|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
1-322 |
0e+00 |
|
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: 506.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 1 MRYNQLGNTGLFVSELCLGTMTFGEnqTGAVWSAVAGLDQGAADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAIKNL 80
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGTMTFGG--GGGFFGAWGGVDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKGR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 81 gvpRKDVIIATKFHGQMGDKPNDRGASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVRYI 160
Cdd:cd19091 79 ---RDDVLIATKVRGRMGEGPNDVGLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVRYI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 161 GLSNWAAWRMAKALGISERKGYARFETVQAYYSIAGRDLERDIVPLMQEEKLGLMVWSPLAGGLLSGKYGPG--APGNGE 238
Cdd:cd19091 156 GVSNFSAWQIMKALGISERRGLARFVALQAYYSLLGRDLEHELMPLALDQGVGLLVWSPLAGGLLSGKYRRGqpAPEGSR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 239 GRRANFDFPPVDKDRAWACVAAMREVGARHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAVKLKLDAEDVAKL 318
Cdd:cd19091 236 LRRTGFDFPPVDRERGYDVVDALREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGAAGLSLTPEEIARL 315
|
....
gi 2229004110 319 DEVS 322
Cdd:cd19091 316 DKVS 319
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-327 |
5.59e-145 |
|
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: 412.26 E-value: 5.59e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 1 MRYNQLGNTGLFVSELCLGTMTFGENqtgavWSAVaglDQGAADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAIKnl 80
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTMTFGGP-----WGGV---DEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALK-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 81 GVPRKDVIIATKFHGQMGDKPNDRGASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVRYI 160
Cdd:COG0667 71 GRPRDDVVIATKVGRRMGPGPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 161 GLSNWAAWRMAKALGISErkGYARFETVQAYYSIAGRDLERDIVPLMQEEKLGLMVWSPLAGGLLSGKYGPGAPGNGEGR 240
Cdd:COG0667 151 GVSNYSAEQLRRALAIAE--GLPPIVAVQNEYSLLDRSAEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGATFPEGDR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 241 RANFDFPPVDKDRAWACVAAMREVGARHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAVKLKLDAEDVAKLDE 320
Cdd:COG0667 229 AATNFVQGYLTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADLELSAEDLAALDA 308
|
....*..
gi 2229004110 321 VSALAPE 327
Cdd:COG0667 309 ALAAVPA 315
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
1-322 |
1.42e-131 |
|
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: 378.07 E-value: 1.42e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 1 MRYNQLGNTGLFVSELCLGTMTFGENQtgavwsavaglDQGAADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAIKNL 80
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGTMNFGGRT-----------DEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAGR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 81 gvpRKDVIIATKFHGQMGDKPNDRGASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVRYI 160
Cdd:cd19087 70 ---RDDIVLATKVFGPMGDDPNDRGLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 161 GLSNWAAWRMAKALGISERKGYARFETVQAYYSIAGRDLERDIVPLMQEEKLGLMVWSPLAGGLLSGKYGPGAPGNGEGR 240
Cdd:cd19087 147 GVSNFAAWQIAKAQGIAARRGLLRFVSEQPMYNLLKRQAELEILPAARAYGLGVIPYSPLAGGLLTGKYGKGKRPESGRL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 241 RANFDFPPVDK-DRAWACVAAMREVGARHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAVKLKLDAEDVAKLD 319
Cdd:cd19087 227 VERARYQARYGlEEYRDIAERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEITLTPELLAEID 306
|
...
gi 2229004110 320 EVS 322
Cdd:cd19087 307 ELF 309
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
3-319 |
8.71e-129 |
|
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: 370.76 E-value: 8.71e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 3 YNQLGNTGLFVSELCLGTMTFGENQTGAvWSavagLDQGAADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAIKNLGv 82
Cdd:cd19079 2 YVRLGNSGLKVSRLCLGCMSFGDPKWRP-WV----LDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEFA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 83 PRKDVIIATKFHGQMGDKPNDRGASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVRYIGL 162
Cdd:cd19079 76 PRDEVVIATKVYFPMGDGPNGRGLSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 163 SNWAAWRMAKALGISERKGYARFETVQAYYSIAGRDLERDIVPLMQEEKLGLMVWSPLAGGLLSGKYGPGAPGNGEGRRA 242
Cdd:cd19079 156 SSMYAWQFAKALHLAEKNGWTKFVSMQNHYNLLYREEEREMIPLCEEEGIGVIPWSPLARGRLARPWGDTTERRRSTTDT 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2229004110 243 NFDFPPVDKDRAWACVAAMREVGARHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAVKLKLDAEDVAKLD 319
Cdd:cd19079 236 AKLKYDYFTEADKEIVDRVEEVAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAALDIKLSEEEIKYLE 312
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
5-319 |
6.01e-122 |
|
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: 353.44 E-value: 6.01e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 5 QLGNTGLFVSELCLGTMTFGenqtgavWSAvaglDQGAADKIVERSLAAGVNFIDTANVYSQ-------GRSEVILGQAI 77
Cdd:cd19081 1 PLGRTGLSVSPLCLGTMVFG-------WTA----DEETSFALLDAFVDAGGNFIDTADVYSAwvpgnagGESETIIGRWL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 78 KNLGvPRKDVIIATKFHGQMGdkPNDRGASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLV 157
Cdd:cd19081 70 KSRG-KRDRVVIATKVGFPMG--PNGPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 158 RYIGLSNWAAWRMAKALGISERKGYARFETVQAYYSIAGRD-LERDIVPLMQEEKLGLMVWSPLAGGLLSGKYGPGAPGN 236
Cdd:cd19081 147 RYIGASNYSAWRLQEALELSRQHGLPRYVSLQPEYNLVDREsFEGELLPLCREEGIGVIPYSPLAGGFLTGKYRSEADLP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 237 GEGRRANFdfppVDK---DRAWACVAAMREVGARHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAVKLKLDAE 313
Cdd:cd19081 227 GSTRRGEA----AKRylnERGLRILDALDEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAGLRLTDE 302
|
....*.
gi 2229004110 314 DVAKLD 319
Cdd:cd19081 303 EVARLD 308
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
6-319 |
1.52e-108 |
|
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: 319.16 E-value: 1.52e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 6 LGNTGLFVSELCLGTMTFGENqtgavWSAvaGLDQGAADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAIKNLgvpRK 85
Cdd:cd19080 3 LGRSGLRVSPLALGTMTFGTE-----WGW--GADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAGN---RD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 86 DVIIATKFHGQM-GDKPNDRGASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVRYIGLSN 164
Cdd:cd19080 73 RIVLATKYTMNRrPGDPNAGGNHRKNLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 165 WAAWRMAKALGISERKGYARFETVQAYYSIAGRDLERDIVPLMQEEKLGLMVWSPLAGGLLSGKYGPGAPGNGEGR-RAN 243
Cdd:cd19080 153 TPAWVVARANTLAELRGWSPFVALQIEYSLLERTPERELLPMARALGLGVTPWSPLGGGLLTGKYQRGEEGRAGEAkGVT 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2229004110 244 FDFPPVDkDRAWACVAAMREVGARHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAVKLKLDAEDVAKLD 319
Cdd:cd19080 233 VGFGKLT-ERNWAIVDVVAAVAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDLTLSPEQLARLD 307
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
10-319 |
3.95e-100 |
|
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: 297.52 E-value: 3.95e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 10 GLFVSELCLGTMTFGenqtGAVWSAVaglDQGAADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAIKNLgvpRKDVII 89
Cdd:cd19084 1 DLKVSRIGLGTWAIG----GTWWGEV---DDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKGR---RDDVVI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 90 ATKFHGQMGDKPND-RGASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVRYIGLSNWAAW 168
Cdd:cd19084 71 ATKCGLRWDGGKGVtKDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 169 RMAKALgiserkGYARFETVQAYYSIAGRDLERDIVPLMQEEKLGLMVWSPLAGGLLSGKYGPGA-PGNGEGRRANFDFP 247
Cdd:cd19084 151 QLEEAR------KYGPIVSLQPPYSMLEREIEEELLPYCRENGIGVLPYGPLAQGLLTGKYKKEPtFPPDDRRSRFPFFR 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2229004110 248 PVDKDRAWACVAAMREVGARHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAVKLKLDAEDVAKLD 319
Cdd:cd19084 225 GENFEKNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDWELTEEELKEID 296
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
10-313 |
5.53e-100 |
|
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: 297.20 E-value: 5.53e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 10 GLFVSELCLGT-MTFGEnqtgavwsavaGLDQGAADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAIKnlGVPRKDVI 88
Cdd:cd19074 1 GLKVSELSLGTwLTFGG-----------QVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALK--GWPRESYV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 89 IATKFHGQMGDKPNDRGASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVRYIGLSNWAAW 168
Cdd:cd19074 68 ISTKVFWPTGPGPNDRGLSRKHIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 169 RMAKALGISERKGYARFETVQAYYSIAGRDLERDIVPLMQEEKLGLMVWSPLAGGLLSGKYGPGAPgNGEGRRANFDFPP 248
Cdd:cd19074 148 QIAEAHDLARQFGLIPPVVEQPQYNMLWREIEEEVIPLCEKNGIGLVVWSPLAQGLLTGKYRDGIP-PPSRSRATDEDNR 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2229004110 249 vDKDRAW------ACVAAMREVGARHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAVKLKLDAE 313
Cdd:cd19074 227 -DKKRRLltdenlEKVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKASGVKLSPE 296
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
16-321 |
2.41e-93 |
|
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: 279.97 E-value: 2.41e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 16 LCLGTMTFGeNQTGAVwsavaglDQGAADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAIKNLGVPRKDVIIATKfhG 95
Cdd:pfam00248 1 IGLGTWQLG-GGWGPI-------SKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKRDKVVIATK--V 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 96 QMGDKPNDRGASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVRYIGLSNWAAWRMAKALg 175
Cdd:pfam00248 71 PDGDGPWPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKAL- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 176 iseRKGYARFETVQAYYSIAGRDLERDIVPLMQEEKLGLMVWSPLAGGLLSGKYGPGAPGNGEGRRANFDFPPVDKDRAw 255
Cdd:pfam00248 150 ---TKGKIPIVAVQVEYNLLRRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPGERRRLLKKGTPLNLEA- 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2229004110 256 acVAAMREVGARHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAVKLKLDAEDVAKLDEV 321
Cdd:pfam00248 226 --LEALEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDEL 289
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
1-321 |
4.94e-93 |
|
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: 280.25 E-value: 4.94e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 1 MRYNQLGNTGLFVSELCLGT-MTFGENqtgavwsavagLDQGAADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAIKN 79
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSwVTFGNQ-----------VDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 80 LGVPRKDVIIATK-FHGQMGDKPNDRGASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVR 158
Cdd:cd19143 70 LGWPRSDYVVSTKiFWGGGGPPPNDRGLSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 159 YIGLSNWAAWRMAKALGISERKGYARFETVQAYYSIAGRD-LERDIVPLMQEEKLGLMVWSPLAGGLLSGKYGPGAPgng 237
Cdd:cd19143 150 YWGTSEWSAQQIEEAHEIADRLGLIPPVMEQPQYNLFHRErVEVEYAPLYEKYGLGTTTWSPLASGLLTGKYNNGIP--- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 238 EGRRANFDFPPVDKDRAW-------ACVAAMREVGARHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAVKL-- 308
Cdd:cd19143 227 EGSRLALPGYEWLKDRKEelgqekiEKVRKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEENLKALEVlp 306
|
330
....*....|...
gi 2229004110 309 KLDAEDVAKLDEV 321
Cdd:cd19143 307 KLTPEVMEKIEAI 319
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
14-304 |
2.68e-87 |
|
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: 262.45 E-value: 2.68e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 14 SELCLGTMTFGENQtgavwsavaglDQGAADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAIKNLGVpRKDVIIATKF 93
Cdd:cd06660 1 SRLGLGTMTFGGDG-----------DEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRGN-RDDVVIATKG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 94 HGQMGDKPNDRGASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVRYIGLSNWAAWRMAKA 173
Cdd:cd06660 69 GHPPGGDPSRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 174 LGISERKGYARFETVQAYYSIAGRD-LERDIVPLMQEEKLGLMVWSPLAGGLlsgkygpgapgngegrranfdfppvdkd 252
Cdd:cd06660 149 LAYAKAHGLPGFAAVQPQYSLLDRSpMEEELLDWAEENGLPLLAYSPLARGP---------------------------- 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2229004110 253 rawacvaamrevgarhgasvAEVALAYILAKPFVTSVIIGAKRLEQLEENLK 304
Cdd:cd06660 201 --------------------AQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
13-321 |
4.48e-84 |
|
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: 257.49 E-value: 4.48e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 13 VSELCLGTMTFGENQTGAvwSAVAGLDqgaadkiveRSLAAGVNFIDTANVYS-------QGRSEVILGQAIKNLGvPRK 85
Cdd:cd19094 1 VSEICLGTMTWGEQNTEA--EAHEQLD---------YAFDEGVNFIDTAEMYPvppspetQGRTEEIIGSWLKKKG-NRD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 86 DVIIATKFHGQMGDKPNDRGA----SRGHIMDSVEQSLERLQMNHIDLYQIHGTD------------------TVTPIDE 143
Cdd:cd19094 69 KVVLATKVAGPGEGITWPRGGgtrlDRENIREAVEGSLKRLGTDYIDLYQLHWPDrytplfgggyytepseeeDSVSFEE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 144 TLRALDDLVSRGLVRYIGLSNWAAWRMAKALGISERKGYARFETVQAYYSIAGRDLERDIVPLMQEEKLGLMVWSPLAGG 223
Cdd:cd19094 149 QLEALGELVKAGKIRHIGLSNETPWGVMKFLELAEQLGLPRIVSIQNPYSLLNRNFEEGLAEACHRENVGLLAYSPLAGG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 224 LLSGKYGPGAPGNGEGRRANF--DFPPVDKDRAWACVAAMREVGARHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEE 301
Cdd:cd19094 229 VLTGKYLDGAARPEGGRLNLFpgYMARYRSPQALEAVAEYVKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLKE 308
|
330 340
....*....|....*....|
gi 2229004110 302 NLKAVKLKLDAEDVAKLDEV 321
Cdd:cd19094 309 NIDAFDVPLSDELLAEIDAV 328
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
13-322 |
3.20e-83 |
|
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: 254.05 E-value: 3.20e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 13 VSELCLGTMTFGENQTgavWSAVaglDQGAADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAIKNlgvPRKDVIIATK 92
Cdd:cd19085 1 VSRLGLGCWQFGGGYW---WGDQ---DDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKG---RRDDVVIATK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 93 FhGQMGDKPNDrgasrghIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVRYIGLSNWAAWRMAK 172
Cdd:cd19085 72 V-SPDNLTPED-------VRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 173 ALGiserkgYARFETVQAYYSIAGRDLERDIVPLMQEEKLGLMVWSPLAGGLLSGKYGPGA---PGNGEGRRANFDFPPV 249
Cdd:cd19085 144 ALD------AGRIDSNQLPYNLLWRAIEYEILPFCREHGIGVLAYSPLAQGLLTGKFSSAEdfpPGDARTRLFRHFEPGA 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2229004110 250 DKdRAWACVAAMREVGARHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAVKLKLDAEDVAKLDEVS 322
Cdd:cd19085 218 EE-ETFEALEKLKEIADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVDLELSPSVLERLDEIS 289
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
3-320 |
1.52e-77 |
|
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: 240.64 E-value: 1.52e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 3 YNQLGNTGLFVSELCLGTMTFGenqtGavWSAVAGLDQGAADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAIKNLgv 82
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTWAIG----G--GPWWGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKGR-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 83 pRKDVIIATK-----------FHGQMGDKPNDRGASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDL 151
Cdd:cd19149 73 -RDKVVLATKcglrwdreggsFFFVRDGVTVYKNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 152 VSRGLVRYIGLSNWAAWRMAKALgiserkGYARFETVQAYYSIAGRDLERDIVPLMQEEKLGLMVWSPLAGGLLSGKYGP 231
Cdd:cd19149 152 KRQGKIRAIGASNVSVEQIKEYV------KAGQLDIIQEKYSMLDRGIEKELLPYCKKNNIAFQAYSPLEQGLLTGKITP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 232 GAPGNGEGRRANFD-FPPVDKDRAWACVAAMREVGARHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAVKLKL 310
Cdd:cd19149 226 DREFDAGDARSGIPwFSPENREKVLALLEKWKPLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPEQAEENAKAGDIRL 305
|
330
....*....|
gi 2229004110 311 DAEDVAKLDE 320
Cdd:cd19149 306 SAEDIATMRS 315
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
13-319 |
5.25e-76 |
|
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: 235.97 E-value: 5.25e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 13 VSELCLGTMTFGeNQTGAVWSavaGLDQGAADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAIKNLGvPRKDVIIATK 92
Cdd:cd19093 2 VSPLGLGTWQWG-DRLWWGYG---EYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELG-DRDEVVIATK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 93 FHgqmgdkPNDRGASRGHIMDSVEQSLERLQMNHIDLYQIHG-TDTVTPIDETLRALDDLVSRGLVRYIGLSNWAAWRMA 171
Cdd:cd19093 77 FA------PLPWRLTRRSVVKALKASLERLGLDSIDLYQLHWpGPWYSQIEALMDGLADAVEEGLVRAVGVSNYSADQLR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 172 KALGISERKGYaRFETVQAYYSIAGRDLERD-IVPLMQEEKLGLMVWSPLAGGLLSGKYGPGAPGNGeGRRANFDFPPVD 250
Cdd:cd19093 151 RAHKALKERGV-PLASNQVEYSLLYRDPEQNgLLPACDELGITLIAYSPLAQGLLTGKYSPENPPPG-GRRRLFGRKNLE 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2229004110 251 KDraWACVAAMREVGARHGASVAEVALAYILAKPFVtsVIIGAKRLEQLEENLKAVKLKLDAEDVAKLD 319
Cdd:cd19093 229 KV--QPLLDALEEIAEKYGKTPAQVALNWLIAKGVV--PIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
13-305 |
1.18e-71 |
|
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: 222.74 E-value: 1.18e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 13 VSELCLGTMTFGENQTGAVwsavaglDQGAADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAIKNlgvPRKDVIIATK 92
Cdd:cd19086 3 VSEIGFGTWGLGGDWWGDV-------DDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKG---RRDKVVIATK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 93 F-HGQMGDKPNDRGASRGHIMDSVEQSLERLQMNHIDLYQIH-GTDTVTPIDETLRALDDLVSRGLVRYIGLSNWAAWRM 170
Cdd:cd19086 73 FgNRFDGGPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLHnPPDEVLDNDELFEALEKLKQEGKIRAYGVSVGDPEEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 171 AKALgiseRKGyaRFETVQAYYSIAGRDLERDIVPLMQEEKLGLMVWSPLAGGLLSGKygpgapgngegrranfdfppvd 250
Cdd:cd19086 153 LAAL----RRG--GIDVVQVIYNLLDQRPEEELFPLAEEHGVGVIARVPLASGLLTGK---------------------- 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2229004110 251 kdrawacvaamrevgarhgasVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKA 305
Cdd:cd19086 205 ---------------------LAQAALRFILSHPAVSTVIPGARSPEQVEENAAA 238
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
18-320 |
4.47e-69 |
|
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: 218.31 E-value: 4.47e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 18 LGTMTFGENQTGAVWSAVAGLDQGAAdkiVERSLAAGVNFIDTANVYSQGRSEVILGQAIKNLgvpRKDVIIATKfhgqM 97
Cdd:cd19102 6 LGTWAIGGGGWGGGWGPQDDRDSIAA---IRAALDLGINWIDTAAVYGLGHSEEVVGRALKGL---RDRPIVATK----C 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 98 GDKPNDRGASRGHIMDS-----VEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVRYIGLSNWAAWRMAK 172
Cdd:cd19102 76 GLLWDEEGRIRRSLKPAsiraeCEASLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 173 ALGIserkgyARFETVQAYYSIAGRDLERDIVPLMQEEKLGLMVWSPLAGGLLSGKYGPG----APGNGEGRRANFdFPP 248
Cdd:cd19102 156 CQAI------HPIASLQPPYSLLRRGIEAEILPFCAEHGIGVIVYSPMQSGLLTGKMTPErvasLPADDWRRRSPF-FQE 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2229004110 249 VDKDRAWACVAAMREVGARHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAVKLKLDAEDVAKLDE 320
Cdd:cd19102 229 PNLARNLALVDALRPIAERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAADLRLTPEELAEIEA 300
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
2-318 |
1.31e-64 |
|
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: 207.07 E-value: 1.31e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 2 RYNQLGNTGLFVSELCLGTMTFGEnqtgavwsAVAGLDQGAADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAIKNlg 81
Cdd:cd19076 1 PTRKLGTQGLEVSALGLGCMGMSA--------FYGPADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKD-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 82 vPRKDVIIATKFHGQMGDKPNDRG--ASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVRY 159
Cdd:cd19076 71 -RRDEVVIATKFGIVRDPGSGFRGvdGRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 160 IGLSNWAA---WRMAKALGISerkgyarfeTVQAYYSIAGRDLERDIVPLMQEEKLGLMVWSPLAGGLLSGKYG-PGAPG 235
Cdd:cd19076 150 IGLSEASAdtiRRAHAVHPIT---------AVQSEYSLWTRDIEDEVLPTCRELGIGFVAYSPLGRGFLTGAIKsPEDLP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 236 NGEGRRANFDFPPVDKDRAWACVAAMREVGARHGASVAEVALAYILAK-PFVTSvIIGAKRLEQLEENLKAVKLKLDAED 314
Cdd:cd19076 221 EDDFRRNNPRFQGENFDKNLKLVEKLEAIAAEKGCTPAQLALAWVLAQgDDIVP-IPGTKRIKYLEENVGALDVVLTPEE 299
|
....
gi 2229004110 315 VAKL 318
Cdd:cd19076 300 LAEI 303
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
10-333 |
1.14e-63 |
|
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: 205.35 E-value: 1.14e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 10 GLFVSELCLGTMTFGENqtgavWSAVAG-LDQGAADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAIKNLGVpRKDVI 88
Cdd:cd19146 8 GVRVSPLCLGAMSFGEA-----WKSMMGeCDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMASRGN-RDEMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 89 IATKF------HGQMGDKPNDRGASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVRYIGL 162
Cdd:cd19146 82 LATKYttgyrrGGPIKIKSNYQGNHAKSLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 163 SNWAAWRMAKALGISERKGYARFETVQAYYSIAGRDLERDIVPLMQEEKLGLMVWsplaGGLLSGKYGPGAPGNGEGRRA 242
Cdd:cd19146 162 SDTPAWVVSKANAYARAHGLTQFVVYQGHWSAAFRDFERDILPMCEAEGMALAPW----GVLGQGQFRTEEEFKRRGRSG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 243 NFDFPPVDKDRAWAcvAAMREVGARHGASVAEVALAYILAK-PFVTSvIIGAKRLEQLEENLKAVKLKLDAEDVAKLDEV 321
Cdd:cd19146 238 RKGGPQTEKERKVS--EKLEKVAEEKGTAITSVALAYVMHKaPYVFP-IVGGRKVEHLKGNIEALGISLSDEEIQEIEDA 314
|
330
....*....|..
gi 2229004110 322 SALAPEYPGWML 333
Cdd:cd19146 315 YPFDVGFPMNFL 326
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
3-316 |
9.45e-63 |
|
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: 202.10 E-value: 9.45e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 3 YNQLGNTGLFVSELCLGT-MTFGENQtgavwsavaglDQGAADKIVERSLAAGVNFIDTANVY--SQGRSEVILGQAIK- 78
Cdd:cd19089 1 YRRCGRSGLHLPAISLGLwHNFGDYT-----------SPEEARELLRTAFDLGITHFDLANNYgpPPGSAEENFGRILKr 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 79 NLGVPRKDVIIATKFHGQMGDKPNDRGASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVR 158
Cdd:cd19089 70 DLRPYRDELVISTKAGYGMWPGPYGDGGSRKYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 159 YIGLSNWAAWRMAKALGISERKGyARFETVQAYYSIAGRDLERDIVPLMQEEKLGLMVWSPLAGGLLSGKYGPGAPGNGE 238
Cdd:cd19089 150 YVGISNYPGAKARRAIALLRELG-VPLIIHQPRYSLLDRWAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKYLNGIPPDSR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 239 GRRANFDFPPVDKD-------RAWACVAAMRevgarhGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAVK-LKL 310
Cdd:cd19089 229 RAAESKFLTEEALTpekleqlRKLNKIAAKR------GQSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAALKnLDF 302
|
....*.
gi 2229004110 311 DAEDVA 316
Cdd:cd19089 303 SEEELA 308
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
10-319 |
3.68e-62 |
|
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: 199.38 E-value: 3.68e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 10 GLFVSELCLGTMTFGENqtgavWSAVAGLDQGAADKIvERSLAAGVNFIDTANVYSQGRSEVILGQAIKnlGVPRKDVII 89
Cdd:cd19072 1 GEEVPVLGLGTWGIGGG-----MSKDYSDDKKAIEAL-RYAIELGINLIDTAEMYGGGHAEELVGKAIK--GFDREDLFI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 90 ATKF---HGqmgdKPNDrgasrghIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVRYIGLSNWA 166
Cdd:cd19072 73 TTKVspdHL----KYDD-------VIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 167 AWRMAKALGISERKGYArfeTVQAYYSIAGRDLERDIVPLMQEEKLGLMVWSPLAGGLLSGKYGPgapgngegrranfdf 246
Cdd:cd19072 142 LEELEEAQSYLKKGPIV---ANQVEYNLFDREEESGLLPYCQKNGIAIIAYSPLEKGKLSNAKGS--------------- 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2229004110 247 ppvdkdrawacvAAMREVGARHGASVAEVALAYILAKPFVTsVIIGAKRLEQLEENLKAVKLKLDAEDVAKLD 319
Cdd:cd19072 204 ------------PLLDEIAKKYGKTPAQIALNWLISKPNVI-AIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
14-305 |
4.53e-61 |
|
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: 197.39 E-value: 4.53e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 14 SELCLGTMTFGENqtgavwsavagLDQGAADKIVERSLAAGVNFIDTANVYSQ----GRSEVILGQAIKNLGVpRKDVII 89
Cdd:cd19082 1 SRIVLGTADFGTR-----------IDEEEAFALLDAFVELGGNFIDTARVYGDwverGASERVIGEWLKSRGN-RDKVVI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 90 ATK-FHGQMGDKPNDRgASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVRYIGLSNWAAW 168
Cdd:cd19082 69 ATKgGHPDLEDMSRSR-LSPEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNWSTE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 169 RMAKALGISERKGYARFETVQAYYSIAgrDLERDIVP-------------LMQEEKLGLMVWSPLAGGLLSGKYGPGAPG 235
Cdd:cd19082 148 RIAEANAYAKAHGLPGFAASSPQWSLA--RPNEPPWPgptlvamdeemraWHEENQLPVFAYSSQARGFFSKRAAGGAED 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 236 NGEGRRAnFDFPPvdkdrAWACVAAMREVGARHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKA 305
Cdd:cd19082 226 DSELRRV-YYSEE-----NFERLERAKELAEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAA 289
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
5-319 |
8.79e-61 |
|
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: 197.26 E-value: 8.79e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 5 QLGNTGLFVSELCLGTmtfgenqtgavwSAVAG------LDQGAADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAIK 78
Cdd:cd19083 3 KLGKSDIDVNPIGLGT------------NAVGGhnlypnLDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 79 nlGVPRKDVIIATKFHGQMGDKPNDRGASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVR 158
Cdd:cd19083 71 --EYNRNEVVIATKGAHKFGGDGSVLNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 159 YIGLSNWAawrmAKALGISERKGYarFETVQAYYSIAGRDLERDIVPLMQEEKLGLMVWSPLAGGLLSGKYGPgapgnge 238
Cdd:cd19083 149 AIGVSNFS----LEQLKEANKDGY--VDVLQGEYNLLQREAEEDILPYCVENNISFIPYFPLASGLLAGKYTK------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 239 grraNFDFPPVD--KDRA----------WACVAAMREVGARHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAV 306
Cdd:cd19083 216 ----DTKFPDNDlrNDKPlfkgerfsenLDKVDKLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKAL 291
|
330
....*....|...
gi 2229004110 307 KLKLDAEDVAKLD 319
Cdd:cd19083 292 DVTLTEEEIAFID 304
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-306 |
6.68e-60 |
|
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: 194.47 E-value: 6.68e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 14 SELCLGTMTFGENqtgavwsavagLDQGAADKIVERSLAAGVNFIDTANVYSQ-------GRSEVILGQAIKNLGVpRKD 86
Cdd:cd19752 1 SELCLGTMYFGTR-----------TDEETSFAILDRYVAAGGNFLDTANNYAFwteggvgGESERLIGRWLKDRGN-RDD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 87 VIIATKFHGQMGDKPNDR----GASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVRYIGL 162
Cdd:cd19752 69 VVIATKVGAGPRDPDGGPespeGLSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 163 SNWAAWRMAKALGISERKGYARFETVQAYYSI----AGRD------LERDIVPLMQEEK-LGLMVWSPlaggLLSGKYG- 230
Cdd:cd19752 149 SNFAAWRLERARQIARQQGWAEFSAIQQRHSYlrprPGADfgvqriVTDELLDYASSRPdLTLLAYSP----LLSGAYTr 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2229004110 231 PGAPgngegRRANFDFPPVDKDRawacvAAMREVGARHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAV 306
Cdd:cd19752 225 PDRP-----LPEQYDGPDSDARL-----AVLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAAL 290
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
18-321 |
5.62e-58 |
|
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: 189.69 E-value: 5.62e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 18 LGTMTFGEnQTGAVWSAvagldqgAADKIVERSLAAGVNFIDTANVYSQGRSEVILGQaiknLGVPRKDVIIATKFHGqm 97
Cdd:cd19075 5 LGTMTFGS-QGRFTTAE-------AAAELLDAFLERGHTEIDTARVYPDGTSEELLGE----LGLGERGFKIDTKANP-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 98 gdkPNDRGASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVRYIGLSNWAAWRMAKALGIS 177
Cdd:cd19075 71 ---GVGGGLSPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEIC 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 178 ERKGYARfETV-QAYYSIAGRDLERDIVPLMQEEKLGLMVWSPLAGGLLSGKYGPGAPGNGEGRranFD----FPPVDKD 252
Cdd:cd19075 148 KENGWVL-PTVyQGMYNAITRQVETELFPCLRKLGIRFYAYSPLAGGFLTGKYKYSEDKAGGGR---FDpnnaLGKLYRD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 253 RAW-----ACVAAMREVGARHGASVAEVALAYI-----LAKPFVTSVIIGAKRLEQLEENLKAVKL-KLDAEDVAKLDEV 321
Cdd:cd19075 224 RYWkpsyfEALEKVEEAAEKEGISLAEAALRWLyhhsaLDGEKGDGVILGASSLEQLEENLAALEKgPLPEEVVKAIDEA 303
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
10-321 |
1.19e-57 |
|
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: 189.05 E-value: 1.19e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 10 GLFVSELCLGTMTFGenqtGAVWsavAGLDQGAADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAIKNLGvPRKDVII 89
Cdd:cd19148 1 DLPVSRIALGTWAIG----GWMW---GGTDEKEAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKEYG-KRDRVVI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 90 ATKFHGQMGD-KPNDRGASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVRYIGLSNWAAW 168
Cdd:cd19148 73 ATKVGLEWDEgGEVVRNSSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSPE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 169 RMakalgiSERKGYARFETVQAYYSIAGRDLERDIVPLMQEEKLGLMVWSPLAGGLLSGKYGPGAPGNGEG-RRANFDFP 247
Cdd:cd19148 153 QM------ETFRKVAPLHTVQPPYNLFEREIEKDVLPYARKHNIVTLAYGALCRGLLSGKMTKDTKFEGDDlRRTDPKFQ 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2229004110 248 PVDKDRAWACVAAMREVG-ARHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAVKLKLDAEDVAKLDEV 321
Cdd:cd19148 227 EPRFSQYLAAVEELDKLAqERYGKSVIHLAVRWLLDQPGVSIALWGARKPEQLDAVDEVFGWSLNDEDMKEIDAI 301
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
1-321 |
1.37e-56 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 187.75 E-value: 1.37e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 1 MRYNQLGNTGLFVSELCLGTMTFGENQTGAvwSAVAGLDQgaadkiverSLAAGVNFIDTANVY-------SQGRSEVIL 73
Cdd:PRK10625 1 MQYHRIPHSSLEVSTLGLGTMTFGEQNSEA--DAHAQLDY---------AVAQGINLIDVAEMYpvpprpeTQGLTETYI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 74 GQAIKNLGvPRKDVIIATKFHG-----QMGDKPNdRGASRGHIMDSVEQSLERLQMNHIDLYQIH--------------- 133
Cdd:PRK10625 70 GNWLAKRG-SREKLIIASKVSGpsrnnDKGIRPN-QALDRKNIREALHDSLKRLQTDYLDLYQVHwpqrptncfgklgys 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 134 ---GTDTVTPIdETLRALDDLVSRGLVRYIGLSNWAAWRMAKALGISERKGYARFETVQAYYSIAGRDLERDIVPLMQEE 210
Cdd:PRK10625 148 wtdSAPAVSLL-ETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEKHDLPRIVTIQNPYSLLNRSFEVGLAEVSQYE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 211 KLGLMVWSPLAGGLLSGKYGPGAPGNGeGRRANFD-FPPVDKDRAWACVAAMREVGARHGASVAEVALAYILAKPFVTSV 289
Cdd:PRK10625 227 GVELLAYSCLAFGTLTGKYLNGAKPAG-ARNTLFSrFTRYSGEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVAST 305
|
330 340 350
....*....|....*....|....*....|..
gi 2229004110 290 IIGAKRLEQLEENLKAVKLKLDAEDVAKLDEV 321
Cdd:PRK10625 306 LLGATTMEQLKTNIESLHLTLSEEVLAEIEAV 337
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
1-314 |
2.13e-56 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 185.35 E-value: 2.13e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 1 MRYNQLGNTGLFVSELCLGTMTFGEnqtgavwsavAGLDQGAADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAIKNL 80
Cdd:COG4989 1 MKRIKLGASGLSVSRIVLGCMRLGE----------WDLSPAEAAALIEAALELGITTFDHADIYGGYTCEALFGEALKLS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 81 GVPRKDVIIATKFHGQMGDKPNDRGA-----SRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRG 155
Cdd:COG4989 71 PSLREKIELQTKCGIRLPSEARDNRVkhydtSKEHIIASVEGSLRRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELKASG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 156 LVRYIGLSNWAAWRMAkALgiserKGYARFE--TVQAYYSIAGRD-LERDIVPLMQEEKLGLMVWSPLAGGLLSGKYGPg 232
Cdd:COG4989 151 KVRHFGVSNFTPSQFE-LL-----QSALDQPlvTNQIELSLLHTDaFDDGTLDYCQLNGITPMAWSPLAGGRLFGGFDE- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 233 apgngegrranfDFPPVDkdrawacvAAMREVGARHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAVKLKLDA 312
Cdd:COG4989 224 ------------QFPRLR--------AALDELAEKYGVSPEAIALAWLLRHPAGIQPVIGTTNPERIKAAAAALDIELTR 283
|
..
gi 2229004110 313 ED 314
Cdd:COG4989 284 EE 285
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
10-320 |
1.00e-54 |
|
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: 181.28 E-value: 1.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 10 GLFVSELCLGTM--TFGENQTgavwsavagLDQGAADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAIKNlgvPRKDV 87
Cdd:cd19078 1 GLEVSAIGLGCMgmSHGYGPP---------PDKEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKP---FRDQV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 88 IIATKF-HGQMGDKPNDRG--ASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVRYIGLSn 164
Cdd:cd19078 69 VIATKFgFKIDGGKPGPLGldSRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLS- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 165 waawrMAKALGIseRKGYARF--ETVQAYYSIAGRDLERDIVPLMQEEKLGLMVWSPLAGGLLSGKYGPGAP-GNGEGRR 241
Cdd:cd19078 148 -----EAGVETI--RRAHAVCpvTAVQSEYSMMWREPEKEVLPTLEELGIGFVPFSPLGKGFLTGKIDENTKfDEGDDRA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 242 ANFDFPPVDKDRAWACVAAMREVGARHGASVAEVALAYILA-KPFVTSvIIGAKRLEQLEENLKAVKLKLDAEDVAKLDE 320
Cdd:cd19078 221 SLPRFTPEALEANQALVDLLKEFAEEKGATPAQIALAWLLAkKPWIVP-IPGTTKLSRLEENIGAADIELTPEELREIED 299
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
14-313 |
7.18e-53 |
|
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: 175.82 E-value: 7.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 14 SELCLGTMTFGenqtgavwSAVAGLDQGAADKIVERSLAAGVNFIDTANVYsqGRSEVILGQAIKnlGVPRKDVIIATKF 93
Cdd:cd19090 1 SALGLGTAGLG--------GVFGGVDDDEAVATIRAALDLGINYIDTAPAY--GDSEERLGLALA--ELPREPLVLSTKV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 94 hGQMGDKPNDRgaSRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTP-----IDETLRALDDLVSRGLVRYIGLSNWAAW 168
Cdd:cd19090 69 -GRLPEDTADY--SADRVRRSVEESLERLGRDRIDLLMIHDPERVPWvdilaPGGALEALLELKEEGLIKHIGLGGGPPD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 169 RMAKALgiseRKGyaRFETVQAY--YSIAGRDLERDIVPLMQEEKLGLMVWSPLAGGLLSGKYGPgapgngEGRRANFDF 246
Cdd:cd19090 146 LLRRAI----ETG--DFDVVLTAnrYTLLDQSAADELLPAAARHGVGVINASPLGMGLLAGRPPE------RVRYTYRWL 213
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2229004110 247 PPVDKDRAwacvAAMREVGARHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAVKLKLDAE 313
Cdd:cd19090 214 SPELLDRA----KRLYELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAAEGPLPEE 276
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
2-308 |
1.38e-52 |
|
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: 176.10 E-value: 1.38e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 2 RYNQLGNTGLFVSELCLGT-MTFGENQTGAVwsavagldqgaADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAIKNL 80
Cdd:cd19141 1 PYRNLGKSGLRVSCLGLGTwVTFGSQISDEV-----------AEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 81 GVPRKDVIIATK-FHGqmGDKPNDRGASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVRY 159
Cdd:cd19141 70 GWRRSSYVITTKiFWG--GKAETERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 160 IGLSNWAAWRMAKALGISERKGYARFETVQAYYSIAGRD-LERDIVPLMQEEKLGLMVWSPLAGGLLSGKYGPGAPGNGE 238
Cdd:cd19141 148 WGTSRWSAMEIMEAYSVARQFNLIPPIVEQAEYHLFQREkVEMQLPELFHKIGVGAMTWSPLACGILSGKYDDGVPEYSR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 239 GRRANFDfppvdkdraWACVAAMREVGARH--------------GASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLK 304
Cdd:cd19141 228 ASLKGYQ---------WLKEKILSEEGRRQqaklkelqiiadrlGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQ 298
|
....
gi 2229004110 305 AVKL 308
Cdd:cd19141 299 AIQV 302
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-306 |
1.40e-52 |
|
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: 173.92 E-value: 1.40e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 1 MRYNQLGNTGLFVSELCLGTMTFgenqtgavwsavagldQGAADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAIKnl 80
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFGGGGL----------------PRESPELLRRALDLGINYFDTAEGYGNGNSEEIIGEALK-- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 81 GVPRKDVIIATKFHgqmgdkPNDRGASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPI---DETLRALDDLVSRGLV 157
Cdd:cd19105 63 GLRRDKVFLATKAS------PRLDKKDKAELLKSVEESLKRLQTDYIDIYQLHGVDTPEERllnEELLEALEKLKKEGKV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 158 RYIGLS--NWAAWRMAKALgiseRKGyaRFETVQAYYSIAGR-DLERDIVPLMQEEKLGLMVWSPLAGGLLSGKYGPGAP 234
Cdd:cd19105 137 RFIGFSthDNMAEVLQAAI----ESG--WFDVIMVAYNFLNQpAELEEALAAAAEKGIGVVAMKTLAGGYLQPALLSVLK 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2229004110 235 GNgegrranfdfppvdkdrawacvaamrevgarhGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAV 306
Cdd:cd19105 211 AK--------------------------------GFSLPQAALKWVLSNPRVDTVVPGMRNFAELEENLAAA 250
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
1-321 |
4.54e-52 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 176.16 E-value: 4.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 1 MRYNQLGNTGLFVSELCLGTMTFGEnqtgavwsavagLDQGAADKIVERSLAAGVNFIDTANVYsqGRSEVILGQAIKNl 80
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGMRLPR------------KDEEEAEALIRRAIDNGINYIDTARGY--GDSEEFLGKALKG- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 81 gvPRKDVIIATKFHGqmgdkpndRGASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLR------ALDDLVSR 154
Cdd:COG1453 66 --PRDKVILATKLPP--------WVRDPEDMRKDLEESLKRLQTDYIDLYLIHGLNTEEDLEKVLKpggaleALEKAKAE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 155 GLVRYIGLSNWAAWRMAKALgIserKGYaRFETVQAYYSIAGRDL--ERDIVPLMQEEKLGLMVWSPLAGGLLsgkygpg 232
Cdd:COG1453 136 GKIRHIGFSTHGSLEVIKEA-I---DTG-DFDFVQLQYNYLDQDNqaGEEALEAAAEKGIGVIIMKPLKGGRL------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 233 apgngegrranFDFPPVDKDRawacvaamrevgARHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAVKL--KL 310
Cdd:COG1453 204 -----------ANPPEKLVEL------------LCPPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENLKTADNlePL 260
|
330
....*....|.
gi 2229004110 311 DAEDVAKLDEV 321
Cdd:COG1453 261 TEEELAILERL 271
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
14-305 |
7.18e-52 |
|
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: 172.42 E-value: 7.18e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 14 SELCLGTMtfgenQTGAVWSAVaglDQGAADKIVERSLAAGVNFIDTANVYsqGRSEVILGQAIKnlGVPRKDVIIATKF 93
Cdd:cd19095 1 SVLGLGTS-----GIGRVWGVP---SEAEAARLLNTALDLGINLIDTAPAY--GRSEERLGRALA--GLRRDDLFIATKV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 94 HGQMGDKPNDRGASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVRYIGLSNWAAwRMAKA 173
Cdd:cd19095 69 GTHGEGGRDRKDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVSGDGE-ELEAA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 174 LGISerkgyaRFETVQAYYSIAGRDlERDIVPLMQEEKLGLMVWSPLAGGLLsgkygpgapgngegrranfdFPPVDKDR 253
Cdd:cd19095 148 IASG------VFDVVQLPYNVLDRE-EEELLPLAAEAGLGVIVNRPLANGRL--------------------RRRVRRRP 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2229004110 254 AWACVAAMREVGARHGA-SVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKA 305
Cdd:cd19095 201 LYADYARRPEFAAEIGGaTWAQAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
1-326 |
3.59e-51 |
|
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: 172.92 E-value: 3.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 1 MRYNQLGNTGLFVSELCLGT-MTFGENQTGAVwsavagldqgaADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAIKN 79
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTwVTFGGQISDEV-----------AERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 80 LGVPRKDVIIATKFHGQmGDKPNDRGASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVRY 159
Cdd:cd19159 70 KGWRRSSLVITTKLYWG-GKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 160 IGLSNWAAWRMAKALGISERKGYARFETVQAYYSIAGRD-LERDIVPLMQEEKLGLMVWSPLAGGLLSGKYGPGAPgngE 238
Cdd:cd19159 149 WGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVP---E 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 239 GRRANFDFPPVDKDR--------AWACVAAMREVGARHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAVKL-- 308
Cdd:cd19159 226 SSRASLKCYQWLKERivseegrkQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlp 305
|
330
....*....|....*...
gi 2229004110 309 KLDAEDVAKLDEVSALAP 326
Cdd:cd19159 306 KMTSHVVNEIDNILRNKP 323
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
10-319 |
7.67e-51 |
|
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: 171.93 E-value: 7.67e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 10 GLFVSELCLGTMTFGEnqtgaVWSAVAG-LDQGAADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAIKNLGVpRKDVI 88
Cdd:cd19147 7 GIRVSPLILGAMSIGD-----AWSGFMGsMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRKN-RDQIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 89 IATKF-------HGQMGDKPNDRGASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVRYIG 161
Cdd:cd19147 81 IATKFttdykayEVGKGKAVNYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 162 LSNWAAWRMAKALGISERKGYARFETVQAYYSIAGRDLERDIVPLMQEEKLGLMVWSPLAGG-LLSGKYGPGAPGNGEGR 240
Cdd:cd19147 161 VSDTPAWVVSAANYYATAHGKTPFSVYQGRWNVLNRDFERDIIPMARHFGMALAPWDVLGGGkFQSKKAVEERKKNGEGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 241 RaNFDFPPVDKDRAWACVAAMREVGARHG-ASVAEVALAYILAK-PFVTSvIIGAKRLEQLEENLKAVKLKLDAEDVAKL 318
Cdd:cd19147 241 R-SFVGGTEQTPEEVKISEALEKVAEEHGtESVTAIALAYVRSKaPNVFP-LVGGRKIEHLKDNIEALSIKLTPEEIEYL 318
|
.
gi 2229004110 319 D 319
Cdd:cd19147 319 E 319
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
1-313 |
1.04e-50 |
|
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: 170.42 E-value: 1.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 1 MRYNQLGNTGLFVSELCLGTMTFGEnqtgaVWSAVaglDQGAADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAIKnl 80
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGASPLGG-----VFGPV---DEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKALK-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 81 GVPRKDVIIATKFhGQMGDKPN---DRGASRghIMDSVEQSLERLQMNHIDLYQIH------GTDTVtpIDETLRALDDL 151
Cdd:cd19163 71 GIPRDSYYLATKV-GRYGLDPDkmfDFSAER--ITKSVEESLKRLGLDYIDIIQVHdiefapSLDQI--LNETLPALQKL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 152 VSRGLVRYIGLSNWAAWRMAKALgiseRKGYARFETVQAY--YSIAGRDLErDIVPLMQEEKLGLMVWSPLAGGLLSGKy 229
Cdd:cd19163 146 KEEGKVRFIGITGYPLDVLKEVL----ERSPVKIDTVLSYchYTLNDTSLL-ELLPFFKEKGVGVINASPLSMGLLTER- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 230 gpGAPGNGEGrranfdfPPVDKDRAWACVAAMREvgarHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAVKLK 309
Cdd:cd19163 220 --GPPDWHPA-------SPEIKEACAKAAAYCKS----RGVDISKLALQFALSNPDIATTLVGTASPENLRKNLEAAEEP 286
|
....
gi 2229004110 310 LDAE 313
Cdd:cd19163 287 LDAH 290
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
3-304 |
2.48e-48 |
|
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: 162.65 E-value: 2.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 3 YNQLGNTGLFVSELCLGTMTFGEnqtgavwsavagLDQGAADKIVERSLAAGVNFIDTANVYsqGRSEVILGQAIKNlgv 82
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPLGR------------LSQEEAAAIIRRALDLGINYFDTAPSY--GDSEEKIGKALKG--- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 83 PRKDVIIATKFHGQMGDKpndrgasrghIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDET------LRALDDLVSRGL 156
Cdd:cd19100 64 RRDKVFLATKTGARDYEG----------AKRDLERSLKRLGTDYIDLYQLHAVDTEEDLDQVfgpggaLEALLEAKEEGK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 157 VRYIGLS--NW-AAWRMAKAlgiserkgyARFETVQAYYSIAGR---DLERDIVPLMQEEKLGLMVWSPLAGGLLSGKyg 230
Cdd:cd19100 134 IRFIGISghSPeVLLRALET---------GEFDVVLFPINPAGDhidSFREELLPLAREKGVGVIAMKVLAGGRLLSG-- 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2229004110 231 pgapgngegrranfdfppvdkdrawacvaamrevgarhGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLK 304
Cdd:cd19100 203 --------------------------------------DPLDPEQALRYALSLPPVDVVIVGMDSPEELDENLA 238
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-323 |
8.29e-48 |
|
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: 163.27 E-value: 8.29e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 19 GTMTFGENqtgavwsavagLDQGAADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAIKNlgVPRKDVIIATKFHGQMg 98
Cdd:cd19103 21 GDQVFGNH-----------LDEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEFLKR--YPREDYIISTKFTPQI- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 99 dkpndRGASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTV---TPidetlrALDDLVSRGLVRYIGLSNWAAWRMAKALG 175
Cdd:cd19103 87 -----AGQSADPVADMLEGSLARLGTDYIDIYWIHNPADVerwTP------ELIPLLKSGKVKHVGVSNHNLAEIKRANE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 176 ISERKGYaRFETVQAYYSIAGRDLERD-IVPLMQEEKLGLMVWSPLAGGLLSGKYGPGAP-GNGEGRRANFDfpPVdKDR 253
Cdd:cd19103 156 ILAKAGV-SLSAVQNHYSLLYRSSEEAgILDYCKENGITFFAYMVLEQGALSGKYDTKHPlPEGSGRAETYN--PL-LPQ 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 254 AWACVAAMREVGARHGASVAEVALAYILAKPfvTSVIIGAKRLEQLEENLKAVKLKLDAEDVAKLDEVSA 323
Cdd:cd19103 232 LEELTAVMAEIGAKHGASIAQVAIAWAIAKG--TTPIIGVTKPHHVEDAARAASITLTDDEIKELEQLAD 299
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
1-321 |
1.02e-47 |
|
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: 163.79 E-value: 1.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 1 MRYNQLGNTGLFVSELCLGTmtfgenqtgavWSAV-AGLDQGAADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAIKN 79
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGT-----------WSTFsTAISEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILKK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 80 LGVPRKDVIIATKFHGQMGdkPNDRGASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVRY 159
Cdd:cd19142 70 KGWKRSSYIVSTKIYWSYG--SEERGLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 160 IGLSNWAawrmakALGISERKGYAR-FETV-----QAYYSIAGRD-LERDIVPLMQEEKLGLMVWSPLAGGLL------- 225
Cdd:cd19142 148 WGTSRWS------PVEIMEAFSIARqFNCPtpiceQSEYHMFCREkMELYMPELYNKVGVGLITWSPLSLGLDpgiseet 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 226 ----------SGKYGPGAPGNGEGRRANfdfppvdkdRAWACVAAMREVGARHGASVAEVALAYILAKPFVTSVIIGAKR 295
Cdd:cd19142 222 rrlvtklsfkSSKYKVGSDGNGIHEETR---------RASHKLRELSLIAERLGCDLTQLLIAWSLKNENVQCVLIGASS 292
|
330 340
....*....|....*....|....*...
gi 2229004110 296 LEQLEENLKAVKL--KLDAEDVAKLDEV 321
Cdd:cd19142 293 LEQLYSQLNSLQLlpKLNSAVMEELERI 320
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
3-307 |
1.21e-47 |
|
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: 163.34 E-value: 1.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 3 YNQLGNTGLFVSELCLGtmtfgenqtgaVWSAVAGLDQ-GAADKIVERSLAAGVNFIDTANVYS--QGRSEVILGQAIK- 78
Cdd:cd19151 2 YNRCGRSGLKLPAISLG-----------LWHNFGDVDRyENSRAMLRRAFDLGITHFDLANNYGppPGSAEENFGRILKe 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 79 NLGVPRKDVIIATKFHGQMGDKPNDRGASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVR 158
Cdd:cd19151 71 DLKPYRDELIISTKAGYTMWPGPYGDWGSKKYLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 159 YIGLSNWAAWRMAKALGISERKGYARFeTVQAYYSIAGRDLERDIVPLMQEEKLGLMVWSPLAGGLLSGKYGPGAPgngE 238
Cdd:cd19151 151 YVGISNYPPEEAREAAAILKDLGTPCL-IHQPKYSMFNRWVEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYLNGIP---E 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2229004110 239 GRRANFDFPPVDKDR----AWACVAAMREVGARHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAVK 307
Cdd:cd19151 227 DSRAAKGSSFLKPEQiteeKLAKVRRLNEIAQARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALD 299
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
1-321 |
1.69e-47 |
|
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: 163.23 E-value: 1.69e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 1 MRYNQLGNTGLFVSELCLGT-MTFGENqtgavwsavagLDQGAADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAIKN 79
Cdd:cd19160 3 MKYRNLGKSGLRVSCLGLGTwVTFGSQ-----------ISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 80 LGVPRKDVIIATK-FHGqmGDKPNDRGASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVR 158
Cdd:cd19160 72 KGWRRSSYVVTTKiYWG--GQAETERGLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 159 YIGLSNWAAWRMAKALGISERKGYARFETVQAYYSIAGRD-LERDIVPLMQEEKLGLMVWSPLAGGLLSGKYGPGAPGNG 237
Cdd:cd19160 150 YWGTSRWSAMEIMEAYSVARQFNLIPPVCEQAEYHLFQREkVEMQLPELYHKIGVGSVTWSPLACGLITGKYDGRVPDTC 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 238 EGRRANFDF-----PPVDKDRAWACVAAMREVGARHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAVKL--KL 310
Cdd:cd19160 230 RAAVKGYQWlkekvQSEEGKKQQAKVKELHPIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGSIQVlsQL 309
|
330
....*....|.
gi 2229004110 311 DAEDVAKLDEV 321
Cdd:cd19160 310 TPQTVMEIDAL 320
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
8-314 |
2.39e-47 |
|
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: 161.57 E-value: 2.39e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 8 NTGLFVSELCLGTMTFGENQTGAvwsavagldQGAADKIVErSLAAGVNFIDTANVYSQGRSEVILGQAIKNLGVPRKDV 87
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADWGESA---------EELLSLIEA-ALELGITTFDHADIYGGGKCEELFGEALALNPGLREKI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 88 IIATKFHGQMGDKPNDRGA-----SRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVRYIGL 162
Cdd:cd19092 71 EIQTKCGIRLGDDPRPGRIkhydtSKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 163 SNWAAWRMAkALgiserKGYARFETV--QAYYSIAGRDLERD-IVPLMQEEKLGLMVWSPLAGGLLSGKYGPGAPgngeg 239
Cdd:cd19092 151 SNFTPSQIE-LL-----QSYLDQPLVtnQIELSLLHTEAIDDgTLDYCQLLDITPMAWSPLGGGRLFGGFDERFQ----- 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2229004110 240 rRANfdfppvdkdrawacvAAMREVGARHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAVKLKLDAED 314
Cdd:cd19092 220 -RLR---------------AALEELAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALDIELTREE 278
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
1-326 |
3.07e-47 |
|
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: 162.56 E-value: 3.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 1 MRYNQLGNTGLFVSELCLGT-MTFGENQTGAVwsavagldqgaADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAIKN 79
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTwVTFGGQITDEM-----------AEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 80 LGVPRKDVIIATK-FHGqmGDKPNDRGASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVR 158
Cdd:cd19158 70 KGWRRSSLVITTKiFWG--GKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 159 YIGLSNWAAWRMAKALGISERKGYARFETVQAYYSIAGRD-LERDIVPLMQEEKLGLMVWSPLAGGLLSGKYGPGAPGNG 237
Cdd:cd19158 148 YWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 238 EGRRANFDFPPvDK------DRAWACVAAMREVGARHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAVKL--K 309
Cdd:cd19158 228 RASLKGYQWLK-DKilseegRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVlpK 306
|
330
....*....|....*..
gi 2229004110 310 LDAEDVAKLDEVSALAP 326
Cdd:cd19158 307 LSSSIVHEIDSILGNKP 323
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
13-311 |
5.72e-47 |
|
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: 159.69 E-value: 5.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 13 VSELCLGTMTFGEnqtGAVWSAVAglDQGAADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAiknLGVPRKDVIIATK 92
Cdd:cd19088 1 VSRLGYGAMRLTG---PGIWGPPA--DREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEA---LHPYPDDVVIATK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 93 F-HGQMGDKPNDRGASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVRYIGLSNwaawrmA 171
Cdd:cd19088 73 GgLVRTGPGWWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSN------V 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 172 KALGISERKGYARFETVQAYYSIAGRDLErDIVPLMQEEKLGLMVWSPLAGGLLSGKYGPGapgngegrranfdfppvdk 251
Cdd:cd19088 147 TVAQIEEARAIVRIVSVQNRYNLANRDDE-GVLDYCEAAGIAFIPWFPLGGGDLAQPGGLL------------------- 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 252 drawacvaamREVGARHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAVKLKLD 311
Cdd:cd19088 207 ----------AEVAARLGATPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
2-321 |
1.02e-46 |
|
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: 160.89 E-value: 1.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 2 RYNQLGNTGLFVSELclgtmTFGENQTGAVWSAVaglDQGAADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAIKNLg 81
Cdd:cd19104 1 KYRRFGRTGLKVSEL-----TFGGGGIGGLMGRT---TREEQIAAVRRALDLGINFFDTAPSYGDGKSEENLGRALKGL- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 82 vpRKDVIIATKfhgqMGDKPNDRGASRGHIMDSVEQSLERLQMNHIDLYQIH----------GTDTVTPID-----ETLR 146
Cdd:cd19104 72 --PAGPYITTK----VRLDPDDLGDIGGQIERSVEKSLKRLKRDSVDLLQLHnrigderdkpVGGTLSTTDvlglgGVAD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 147 ALDDLVSRGLVRYIGLSnwaAWRMAKAlgISERKGYARFETVQAYYS-----------IAGRDLE-RDIVPLMQEEKLGL 214
Cdd:cd19104 146 AFERLRSEGKIRFIGIT---GLGNPPA--IRELLDSGKFDAVQVYYNllnpsaaearpRGWSAQDyGGIIDAAAEHGVGV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 215 MVWSPLAGGLLSGK--YGPGAPGNGEGRRAnfdfppVDKDRAwacvAAMREVGARHGASVAEVALAYILAKPFVTSVIIG 292
Cdd:cd19104 221 MGIRVLAAGALTTSldRGREAPPTSDSDVA------IDFRRA----AAFRALAREWGETLAQLAHRFALSNPGVSTVLVG 290
|
330 340 350
....*....|....*....|....*....|
gi 2229004110 293 AKRLEQLEENLKAVKL-KLDAEDVAKLDEV 321
Cdd:cd19104 291 VKNREELEEAVAAEAAgPLPAENLARLEAL 320
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
47-319 |
5.38e-46 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 157.14 E-value: 5.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 47 VERSLAAGVNFIDTANVYsqgRSEVILGQAIKNLGVPRKDVIIATKFhgqmgdkPNDRgASRGHIMDSVEQSLERLQMNH 126
Cdd:COG0656 24 VRTALEAGYRHIDTAAMY---GNEEGVGEAIAASGVPREELFVTTKV-------WNDN-HGYDDTLAAFEESLERLGLDY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 127 IDLYQIH--GTDtvtPIDETLRALDDLVSRGLVRYIGLSNWAAWRMAKALGISErkgyARFETVQAYYSIAGRdlERDIV 204
Cdd:COG0656 93 LDLYLIHwpGPG---PYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETG----VKPAVNQVELHPYLQ--QRELL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 205 PLMQEEKLGLMVWSPLA-GGLLSGkygpgapgngegrranfdfpPVdkdrawacvaaMREVGARHGASVAEVALAYILAK 283
Cdd:COG0656 164 AFCREHGIVVEAYSPLGrGKLLDD--------------------PV-----------LAEIAEKHGKTPAQVVLRWHLQR 212
|
250 260 270
....*....|....*....|....*....|....*.
gi 2229004110 284 PFVtsVIIGAKRLEQLEENLKAVKLKLDAEDVAKLD 319
Cdd:COG0656 213 GVV--VIPKSVTPERIRENLDAFDFELSDEDMAAID 246
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
5-318 |
1.67e-45 |
|
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: 157.59 E-value: 1.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 5 QLGNTGLFVSELCLGTMTFgenqtgavwSAVAGLDQGAADKI--VERSLAAGVNFIDTANVYSQGRSEVILGQAIKnlGV 82
Cdd:cd19145 4 KLGSQGLEVSAQGLGCMGL---------SGDYGAPKPEEEGIalIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALK--DG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 83 PRKDVIIATKF--HGQMGDKPNDRGASrGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVRYI 160
Cdd:cd19145 73 PREKVQLATKFgiHEIGGSGVEVRGDP-AYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 161 GLSNwaawrmAKALGIseRKGYA--RFETVQAYYSIAGRDLERDIVPLMQEEKLGLMVWSPLAGGLLSGkyGPGA---PG 235
Cdd:cd19145 152 GLSE------ASADTI--RRAHAvhPITAVQLEWSLWTRDIEEEIIPTCRELGIGIVPYSPLGRGFFAG--KAKLeelLE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 236 NGEGRRA--NFDFPPVDKDRA-WACVAAMREvgaRHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAVKLKLDA 312
Cdd:cd19145 222 NSDVRKShpRFQGENLEKNKVlYERVEALAK---KKGCTPAQLALAWVLHQGEDVVPIPGTTKIKNLNQNIGALSVKLTK 298
|
....*.
gi 2229004110 313 EDVAKL 318
Cdd:cd19145 299 EDLKEI 304
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
5-326 |
1.31e-44 |
|
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: 155.68 E-value: 1.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 5 QLGNTGLFVSELCLGTMTFgenqtgavwSAVAG--LDQGAADKIVERSLAAGVNFIDTANVYsqGRSEVILGQAIKNLGV 82
Cdd:cd19144 5 TLGRNGPSVPALGFGAMGL---------SAFYGppKPDEERFAVLDAAFELGCTFWDTADIY--GDSEELIGRWFKQNPG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 83 PRKDVIIATKFHGQMgDKPNDRGASRG---HIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVRY 159
Cdd:cd19144 74 KREKIFLATKFGIEK-NVETGEYSVDGspeYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 160 IGLSNWAAWRMAKALGISErkgyarFETVQAYYSIAGRDLERDIVPLMQEEK-LGLMV--WSPLAGGLLSGKY-GPGAPG 235
Cdd:cd19144 153 IGLSECSAETLRRAHAVHP------IAAVQIEYSPFSLDIERPEIGVLDTCReLGVAIvaYSPLGRGFLTGAIrSPDDFE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 236 NGEGRRANFDFPPVDKDRAWACVAAMREVGARHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAVKLKLDAEDV 315
Cdd:cd19144 227 EGDFRRMAPRFQAENFPKNLELVDKIKAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLGALKVKLTEEEE 306
|
330
....*....|.
gi 2229004110 316 AKLDEVSALAP 326
Cdd:cd19144 307 KEIREIAEEAE 317
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
53-319 |
8.45e-42 |
|
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: 146.62 E-value: 8.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 53 AGVNFIDTANVYSQGRSEVILGQAIKNlgvPRKDVIIATKFHgqmgdkPndRGASRGHIMDSVEQSLERLQMNHIDLYQI 132
Cdd:cd19138 41 LGMTLIDTAEMYGDGGSEELVGEAIRG---RRDKVFLVSKVL------P--SNASRQGTVRACERSLRRLGTDYLDLYLL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 133 HGTDTVtPIDETLRALDDLVSRGLVRYIGLSNWAAWRMAKALGISERKGYArfeTVQAYYSIAGRDLERDIVPLMQEEKL 212
Cdd:cd19138 110 HWRGGV-PLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVPGGGNCA---ANQVLYNLGSRGIEYDLLPWCREHGV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 213 GLMVWSPLA-GGLLsgkygpgapgnGEGRRANfdfppvdkdrawacvAAMREVGARHGASVAEVALAYILAKPFVTSvII 291
Cdd:cd19138 186 PVMAYSPLAqGGLL-----------RRGLLEN---------------PTLKEIAARHGATPAQVALAWVLRDGNVIA-IP 238
|
250 260
....*....|....*....|....*...
gi 2229004110 292 GAKRLEQLEENLKAVKLKLDAEDVAKLD 319
Cdd:cd19138 239 KSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
3-316 |
8.20e-41 |
|
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: 145.29 E-value: 8.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 3 YNQLGNTGLFVSELCLGTM-TFGENQTGAVWSAvagldqgaadkIVERSLAAGVNFIDTANVYS--QGRSEVILGQAIKN 79
Cdd:cd19150 2 YRRCGKSGLKLPALSLGLWhNFGDDTPLETQRA-----------ILRTAFDLGITHFDLANNYGppPGSAEENFGRILRE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 80 LGVPRKD-VIIATKFHGQMGDKPNDRGASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVR 158
Cdd:cd19150 71 DFAGYRDeLIISTKAGYDMWPGPYGEWGSRKYLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 159 YIGLSNWAAWRMAKALGISERKGYARFeTVQAYYSIAGRDLERD-IVPLMQEEKLGLMVWSPLAGGLLSGKYGPGAPGNG 237
Cdd:cd19150 151 YVGISSYSPERTREAAAILRELGTPLL-IHQPSYNMLNRWVEESgLLDTLQELGVGCIAFTPLAQGLLTDKYLNGIPEGS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 238 EGRRANFDFPPVDKDRAWACVAAMREVGARHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAVK-LKLDAEDVA 316
Cdd:cd19150 230 RASKERSLSPKMLTEANLNSIRALNEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGALDnLTFSADELA 309
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
1-320 |
9.46e-41 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 146.29 E-value: 9.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 1 MRYNQLGNTGLFVSELCLGTM-TFGENQTgavwsavagLDQGAAdkIVERSLAAGVNFIDTANVYS--QGRSEVILGQAI 77
Cdd:PRK09912 13 MQYRYCGKSGLRLPALSLGLWhNFGHVNA---------LESQRA--ILRKAFDLGITHFDLANNYGppPGSAEENFGRLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 78 KNLGVP-RKDVIIATKFHGQMGDKPNDRGASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGL 156
Cdd:PRK09912 82 REDFAAyRDELIISTKAGYDMWPGPYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 157 VRYIGLSNWAAWRMAKALGISeRKGYARFETVQAYYSIAGRDLERD-IVPLMQEEKLGLMVWSPLAGGLLSGKYGPGAPG 235
Cdd:PRK09912 162 ALYVGISSYSPERTQKMVELL-REWKIPLLIHQPSYNLLNRWVDKSgLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 236 NG----EGRRANFDFPPVDKDRAWACVAAMREVGARHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAVK-LKL 310
Cdd:PRK09912 241 DSrmhrEGNKVRGLTPKMLTEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQALNnLTF 320
|
330
....*....|
gi 2229004110 311 DAEDVAKLDE 320
Cdd:PRK09912 321 STEELAQIDQ 330
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
45-319 |
6.15e-38 |
|
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381363 [Multi-domain] Cd Length: 260 Bit Score: 136.16 E-value: 6.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 45 KIVERSLAAGVNFIDTANVYSQGRSEVILGQAIKNLgvPRKDVIIATK-FHGQMgdkpndrgaSRGHIMDSVEQSLERLQ 123
Cdd:cd19137 30 ELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKDF--PREDLFIVTKvWPTNL---------RYDDLLRSLQNSLRRLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 124 MNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVRYIGLSNWAAWRMAKAlgiserKGYARFETV--QAYYSIAGRD-LE 200
Cdd:cd19137 99 TDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEA------ISKSQTPIVcnQVKYNLEDRDpER 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 201 RDIVPLMQEEKLGLMVWSPLAGGLLsgkygpgaPGNGEgrranfdfppvdkdrawacvaaMREVGARHGASVAEVALAYI 280
Cdd:cd19137 173 DGLLEYCQKNGITVVAYSPLRRGLE--------KTNRT----------------------LEEIAKNYGKTIAQIALAWL 222
|
250 260 270
....*....|....*....|....*....|....*....
gi 2229004110 281 LAKPFVTSvIIGAKRLEQLEENLKAVKLKLDAEDVAKLD 319
Cdd:cd19137 223 IQKPNVVA-IPKAGRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
14-307 |
6.40e-38 |
|
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: 136.15 E-value: 6.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 14 SELCLGTMTFGENQTGAVwsavaglDQGAADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAIKNLgvPRKDVIIATKF 93
Cdd:cd19096 1 SVLGFGTMRLPESDDDSI-------DEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKEG--PREKFYLATKL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 94 HGQMGDKPNDrgasrghIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDET-----LRALDDLVSRGLVRYIGLSNWAAW 168
Cdd:cd19096 72 PPWSVKSAED-------FRRILEESLKRLGVDYIDFYLLHGLNSPEWLEKArkgglLEFLEKAKKEGLIRHIGFSFHDSP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 169 RMAKALgISERkgyaRFETVQAYYSIAGRDLERDI--VPLMQEEKLGLMVWSPLAGGLLSgkygpgapgngegrranfDF 246
Cdd:cd19096 145 ELLKEI-LDSY----DFDFVQLQYNYLDQENQAGRpgIEYAAKKGMGVIIMEPLKGGGLA------------------NN 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2229004110 247 PPVDKDRAWacvaamrevgaRHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAVK 307
Cdd:cd19096 202 PPEALAILC-----------GAPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENIAAAD 251
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
48-321 |
8.81e-38 |
|
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: 136.96 E-value: 8.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 48 ERSLAAGVNFIDTANVYsqGRSEVILGQAIK---NLGVPRKDVIIATKFHGQmgdkPNDRGASRGHIMDSVEQSLERLQM 124
Cdd:cd19101 30 AAYVDAGLTTFDCADIY--GPAEELIGEFRKrlrRERDAADDVQIHTKWVPD----PGELTMTRAYVEAAIDRSLKRLGV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 125 NHIDLYQIHGTDT-VTPIDETLRALDDLVSRGLVRYIGLSNWAAWRMAKAL--GIserkgyaRFETVQAYYSIAGRDLER 201
Cdd:cd19101 104 DRLDLVQFHWWDYsDPGYLDAAKHLAELQEEGKIRHLGLTNFDTERLREILdaGV-------PIVSNQVQYSLLDRRPEN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 202 DIVPLMQEEKLGLMVWSPLAGGLLSGKYgPGAPgngEGRRANFDFPPVDKDR----AW-------ACVAAMREVGARHGA 270
Cdd:cd19101 177 GMAALCEDHGIKLLAYGTLAGGLLSEKY-LGVP---EPTGPALETRSLQKYKlmidEWggwdlfqELLRTLKAIADKHGV 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2229004110 271 SVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAVKLKLDAEDVAKLDEV 321
Cdd:cd19101 253 SIANVAVRWVLDQPGVAGVIVGARNSEHIDDNVRAFSFRLDDEDRAAIDAV 303
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
35-319 |
1.01e-37 |
|
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: 135.30 E-value: 1.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 35 VAGLDQGAADKIVERSLAAGVNFIDTANVYsqgRSEVILGQAIKNLGVPRKDVIIATKFHgqmgdkpnDRGASRGHIMDS 114
Cdd:cd19071 8 TYKLKPEETAEAVLAALEAGYRHIDTAAAY---GNEAEVGEAIRESGVPREELFITTKLW--------PTDHGYERVREA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 115 VEQSLERLQMNHIDLYQIH------GTDTVTPIDETLRALDDLVSRGLVRYIGLSNWAAWRMAKALGiserkgYARFE-- 186
Cdd:cd19071 77 LEESLKDLGLDYLDLYLIHwpvpgkEGGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLA------AARIKpa 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 187 TVQAYYSIAGRDleRDIVPLMQEEKLGLMVWSPLAGGllsgkygpgapgngegRRANFDFPpvdkdrawacvaAMREVGA 266
Cdd:cd19071 151 VNQIELHPYLQQ--KELVEFCKEHGIVVQAYSPLGRG----------------RRPLLDDP------------VLKEIAK 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2229004110 267 RHGASVAEVALAYILAKPFVtsVIIGAKRLEQLEENLKAVKLKLDAEDVAKLD 319
Cdd:cd19071 201 KYGKTPAQVLLRWALQRGVV--VIPKSSNPERIKENLDVFDFELSEEDMAAID 251
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-309 |
1.28e-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: 381323 [Multi-domain] Cd Length: 267 Bit Score: 135.73 E-value: 1.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 14 SELCLGTMTFG-----ENQTGAVwsavaglDQGAADKIVERSLAAGVNFIDTANVYsqGRSEVILGQAIKNLgvprKDVI 88
Cdd:cd19097 1 SKLALGTAQFGldygiANKSGKP-------SEKEAKKILEYALKAGINTLDTAPAY--GDSEKVLGKFLKRL----DKFK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 89 IATKFHGqmgdKPNDRGASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETLR-ALDDLVSRGLVRYIGLSNWAA 167
Cdd:cd19097 68 IITKLPP----LKEDKKEDEAAIEASVEASLKRLKVDSLDGLLLHNPDDLLKHGGKLVeALLELKKEGLIRKIGVSVYSP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 168 WRMAKALGISerkgyaRFETVQAYYSIA-GRDLERDIVPLMQEEKLGLMVWSPLAGGLLSGKygpgapgnGEGRRANFDF 246
Cdd:cd19097 144 EELEKALESF------KIDIIQLPFNILdQRFLKSGLLAKLKKKGIEIHARSVFLQGLLLME--------PDKLPAKFAP 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2229004110 247 --PPVDKDRAWAcvaamrevgARHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAVKLK 309
Cdd:cd19097 210 akPLLKKLHELA---------KKLGLSPLELALGFVLSLPEIDKIVVGVDSLEQLKEIIAAFKKP 265
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
9-319 |
6.55e-37 |
|
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: 134.67 E-value: 6.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 9 TGLFVSELCLGTMTFgenqtgaVWSAVAgLDQGAADKIVERSLAAGVNFIDTANVYSQGRSEV---ILGQAIKNLGVPRK 85
Cdd:cd19077 1 NGKLVGPIGLGLMGL-------TWRPNP-TPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHAnlkLLARFFRKYPEYAD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 86 DVIIATKFHGQMGDKPNDrgASRGHIMDSVEQSLERLQMN-HIDLYQIHGTDTVTPIDETLRALDDLVSRGLVRYIGLSN 164
Cdd:cd19077 73 KVVLSVKGGLDPDTLRPD--GSPEAVRKSIENILRALGGTkKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 165 WAAWRMAKALGIserkgyARFETVQAYYSIAGRD-LERDIVPLMQEEKLGLMVWSPLAGGLLSGKYGPGAPGNGEGRRAN 243
Cdd:cd19077 151 VSAETIRRAHAV------HPIAAVEVEYSLFSREiEENGVLETCAELGIPIIAYSPLGRGLLTGRIKSLADIPEGDFRRH 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2229004110 244 FD-FPPVDKDRAWACVAAMREVGARHGASVAEVALAYILAKPFVTSV-IIGAKRLEQLEENLKAVKLKLDAEDVAKLD 319
Cdd:cd19077 225 LDrFNGENFEKNLKLVDALQELAEKKGCTPAQLALAWILAQSGPKIIpIPGSTTLERVEENLKAANVELTDEELKEIN 302
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
3-326 |
1.13e-36 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 134.52 E-value: 1.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 3 YNQLGNTGLFVSelCLGtmtFGENQTGAVWSAVAGLDQGAAdkiVERSLAAGVNFIDTANVYSQGRSEVILGQAIKNLGV 82
Cdd:PLN02587 1 LRELGSTGLKVS--SVG---FGASPLGSVFGPVSEEDAIAS---VREAFRLGINFFDTSPYYGGTLSEKVLGKALKALGI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 83 PRKDVIIATKFhGQMGDKpNDRGASRghIMDSVEQSLERLQMNHIDLYQIH-----GTDTVtpIDETLRALDDLVSRGLV 157
Cdd:PLN02587 73 PREKYVVSTKC-GRYGEG-FDFSAER--VTKSVDESLARLQLDYVDILHCHdiefgSLDQI--VNETIPALQKLKESGKV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 158 RYIGLSNWAAWRMAKALgisERKGYARFETVQAY--YSIAGRDLErDIVPLMQEEKLGLMVWSPLAGGLLSGKygpGAPg 235
Cdd:PLN02587 147 RFIGITGLPLAIFTYVL---DRVPPGTVDVILSYchYSLNDSSLE-DLLPYLKSKGVGVISASPLAMGLLTEN---GPP- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 236 ngegrranfDFPPVDKDRAWACVAAMREVGARhGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAV-KLKLDAED 314
Cdd:PLN02587 219 ---------EWHPAPPELKSACAAAATHCKEK-GKNISKLALQYSLSNKDISTTLVGMNSVQQVEENVAAAtELETSGID 288
|
330
....*....|...
gi 2229004110 315 VAKLDEVSA-LAP 326
Cdd:PLN02587 289 EELLSEVEAiLAP 301
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
6-306 |
9.68e-36 |
|
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: 131.50 E-value: 9.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 6 LGNTGLFVSELCLGTMTFGENQTGavwsavaGLDQGAADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAIKNLGVPRK 85
Cdd:cd19153 5 LEIALGNVSPVGLGTAALGGVYGD-------GLEQDEAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAALQVPRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 86 DVIIATKFhGQMGDKPNDRGASRghIMDSVEQSLERLQMNHIDLYQIHGTDTV---TPIDETLRALDDLVSRGLVRYIGL 162
Cdd:cd19153 78 SYTVATKV-GRYRDSEFDYSAER--VRASVATSLERLHTTYLDVVYLHDIEFVdydTLVDEALPALRTLKDEGVIKRIGI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 163 SNWAAWRMAKALgisERKGYARFETVQAY--YSIAGRDLERDIVPLMQEEKLGLMVWSPLAGGLLSGKyGPGA--PGNGE 238
Cdd:cd19153 155 AGYPLDTLTRAT---RRCSPGSLDAVLSYchLTLQDARLESDAPGLVRGAGPHVINASPLSMGLLTSQ-GPPPwhPASGE 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2229004110 239 GRranfdfppvdkdrawACVAAMREVGARHGASVAEVALAYILA-KPFVTSVIIGAKRLEQLEENLKAV 306
Cdd:cd19153 231 LR---------------HYAAAADAVCASVEASLPDLALQYSLAaHAGVGTVLLGPSSLAQLRSMLAAV 284
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
45-319 |
2.03e-34 |
|
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: 126.62 E-value: 2.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 45 KIVERSLAAGVNFIDTANVYSqgrSEVILGQAIKNLGVPRKDVIIATK-FHGQMgdKPNDrgasrghIMDSVEQSLERLQ 123
Cdd:cd19073 18 NAVKEALELGYRHIDTAEIYN---NEAEVGEAIAESGVPREDLFITTKvWRDHL--RPED-------LKKSVDRSLEKLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 124 MNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVRYIGLSNWAAWRMAKALGISErkgyARFETVQAYYSIAGRdlERDI 203
Cdd:cd19073 86 TDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISP----LPIAVNQVEFHPFLY--QAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 204 VPLMQEEKLGLMVWSPLAGGLLsgkygpgapgngegrranFDFPPVdkdrawacvaamREVGARHGASVAEVALAYILAK 283
Cdd:cd19073 160 LEYCRENDIVITAYSPLARGEV------------------LRDPVI------------QEIAEKYDKTPAQVALRWLVQK 209
|
250 260 270
....*....|....*....|....*....|....*.
gi 2229004110 284 PFVtsVIIGAKRLEQLEENLKAVKLKLDAEDVAKLD 319
Cdd:cd19073 210 GIV--VIPKASSEDHLKENLAIFDWELTSEDVAKID 243
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
37-320 |
2.59e-34 |
|
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: 126.60 E-value: 2.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 37 GLDQGAADKIVERSLAAGVNFIDTANVYSqgrSEVILGQAIKNLGVPRKDVIIATKFHgqmgdkPNDrgASRGHIMDSVE 116
Cdd:cd19140 17 PLTGEECTRAVEHALELGYRHIDTAQMYG---NEAQVGEAIAASGVPRDELFLTTKVW------PDN--YSPDDFLASVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 117 QSLERLQMNHIDLYQIHGTDTVTPIDETLRALDDLVSRGLVRYIGLSNWAAWRMAKALGISErkgyARFETVQAYYSIAg 196
Cdd:cd19140 86 ESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSE----APLFTNQVEYHPY- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 197 rdLERDIVpLMQEEKLGLMV--WSPLAggllsgkygpgapgNGEgrranfdfppVDKDrawacvAAMREVGARHGASVAE 274
Cdd:cd19140 161 --LDQRKL-LDAAREHGIALtaYSPLA--------------RGE----------VLKD------PVLQEIGRKHGKTPAQ 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2229004110 275 VALAYILAKPFVtSVIIGAKRLEQLEENLKAVKLKLDAEDVAKLDE 320
Cdd:cd19140 208 VALRWLLQQEGV-AAIPKATNPERLEENLDIFDFTLSDEEMARIAA 252
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-304 |
1.29e-30 |
|
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: 1.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 11 LFVSELCLGTMTFGENQTGavwsavaglDQGAADkIVERSLAAGVNFIDTANVYSQGRSEVILGQAIKNL----GVPRKD 86
Cdd:cd19099 1 LTLSSLGLGTYRGDSDDET---------DEEYRE-ALKAALDSGINVIDTAINYRGGRSERLIGKALRELiekgGIKRDE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 87 VIIATK-----------------FHGQMGDKPNDRGASRGH--------IMDSVEQSLERLQMNHIDLYQIH-------- 133
Cdd:cd19099 71 VVIVTKagyipgdgdeplrplkyLEEKLGRGLIDVADSAGLrhcispayLEDQIERSLKRLGLDTIDLYLLHnpeeqlle 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 134 --GTDTVTPIDETLRALDDLVSRGLVRYIGLSNWAAWRMAKALG--ISERKGYA----------RFETVQAYYSIA---- 195
Cdd:cd19099 151 lgEEEFYDRLEEAFEALEEAVAEGKIRYYGISTWDGFRAPPALPghLSLEKLVAaaeevggdnhHFKVIQLPLNLLepea 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 196 ---GRDLERDIVPLMQ---EEKLGLMVWSPLAGGLLsgkygpgapgNGEGRRANFDFPPvdkdrawacvaamrevgarHG 269
Cdd:cd19099 231 lteKNTVKGEALSLLEaakELGLGVIASRPLNQGQL----------LGELRLADLLALP-------------------GG 281
|
330 340 350
....*....|....*....|....*....|....*
gi 2229004110 270 ASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLK 304
Cdd:cd19099 282 ATLAQRALQFARSTPGVDSALVGMRRPEHVDENLA 316
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
47-320 |
2.40e-30 |
|
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: 115.91 E-value: 2.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 47 VERSLAAGVNFIDTANVYSqgrSEVILGQAIKNLGVPRKDVIIATKFHGQmgdkpndrGASRGHIMDSVEQSLERLQMNH 126
Cdd:cd19139 20 VRTALELGYRHIDTAQIYD---NEAAVGQAIAESGVPRDELFITTKIWID--------NLSKDKLLPSLEESLEKLRTDY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 127 IDLYQIH--GTDTVTPIDETLRALDDLVSRGLVRYIGLSNWAAWRMAKALGISerkGYARFETVQAyysiagrdlerDIV 204
Cdd:cd19139 89 VDLTLIHwpSPNDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVV---GAGAIATNQI-----------ELS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 205 PLMQEEKlgLMVWSPLAGGLLSGkYGPGAPGNgegrranfdfppVDKDrawacvAAMREVGARHGASVAEVALAYILAKP 284
Cdd:cd19139 155 PYLQNRK--LVAHCKQHGIHVTS-YMTLAYGK------------VLDD------PVLAAIAERHGATPAQIALAWAMARG 213
|
250 260 270
....*....|....*....|....*....|....*.
gi 2229004110 285 FvtSVIIGAKRLEQLEENLKAVKLKLDAEDVAKLDE 320
Cdd:cd19139 214 Y--AVIPSSTKREHLRSNLLALDLTLDADDMAAIAA 247
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
35-313 |
2.97e-30 |
|
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: 116.69 E-value: 2.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 35 VAGLDQGAADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAIKnlGVPRKDVIIATKF--------HGQMGDKPNDRGA 106
Cdd:cd19162 13 LARAGEDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALA--RHPRAEYVVSTKVgrllepgaAGRPAGADRRFDF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 107 SRGHIMDSVEQSLERLQMNHIDLYQIH--GTDTVTPIDETLRALDDLVSRGLVRYIGLsnwAAWRMAKALGISERkgyAR 184
Cdd:cd19162 91 SADGIRRSIEASLERLGLDRLDLVFLHdpDRHLLQALTDAFPALEELRAEGVVGAIGV---GVTDWAALLRAARR---AD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 185 FETV--QAYYSIAGRDLERDIVPLMQEEKLGLMVWSPLAGGLLSGkygpgapgnGEGRRANFDFPPVDKDRaWACVAAMR 262
Cdd:cd19162 165 VDVVmvAGRYTLLDRRAATELLPLCAAKGVAVVAAGVFNSGILAT---------DDPAGDRYDYRPATPEV-LARARRLA 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2229004110 263 EVGARHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAVKLKLDAE 313
Cdd:cd19162 235 AVCRRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLALLRTPIPAE 285
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
23-321 |
6.43e-30 |
|
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: 115.41 E-value: 6.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 23 FGenqTGAVW--SAVAGLDQGAADKIVErSLAAGVNFIDTANVYSqgrSEVILGQAIKNLGVPRKDVIIATKFHGQMGDk 100
Cdd:cd19120 9 FG---TGTAWykSGDDDIQRDLVDSVKL-ALKAGFRHIDTAEMYG---NEKEVGEALKESGVPREDLFITTKVSPGIKD- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 101 pndrgasrghIMDSVEQSLERLQMNHIDLYQIH----GTDTVTPIDETLRALDDLVSRGLVRYIGLSNWAAWRMAKALGI 176
Cdd:cd19120 81 ----------PREALRKSLAKLGVDYVDLYLIHspffAKEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 177 SerKGYARFETVQAYYSIAGRDLerDIVPLMQEEKLGLMVWSPLAggllsgkygpgapgngegrranfdfpPVDKDRAWA 256
Cdd:cd19120 151 A--KIKPAVNQIEFHPYLYPQQP--ALLEYCREHGIVVSAYSPLS--------------------------PLTRDAGGP 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2229004110 257 CVAAMREVGARHGASVAEVALAYILAKPFVtsVIIGAKRLEQLEENLKAVKLKLDAEDVAKLDEV 321
Cdd:cd19120 201 LDPVLEKIAEKYGVTPAQVLLRWALQKGIV--VVTTSSKEERMKEYLEAFDFELTEEEVEEIDKA 263
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
43-313 |
1.08e-28 |
|
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: 112.70 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 43 ADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAIKNLgvPRKDVIIATK----FHGQMGDKPNDRG------------- 105
Cdd:cd19152 22 AKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALREL--GREDYVISTKvgrlLVPLQEVEPTFEPgfwnplpfdavfd 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 106 ASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDETL-----------RALDDLVSRGLVRYIGL-SNwaAWRMAKA 173
Cdd:cd19152 100 YSYDGILRSIEDSLQRLGLSRIDLLSIHDPDEDLAGAESDehfaqaikgafRALEELREEGVIKAIGLgVN--DWEVILR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 174 LgISErkgyARFETVQayysIAGR------DLERDIVPLMQEEKLGLMVWSPLAGGLLSGKYGPGAPGNGEGrranfdfP 247
Cdd:cd19152 178 I-LEE----ADLDWVM----LAGRytlldhSAARELLPECEKRGVKVVNAGPFNSGFLAGGDNFDYYEYGPA-------P 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2229004110 248 P--VDKDRAWACVAAmrevgaRHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAVKLKLDAE 313
Cdd:cd19152 242 PelIARRDRIEALCE------QHGVSLAAAALQFALAPPAVASVAPGASSPERVEENVALLATEIPAA 303
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
47-328 |
8.98e-26 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 103.95 E-value: 8.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 47 VERSLAAGVNFIDTANVYsqgRSEVILGQAIKNLGVPRKDVIIATK-----FhgqmgdkpndrgaSRGHIMDSVEQSLER 121
Cdd:PRK11172 22 VKTALELGYRAIDTAQIY---DNEAAVGQAIAESGVPRDELFITTKiwidnL-------------AKDKLIPSLKESLQK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 122 LQMNHIDLYQIH--GTDTVTPIDETLRALDDLVSRGLVRYIGLSNWAAWRMAKALgiserkgyarfETVQAyYSIAGRDL 199
Cdd:PRK11172 86 LRTDYVDLTLIHwpSPNDEVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQAI-----------AAVGA-ENIATNQI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 200 ErdIVPLMQEEKL-------GLMVWS--PLAggllsgkYGpgapgngegrranfdfpPVDKDrawacvAAMREVGARHGA 270
Cdd:PRK11172 154 E--LSPYLQNRKVvafakehGIHVTSymTLA-------YG-----------------KVLKD------PVIARIAAKHNA 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2229004110 271 SVAEVALAYILAKPFvtSVIIGAKRLEQLEENLKAVKLKLDAED---VAKLD----EVS--ALAPEY 328
Cdd:PRK11172 202 TPAQVILAWAMQLGY--SVIPSSTKRENLASNLLAQDLQLDAEDmaaIAALDrngrLVSpeGLAPEW 266
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
43-305 |
3.16e-25 |
|
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: 103.56 E-value: 3.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 43 ADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAIKNLgvPRKDVIIATKFHGQMgdKPNDRGASRGH------------ 110
Cdd:cd19161 22 ADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREK--PRDEFVLSTKVGRLL--KPAREGSVPDPngfvdplpfeiv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 111 -------IMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDET------------LRALDDLVSRGLVRYIGLSNWAAWRMA 171
Cdd:cd19161 98 ydysydgIMRSFEDSLQRLGLNRIDILYVHDIGVYTHGDRKerhhfaqlmsggFKALEELKKAGVIKAFGLGVNEVQICL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 172 KALGiserkgYARFET--VQAYYSIAGRDLERDIVPLMQEEKLGLMVWSPLAGGLLSgkygpgapgNGEGRRANFDFPPV 249
Cdd:cd19161 178 EALD------EADLDCflLAGRYSLLDQSAEEEFLPRCEQRGTSLVIGGVFNSGILA---------TGTKSGAKFNYGDA 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2229004110 250 DK---DRawacVAAMREVGARHGASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKA 305
Cdd:cd19161 243 PAeiiSR----VMEIEKICDAYNVPLAAAALQFPLRHPAVASVLTGARNPAQLRQNVEA 297
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
39-319 |
1.36e-24 |
|
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: 100.34 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 39 DQGAADKIVERSLAAGVNFIDTANVYsqgRSEVILGQAIKNLGVPRKDVIIATKFHGQ-MGDKPndrgasrghIMDSVEQ 117
Cdd:cd19133 21 DPEECERAVLEAIKAGYRLIDTAAAY---GNEEAVGRAIKKSGIPREELFITTKLWIQdAGYEK---------AKKAFER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 118 SLERLQMNHIDLYQIHgtdtvTP---IDETLRALDDLVSRGLVRYIGLSNWAAWRMAKALgiserkgyARFETVQA---- 190
Cdd:cd19133 89 SLKRLGLDYLDLYLIH-----QPfgdVYGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLI--------LHNEVKPAvnqi 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 191 ----YYSiagrdlERDIVPLMQEEKLGLMVWSPLaggllsgkygpgapgnGEGRRANFDFPpvdkdrawacvaAMREVGA 266
Cdd:cd19133 156 ethpFNQ------QIEAVEFLKKYGVQIEAWGPF----------------AEGRNNLFENP------------VLTEIAE 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2229004110 267 RHGASVAEVALAYILAKPFVtsVIIGAKRLEQLEENLKAVKLKLDAEDVAKLD 319
Cdd:cd19133 202 KYGKSVAQVILRWLIQRGIV--VIPKSVRPERIAENFDIFDFELSDEDMEAIA 252
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
39-319 |
3.75e-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: 99.63 E-value: 3.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 39 DQGAADKIVERSLAAGVNFIDTANVYsqgRSEVILGQAIKNL----GVPRKDVIIATKFhgqmgdKPNDRGASRGhiMDS 114
Cdd:cd19136 13 GEEEVRQAVDAALKAGYRLIDTASVY---RNEADIGKALRDLlpkyGLSREDIFITSKL------APKDQGYEKA--RAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 115 VEQSLERLQMNHIDLYQIH--GTDTVTPID--------ETLRALDDLVSRGLVRYIGLSNWAAWRMAkalgisERKGYAR 184
Cdd:cd19136 82 CLGSLERLGTDYLDLYLIHwpGVQGLKPSDprnaelrrESWRALEDLYKEGKLRAIGVSNYTVRHLE------ELLKYCE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 185 -------FEtVQAYYsiagrdLERDIVPLMQEEKLGLMVWSPLaggllsgkygpgapgnGEGRRANFDFPPVdkdrawac 257
Cdd:cd19136 156 vppavnqVE-FHPHL------VQKELLKFCKDHGIHLQAYSSL----------------GSGDLRLLEDPTV-------- 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2229004110 258 vaamREVGARHGASVAEVALAYILAKPfvTSVIIGAKRLEQLEENLKAVKLKLDAEDVAKLD 319
Cdd:cd19136 205 ----LAIAKKYGRTPAQVLLRWALQQG--IGVIPKSTNPERIAENIKVFDFELSEEDMAELN 260
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
13-305 |
4.55e-23 |
|
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: 97.35 E-value: 4.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 13 VSELCLGTMTFGENQTGAVWSAvagldqgAADKIVERSLAAGVNFIDTANVYsqGRSEVILGQAIKNL--GVPRKDVIIA 90
Cdd:cd19164 13 LPPLIFGAATFSYQYTTDPESI-------PPVDIVRRALELGIRAFDTSPYY--GPSEIILGRALKALrdEFPRDTYFII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 91 TKFhGQMGdkPNDRGASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTVTP--IDETLRALDDLVSRGLVRYIGLSnwaAW 168
Cdd:cd19164 84 TKV-GRYG--PDDFDYSPEWIRASVERSLRRLHTDYLDLVYLHDVEFVADeeVLEALKELFKLKDEGKIRNVGIS---GY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 169 RMAKALGISERKGYARFETVQAYYSIAGRDLERDiVPLMQEEKL-------GLMVWSPLAGGLLSGKygpGAPgngegrr 241
Cdd:cd19164 158 PLPVLLRLAELARTTAGRPLDAVLSYCHYTLQNT-TLLAYIPKFlaaagvkVVLNASPLSMGLLRSQ---GPP------- 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2229004110 242 anfDFPPVDKDRAWACVAAMREVGArHGASVAEVALAYILAKPF-VTSVIIGAKRLEQLEENLKA 305
Cdd:cd19164 227 ---EWHPASPELRAAAAKAAEYCQA-KGTDLADVALRYALREWGgEGPTVVGCSNVDELEEAVEA 287
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
47-322 |
6.84e-23 |
|
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: 96.71 E-value: 6.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 47 VERSLAAGVNFIDTANVYsqgRSEVILGQAIKNL----GVPRKDVIIATKFHGQMgDKPNDrgasrghIMDSVEQSLERL 122
Cdd:cd19154 31 VRTALKAGYRLIDTAFLY---QNEEAIGEALAELleegVVKREDLFITTKLWTHE-HAPED-------VEEALRESLKKL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 123 QMNHIDLYQIH-----------------GTDTVTPID--ETLRALDDLVSRGLVRYIGLSNWAAWRMAKALGISERKGYA 183
Cdd:cd19154 100 QLEYVDLYLIHapaafkddegesgtmenGMSIHDAVDveDVWRGMEKVYDEGLTKAIGVSNFNNDQIQRILDNARVKPHN 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 184 RFETVQAYYSiagrdlERDIVPLMQEEKLGLMVWSPLaggllsgkygpGAPGngegrRANFDFPP-VDKDRAWACVAAMR 262
Cdd:cd19154 180 NQVECHLYFP------QKELVEFCKKHNISVTSYATL-----------GSPG-----RANFTKSTgVSPAPNLLQDPIVK 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 263 EVGARHGASVAEVALAYILAKPFVtsVIIGAKRLEQLEENLKAVKLKLDAEDVAKLDEVS 322
Cdd:cd19154 238 AIAEKHGKTPAQVLLRYLLQRGIA--VIPKSATPSRIKENFNIFDFSLSEEDMATLEEIE 295
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
47-320 |
1.22e-21 |
|
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: 92.95 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 47 VERSLAAGVNFIDTANVYsqgRSEVILGQAIKNL----GVPRKDVIIATK----FHGQmgdkpndrgasrGHIMDSVEQS 118
Cdd:cd19111 23 VDYALFVGYRHIDTALSY---QNEKAIGEALKWWlkngKLKREEVFITTKlppvYLEF------------KDTEKSLEKS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 119 LERLQMNHIDLYQIHG-------------TDTVTPIDETLRALDDLVSRGLVRYIGLSNWAAWRMAKALGISERKGYARF 185
Cdd:cd19111 88 LENLKLPYVDLYLIHHpcgfvnkkdkgerELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINKILAYAKVKPSNLQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 186 ETVQAYYSiagrdlERDIVPLMQEEKLGLMVWSPLaggllsgkygpGAPGngegrRANFDFP---PVD-KDRAwacVAAM 261
Cdd:cd19111 168 LECHAYLQ------QRELRKFCNKKNIVVTAYAPL-----------GSPG-----RANQSLWpdqPDLlEDPT---VLAI 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2229004110 262 REvgaRHGASVAEVALAYILAKPfvTSVIIGAKRLEQLEENLKAVKLKLDAEDVAKLDE 320
Cdd:cd19111 223 AK---ELDKTPAQVLLRFVLQRG--TGVLPKSTNKERIEENFEVFDFELTEEHFKKLKT 276
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
1-318 |
5.89e-21 |
|
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a founding member of aldo-keto reductase family 3 member G1 (AKR3G1). It is an aldo/keto reductase that catalyzes the NADPH-dependent reduction of aldehyde- and ketone-groups of different classes of carbonyl compounds to the corresponding alcohols.
Pssm-ID: 381349 [Multi-domain] Cd Length: 297 Bit Score: 91.32 E-value: 5.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 1 MRYNQLgNTGLFVSELCLGTMTFGENQTGAVwsavagldqgaadkiVERSLAAGVNFIDTANVYsQGRSEV--ILGQAIK 78
Cdd:cd19123 1 MKTLPL-SNGDLIPALGLGTWKSKPGEVGQA---------------VKQALEAGYRHIDCAAIY-GNEAEIgaALAEVFK 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 79 NLGVPRKDVIIATK----FHgqmgdKPND-RGAsrghimdsVEQSLERLQMNHIDLYQIH--------------GTDTVT 139
Cdd:cd19123 64 EGKVKREDLWITSKlwnnSH-----APEDvLPA--------LEKTLADLQLDYLDLYLMHwpvalkkgvgfpesGEDLLS 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 140 ----PIDETLRALDDLVSRGLVRYIGLSNWAAWRMAKALGiserkgyarfetvQAYYSIAGRDLErdIVPLMQEEKL--- 212
Cdd:cd19123 131 lspiPLEDTWRAMEELVDKGLCRHIGVSNFSVKKLEDLLA-------------TARIKPAVNQVE--LHPYLQQPELlaf 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 213 ----GLMV--WSPLaggllsGKYGPGAPGNGEGRRANFDFPpvdkdrawacvaAMREVGARHGASVAEVALAYILAKPfv 286
Cdd:cd19123 196 crdnGIHLtaYSPL------GSGDRPAAMKAEGEPVLLEDP------------VINKIAEKHGASPAQVLIAWAIQRG-- 255
|
330 340 350
....*....|....*....|....*....|..
gi 2229004110 287 TSVIIGAKRLEQLEENLKAVKLKLDAEDVAKL 318
Cdd:cd19123 256 TVVIPKSVNPERIQQNLEAAEVELDASDMATI 287
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
38-318 |
1.02e-20 |
|
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: 91.01 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 38 LDQGAADKIVERSLAAGVNFIDTANVYsqgRSEVILGQAIKNLG----VPRKDVIIATKFHGqmgdkpndrgASRGHIMD 113
Cdd:cd19112 21 MEPGEIKELILNAIKIGYRHFDCAADY---KNEKEVGEALAEAFktglVKREDLFITTKLWN----------SDHGHVIE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 114 SVEQSLERLQMNHIDLYQIH----------GT-------------DTVTPIDETLRALDDLVSRGLVRYIGLSNWAAWRM 170
Cdd:cd19112 88 ACKDSLKKLQLDYLDLYLVHfpvatkhtgvGTtgsalgedgvldiDVTISLETTWHAMEKLVSAGLVRSIGISNYDIFLT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 171 AKALGISERK-GYARFETvQAYYSiagRDlerDIVPLMQEEKLGLMVWSPLAGGLlsgkygpgapGNGE--GRRANFDFP 247
Cdd:cd19112 168 RDCLAYSKIKpAVNQIET-HPYFQ---RD---SLVKFCQKHGISVTAHTPLGGAA----------ANAEwfGSVSPLDDP 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2229004110 248 pvdkdrawacvaAMREVGARHGASVAEVALAYILAKPfvTSVIIGAKRLEQLEENLKAVKLKLDAEDVAKL 318
Cdd:cd19112 231 ------------VLKDLAKKYGKSAAQIVLRWGIQRN--TAVIPKSSKPERLKENIDVFDFQLSKEDMKLI 287
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
38-319 |
3.10e-19 |
|
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: 85.78 E-value: 3.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 38 LDQGAADKIVERSLAAGVNFIDTANVYsqgRSEVILGQAIKNLGVPRKDVIIATKFHGqmgdkpndRGASRGHIMDSVEQ 117
Cdd:cd19132 17 LKGDEGVEAVVAALQAGYRLLDTAFNY---ENEGAVGEAVRRSGVPREELFVTTKLPG--------RHHGYEEALRTIEE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 118 SLERLQMNHIDLYQIH----GTDTVTpidETLRALDDLVSRGLVRYIGLSNWAAW---RMAKALG-------ISERKGYA 183
Cdd:cd19132 86 SLYRLGLDYVDLYLIHwpnpSRDLYV---EAWQALIEAREEGLVRSIGVSNFLPEhldRLIDETGvtpavnqIELHPYFP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 184 RFETVQAyysiagrDLERDIVPlmqeeklglMVWSPLaggllsgkygpgapgngeGRRAN-FDFPPVdkdrawacvaamR 262
Cdd:cd19132 163 QAEQRAY-------HREHGIVT---------QSWSPL------------------GRGSGlLDEPVI------------K 196
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2229004110 263 EVGARHGASVAEVALAYILAKPfvTSVIIGAKRLEQLEENLKAVKLKLDAEDVAKLD 319
Cdd:cd19132 197 AIAEKHGKTPAQVVLRWHVQLG--VVPIPKSANPERQRENLAIFDFELSDEDMAAIA 251
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
31-319 |
3.15e-19 |
|
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: 85.89 E-value: 3.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 31 VWSAvaglDQGAADKIVERSLAAGVNFIDTANVYsqgRSEVILGQAIKNLGVPRKDVIIATKF--HGQMGDKPndrgasr 108
Cdd:cd19131 17 VWQV----SNDEAASAVREALEVGYRSIDTAAIY---GNEEGVGKAIRASGVPREELFITTKLwnSDQGYDST------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 109 ghiMDSVEQSLERLQMNHIDLYQIH----GTDTVTpidETLRALDDLVSRGLVRYIGLSNWAAWRMAKALGiserkgyaR 184
Cdd:cd19131 83 ---LRAFDESLRKLGLDYVDLYLIHwpvpAQDKYV---ETWKALIELKKEGRVKSIGVSNFTIEHLQRLID--------E 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 185 FETVQAYYSIagrdlerDIVPLMQE-------EKLGLMV--WSPLA-GGLLSGkygpgapgngegrranfdfpPVdkdra 254
Cdd:cd19131 149 TGVVPVVNQI-------ELHPRFQQrelrafhAKHGIQTesWSPLGqGGLLSD--------------------PV----- 196
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2229004110 255 wacvaaMREVGARHGASVAEVALAYILAKPFVtsVIIGAKRLEQLEENLKAVKLKLDAED---VAKLD 319
Cdd:cd19131 197 ------IGEIAEKHGKTPAQVVIRWHLQNGLV--VIPKSVTPSRIAENFDVFDFELDADDmqaIAGLD 256
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
47-320 |
3.32e-19 |
|
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a founding member of aldo-keto reductase family 2 member E4 (AKR2E4). It is a NADP-dependent oxidoreductase with high 3-dehydroecdysone reductase activity. It may play a role in the regulation of molting and has lower activity with phenylglyoxal and isatin (in vitro). This family also includes 3-dehydroecdysone 3b-reductase from Spodoptera littoralis and Trichoplusia ni, DL-glyceraldehyde reductase from Drosophila melanogaster, aldo-keto reductase from Bombyx mori, which correspond to aldo-keto reductase family 2 member E1, E2, E3 and E5 (AKR2E1/2/3/5), respectively.
Pssm-ID: 381342 [Multi-domain] Cd Length: 292 Bit Score: 86.18 E-value: 3.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 47 VERSLAAGVNFIDTANVYsqgRSEVILGQAIKNL----GVPRKDVIIATK----FHgqmgdkpndrgaSRGHIMDSVEQS 118
Cdd:cd19116 31 VKHAIEAGYRHIDTAYLY---GNEAEVGEAIREKiaegVVKREDLFITTKlwnsYH------------EREQVEPALRES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 119 LERLQMNHIDLYQIH--------------GTDTVTPID--ETLRALDDLVSRGLVRYIGLSNWAAWRMAKALGISERKGY 182
Cdd:cd19116 96 LKRLGLDYVDLYLIHwpvafkenndsesnGDGSLSDIDylETWRGMEDLVKLGLTRSIGVSNFNSEQINRLLSNCNIKPA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 183 ARFETVQAYYSiagrdlERDIVPLMQEEKLGLMVWSPLaggllsGKYGPgapgngegrrANFDFPPVDKDRawacvAAMR 262
Cdd:cd19116 176 VNQIEVHPTLT------QEKLVAYCQSNGIVVMAYSPF------GRLVP----------RGQTNPPPRLDD-----PTLV 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2229004110 263 EVGARHGASVAEVALAYILAKPFVtsVIIGAKRLEQLEENLKAVKLKLDAEDVAKLDE 320
Cdd:cd19116 229 AIAKKYGKTTAQIVLRYLIDRGVV--PIPKSSNKKRIKENIDIFDFQLTPEEVAALNS 284
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
31-321 |
4.80e-19 |
|
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: 86.04 E-value: 4.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 31 VWSAVAGLD--QGAADKI---VERSLAAGVNFIDTANVYsqgRSEVILGQAIKNL----GVPRKDVIIATKFhgqmgdkp 101
Cdd:cd19155 10 EKMPVVGLGtwQSSPEEIetaVDTALEAGYRHIDTAYVY---RNEAAIGNVLKKWidsgKVKREELFIVTKL-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 102 nDRGASRGHimdSVE----QSLERLQMNHIDLYQIHG---------------------TDTVTPIDETLRALDDLVSRGL 156
Cdd:cd19155 79 -PPGGNRRE---KVEkfllKSLEKLQLDYVDLYLIHFpvgslskeddsgkldptgehkQDYTTDLLDIWKAMEAQVDQGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 157 VRYIGLSNWAAWRMAKALGISERKGYARFETVQAYYSiagrdlERDIVPLMQEEKLGLMVWSPLAggllsgkyGPGA--- 233
Cdd:cd19155 155 TRSIGLSNFNREQMARILKNARIKPANLQVELHVYLQ------QKDLVDFCSTHSITVTAYAPLG--------SPGAahf 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 234 -PGNGEGRRANFDfpPVDkdrawacVAAMREVGARHGASVAEVALAYILAKPFVtsVIIGAKRLEQLEENLKAVKLKLDA 312
Cdd:cd19155 221 sPGTGSPSGSSPD--LLQ-------DPVVKAIAERHGKSPAQVLLRWLMQRGVV--VIPKSTNAARIKENFQVFDFELTE 289
|
....*....
gi 2229004110 313 EDVAKLDEV 321
Cdd:cd19155 290 ADMAKLSSL 298
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
31-319 |
5.11e-19 |
|
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: 85.18 E-value: 5.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 31 VWSAVAGldqGAADKIVERSLAAGVNFIDTANVYsqgRSEVILGQAIKNLGVPRKDVIIATKFHGQmgdkpnDRGASRGh 110
Cdd:cd19126 16 VFQTPDG---DETERAVQTALENGYRSIDTAAIY---KNEEGVGEAIRESGVPREELFVTTKLWND------DQRARRT- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 111 iMDSVEQSLERLQMNHIDLYQIH--GTDTvtpIDETLRALDDLVSRGLVRYIGLSNWAAWRMAKALGISERKGYARFETV 188
Cdd:cd19126 83 -EDAFQESLDRLGLDYVDLYLIHwpGKDK---FIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHADVVPAVNQVEF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 189 QAYYSiagrdlERDIVPLMQEEKLGLMVWSPLA-GGLLSGKygpgapgngegrranfdfppvdkdrawacvaAMREVGAR 267
Cdd:cd19126 159 HPYLT------QKELRGYCKSKGIVVEAWSPLGqGGLLSNP-------------------------------VLAAIGEK 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2229004110 268 HGASVAEVALAYILAKPFVTsvIIGAKRLEQLEENLKAVKLKLDAEDVAKLD 319
Cdd:cd19126 202 YGKSAAQVVLRWDIQHGVVT--IPKSVHASRIKENADIFDFELSEDDMTAID 251
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
52-327 |
3.04e-18 |
|
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: 83.93 E-value: 3.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 52 AAGVNFIDTANVYsqGRSEVILGQAIKNLGVPRKDVIIATKFhG-------QMGDKPNDRGA-SRGHIMDSVEQSLERLQ 123
Cdd:cd19098 46 AAGVRYFDAARSY--GRAEEFLGSWLRSRNIAPDAVFVGSKW-GytytadwQVDAAVHEVKDhSLARLLKQWEETRSLLG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 124 mNHIDLYQIHGTDTVTPIDETLRALDDLVS--RGLVRyIGLSNWA---AWRMAKALGIsERKGYARFETVQAYYSIagrd 198
Cdd:cd19098 123 -KHLDLYQIHSATLESGVLEDADVLAALAElkAEGVK-IGLSLSGpqqAETLRRALEI-EIDGARLFDSVQATWNL---- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 199 LERDIVPLMQEEK---LGLMVWSPLAGGLLSGKygpgapgngegrranfdfPPVDKDRAwaCVAAMREVGARHGASVAEV 275
Cdd:cd19098 196 LEQSAGEALEEAHeagMGVIVKEALANGRLTDR------------------NPSPELAP--LMAVLKAVADRLGVTPDAL 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2229004110 276 ALAYILAKPFVTSVIIGAKRLEQLEENLKAVKLKLDAEDVAKLDEVsALAPE 327
Cdd:cd19098 256 ALAAVLAQPFVDVVLSGAATPEQLRSNLRALDVSLDLELLAALADL-AEPPE 306
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
54-164 |
1.27e-17 |
|
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381361 [Multi-domain] Cd Length: 265 Bit Score: 81.22 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 54 GVNFIDTANVYsqgRSEVILGQAIKNLGVPRKDVIIATKFHgqmgdkPNDRGASRghIMDSVEQSLERLQMNHIDLYQIH 133
Cdd:cd19135 39 GYRHIDTAKRY---GCEELLGKAIKESGVPREDLFLTTKLW------PSDYGYES--TKQAFEASLKRLGVDYLDLYLLH 107
|
90 100 110
....*....|....*....|....*....|....*...
gi 2229004110 134 GTDTVTPID-------ETLRALDDLVSRGLVRYIGLSN 164
Cdd:cd19135 108 WPDCPSSGKnvketraETWRALEELYDEGLCRAIGVSN 145
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
31-323 |
4.10e-17 |
|
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: 79.87 E-value: 4.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 31 VWSAVAGldqGAADKIVERSLAAGVNFIDTANVYSqgrSEVILGQAIKNLGVPRKDVIIATKFHGQmgdkpnDRGASRgh 110
Cdd:cd19156 16 VWRVQDG---AEAENAVKWAIEAGYRHIDTAAIYK---NEEGVGQGIRESGVPREEVFVTTKLWNS------DQGYES-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 111 IMDSVEQSLERLQMNHIDLYQIHGTDTVTPIDeTLRALDDLVSRGLVRYIGLSNWAAWRMAKALgiSERKGYARFETVQA 190
Cdd:cd19156 82 TLAAFEESLEKLGLDYVDLYLIHWPVKGKFKD-TWKAFEKLYKEKKVRAIGVSNFHEHHLEELL--KSCKVAPMVNQIEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 191 YYSIAGRDLERdivpLMQEEKLGLMVWSPLAGG-LLSGkygpgapgngegrranfdfppvdkdrawacvAAMREVGARHG 269
Cdd:cd19156 159 HPLLTQEPLRK----FCKEKNIAVEAWSPLGQGkLLSN-------------------------------PVLKAIGKKYG 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2229004110 270 ASVAEVALAYILAKPFVTsvIIGAKRLEQLEENLKAVKLKLDAEDVAKLDEVSA 323
Cdd:cd19156 204 KSAAQVIIRWDIQHGIIT--IPKSVHEERIQENFDVFDFELTAEEIRQIDGLNT 255
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
47-320 |
4.63e-17 |
|
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 79.74 E-value: 4.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 47 VERSLAAGVNFIDTANVYsqgRSEVILGQAIKNLGVPRKDVIIATKFHGqmgdkpNDRGASRghIMDSVEQSLERLQMNH 126
Cdd:cd19157 30 VKTALKNGYRSIDTAAIY---GNEEGVGKGIKESGIPREELFITSKVWN------ADQGYDS--TLKAFEASLERLGLDY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 127 IDLYQIHgtdtvTPID----ETLRALDDLVSRGLVRYIGLSNWAAWRMAKALGISERKGYARfetvQAYYSiaGRDLERD 202
Cdd:cd19157 99 LDLYLIH-----WPVKgkykETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAEIVPMVN----QVEFH--PRLTQKE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 203 IVPLMQEEKLGLMVWSPLAGGLLsgkygpgapgngegrranFDFPpvdkdrawacvaAMREVGARHGASVAEVALAYILA 282
Cdd:cd19157 168 LRDYCKKQGIQLEAWSPLMQGQL------------------LDNP------------VLKEIAEKYNKSVAQVILRWDLQ 217
|
250 260 270
....*....|....*....|....*....|....*...
gi 2229004110 283 KPFVTsvIIGAKRLEQLEENLKAVKLKLDAEDVAKLDE 320
Cdd:cd19157 218 NGVVT--IPKSIKEHRIIENADVFDFELSQEDMDKIDA 253
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
31-327 |
1.68e-16 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 78.58 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 31 VWSAVaglDQGAADKIVErSLAAGVNFIDTANVYsqgRSEVILGQAIKNLGVPRKDVIIATKFHgqmgdkpNDRgasRGH 110
Cdd:PRK11565 22 VWQAS---NEEVITAIHK-ALEVGYRSIDTAAIY---KNEEGVGKALKEASVAREELFITTKLW-------NDD---HKR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 111 IMDSVEQSLERLQMNHIDLYQIHGtdTVTPID---ETLRALDDLVSRGLVRYIGLSNWAAWRMAKALGiserkgyarfET 187
Cdd:PRK11565 85 PREALEESLKKLQLDYVDLYLMHW--PVPAIDhyvEAWKGMIELQKEGLIKSIGVCNFQIHHLQRLID----------ET 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 188 vqayySIAGRDLERDIVPLMQEEKL---------GLMVWSPLAGGllsgkygpgapgnGEGRranFDFPPVdkdrawacv 258
Cdd:PRK11565 153 -----GVTPVINQIELHPLMQQRQLhawnathkiQTESWSPLAQG-------------GKGV---FDQKVI--------- 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2229004110 259 aamREVGARHGASVAEVALAYILAKPFVtsVIIGAKRLEQLEENLKAVKLKLDAED---VAKLDEVSALAPE 327
Cdd:PRK11565 203 ---RDLADKYGKTPAQIVIRWHLDSGLV--VIPKSVTPSRIAENFDVFDFRLDKDElgeIAKLDQGKRLGPD 269
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
39-325 |
3.65e-16 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 77.70 E-value: 3.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 39 DQGAADKIVERSLAAGVNFIDTANVYSQGRSEVILGQAiknLGVPRKDVIIATKFHGQMGDK---PNDRgaSRGHIMDSV 115
Cdd:PRK10376 38 DRDAAIAVLREAVALGVNHIDTSDFYGPHVTNQLIREA---LHPYPDDLTIVTKVGARRGEDgswLPAF--SPAELRRAV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 116 EQSLERLQMNHIDL------YQIHGTDTvTPIDETLRALDDLVSRGLVRYIGLSNWAAWRMAKALGISErkgyarFETVQ 189
Cdd:PRK10376 113 HDNLRNLGLDVLDVvnlrlmGDGHGPAE-GSIEEPLTVLAELQRQGLVRHIGLSNVTPTQVAEARKIAE------IVCVQ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 190 AYYSIAGRDLERDIVPLMQEeklGLmvwsplaggllsgKYGPGAPGNGegrranfdFPPVDKDrawacvaAMREVGARHG 269
Cdd:PRK10376 186 NHYNLAHRADDALIDALARD---GI-------------AYVPFFPLGG--------FTPLQSS-------TLSDVAASLG 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2229004110 270 ASVAEVALAYILAKPFVTSVIIGAKRLEQLEENLKAVKLKLDAEDVAKLDEVSALA 325
Cdd:PRK10376 235 ATPMQVALAWLLQRSPNILLIPGTSSVAHLRENLAAAELVLSEEVLAELDGIAREA 290
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
42-319 |
3.16e-15 |
|
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: 74.56 E-value: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 42 AADKIVERSLAAGVNFIDTANVYSqgrSEVILGQAIKNLGVPRKDVIIATKFHgqmgdkpNDRgasRGH--IMDSVEQSL 119
Cdd:cd19130 24 DTQRAVATALEVGYRHIDTAAIYG---NEEGVGAAIAASGIPRDELFVTTKLW-------NDR---HDGdePAAAFAESL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 120 ERLQMNHIDLYQIH-GTDTVTPIDETLRALDDLVSRGLVRYIGLSNWAAWRMAKALGISERKGYARFETVQAYYSiagrd 198
Cdd:cd19130 91 AKLGLDQVDLYLVHwPTPAAGNYVHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVAATGVVPAVNQIELHPAYQ----- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 199 lERDIVPLMQEEKLGLMVWSPLAGGLLsgkygpgapgngegrranFDFPPVDKdrawacvaamreVGARHGASVAEVALA 278
Cdd:cd19130 166 -QRTIRDWAQAHDVKIEAWSPLGQGKL------------------LGDPPVGA------------IAAAHGKTPAQIVLR 214
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2229004110 279 YILAKPFVtsVIIGAKRLEQLEENLKAVKLKLDAEDVAKLD 319
Cdd:cd19130 215 WHLQKGHV--VFPKSVRRERMEDNLDVFDFDLTDTEIAAID 253
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
32-315 |
4.08e-15 |
|
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: 74.48 E-value: 4.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 32 WSAVAGLDQGAadkiVERSLAAGVNFIDTANVYsqGRSEVI---LGQAIKNLGVPRKDVIIATKFHGQMGDKPNdrgasr 108
Cdd:cd19128 9 YKITESESKEA----VKNAIKAGYRHIDCAYYY--GNEAFIgiaFSEIFKDGGVKREDLFITSKLWPTMHQPEN------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 109 ghIMDSVEQSLERLQMNHIDLYQIH-------------------GTDTVTPIDETLRALDDLVSRGLVRYIGLSNWAAWR 169
Cdd:cd19128 77 --VKEQLLITLQDLQLEYLDLFLIHwplafdmdtdgdprddnqiQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 170 MAKALGISERKGYARFETVQAYYSiagrdlERDIVPLMQEEKLGLMVWSPLAggllsGKYGPGApgngegrranfdfppv 249
Cdd:cd19128 155 LTDLLNYCKIKPFMNQIECHPYFQ------NDKLIKFCIENNIHVTAYRPLG-----GSYGDGN---------------- 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2229004110 250 dkdRAWACVAAMREVGARHGASVAEVALAYILAK-PFVTSVIIGAKRLEQLEENLKAVKLKLDAEDV 315
Cdd:cd19128 208 ---LTFLNDSELKALATKYNTTPPQVIIAWHLQKwPKNYSVIPKSANKSRCQQNFDINDLALTKEDM 271
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
8-322 |
4.38e-15 |
|
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: 74.46 E-value: 4.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 8 NTGLFVSELCLGTmtfgenqtgavWSAVagldQGAADKIVERSLAAGVNFIDTANVYsqgRSEVILGQAIKNLGVPRKDV 87
Cdd:cd19117 9 NTGAEIPAVGLGT-----------WQSK----PNEVAKAVEAALKAGYRHIDTAAIY---GNEEEVGQGIKDSGVPREEI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 88 IIATKFHGQMGDKPNdrgasrghimDSVEQSLERLQMNHIDLYQIH------------------GTDTVTP---IDETLR 146
Cdd:cd19117 71 FITTKLWCTWHRRVE----------EALDQSLKKLGLDYVDLYLMHwpvpldpdgndflfkkddGTKDHEPdwdFIKTWE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 147 ALDDLVSRGLVRYIGLSNWAAWRMAKALGISERKgyarfeTVQAYYSIagrdlerDIVPLMQEEKLGLMVWSPlagGLLS 226
Cdd:cd19117 141 LMQKLPATGKVKAIGVSNFSIKNLEKLLASPSAK------IVPAVNQI-------ELHPLLPQPKLVDFCKSK---GIHA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 227 GKYGPGAPGNGegrranfdfpPVDKDRawacvaAMREVGARHGASVAEVALAYILAKPfvTSVIIGAKRLEQLEENLKAv 306
Cdd:cd19117 205 TAYSPLGSTNA----------PLLKEP------VIIKIAKKHGKTPAQVIISWGLQRG--YSVLPKSVTPSRIESNFKL- 265
|
330
....*....|....*.
gi 2229004110 307 kLKLDAEDVAKLDEVS 322
Cdd:cd19117 266 -FTLSDEEFKEIDELH 280
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
8-321 |
2.24e-14 |
|
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: 72.18 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 8 NTGLFVSELCLGTmtfgenqtgavWSAvaglDQGAADKIVERSLAAGVNFIDTANVYsQGRSEVilGQAIK---NLGVPR 84
Cdd:cd19121 7 NTGASIPAVGLGT-----------WQA----KAGEVKAAVAHALKIGYRHIDGALCY-QNEDEV--GEGIKeaiAGGVKR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 85 KDVIIATKFHGQMGDKPNDrgasrghimdSVEQSLERLQMNHIDLYQIH--------GTDTVTP--------ID------ 142
Cdd:cd19121 69 EDLFVTTKLWSTYHRRVEL----------CLDRSLKSLGLDYVDLYLVHwpvllnpnGNHDLFPtlpdgsrdLDwdwnhv 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 143 ETLRALDDLVSRGLVRYIGLSNWAAWRMAKALgiserkgyARFETVQAYYSIAGRDL--ERDIVPLMQEEKLGLMVWSPL 220
Cdd:cd19121 139 DTWKQMEKVLKTGKTKAIGVSNYSIPYLEELL--------KHATVVPAVNQVENHPYlpQQELVDFCKEKGILIEAYSPL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 221 aggllsgkygpGAPGNgegrranfdfpPVDKDRawacvaAMREVGARHGASVAEVALAYILAKPFVtsVIIGAKRLEQLE 300
Cdd:cd19121 211 -----------GSTGS-----------PLISDE------PVVEIAKKHNVGPGTVLISYQVARGAV--VLPKSVTPDRIK 260
|
330 340
....*....|....*....|.
gi 2229004110 301 ENLKAVklKLDAEDVAKLDEV 321
Cdd:cd19121 261 SNLEII--DLDDEDMNKLNDI 279
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
47-320 |
3.23e-14 |
|
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) is a founding member of the aldo-keto reductase family 5 member B1 (AKR5B1). M6DH (EC 1.1.1.218), also called naloxone reductase, oxidizes the C-6 hydroxy group of morphine and codeine.
Pssm-ID: 381353 [Multi-domain] Cd Length: 268 Bit Score: 71.67 E-value: 3.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 47 VERSLAAGVNFIDTANVYsqgRSEVILGQAIKNLGVPRKDVIIATK-FHGQMGDKPNDRGasrghimdsVEQSLERLQMN 125
Cdd:cd19127 28 VATALADGYRLIDTAAAY---GNEREVGEGIRRSGVDRSDIFVTTKlWISDYGYDKALRG---------FDASLRRLGLD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 126 HIDLYQIHGTdTVTPIDETL---RALDDLVSRGLVRYIGLSNWAAWRMAK---------ALGISERKGYARFETVQAYYS 193
Cdd:cd19127 96 YVDLYLLHWP-VPNDFDRTIqayKALEKLLAEGRVRAIGVSNFTPEHLERlidattvvpAVNQVELHPYFSQKDLRAFHR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 194 IAGrdlerdIVPlmqeeklglMVWSPLAGGLLSGKYGPGAPGNgegrranfdfPPVDkdrawacvAAMREVGARHGASVA 273
Cdd:cd19127 175 RLG------IVT---------QAWSPIGGVMRYGASGPTGPGD----------VLQD--------PTITGLAEKYGKTPA 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2229004110 274 EVALAYILAKPFvtSVIIGAKRLEQLEENLKAVKLKLDAEDVAKLDE 320
Cdd:cd19127 222 QIVLRWHLQNGV--SAIPKSVHPERIAENIDIFDFALSAEDMAAIDA 266
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
47-319 |
5.26e-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: 5.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 47 VERSLAAGVNFIDTANVYSqgrSEVILGQAIKN-----LGVPRKDVIIATKF----HgqmgdKPNDrgasrghIMDSVEQ 117
Cdd:cd19106 26 VKYALDAGYRHIDCAAVYG---NEQEVGEALKEkvgpgKAVPREDLFVTSKLwntkH-----HPED-------VEPALRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 118 SLERLQMNHIDLYQIH-------GTD------------TVTPIDETLRALDDLVSRGLVRYIGLSNWAAWRMAKALGISe 178
Cdd:cd19106 91 TLKDLQLDYLDLYLIHwpyaferGDNpfpknpdgtiryDSTHYKETWKAMEKLVDKGLVKAIGLSNFNSRQIDDILSVA- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 179 rkgyarfetvqayySIAGRDLERDIVPLMQEEKLGLMVWSPlagGLLSGKYGP-GAPgngegrranfdfppvdkDRAWAC 257
Cdd:cd19106 170 --------------RIKPAVLQVECHPYLAQNELIAHCKAR---GLVVTAYSPlGSP-----------------DRPWAK 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 258 V--------AAMREVGARHGASVAEVALAYILAKPFVtsVIIGAKRLEQLEENLKAVKLKLDAEDVAKLD 319
Cdd:cd19106 216 PdepvlleePKVKALAKKYNKSPAQILLRWQVQRGVV--VIPKSVTPSRIKQNIQVFDFTLSPEEMKQLD 283
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
25-319 |
1.26e-13 |
|
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding member of aldo-keto reductase family 5 member H1 (AKR5H1). It is a NADPH-dependent aldo-keto reductase that reduces methylglyoxal and phenylglyoxal.
Pssm-ID: 381360 [Multi-domain] Cd Length: 263 Bit Score: 69.88 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 25 ENQTGAVWSAVAGLDQGAADKIVERSLAAGVNFIDTANVYSqgrSEVILGQAIKNLGVPRKDVIIATKFhgqmgdKPNDR 104
Cdd:cd19134 8 DNTMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYG---NEAAVGRAIAASGIPRGELFVTTKL------ATPDQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 105 GASRGhiMDSVEQSLERLQMNHIDLYQIH--GTDTVTPIDeTLRALDDLVSRGLVRYIGLSNWAAWRMAKALGISerkgy 182
Cdd:cd19134 79 GFTAS--QAACRASLERLGLDYVDLYLIHwpAGREGKYVD-SWGGLMKLREEGLARSIGVSNFTAEHLENLIDLT----- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 183 arfetvqaYYSIAGRDLErdIVPLMQEEKL-------GLMV--WSPLAGGLLsgkygpgapgngegrranFDFPPVDKdr 253
Cdd:cd19134 151 --------FFTPAVNQIE--LHPLLNQAELrkvnaqhGIVTqaYSPLGVGRL------------------LDNPAVTA-- 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2229004110 254 awacvaamreVGARHGASVAEVALAYILAKPFVtsVIIGAKRLEQLEENLKAVKLKLDAEDVAKLD 319
Cdd:cd19134 201 ----------IAAAHGRTPAQVLLRWSLQLGNV--VISRSSNPERIASNLDVFDFELTADHMDALD 254
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
58-321 |
5.06e-13 |
|
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes Glycine max NAD(P)H-dependent 6'-deoxychalcone synthase (6DCS, EC 3.1.170), chalcone reductase (CHR, EC 2.3.1.74) from Medicago sativa, Glycyrrhiza echinate, and Glycyrrhiza glabra, which are founding members of aldo-keto reductase family 4 member A1 (AKR4A1), A2 (AKR4A2), A3 (AKR4A3), and A4 (AKR4A4), respectively. NAD(P)H-6DCS co-acts with chalcone synthase in formation of 4,2',4'-trihydroxychalcone, involved in the biosynthesis of glyceollin type phytoalexins. CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. The AKR4B family of AKR includes Sesbania rostrate chalcone reductase (CHR, AKR4B1), Papaver somniferum codeinone reductase (COR, AKR4B2/ AKR4B3), Fragaria x ananassa D-galacturonate reductase (GalUR, AKR4B4), deoxymugineic acid synthase 1 (DMAS1) from Zea mays (AKR4B5), Oryza sativa (AKR4B6), Hordeum vulgare (AKR4B7), Triticum aestivum (AKR4B8), and Erythroxylum coca methylecgonone reductase (MecgoR, AKR4B10). CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. NADPH-dependent COR and non-functional NADPH-dependent COR from Papaver somniferum are founding members of aldo-keto reductase family 4 member B2 (AKR4B2) and B3 (AKR4B3), respectively. NADPH-dependent COR (EC 1.1.1.247) reduces codeinone to codeine in the penultimate step in morphine biosynthesis. It can use morphinone, hydrocodone, and hydromorphone as substrates during reductive reaction with NADPH as cofactor, and morphine and dihydrocodeine as substrates during oxidative reaction with NADP as cofactor. GalUR (EC 1.1.1.365), also called aldo-keto reductase 2 (AKR2), is involved in ascorbic acid (vitamin C) biosynthesis by catalyzing the conversion from L-galactonate and NADP(+) to D-galacturonate and NADPH. DMAS1 (EC 1.1.1.285) catalyzes the reduction of a 3''-keto intermediate during the biosynthesis of 2'-deoxymugineic acid (DMA) from L-Met. It is involved in the formation of phytosiderophores (MAs) belonging to the mugineic acid family and required to acquire iron. MecgoR catalyzes the stereospecific reduction of methylecgonone to methylecgonine, the penultimate step in cocaine biosynthesis.
Pssm-ID: 381350 [Multi-domain] Cd Length: 281 Bit Score: 68.45 E-value: 5.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 58 IDTANVYsqgRSEVILGQAIK-----NLGVPRKDVIIATKFhgQMGDkpndrgASRGHIMDSVEQSLERLQMNHIDLYQI 132
Cdd:cd19124 37 FDTAAAY---GTEEALGEALAealrlGLVKSRDELFVTSKL--WCSD------AHPDLVLPALKKSLRNLQLEYVDLYLI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 133 H--------------GTDTVTPID--ETLRALDDLVSRGLVRYIGLSNWAAWRMAKALGIserkgyarfetvqAYYSIAG 196
Cdd:cd19124 106 HwpvslkpgkfsfpiEEEDFLPFDikGVWEAMEECQRLGLTKAIGVSNFSCKKLQELLSF-------------ATIPPAV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 197 RDLERDivPLMQEEKL-------GLMV--WSPLaggllsgkygpGAPGNGEGRRANFDFPpvdkdrawacvaAMREVGAR 267
Cdd:cd19124 173 NQVEMN--PAWQQKKLrefckanGIHVtaYSPL-----------GAPGTKWGSNAVMESD------------VLKEIAAA 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2229004110 268 HGASVAEVALAYILAKPfvTSVIIGAKRLEQLEENLKAVKLKLDAEDVAKLDEV 321
Cdd:cd19124 228 KGKTVAQVSLRWVYEQG--VSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
28-321 |
1.40e-12 |
|
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: 67.37 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 28 TGAVWSAVaGL-----DQGAADKIVERSLAAGVNFIDTANVYSqgrSEVILGQAIKNLG----VPRKDVIIATKFHGQMG 98
Cdd:cd19125 7 TGAKIPAV-GLgtwqaDPGVVGNAVKTAIKEGYRHIDCAAIYG---NEKEIGKALKKLFedgvVKREDLFITSKLWCTDH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 99 DKPNDRGAsrghimdsVEQSLERLQMNHIDLYQIH-------GTDTVTP-------IDETLRALDDLVSRGLVRYIGLSN 164
Cdd:cd19125 83 APEDVPPA--------LEKTLKDLQLDYLDLYLIHwpvrlkkGAHMPEPeevlppdIPSTWKAMEKLVDSGKVRAIGVSN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 165 WAAWRMAKALGISERKGyarfetvqayysiAGRDLErdIVPLMQEEKL-------GLMV--WSPLaggllsgkygpGAPG 235
Cdd:cd19125 155 FSVKKLEDLLAVARVPP-------------AVNQVE--CHPGWQQDKLhefckskGIHLsaYSPL-----------GSPG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 236 NGEGRRANFDFPPVDKdrawacvaamreVGARHGASVAEVALAYILAKPfvTSVIIGAKRLEQLEENLKAVKLKLDAEDV 315
Cdd:cd19125 209 TTWVKKNVLKDPIVTK------------VAEKLGKTPAQVALRWGLQRG--TSVLPKSTNEERIKENIDVFDWSIPEEDF 274
|
....*.
gi 2229004110 316 AKLDEV 321
Cdd:cd19125 275 AKFSSI 280
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
8-321 |
5.14e-11 |
|
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: 62.43 E-value: 5.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 8 NTGLFVSELCLGTmtfgenqtgavWSAVAGlDQGAAdkiVERSLAAGVNFIDTANVYsQGRSEVilGQAIKNL-----GV 82
Cdd:cd19118 2 NTGNKIPAIGLGT-----------WQAEPG-EVGAA---VKIALKAGYRHLDLAKVY-QNQHEV--GQALKELlkeepGV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 83 PRKDVIIATKFHgqmgdkpNDRGAsRGHIMDSVEQSLERLQMNHIDLYQIH-------GTD----TVTPIDETLRALDDL 151
Cdd:cd19118 64 KREDLFITSKLW-------NNSHR-PEYVEPALDDTLKELGLDYLDLYLIHwpvafkpTGDlnplTAVPTNGGEVDLDLS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 152 VS-------------RGLVRYIGLSNWAAwRMAKALgISERKGYARFETVQAYysiaGRDLERDIVPLMQEEKLGLMVWS 218
Cdd:cd19118 136 VSlvdtwkamvelkkTGKVKSIGVSNFSI-DHLQAI-IEETGVVPAVNQIEAH----PLLLQDELVDYCKSKNIHITAYS 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 219 PLAGGLLsgkygpGAPgngegrranfdfPPVDKDrawacvaAMREVGARHGASVAEVALAYILAKPFvtSVIIGAKRLEQ 298
Cdd:cd19118 210 PLGNNLA------GLP------------LLVQHP-------EVKAIAAKLGKTPAQVLIAWGIQRGH--SVIPKSVTPSR 262
|
330 340
....*....|....*....|...
gi 2229004110 299 LEENLKAVklKLDAEDVAKLDEV 321
Cdd:cd19118 263 IRSNFEQV--ELSDDEFNAVTAL 283
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
41-318 |
2.86e-10 |
|
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: 60.51 E-value: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 41 GAADKIVERSLAAGVNFIDTANVYsQGRSEVILG--QAIKNLGVPRKDVIIATKFHGQMGDKPNDRGAsrghimdsVEQS 118
Cdd:cd19107 17 GQVTEAVKVAIDAGYRHIDCAYVY-QNENEVGEAiqEKIKEQVVKREDLFIVSKLWCTFHEKGLVKGA--------CQKT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 119 LERLQMNHIDLYQIH-------GTDTVtPIDE-------------TLRALDDLVSRGLVRYIGLSNWAAWRMAKALGISE 178
Cdd:cd19107 88 LSDLKLDYLDLYLIHwptgfkpGKELF-PLDEsgnvipsdttfldTWEAMEELVDEGLVKAIGVSNFNHLQIERILNKPG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 179 RKgyarfetvqayYSIAGRDLErdIVPLMQEEKL-------GLMV--WSPLaggllsgkygpGAPgngegrranfdfppv 249
Cdd:cd19107 167 LK-----------YKPAVNQIE--CHPYLTQEKLiqycqskGIVVtaYSPL-----------GSP--------------- 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2229004110 250 dkDRAWAC--------VAAMREVGARHGASVAEVALAYILAKPFVtsVIIGAKRLEQLEENLKAVKLKLDAEDVAKL 318
Cdd:cd19107 208 --DRPWAKpedpslleDPKIKEIAAKHNKTTAQVLIRFPIQRNLV--VIPKSVTPERIAENFKVFDFELSSEDMATI 280
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
39-164 |
1.31e-09 |
|
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: 58.24 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 39 DQGAADKIVERSLAAGVNFIDTANVYsqgRSEVILGQAIKNL----GVPRKDVIIATKF----HGQMGDKPndrgasrgh 110
Cdd:cd19129 17 DPSATRNAVKAALEAGFRHFDCAERY---RNEAEVGEAMQEVfkagKIRREDLFVTTKLwntnHRPERVKP--------- 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2229004110 111 imdSVEQSLERLQMNHIDLYQIHGTDTVTPIDE--------------------TLRALDDLVSRGLVRYIGLSN 164
Cdd:cd19129 85 ---AFEASLKRLQLDYLDLYLIHTPFAFQPGDEqdprdangnviyddgvtlldTWRAMERLVDEGRCKAIGLSD 155
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
41-325 |
2.87e-09 |
|
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) from Mus musculus (liver, AKR1E1) and Homo sapiens (AKR1E2). 1,5-anhydro-D-fructose reductase), also called AF reductase, or aldo-keto reductase family 1 member C-like protein 2 (AKR1CL2), catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. AKR1E2 is a testis aldo-keto reductase (tAKR), which is also known as testis-specific protein (TSP), or LoopADR.
Pssm-ID: 381336 [Multi-domain] Cd Length: 301 Bit Score: 57.28 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 41 GAADKIVERSLAAGVNFIDTANVYsQGRSEVILG--QAIKNLGVPRKDVIIATKFHGQMGDKPNDRGASRghimdsveQS 118
Cdd:cd19110 17 GEVTEAVKVAIDAGYRHFDCAYLY-HNESEVGAGirEKIKEGVVRREDLFIVSKLWCTCHKKSLVKTACT--------RS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 119 LERLQMNHIDLYQIH------GTDTVTPIDE-------------TLRALDDLVSRGLVRYIGLSNWAAWRMAKALGiser 179
Cdd:cd19110 88 LKALKLNYLDLYLIHwpmgfkPGEPDLPLDRsgmvipsdtdfldTWEAMEDLVIEGLVKNIGVSNFNHEQLERLLN---- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 180 KGYARFETVQAYYSIAGRDLERDIVPLMQEEKLGLMVWSPLAggllsgkygpgapGNGEGrranfdFPPVDKdrawacvA 259
Cdd:cd19110 164 KPGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLG-------------GSCEG------VDLIDD-------P 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2229004110 260 AMREVGARHGASVAEVALAYILAKPFVtsVIIGAKRLEQLEENLKAVKLKL---DAEDVAKLDEVSALA 325
Cdd:cd19110 218 VIQRIAKKHGKSPAQILIRFQIQRNVI--VIPKSVTPSRIKENIQVFDFELtehDMDNLLSLDRNLRLA 284
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
40-308 |
2.12e-08 |
|
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: 54.94 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 40 QGAADKIVERSLAAGVNFIDTANVYsQGRSEVilGQAIK-----NLGVPRKDVIIATKFHGQMgDKPNDrgasrghIMDS 114
Cdd:cd19122 23 KGETYAAVTKALDVGYRHLDCAWFY-LNEDEV--GDAVRdflkeNPSVKREDLFICTKVWNHL-HEPED-------VKWS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 115 VEQSLERLQMNHIDLYQIH---------------GTDTVTPIDETL--------RALDDLVSRGLVRYIGLSNWAAWRMA 171
Cdd:cd19122 92 IDNSLKNLKLDYIDLFLVHwpiaaekndqrspklGPDGKYVILKDLtenpeptwRAMEEIYESGKAKAIGVSNWTIPGLK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 172 KALGISERKGYARfetvqayysiagrdlERDIVPLMQEEKLglmVWSPLAGGLLSGKYGP-----GAPGNGEGRRANfdf 246
Cdd:cd19122 172 KLLSFAKVKPHVN---------------QIEIHPFLPNEEL---VDYCFSNDILPEAYSPlgsqnQVPSTGERVSEN--- 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2229004110 247 ppvdkdrawacvAAMREVGARHGASVAEVALAYILAKPFVtsVIIGAKRLEQLEENLKAVKL 308
Cdd:cd19122 231 ------------PTLNEVAEKGGYSLAQVLIAWGLRRGYV--VLPKSSTPSRIESNFKSIEL 278
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
43-324 |
2.82e-07 |
|
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose reductase xyl1 (XR, EC 1.1.1.307) is a founding member of aldo-keto reductase family 2 member D1 (AKR2D1). It catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol in a NAD(P)H dependent manner.
Pssm-ID: 381341 [Multi-domain] Cd Length: 311 Bit Score: 51.27 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 43 ADKIVErSLAAGVNFIDTANVYSqgrSEVILGQ----AIKNLGVPRKDVIIATKFHGQMGDKPndrgasrgHIMDSVEQS 118
Cdd:cd19115 29 ADQVYN-AIKAGYRLFDGACDYG---NEVEAGQgvarAIKEGIVKREDLFIVSKLWNTFHDGE--------RVEPICRKQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 119 LERLQMNHIDLYQIH--------------------GTDTV----TPIDETLRALDDLVSRGLVRYIGLSNWAAWRMAKAL 174
Cdd:cd19115 97 LADWGIDYFDLFLIHfpialkyvdpavryppgwfyDGKKVefsnAPIQETWTAMEKLVDKGLARSIGVSNFSAQLLMDLL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 175 giserkGYARFE--TVQ----AYYSiagrdlERDIVPLMQEEKLGLMVWSplaggllsgKYGPGAPGNGEGRRANfDFPP 248
Cdd:cd19115 177 ------RYARIRpaTLQiehhPYLT------QPRLVKYAQKEGIAVTAYS---------SFGPQSFLELDLPGAK-DTPP 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2229004110 249 V-DKDrawacvaAMREVGARHGASVAEVALAYilAKPFVTSVIIGAKRLEQLEENLKAVKLKLDAEDvakLDEVSAL 324
Cdd:cd19115 235 LfEHD-------VIKSIAEKHGKTPAQVLLRW--ATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEE---IKAISAL 299
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
47-164 |
3.28e-07 |
|
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: 51.08 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 47 VERSLAAGVNFIDTANVYsQGRSEVilGQAI----KNLGVPRKDVIIATK-----FHGQMgdkpndrgasrghIMDSVEQ 117
Cdd:cd19108 33 TKLAIDAGFRHIDSAYLY-QNEEEV--GQAIrskiADGTVKREDIFYTSKlwctfHRPEL-------------VRPALEK 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2229004110 118 SLERLQMNHIDLYQIH------GTDTVTPIDETLRALDDLV-------------SRGLVRYIGLSN 164
Cdd:cd19108 97 SLKKLQLDYVDLYLIHfpvalkPGEELFPKDENGKLIFDTVdlcatweamekckDAGLAKSIGVSN 162
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
42-319 |
5.44e-07 |
|
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: 50.52 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 42 AADKIVErSLAAGVNFIDTANVYSQGRsEVILG--QAIKNLGVPRKDVIIATKFHGQMGDKPNDRGAsrghimdsVEQSL 119
Cdd:cd19113 26 AADQIYQ-AIKAGYRLFDGAEDYGNEK-EVGEGvnRAIDEGLVKREELFLTSKLWNNFHDPKNVETA--------LNKTL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 120 ERLQMNHIDLYQIH----------------------GTDTV---TPIDETLRALDDLVSRGLVRYIGLSNWAAwrmakAL 174
Cdd:cd19113 96 SDLKLDYVDLFLIHfpiafkfvpieekyppgfycgdGDNFVyedVPILDTWKALEKLVDAGKIKSIGVSNFPG-----AL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 175 GISERKGyARFETVQayysiagrdLERDIVPLMQEEKlgLMVWSPLAGGLLSG--KYGPGAPGNGEGRRAnFDFPPVDKD 252
Cdd:cd19113 171 ILDLLRG-ATIKPAV---------LQIEHHPYLQQPK--LIEYAQKAGITITAysSFGPQSFVELNQGRA-LNTPTLFEH 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 253 RawacvaAMREVGARHGASVAEVALAYILAKPFvtSVIIGAKRLEQLEENLKAVKLKL---DAEDVAKLD 319
Cdd:cd19113 238 D------TIKSIAAKHNKTPAQVLLRWATQRGI--AVIPKSNLPERLLQNLSVNDFDLtkeDFEEIAKLD 299
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
7-329 |
5.50e-06 |
|
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes 3-oxo-5-beta-steroid 4-dehydrogenase (EC 1.3.1.3) from Homo sapiens (AKR1D1), Rattus norvegicus (liver, AKR1D2), and Oryctolagus cuniculus (AKR1D3). 3-oxo-5-beta-steroid 4-dehydrogenase, also called delta(4)-3-ketosteroid 5-beta-reductase (EC 1.3.99.6), or delta(4)-3-oxosteroid 5-beta-reductase, or 5-beta-reductase, efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites.
Pssm-ID: 381335 [Multi-domain] Cd Length: 308 Bit Score: 47.49 E-value: 5.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 7 GNTglfVSELCLGTmtFGENQTGAvwsavagldQGAADKIVERSLAAGVNFIDTANVYSqgrSEVILGQAIKNL----GV 82
Cdd:cd19109 1 GNS---IPIIGLGT--YSEPKTTP---------KGACAEAVKVAIDTGYRHIDGAYIYQ---NEHEVGQAIREKiaegKV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 83 PRKDVIIATK----FHGQMGDKPndrgasrghimdSVEQSLERLQMNHIDLYQIH------GTDTVTPIDE--------- 143
Cdd:cd19109 64 KREDIFYCGKlwntCHPPELVRP------------TLERTLKVLQLDYVDLYIIEmpmafkPGDEIYPRDEngkwlyhkt 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 144 ----TLRALDDLVSRGLVRYIGLSNWAAWRMAKAL---GISERKGYARFEtVQAYYSiagrdlERDIVPLMQEEKLGLMV 216
Cdd:cd19109 132 nlcaTWEALEACKDAGLVKSIGVSNFNRRQLELILnkpGLKHKPVSNQVE-CHPYFT------QPKLLEFCQQHDIVIVA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229004110 217 WSPLaggllsgkygpGAPGNgeGRRANFDFPPVDKDrawacvAAMREVGARHGASVAEVALAYILAKPFVtsVIIGAKRL 296
Cdd:cd19109 205 YSPL-----------GTCRD--PIWVNVSSPPLLED------PLLNSIGKKYNKTAAQVVLRFNIQRGVV--VIPKSFNP 263
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2229004110 297 EQLEENLKAVKLKLDAEDVAKLDE-------VSALA----PEYP 329
Cdd:cd19109 264 ERIKENFQIFDFSLTEEEMKDIEAlnknvryVELLMwrdhPEYP 307
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
101-138 |
1.78e-03 |
|
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the first CH domain.
Pssm-ID: 409081 Cd Length: 107 Bit Score: 37.68 E-value: 1.78e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2229004110 101 PNDRGASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTV 138
Cdd:cd21232 49 PKERGSTRVHALNNVNRVLQVLHQNNVELVNIGGTDIV 86
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
101-138 |
2.05e-03 |
|
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain.
Pssm-ID: 409080 Cd Length: 111 Bit Score: 37.59 E-value: 2.05e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2229004110 101 PNDRGASRGHIMDSVEQSLERLQMNHIDLYQIHGTDTV 138
Cdd:cd21231 53 VKEKGSTRVHALNNVNKALQVLQKNNVDLVNIGSADIV 90
|
|
| |
