALADGYRLIDTAAAYG---NEREVGEGIR--RSGVdrsdiFVT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 93 TKAGLVRTGPNEwhpvgapkyLRQQLEMSLRRLKLERIDLYQLHRIDPKVpVEESLGELKALQK---EGKIRHIGLSEVS 169
Cdd:cd19127 69 TKLWISDYGYDK---------ALRGFDASLRRLGLDYVDLYLLHWPVPND-FDRTIQAYKALEKllaEGRVRAIGVSNFT 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 170 VEEIQRARKVVDIVSVQNRYNLTDRVHEKVLDYCEKeNLGFI--PWFPLA------TGGLAKPGSTLD-----SVAKQHD 236
Cdd:cd19127 139 PEHLERLIDATTVVPAVNQVELHPYFSQKDLRAFHR-RLGIVtqAWSPIGgvmrygASGPTGPGDVLQdptitGLAEKYG 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1485949817 237 ATPAQIALSWLLARSpvMLPIPGTSSVKHLEENLAGAEVKLTKDELAAVDA 287
Cdd:cd19127 218 KTPAQIVLRWHLQNG--VSAIPKSVHPERIAENIDIFDFALSAEDMAAIDA 266
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
8-274 |
4.10e-18 |
|
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: 82.20 E-value: 4.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 8 PAEKSGTFKLGgdlpVHRLGYGAMQLTGpgIWGPPKDRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEAL----- 82
Cdd:cd19153 1 FGETLEIALGN----VSPVGLGTAALGG--VYGDGLEQDEAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALaalqv 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 83 --HPYakgvVVATKAGLVRTGPNEWhpvgAPKYLRQQLEMSLRRLKLERIDLYQLHRI---DPKVPVEESLGELKALQKE 157
Cdd:cd19153 75 prSSY----TVATKVGRYRDSEFDY----SAERVRASVATSLERLHTTYLDVVYLHDIefvDYDTLVDEALPALRTLKDE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 158 GKIRHIGLSEVSVEEIQRARKVVDIVSVQ-----NRYNLTDRVHEKVLDYCEKENL-----------------GFIPWFP 215
Cdd:cd19153 147 GVIKRIGIAGYPLDTLTRATRRCSPGSLDavlsyCHLTLQDARLESDAPGLVRGAGphvinasplsmglltsqGPPPWHP 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1485949817 216 lATGGLAKPGSTLDSVAKQHDATPAQIALSWLLA----RSPVMLpipGTSSVKHLEENLAGAE 274
Cdd:cd19153 227 -ASGELRHYAAAADAVCASVEASLPDLALQYSLAahagVGTVLL---GPSSLAQLRSMLAAVD 285
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
49-166 |
4.62e-18 |
|
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: 82.32 E-value: 4.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 49 VRVLRRALELGVDFIDTADSYGPyvSEEIIAEALHPYAKG-----VVVATKAGlvRTGPNEWHPvgAPKYLRQQLEMSLR 123
Cdd:cd19164 37 VDIVRRALELGIRAFDTSPYYGP--SEIILGRALKALRDEfprdtYFIITKVG--RYGPDDFDY--SPEWIRASVERSLR 110
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1485949817 124 RLKLERIDLYQLHRI----DPKvpVEESLGELKALQKEGKIRHIGLS 166
Cdd:cd19164 111 RLHTDYLDLVYLHDVefvaDEE--VLEALKELFKLKDEGKIRNVGIS 155
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
31-286 |
2.85e-17 |
|
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: 80.26 E-value: 2.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 31 MQLTGPGIW-GPPKDRAEAVRVlrrALELGVDFIDTADSYGpyvSEEIIAEALHPY-AKGVV------VATKagLVRTGp 102
Cdd:cd19155 12 MPVVGLGTWqSSPEEIETAVDT---ALEAGYRHIDTAYVYR---NEAAIGNVLKKWiDSGKVkreelfIVTK--LPPGG- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 103 NEWHPVgaPKYLRQqlemSLRRLKLERIDLY---------------------QLHRIDPKVPVEESLGELKALQKEGKIR 161
Cdd:cd19155 83 NRREKV--EKFLLK----SLEKLQLDYVDLYlihfpvgslskeddsgkldptGEHKQDYTTDLLDIWKAMEAQVDQGLTR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 162 HIGLSEVSVEEIQRARKVVDIVSVQNRYNLTDRVHEKVL-DYCEKENLGFIPWFPLATGGLAK--------PGSTLD--- 229
Cdd:cd19155 157 SIGLSNFNREQMARILKNARIKPANLQVELHVYLQQKDLvDFCSTHSITVTAYAPLGSPGAAHfspgtgspSGSSPDllq 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1485949817 230 -----SVAKQHDATPAQIALSWLLARSPVMlpIPGTSSVKHLEENLAGAEVKLTKDELAAVD 286
Cdd:cd19155 237 dpvvkAIAERHGKSPAQVLLRWLMQRGVVV--IPKSTNAARIKENFQVFDFELTEADMAKLS 296
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
45-284 |
2.48e-16 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 77.77 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 45 RAEAVRVLRRALELGVDFIDTADSYGpyVSEEIIA---EALHPYAKGVVVATKAGLVRTGpnEWHPVGAP--------KY 113
Cdd:cd19098 34 RAHTHAVLDAAWAAGVRYFDAARSYG--RAEEFLGswlRSRNIAPDAVFVGSKWGYTYTA--DWQVDAAVhevkdhslAR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 114 LRQQLEMSLRRLKlERIDLYQLHRIDPKVPV---EESLGELKALQKEGkiRHIGLSEVSVEEIQRARKVVDIV------- 183
Cdd:cd19098 110 LLKQWEETRSLLG-KHLDLYQIHSATLESGVledADVLAALAELKAEG--VKIGLSLSGPQQAETLRRALEIEidgarlf 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 184 -SVQNRYNLTDRVHEKVLDYCEKENLGFIPWFPLATG---------GLAKPGSTLDSVAKQHDATPAQIALSWLLARSPV 253
Cdd:cd19098 187 dSVQATWNLLEQSAGEALEEAHEAGMGVIVKEALANGrltdrnpspELAPLMAVLKAVADRLGVTPDALALAAVLAQPFV 266
|
250 260 270
....*....|....*....|....*....|.
gi 1485949817 254 MLPIPGTSSVKHLEENLAGAEVKLTKDELAA 284
Cdd:cd19098 267 DVVLSGAATPEQLRSNLRALDVSLDLELLAA 297
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
35-256 |
7.02e-16 |
|
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: 75.85 E-value: 7.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 35 GPGIW-GPPKDRAEAVRVlrrALELGVDFIDTADSYGpyvSEEIIAEALHPYAKGVVVATKAGLVRTgpNEWHPVGAPKY 113
Cdd:cd19125 15 GLGTWqADPGVVGNAVKT---AIKEGYRHIDCAAIYG---NEKEIGKALKKLFEDGVVKREDLFITS--KLWCTDHAPED 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 114 LRQQLEMSLRRLKLERIDLYQLH--------------RIDPKVPVEESLGELKALQKEGKIRHIGLSEVSVEEIQrarkv 179
Cdd:cd19125 87 VPPALEKTLKDLQLDYLDLYLIHwpvrlkkgahmpepEEVLPPDIPSTWKAMEKLVDSGKVRAIGVSNFSVKKLE----- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 180 vDIVSVQNRYNLTDRV--H-----EKVLDYCEKENLGFIPWFPLATGG--------LAKPgsTLDSVAKQHDATPAQIAL 244
Cdd:cd19125 162 -DLLAVARVPPAVNQVecHpgwqqDKLHEFCKSKGIHLSAYSPLGSPGttwvkknvLKDP--IVTKVAEKLGKTPAQVAL 238
|
250
....*....|..
gi 1485949817 245 SWLLARSPVMLP 256
Cdd:cd19125 239 RWGLQRGTSVLP 250
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
45-284 |
2.33e-15 |
|
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: 74.67 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 45 RAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHPYAKG-VVVATKAGLV--------RTGPNEWHPvGAPKYLR 115
Cdd:cd19161 19 NADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKPRDeFVLSTKVGRLlkparegsVPDPNGFVD-PLPFEIV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 116 ---------QQLEMSLRRLKLERIDLYQLHRIDPKVPVEE---------------SLGELKalqKEGKIRHIGLSEVSVE 171
Cdd:cd19161 98 ydysydgimRSFEDSLQRLGLNRIDILYVHDIGVYTHGDRkerhhfaqlmsggfkALEELK---KAGVIKAFGLGVNEVQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 172 EIQRARKV--VDIVSVQNRYNLTDRVHEK-VLDYCEKENLGFIPWFPLATGGLA---KPGSTLD---------------- 229
Cdd:cd19161 175 ICLEALDEadLDCFLLAGRYSLLDQSAEEeFLPRCEQRGTSLVIGGVFNSGILAtgtKSGAKFNygdapaeiisrvmeie 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1485949817 230 SVAKQHDATPAQIALSWLLARSPVMLPIPGTSSVKHLEENLAGAEVKLTKDELAA 284
Cdd:cd19161 255 KICDAYNVPLAAAALQFPLRHPAVASVLTGARNPAQLRQNVEAFQTDIPEELWQA 309
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
27-269 |
3.07e-15 |
|
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: 74.42 E-value: 3.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 27 GYGAMQLTGPGIWGP-PKDRAEAVRVlrrALELGVDFIDTADSYGpyvSEEIIAEALHP-YAKGVV------VATKAglv 98
Cdd:cd19129 2 GSGAIPALGFGTLIPdPSATRNAVKA---ALEAGFRHFDCAERYR---NEAEVGEAMQEvFKAGKIrredlfVTTKL--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 99 rtgpneWHPVGAPKYLRQQLEMSLRRLKLERIDLYQLH---------RIDPK-----------VPVEESLGELKALQKEG 158
Cdd:cd19129 73 ------WNTNHRPERVKPAFEASLKRLQLDYLDLYLIHtpfafqpgdEQDPRdangnviyddgVTLLDTWRAMERLVDEG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 159 KIRHIGLSEVSVEEIQR----ARKVVDIVSVQNRYNLTDrvhEKVLDYCEKENLGFIPWFPLATGglAKPGSTLD----S 230
Cdd:cd19129 147 RCKAIGLSDVSLEKLREifeaARIKPAVVQVESHPYLPE---WELLDFCKNHGIVLQAFAPLGHG--MEPKLLEDpvitA 221
|
250 260 270
....*....|....*....|....*....|....*....
gi 1485949817 231 VAKQHDATPAQIALSWLLARSPVMLPIPGTSSvkHLEEN 269
Cdd:cd19129 222 IARRVNKTPAQVLLAWAIQRGTALLTTSKTPS--RIREN 258
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
21-287 |
4.81e-15 |
|
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo sapiens, Rattus norvegicus, and Mus musculus, are founding members of aldo-keto reductase family 6 member A9 (AKR6A9), A12 (AKR6A12), A14 (AKR6A14), respectively. KCAB3B, also called Shaker channel b-subunit 3 (Kvb3), K(+) channel subunit beta-3, or Kv-beta-3, is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. It alters the functional properties of Kv1.5.
Pssm-ID: 381386 [Multi-domain] Cd Length: 325 Bit Score: 74.25 E-value: 4.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 21 LPVHRLGYGAMQLT--GPGIW---GPPKDRAEAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHpyAKG-----VV 90
Cdd:cd19160 3 MKYRNLGKSGLRVSclGLGTWvtfGSQISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILK--SKGwrrssYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 91 VATKagLVRTGPNEWHPVGAPKYLRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSEVSV 170
Cdd:cd19160 81 VTTK--IYWGGQAETERGLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRWSA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 171 EEIQRARKV------VDIVSVQNRYNL--TDRVHEKVLDYCEKENLGFIPWFPLATGGLA-------------------- 222
Cdd:cd19160 159 MEIMEAYSVarqfnlIPPVCEQAEYHLfqREKVEMQLPELYHKIGVGSVTWSPLACGLITgkydgrvpdtcraavkgyqw 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 223 ---KPGST-----------LDSVAKQHDATPAQIALSWLLARSPVMLPIPGTSSVKHLEENLAGAEV--KLTKDELAAVD 286
Cdd:cd19160 239 lkeKVQSEegkkqqakvkeLHPIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGSIQVlsQLTPQTVMEID 318
|
.
gi 1485949817 287 A 287
Cdd:cd19160 319 A 319
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
31-287 |
6.69e-15 |
|
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: 73.21 E-value: 6.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 31 MQLTGPGIW-GPPKDRAEAVRVlrrALELGVDFIDTADSYGpyvSEEIIAEALHPYAKGVVVATKAGLVRTGpNEWHPVG 109
Cdd:cd19118 7 IPAIGLGTWqAEPGEVGAAVKI---ALKAGYRHLDLAKVYQ---NQHEVGQALKELLKEEPGVKREDLFITS-KLWNNSH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 110 APKYLRQQLEMSLRRLKLERIDLYQLH---------RIDPKVPVEESLGELK---------------ALQKEGKIRHIGL 165
Cdd:cd19118 80 RPEYVEPALDDTLKELGLDYLDLYLIHwpvafkptgDLNPLTAVPTNGGEVDldlsvslvdtwkamvELKKTGKVKSIGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 166 SEVSVEEIQrarKVVDIVSVQNRYNLTDR----VHEKVLDYCEKENLGFIPWFPLATGGLAKP----GSTLDSVAKQHDA 237
Cdd:cd19118 160 SNFSIDHLQ---AIIEETGVVPAVNQIEAhpllLQDELVDYCKSKNIHITAYSPLGNNLAGLPllvqHPEVKAIAAKLGK 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1485949817 238 TPAQIALSWLLARSPVMLPIPGTSSvkHLEENLagAEVKLTKDELAAVDA 287
Cdd:cd19118 237 TPAQVLIAWGIQRGHSVIPKSVTPS--RIRSNF--EQVELSDDEFNAVTA 282
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
31-287 |
2.61e-14 |
|
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: 71.65 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 31 MQLTGPGIW-GPPKDRAEAVRVlrrALELGVDFIDTADSYGpyvSEEIIAEALHPYAKGVVVATKAGLVRTGpNEWHPVG 109
Cdd:cd19106 7 MPLIGLGTWkSKPGQVKAAVKY---ALDAGYRHIDCAAVYG---NEQEVGEALKEKVGPGKAVPREDLFVTS-KLWNTKH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 110 APKYLRQQLEMSLRRLKLERIDLYQLH------RID---PK----------VPVEESLGELKALQKEGKIRHIGLSEVSv 170
Cdd:cd19106 80 HPEDVEPALRKTLKDLQLDYLDLYLIHwpyafeRGDnpfPKnpdgtirydsTHYKETWKAMEKLVDKGLVKAIGLSNFN- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 171 eeiqrARKVVDIVSVQNRYNLTDRV-------HEKVLDYCEKENLGFIPWFPLATG--GLAKPGS-------TLDSVAKQ 234
Cdd:cd19106 159 -----SRQIDDILSVARIKPAVLQVechpylaQNELIAHCKARGLVVTAYSPLGSPdrPWAKPDEpvlleepKVKALAKK 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1485949817 235 HDATPAQIALSWLLARSPVMLPIPGTSSvkHLEENLAGAEVKLTKDELAAVDA 287
Cdd:cd19106 234 YNKSPAQILLRWQVQRGVVVIPKSVTPS--RIKQNIQVFDFTLSPEEMKQLDA 284
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
31-282 |
5.10e-14 |
|
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: 70.37 E-value: 5.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 31 MQLTGPGIWGPPKDRAEAVRVLRRALELGVDFIDTADSYGpyvSEEIIAEALHPyakgvvvATKAGLVRT---------- 100
Cdd:cd19124 5 MPVIGMGTASDPPSPEDIKAAVLEAIEVGYRHFDTAAAYG---TEEALGEALAE-------ALRLGLVKSrdelfvtskl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 101 GPNEWHP---VGApkyLRQqlemSLRRLKLERIDLYQLH---RIDP---KVPVEESL-------GELKAL---QKEGKIR 161
Cdd:cd19124 75 WCSDAHPdlvLPA---LKK----SLRNLQLEYVDLYLIHwpvSLKPgkfSFPIEEEDflpfdikGVWEAMeecQRLGLTK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 162 HIGLSEVSVEEIQRARKVVDIVSVQNRYNLTDRVHEKVL-DYCEKENLGFIPWFPLATGGlAKPGST-------LDSVAK 233
Cdd:cd19124 148 AIGVSNFSCKKLQELLSFATIPPAVNQVEMNPAWQQKKLrEFCKANGIHVTAYSPLGAPG-TKWGSNavmesdvLKEIAA 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1485949817 234 QHDATPAQIALSWLLARSPVMlpIPGTSSVKHLEENLAGAEVKLTKDEL 282
Cdd:cd19124 227 AKGKTVAQVSLRWVYEQGVSL--VVKSFNKERMKQNLDIFDWELTEEDL 273
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
31-287 |
2.62e-13 |
|
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: 69.01 E-value: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 31 MQLTGPGIWGPPKDRAEAVrvLRRALELGVDFIDTADSYGpyvSEEIIAEalhpyakGVVVATKAGLVR-----TGPNEW 105
Cdd:cd19113 11 MPSVGFGCWKLDNATAADQ--IYQAIKAGYRLFDGAEDYG---NEKEVGE-------GVNRAIDEGLVKreelfLTSKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 106 HPVGAPKYLRQQLEMSLRRLKLERIDLYQLH-RIDPK-VPVEES--------------------LGELKALQK---EGKI 160
Cdd:cd19113 79 NNFHDPKNVETALNKTLSDLKLDYVDLFLIHfPIAFKfVPIEEKyppgfycgdgdnfvyedvpiLDTWKALEKlvdAGKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 161 RHIGLSEVS---VEEIQRARKVVDIV-SVQNRYNLTdrvHEKVLDYCEKENL---GFIPWFPLA----TGGLAKPGSTL- 228
Cdd:cd19113 159 KSIGVSNFPgalILDLLRGATIKPAVlQIEHHPYLQ---QPKLIEYAQKAGItitAYSSFGPQSfvelNQGRALNTPTLf 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1485949817 229 -----DSVAKQHDATPAQIALSWLLARSPVMlpIPGTSSVKHLEENLAGAEVKLTKDELAAVDA 287
Cdd:cd19113 236 ehdtiKSIAAKHNKTPAQVLLRWATQRGIAV--IPKSNLPERLLQNLSVNDFDLTKEDFEEIAK 297
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
31-287 |
3.79e-13 |
|
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 (NADP-dependent D-sorbitol-6-phosphate dehydrogenase or NADP-S6PDH) from Malus domestica, and AKR2A2 (NADPH-dependent mannose-6-phosphate reductase or NADPH-M6PR) from Apium graveolens. NADP-S6PDH (EC 1.1.1.200), also called aldose-6-phosphate reductase [NADPH], synthesizes sorbitol-6-phosphate, a key intermediate in the synthesis of sorbitol which is a major photosynthetic product in many members of the Rosaceae family. NADPH-M6PR (EC 1.1.1.224), also called NADPH-dependent M6P reductase, is a key enzyme involved in mannitol biosynthesis.
Pssm-ID: 381338 [Multi-domain] Cd Length: 308 Bit Score: 68.28 E-value: 3.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 31 MQLTGPGIWgpPKDRAEAVRVLRRALELGVDFIDTADSYGpyvSEEIIAEALhpyakgvVVATKAGLVR------TGP-- 102
Cdd:cd19112 11 MPVIGLGVW--RMEPGEIKELILNAIKIGYRHFDCAADYK---NEKEVGEAL-------AEAFKTGLVKredlfiTTKlw 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 103 NEWHpvgapKYLRQQLEMSLRRLKLERIDLYQLH-----------------------RIDPKVPVEESLGELKALQKEGK 159
Cdd:cd19112 79 NSDH-----GHVIEACKDSLKKLQLDYLDLYLVHfpvatkhtgvgttgsalgedgvlDIDVTISLETTWHAMEKLVSAGL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 160 IRHIGLSEVSV---EEIQRARKVVDIVSVQNRYNLTDRvhEKVLDYCEKENLGFIPWFPLAtGGLAKP---GST------ 227
Cdd:cd19112 154 VRSIGISNYDIfltRDCLAYSKIKPAVNQIETHPYFQR--DSLVKFCQKHGISVTAHTPLG-GAAANAewfGSVsplddp 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1485949817 228 -LDSVAKQHDATPAQIALSWLLARSPVMlpIPGTSSVKHLEENLAGAEVKLTKDELAAVDA 287
Cdd:cd19112 231 vLKDLAKKYGKSAAQIVLRWGIQRNTAV--IPKSSKPERLKENIDVFDFQLSKEDMKLIKS 289
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
21-286 |
4.01e-13 |
|
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo sapiens, Mus musculus, Mustela putorius, Rattus norvegicus, and Kvb1.1, Kvb1.2 from Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A3 (AKR6A3), A8 (AKR6A8), A10a (AKR6A10a), A13 (AKR6A13), A7 (AKR6A7) and A10b (AKR6A10b), respectively. KCAB1B, also called Shaker channel b-subunit 1(Kvb1), K(+) channel subunit beta-1, or Kv-beta-1, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It modulates action potentials via its effect on the pore-forming alpha subunits.
Pssm-ID: 381385 [Multi-domain] Cd Length: 323 Bit Score: 68.53 E-value: 4.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 21 LPVHRLGYGAMQLT--GPGIW----GPPKDRAeAVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHPYA---KGVVV 91
Cdd:cd19159 1 MKYRNLGKSGLRVSclGLGTWvtfgGQISDEV-AERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwrrSSLVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 92 ATKagLVRTGPNEWHPVGAPKYLRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSEVSVE 171
Cdd:cd19159 80 TTK--LYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 172 EIQRARKV------VDIVSVQNRYNLTDR--VHEKVLDYCEKENLGFIPWFPLATGGLAK------PGST---------- 227
Cdd:cd19159 158 EIMEAYSVarqfnmIPPVCEQAEYHLFQRekVEVQLPELYHKIGVGAMTWSPLACGIISGkygngvPESSraslkcyqwl 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1485949817 228 ------------------LDSVAKQHDATPAQIALSWLLARSPVMLPIPGTSSVKHLEENLAGAEV--KLTKDELAAVD 286
Cdd:cd19159 238 kerivseegrkqqnklkdLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEID 316
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
31-286 |
8.00e-13 |
|
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: 67.14 E-value: 8.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 31 MQLTGPGIWGPPKDRAEAVRVLRRALELGVDFIDTADSYGpyvSEEIIAEAL-HPYAKGVV------VATKaglvrTGPN 103
Cdd:cd19119 12 IPALGLGTASPHEDRAEVKEAVEAAIKEGYRHIDTAYAYE---TEDFVGEAIkRAIDDGSIkreelfITTK-----VWPT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 104 EWhpvgapKYLRQQLEMSLRRLKLERIDLYQLH------RID-----PKVPVEES-----------LGELKALQKE---G 158
Cdd:cd19119 84 FY------DEVERSLDESLKALGLDYVDLLLVHwpvcfeKDSddsgkPFTPVNDDgktryaasgdhITTYKQLEKIyldG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 159 KIRHIGLSEVSVEEIQRARKVVDIVSVQNRYNLTDRVHEKVL-DYCEKENLGFIPWFPLATGGLAKPGSTL-DSVAKQHD 236
Cdd:cd19119 158 RAKAIGVSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLrDFCFKHGILVTAYSPLGSHGAPNLKNPLvKKIAEKYN 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1485949817 237 ATPAQIALSWLLARSPVMLPipgtSSVKHLEENLAGAEVKLTKDELAAVD 286
Cdd:cd19119 238 VSTGDILISYHVRQGVIVLP----KSLKPVRIVSNGKIVSLTKEDLQKLD 283
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
12-286 |
3.80e-12 |
|
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are founding members of aldo-keto reductase family 3 member A1 (AKR3A1) and A2 (AKR3A2), respectively. Gcy1p, also called galactose-inducible crystallin-like protein 1, is a glycerol dehydrogenase involved in glycerol catabolism under microaerobic conditions. It has mRNA binding activity. Ypr1p acts as a 2-methylbutyraldehyde reductase that displays high specific activity towards 2-methylbutyraldehyde, as well as other aldehydes such as hexanal.
Pssm-ID: 381343 [Multi-domain] Cd Length: 284 Bit Score: 65.21 E-value: 3.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 12 SGTFKLGGDLPVHRLGYGAMQltgpgiwGPPKDRAEAVRVlrrALELGVDFIDTADSYGpyvSEEIIAEALHpyAKGV-- 89
Cdd:cd19117 3 SKTFKLNTGAEIPAVGLGTWQ-------SKPNEVAKAVEA---ALKAGYRHIDTAAIYG---NEEEVGQGIK--DSGVpr 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 90 ---VVATKAGlvrtgpNEWHpvgapKYLRQQLEMSLRRLKLERIDLYQLH---RIDPKVPVEESL--------------- 148
Cdd:cd19117 68 eeiFITTKLW------CTWH-----RRVEEALDQSLKKLGLDYVDLYLMHwpvPLDPDGNDFLFKkddgtkdhepdwdfi 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 149 ---GELKALQKEGKIRHIGLSEVSVEEIQR--ARKVVDIVSVQNRYNLTDRV-HEKVLDYCEKENLGFIPWFPL-ATGGL 221
Cdd:cd19117 137 ktwELMQKLPATGKVKAIGVSNFSIKNLEKllASPSAKIVPAVNQIELHPLLpQPKLVDFCKSKGIHATAYSPLgSTNAP 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1485949817 222 AKPGSTLDSVAKQHDATPAQIALSWLLARSPVMLPIPGTSSvkHLEENLAGAEvkLTKDELAAVD 286
Cdd:cd19117 217 LLKEPVIIKIAKKHGKTPAQVIISWGLQRGYSVLPKSVTPS--RIESNFKLFT--LSDEEFKEID 277
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
15-286 |
4.77e-12 |
|
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, EC 1.1.1.365), also called D-galacturonic acid reductase, or GalUR, is a founding member of aldo-keto reductase family 3 member D1 (AKR3D1). It mediates the reduction of D-galacturonate to L-galactonate, the first step in D-galacturonate catabolic process. It also has activity with D-glucuronate and DL-glyceraldehyde. Its activity is seen only with NADPH and not with NADH.
Pssm-ID: 381347 [Multi-domain] Cd Length: 279 Bit Score: 64.86 E-value: 4.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 15 FKLGGDLPVHRLGYGAMQLTGPgiwgppkdraEAVRVLRRALELGVDFIDTADSYGpyvSEEIIAEALHPYAKGVVVATK 94
Cdd:cd19121 4 FKLNTGASIPAVGLGTWQAKAG----------EVKAAVAHALKIGYRHIDGALCYQ---NEDEVGEGIKEAIAGGVKRED 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 95 AGLVRTGPNEWHpvgapKYLRQQLEMSLRRLKLERIDLYQLH--------RIDPKVPVEE--------------SLGELK 152
Cdd:cd19121 71 LFVTTKLWSTYH-----RRVELCLDRSLKSLGLDYVDLYLVHwpvllnpnGNHDLFPTLPdgsrdldwdwnhvdTWKQME 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 153 ALQKEGKIRHIGLSEVSV---EEIQRARKVVDIVS-VQNRYNLTdrvHEKVLDYCEKENLGFIPWFPL-ATGGLAKPGST 227
Cdd:cd19121 146 KVLKTGKTKAIGVSNYSIpylEELLKHATVVPAVNqVENHPYLP---QQELVDFCKEKGILIEAYSPLgSTGSPLISDEP 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1485949817 228 LDSVAKQHDATPAQIALSWLLARSPVMlpIPGTSSVKHLEENLagAEVKLTKDELAAVD 286
Cdd:cd19121 223 VVEIAKKHNVGPGTVLISYQVARGAVV--LPKSVTPDRIKSNL--EIIDLDDEDMNKLN 277
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
11-219 |
4.15e-11 |
|
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.
Pssm-ID: 381368 [Multi-domain] Cd Length: 325 Bit Score: 62.48 E-value: 4.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 11 KSGtfklggdLPVHRLGYGAMQLTGPGIwgpPKDRAEAVRVLrrALELGVDFIDTADSYGPYVSEEIIAEALHPYA---K 87
Cdd:cd19142 8 KSG-------LRVSNVGLGTWSTFSTAI---SEEQAEEIVTL--AYENGINYFDTSDAFTSGQAETELGRILKKKGwkrS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 88 GVVVATK---------AGLVRtgpnewhpvgapKYLRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESLGELKALQKEG 158
Cdd:cd19142 76 SYIVSTKiywsygseeRGLSR------------KHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1485949817 159 KIRHIGLSEVSVEEIQ------RARKVVDIVSVQNRYNLTDRvhEKV----LDYCEKENLGFIPWFPLATG 219
Cdd:cd19142 144 LIMYWGTSRWSPVEIMeafsiaRQFNCPTPICEQSEYHMFCR--EKMelymPELYNKVGVGLITWSPLSLG 212
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
48-281 |
7.45e-11 |
|
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381367 [Multi-domain] Cd Length: 310 Bit Score: 61.69 E-value: 7.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 48 AVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHPYA---KGVVVATKagLVRTGPNEWHPVGAPKYLRQQLEMSLRR 124
Cdd:cd19141 32 AEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKGwrrSSYVITTK--IFWGGKAETERGLSRKHIIEGLKASLER 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 125 LKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSEVSVEEIQRARKV------VDIVSVQNRYNLTDRvhEK 198
Cdd:cd19141 110 LQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSAMEIMEAYSVarqfnlIPPIVEQAEYHLFQR--EK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 199 VLDYC----EKENLGFIPWFPLATG---GLAKPGSTLDS-------------------------------VAKQHDATPA 240
Cdd:cd19141 188 VEMQLpelfHKIGVGAMTWSPLACGilsGKYDDGVPEYSraslkgyqwlkekilseegrrqqaklkelqiIADRLGCTLP 267
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1485949817 241 QIALSWLLARSPVMLPIPGTSSVKHLEENLAGAEV--KLTKDE 281
Cdd:cd19141 268 QLAIAWCLKNEGVSSVLLGASSTEQLYENLQAIQVlpKLTPNI 310
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
18-287 |
8.29e-11 |
|
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: 61.35 E-value: 8.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 18 GGDLPVHRLG-YGAMQLTgpgiwgPPKDRAEAVRVlrrALELGVDFIDTADSYGpyvSEEIIAEALH-PYAKGVVvaTKA 95
Cdd:cd19109 1 GNSIPIIGLGtYSEPKTT------PKGACAEAVKV---AIDTGYRHIDGAYIYQ---NEHEVGQAIReKIAEGKV--KRE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 96 GLVRTGP--NEWHPvgaPKYLRQQLEMSLRRLKLERIDLYQLHRI------DPKVPVEE-------------SLGELKAL 154
Cdd:cd19109 67 DIFYCGKlwNTCHP---PELVRPTLERTLKVLQLDYVDLYIIEMPmafkpgDEIYPRDEngkwlyhktnlcaTWEALEAC 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 155 QKEGKIRHIGLSEVSVEEIQ--------RARKVVDIVSVQNRYNltdrvHEKVLDYCEKENLGFIPWFPLATGGLAK--- 223
Cdd:cd19109 144 KDAGLVKSIGVSNFNRRQLElilnkpglKHKPVSNQVECHPYFT-----QPKLLEFCQQHDIVIVAYSPLGTCRDPIwvn 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1485949817 224 -------PGSTLDSVAKQHDATPAQIALSWLLARSPVMlpIPGTSSVKHLEENLAGAEVKLTKDELAAVDA 287
Cdd:cd19109 219 vssppllEDPLLNSIGKKYNKTAAQVVLRFNIQRGVVV--IPKSFNPERIKENFQIFDFSLTEEEMKDIEA 287
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
35-286 |
1.45e-10 |
|
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) from Mus musculus (liver, AKR1E1) and Homo sapiens (AKR1E2). 1,5-anhydro-D-fructose reductase), also called AF reductase, or aldo-keto reductase family 1 member C-like protein 2 (AKR1CL2), catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. AKR1E2 is a testis aldo-keto reductase (tAKR), which is also known as testis-specific protein (TSP), or LoopADR.
Pssm-ID: 381336 [Multi-domain] Cd Length: 301 Bit Score: 60.74 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 35 GPGIW-GPPKDRAEAVRVlrrALELGVDFIDTADSYgpYVSEEIiaealhpyAKGVVVATKAGLVR-----TGPNEWHPV 108
Cdd:cd19110 8 GLGTWkASPGEVTEAVKV---AIDAGYRHFDCAYLY--HNESEV--------GAGIREKIKEGVVRredlfIVSKLWCTC 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 109 GAPKYLRQQLEMSLRRLKLERIDLYQLHRI------DPKVPVEES----------LGELKALQK---EGKIRHIGLSEVS 169
Cdd:cd19110 75 HKKSLVKTACTRSLKALKLNYLDLYLIHWPmgfkpgEPDLPLDRSgmvipsdtdfLDTWEAMEDlviEGLVKNIGVSNFN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 170 VEEIQRarkVVDIVSVQNRyNLTDRV-------HEKVLDYCEKENLGFIPWFPLATGGLAKP---GSTLDSVAKQHDATP 239
Cdd:cd19110 155 HEQLER---LLNKPGLRVK-PVTNQIechpyltQKKLISFCQSRNVSVTAYRPLGGSCEGVDlidDPVIQRIAKKHGKSP 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1485949817 240 AQIALSWLLARSPVMlpIPGTSSVKHLEENLAGAEVKLTK---DELAAVD 286
Cdd:cd19110 231 AQILIRFQIQRNVIV--IPKSVTPSRIKENIQVFDFELTEhdmDNLLSLD 278
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
48-287 |
1.60e-10 |
|
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.
Pssm-ID: 381384 [Multi-domain] Cd Length: 324 Bit Score: 60.87 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 48 AVRVLRRALELGVDFIDTADSYGPYVSEEIIAEALHPYA---KGVVVATKagLVRTGPNEWHPVGAPKYLRQQLEMSLRR 124
Cdd:cd19158 33 AEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwrrSSLVITTK--IFWGGKAETERGLSRKHIIEGLKASLER 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 125 LKLERIDLYQLHRIDPKVPVEESLGELKALQKEGKIRHIGLSEVSVEEIQRARKV------VDIVSVQNRYNLTDR--VH 196
Cdd:cd19158 111 LQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVarqfnlIPPICEQAEYHMFQRekVE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 197 EKVLDYCEKENLGFIPWFPLATG---------------------------GLAKPG-------STLDSVAKQHDATPAQI 242
Cdd:cd19158 191 VQLPELFHKIGVGAMTWSPLACGivsgkydsgippysraslkgyqwlkdkILSEEGrrqqaklKELQAIAERLGCTLPQL 270
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1485949817 243 ALSWLLARSPVMLPIPGTSSVKHLEENLAGAEV--KLTKDELAAVDA 287
Cdd:cd19158 271 AIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVlpKLSSSIVHEIDS 317
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
35-289 |
1.60e-09 |
|
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis.
Pssm-ID: 381348 [Multi-domain] Cd Length: 291 Bit Score: 57.63 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 35 GPGIWGPPKDRAEAVRVLRRALELGVDFIDTAdsyGPYVSEEIIAEALHPYAK--------GVVVATKAglvrtgpneWH 106
Cdd:cd19122 13 GFGTFANEGAKGETYAAVTKALDVGYRHLDCA---WFYLNEDEVGDAVRDFLKenpsvkreDLFICTKV---------WN 80
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 107 PVGAPKYLRQQLEMSLRRLKLERIDLYQLH-------------RIDP--KVPVEESLGE-----LKALQK---EGKIRHI 163
Cdd:cd19122 81 HLHEPEDVKWSIDNSLKNLKLDYIDLFLVHwpiaaekndqrspKLGPdgKYVILKDLTEnpeptWRAMEEiyeSGKAKAI 160
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 164 GLSEVSVEEIQRARKVVDIVSVQNRYNLTDRV-HEKVLDYCEKENLGFIPWFPL-------ATGGLAKPGSTLDSVAKQH 235
Cdd:cd19122 161 GVSNWTIPGLKKLLSFAKVKPHVNQIEIHPFLpNEELVDYCFSNDILPEAYSPLgsqnqvpSTGERVSENPTLNEVAEKG 240
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250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1485949817 236 DATPAQIALSWLLARSPVMLpiPGTSSVKHLEENLAGAEvkLTKDELAAVDAQA 289
Cdd:cd19122 241 GYSLAQVLIAWGLRRGYVVL--PKSSTPSRIESNFKSIE--LSDEDFEAINQVA 290
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|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
31-286 |
3.52e-09 |
|
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.
Pssm-ID: 381340 [Multi-domain] Cd Length: 302 Bit Score: 56.80 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 31 MQLTGPGIWGPPKDRAEavRVLRRALELGVDFIDTADSYGPYVSeeiiaealhpYAKGVVVATKAGLVRTGP-----NEW 105
Cdd:cd19114 4 MPLVGFGTAKIKANETE--EVIYNAIKVGYRLIDGALLYGNEAE----------VGRGIRKAIQEGLVKREDlfivtKLW 71
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 106 HPVGAPKYLRQQLEMSLRRLKLERIDLYQLH------RIDP-------------------KVPVEESLGELKALQKEGKI 160
Cdd:cd19114 72 NNFHGKDHVREAFDRQLKDYGLDYIDLYLIHfpipaaYVDPaenypflwkdkelkkfpleQSPMQECWREMEKLVDAGLV 151
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 161 RHIGLSEVSVEEI----QRARKVVDIVSVQNRYNLTdrvHEKVLDYCEKENLGFIPWF---PLATGGLAKPGSTL----- 228
Cdd:cd19114 152 RNIGIANFNVQLIldllTYAKIKPAVLQIEHHPYLQ---QKRLIDWAKKQGIQITAYSsfgNAVYTKVTKHLKHFtnlle 228
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250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1485949817 229 ----DSVAKQHDATPAQIALSWLLARSPVMlpIPGTSSVKHLEENLAGAEVKLTKDELAAVD 286
Cdd:cd19114 229 hpvvKKLADKHKRDTGQVLLRWAVQRNITV--IPKSVNVERMKTNLDITSYKLDEEDMEALY 288
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|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
31-285 |
3.69e-09 |
|
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase (AR, EC 1.1.1.21) from Homo sapiens (AKR1B1), Oryctolagus cuniculus (kidney, AKR1B2), Mus musculus (AKR1B3), Rattus norvegicus (lens, AKR1B4), Bos taurus (lens/testis, AKR1B5), and Sus scrofa (lens, AKR1B6), aldose reductase-related protein 1 (ALD1, EC1.1.1.21) from Mus musculus (AKR1B7), Rattus norvegicus (AKR1B14), and Homo sapiens (AKR1B15), Mus musculus fibroblast growth factor induced protein (FR-1 or AKR1B8, EC 1.1.1.21), Cricetulus griseus aldose reductase-related protein 2 (ALD2 or AKR1B9, EC 1.1.1.21), aldose reductase-like from Homo sapiens (ARL-1 or AKR1B10) and Rattus norvegicus (AKR1B13), aldo-keto reductase from Gallus domesticus (eye, tongue, esophagus, AKR1B12), and Oryctolagus cuniculus AR-like protein (3beta-HSD, AKR1B19). AR, also called aldehyde reductase, catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. ALD1 reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. It may play a role in the metabolism of xenobiotic aromatic aldehydes. FR-1, also called aldose reductase-related protein 2, or fibroblast growth factor-regulated protein (FGFRP), is induced by fibroblast growth factor-1. It may play a role in the regulation of the cell cycle. FR-1 belongs to the NADPH-dependent aldo-keto reductase family. ALD2 is an inducible aldo-keto reductase with a preference for aliphatic substrates. It can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. ARL-1, also called aldose reductase-like, or aldose reductase-related protein (ARP), or small intestine reductase, or SI reductase, acts as all-trans-retinaldehyde reductase that can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). It may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. AKR1B15, also called estradiol 17-beta-dehydrogenase AKR1B15, is a mitochondrial aldo-keto reductase that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. It has a strong selectivity towards NADP(H). AKR1B19 is aldose reductase-like that may show 3-beta-hydroxysteroid dehydrogenase (3beta-HSD) activity.
Pssm-ID: 381333 [Multi-domain] Cd Length: 307 Bit Score: 56.66 E-value: 3.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 31 MQLTGPGIW-GPPKDRAEAVRVlrrALELGVDFIDTADSYGpyvSEEIIAEALHPYAKGVVVATKAGLVRTgpNEWHPVG 109
Cdd:cd19107 4 MPILGLGTWkSPPGQVTEAVKV---AIDAGYRHIDCAYVYQ---NENEVGEAIQEKIKEQVVKREDLFIVS--KLWCTFH 75
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 110 APKYLRQQLEMSLRRLKLERIDLYQLH---------RIDPK------VPVEESLGE----LKALQKEGKIRHIGLSEVSV 170
Cdd:cd19107 76 EKGLVKGACQKTLSDLKLDYLDLYLIHwptgfkpgkELFPLdesgnvIPSDTTFLDtweaMEELVDEGLVKAIGVSNFNH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 171 EEIQRA--------RKVVDIVSVQNrYnLTdrvHEKVLDYCEKENLGFIPWFPLATGG--LAKPG--STLD-----SVAK 233
Cdd:cd19107 156 LQIERIlnkpglkyKPAVNQIECHP-Y-LT---QEKLIQYCQSKGIVVTAYSPLGSPDrpWAKPEdpSLLEdpkikEIAA 230
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250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1485949817 234 QHDATPAQIALSWLLARSPVMlpIPGTSSVKHLEENLAGAEVKLTKDELAAV 285
Cdd:cd19107 231 KHNKTTAQVLIRFPIQRNLVV--IPKSVTPERIAENFKVFDFELSSEDMATI 280
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|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
27-287 |
7.86e-09 |
|
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose reductase xyl1 (XR, EC 1.1.1.307) is a founding member of aldo-keto reductase family 2 member D1 (AKR2D1). It catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol in a NAD(P)H dependent manner.
Pssm-ID: 381341 [Multi-domain] Cd Length: 311 Bit Score: 55.50 E-value: 7.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 27 GYgAMQLTGPGIWGPPKDR-AEAVRvlrRALELGVDFIDTADSYGPYVseeiiaEAlhpyAKGVVVATKAGLVRtgpNE- 104
Cdd:cd19115 10 GY-DMPLVGFGLWKVNNDTcADQVY---NAIKAGYRLFDGACDYGNEV------EA----GQGVARAIKEGIVK---REd 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 105 -------WHPVGAPKYLRQQLEMSLRRLKLERIDLYQLH------RIDP------------------KVPVEESLGELKA 153
Cdd:cd19115 73 lfivsklWNTFHDGERVEPICRKQLADWGIDYFDLFLIHfpialkYVDPavryppgwfydgkkvefsNAPIQETWTAMEK 152
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 154 LQKEGKIRHIGLSEVSVEEI----QRARKVVDIVSVQNRYNLTdrvHEKVLDYCEKENL---GFIPWFPLATGGLAKPGS 226
Cdd:cd19115 153 LVDKGLARSIGVSNFSAQLLmdllRYARIRPATLQIEHHPYLT---QPRLVKYAQKEGIavtAYSSFGPQSFLELDLPGA 229
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250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1485949817 227 ----------TLDSVAKQHDATPAQIALSWLLARSPVMlpIPGTSSVKHLEENLAGAEVKLTKDELAAVDA 287
Cdd:cd19115 230 kdtpplfehdVIKSIAEKHGKTPAQVLLRWATQRGIAV--IPKSNNPKRLAQNLDVTGFDLEAEEIKAISA 298
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|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
42-286 |
3.51e-08 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 53.77 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 42 PKDRA-EAVRVlrrALELGVDFIDTADSYGpyvSEEIIAEALHP-YAKGVV------VATKAglvrtgpneWHPVGAPKY 113
Cdd:cd19108 25 PKSKAlEATKL---AIDAGFRHIDSAYLYQ---NEEEVGQAIRSkIADGTVkredifYTSKL---------WCTFHRPEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 114 LRQQLEMSLRRLKLERIDLYQLHRIDPKVPVEESL-----GEL-----------KALQK---EGKIRHIGLSEVSVEEIQ 174
Cdd:cd19108 90 VRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELFpkdenGKLifdtvdlcatwEAMEKckdAGLAKSIGVSNFNRRQLE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485949817 175 RA--------RKVVDIVSVQNRYNltdrvHEKVLDYCEKENLGFIPWFPLATGG------------LAKPgsTLDSVAKQ 234
Cdd:cd19108 170 MIlnkpglkyKPVCNQVECHPYLN-----QSKLLDFCKSKDIVLVAYSALGSQRdkewvdqnspvlLEDP--VLCALAKK 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1485949817 235 HDATPAQIALSWLLARSPVMLpipGTS-SVKHLEENLAGAEVKLTKDELAAVD 286
Cdd:cd19108 243 HKRTPALIALRYQLQRGVVVL---AKSfNEKRIKENLQVFEFQLTSEDMKALD 292
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