|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
1-321 |
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: 524.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 1 MRYQKLGNTGLFVSRLCLGTMTFGGEGGMWGKIGQLRQAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNLkv 80
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGTMTFGGGGGFFGAWGGVDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKGR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 81 pRENVVVATKVFGETGtAGVNSRGSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRYIG 160
Cdd:cd19091 79 -RDDVLIATKVRGRMG-EGPNDVGLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVRYIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 161 VSNWAAWQIVKALGISARLGLSRFASLQAYYTIAGRDLERELIPMMQSEGVGLMVWSPLAGGLLSGKYDREGQTAEGGR- 239
Cdd:cd19091 157 VSNFSAWQIMKALGISERRGLARFVALQAYYSLLGRDLEHELMPLALDQGVGLLVWSPLAGGLLSGKYRRGQPAPEGSRl 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 240 -RQAFDFPPVNKDRAFDCIDVMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVDIQLSEVELAQLD 318
Cdd:cd19091 237 rRTGFDFPPVDRERGYDVVDALREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGAAGLSLTPEEIARLD 316
|
...
gi 1558667949 319 AVS 321
Cdd:cd19091 317 KVS 319
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-322 |
1.23e-146 |
|
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: 416.12 E-value: 1.23e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 1 MRYQKLGNTGLFVSRLCLGTMTFGGeggMWGKIGQlrqAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNLkv 80
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTMTFGG---PWGGVDE---AEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALKGR-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 81 PRENVVVATKVFGETGtAGVNSRGSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRYIG 160
Cdd:COG0667 73 PRDDVVIATKVGRRMG-PGPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 161 VSNWAAWQIVKALGISArlGLSRFASLQAYYTIAGRDLERELIPMMQSEGVGLMVWSPLAGGLLSGKYDREGQTAEGGRR 240
Cdd:COG0667 152 VSNYSAEQLRRALAIAE--GLPPIVAVQNEYSLLDRSAEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGATFPEGDRA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 241 QAFDFPPVNKDRAFDCIDVMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVDIQLSEVELAQLDAV 320
Cdd:COG0667 230 ATNFVQGYLTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADLELSAEDLAALDAA 309
|
..
gi 1558667949 321 SA 322
Cdd:COG0667 310 LA 311
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
1-321 |
6.65e-137 |
|
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: 391.17 E-value: 6.65e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 1 MRYQKLGNTGLFVSRLCLGTMTFGGEGGmwgkigqlrQAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNLkv 80
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGTMNFGGRTD---------EETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAGR-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 81 pRENVVVATKVFGETGTaGVNSRGSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRYIG 160
Cdd:cd19087 70 -RDDIVLATKVFGPMGD-DPNDRGLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 161 VSNWAAWQIVKALGISARLGLSRFASLQAYYTIAGRDLERELIPMMQSEGVGLMVWSPLAGGLLSGKYdREGQTAEGGRR 240
Cdd:cd19087 148 VSNFAAWQIAKAQGIAARRGLLRFVSEQPMYNLLKRQAELEILPAARAYGLGVIPYSPLAGGLLTGKY-GKGKRPESGRL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 241 QAFDFPPVNK--DRAFDCIDVMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVDIQLSEVELAQLD 318
Cdd:cd19087 227 VERARYQARYglEEYRDIAERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEITLTPELLAEID 306
|
...
gi 1558667949 319 AVS 321
Cdd:cd19087 307 ELF 309
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
3-318 |
7.04e-135 |
|
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: 386.17 E-value: 7.04e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 3 YQKLGNTGLFVSRLCLGTMTFGGEG-GMWGkigqLRQAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNLkVP 81
Cdd:cd19079 2 YVRLGNSGLKVSRLCLGCMSFGDPKwRPWV----LDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEF-AP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 82 RENVVVATKVFGETGTaGVNSRGSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRYIGV 161
Cdd:cd19079 77 RDEVVIATKVYFPMGD-GPNGRGLSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 162 SNWAAWQIVKALGISARLGLSRFASLQAYYTIAGRDLERELIPMMQSEGVGLMVWSPLAGGLLSGKYDREGQTAEGGRRQ 241
Cdd:cd19079 156 SSMYAWQFAKALHLAEKNGWTKFVSMQNHYNLLYREEEREMIPLCEEEGIGVIPWSPLARGRLARPWGDTTERRRSTTDT 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1558667949 242 AFDFPPVNKDRAFDCIDVMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVDIQLSEVELAQLD 318
Cdd:cd19079 236 AKLKYDYFTEADKEIVDRVEEVAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAALDIKLSEEEIKYLE 312
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
5-318 |
7.97e-116 |
|
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: 337.65 E-value: 7.97e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 5 KLGNTGLFVSRLCLGTMTFGGEGGmwgkigqlrQAEAEQLVGSALDAGINFIDTADVYS-------EGRSEMLTGQALKN 77
Cdd:cd19081 1 PLGRTGLSVSPLCLGTMVFGWTAD---------EETSFALLDAFVDAGGNFIDTADVYSawvpgnaGGESETIIGRWLKS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 78 lKVPRENVVVATKVFGETGtagVNSRGSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVR 157
Cdd:cd19081 72 -RGKRDRVVIATKVGFPMG---PNGPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 158 YIGVSNWAAWQIVKALGISARLGLSRFASLQAYYTIAGRD-LERELIPMMQSEGVGLMVWSPLAGGLLSGKYDREGQTAE 236
Cdd:cd19081 148 YIGASNYSAWRLQEALELSRQHGLPRYVSLQPEYNLVDREsFEGELLPLCREEGIGVIPYSPLAGGFLTGKYRSEADLPG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 237 GGRRQAFdFPPVNKDRAFDCIDVMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVDIQLSEVELAQ 316
Cdd:cd19081 228 STRRGEA-AKRYLNERGLRILDALDEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAGLRLTDEEVAR 306
|
..
gi 1558667949 317 LD 318
Cdd:cd19081 307 LD 308
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
10-318 |
2.30e-114 |
|
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: 333.72 E-value: 2.30e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 10 GLFVSRLCLGTMTFGGegGMWGKIgqlRQAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNLkvpRENVVVAT 89
Cdd:cd19084 1 DLKVSRIGLGTWAIGG--TWWGEV---DDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKGR---RDDVVIAT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 90 KVFGETGTAGVNSRGSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRYIGVSNWAAWQI 169
Cdd:cd19084 73 KCGLRWDGGKGVTKDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 170 VKAlgisarLGLSRFASLQAYYTIAGRDLERELIPMMQSEGVGLMVWSPLAGGLLSGKYDREGQTAEGGRRQAF-DFPPV 248
Cdd:cd19084 153 EEA------RKYGPIVSLQPPYSMLEREIEEELLPYCRENGIGVLPYGPLAQGLLTGKYKKEPTFPPDDRRSRFpFFRGE 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 249 NKDRAFDCIDVMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVDIQLSEVELAQLD 318
Cdd:cd19084 227 NFEKNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDWELTEEELKEID 296
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
6-318 |
8.39e-111 |
|
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: 324.94 E-value: 8.39e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 6 LGNTGLFVSRLCLGTMTFGGEGGmWGkigqLRQAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNLkvpRENV 85
Cdd:cd19080 3 LGRSGLRVSPLALGTMTFGTEWG-WG----ADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAGN---RDRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 86 VVATKVFGETGTAGVNSRGSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRYIGVSNWA 165
Cdd:cd19080 75 VLATKYTMNRRPGDPNAGGNHRKNLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 166 AWQIVKALGISARLGLSRFASLQAYYTIAGRDLERELIPMMQSEGVGLMVWSPLAGGLLSGKYDREGQTAEGGRRQAFDF 245
Cdd:cd19080 155 AWVVARANTLAELRGWSPFVALQIEYSLLERTPERELLPMARALGLGVTPWSPLGGGLLTGKYQRGEEGRAGEAKGVTVG 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1558667949 246 PPVNKDRAFDCIDVMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVDIQLSEVELAQLD 318
Cdd:cd19080 235 FGKLTERNWAIVDVVAAVAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDLTLSPEQLARLD 307
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
10-311 |
7.38e-108 |
|
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: 317.23 E-value: 7.38e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 10 GLFVSRLCLGT-MTFGGeggmwgkigQLRQAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKnlKVPRENVVVA 88
Cdd:cd19074 1 GLKVSELSLGTwLTFGG---------QVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALK--GWPRESYVIS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 89 TKVFGETGtAGVNSRGSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRYIGVSNWAAWQ 168
Cdd:cd19074 70 TKVFWPTG-PGPNDRGLSRKHIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 169 IVKALGISARLGLSRFASLQAYYTIAGRDLERELIPMMQSEGVGLMVWSPLAGGLLSGKYdREGQTAEGGRRQAFDFPPV 248
Cdd:cd19074 149 IAEAHDLARQFGLIPPVVEQPQYNMLWREIEEEVIPLCEKNGIGLVVWSPLAQGLLTGKY-RDGIPPPSRSRATDEDNRD 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1558667949 249 NKDRAF-----DCIDVMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVDIQLSE 311
Cdd:cd19074 228 KKRRLLtdenlEKVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKASGVKLSP 295
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
16-320 |
2.04e-98 |
|
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: 292.68 E-value: 2.04e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 16 LCLGTMTFGGEGGMWGKigqlrqAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNLKVPRENVVVATKVFGET 95
Cdd:pfam00248 1 IGLGTWQLGGGWGPISK------EEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKRDKVVIATKVPDGD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 96 GTAGVnsrGSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRYIGVSNWAAWQIVKALgi 175
Cdd:pfam00248 75 GPWPS---GGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKAL-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 176 saRLGLSRFASLQAYYTIAGRDLERELIPMMQSEGVGLMVWSPLAGGLLSGKYDREGQTAEGGRRQAFdfpPVNKDRAFD 255
Cdd:pfam00248 150 --TKGKIPIVAVQVEYNLLRRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPGERRRLL---KKGTPLNLE 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1558667949 256 CIDVMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVDIQLSEVELAQLDAV 320
Cdd:pfam00248 225 ALEALEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDEL 289
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
1-320 |
5.31e-98 |
|
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: 292.96 E-value: 5.31e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 1 MRYQKLGNTGLFVSRLCLGT-MTFGGeggmwgkigQLRQAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNLK 79
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSwVTFGN---------QVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 80 VPRENVVVATKVFGETGTAGVNSRGSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRYI 159
Cdd:cd19143 72 WPRSDYVVSTKIFWGGGGPPPNDRGLSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 160 GVSNWAAWQIVKALGISARLGLSRFASLQAYYTIAGRD-LERELIPMMQSEGVGLMVWSPLAGGLLSGKYDREGqtAEGG 238
Cdd:cd19143 152 GTSEWSAQQIEEAHEIADRLGLIPPVMEQPQYNLFHRErVEVEYAPLYEKYGLGTTTWSPLASGLLTGKYNNGI--PEGS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 239 R-------RQAFDFPPVNKDRaFDCIDVMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVDI--QL 309
Cdd:cd19143 230 RlalpgyeWLKDRKEELGQEK-IEKVRKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEENLKALEVlpKL 308
|
330
....*....|.
gi 1558667949 310 SEVELAQLDAV 320
Cdd:cd19143 309 TPEVMEKIEAI 319
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
14-303 |
1.92e-88 |
|
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: 265.15 E-value: 1.92e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 14 SRLCLGTMTFGGEGGmwgkigqlrQAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNLKVpRENVVVATKVfG 93
Cdd:cd06660 1 SRLGLGTMTFGGDGD---------EEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRGN-RDDVVIATKG-G 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 94 ETGTAGVNSRGSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRYIGVSNWAAWQIVKAL 173
Cdd:cd06660 70 HPPGGDPSRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 174 GISARLGLSRFASLQAYYTIAGRD-LERELIPMMQSEGVGLMVWSPLAGGLlsgkydregqtaeggrrqafdfppvnkdr 252
Cdd:cd06660 150 AYAKAHGLPGFAAVQPQYSLLDRSpMEEELLDWAEENGLPLLAYSPLARGP----------------------------- 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1558667949 253 afdcidvmrviaeakgvsvAQIALAWLLHQSAVSSVIIGAKRPEQLADNLA 303
Cdd:cd06660 201 -------------------AQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
13-320 |
5.43e-86 |
|
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: 262.50 E-value: 5.43e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 13 VSRLCLGTMTFGGeggmwgkigQLRQAEAEQLVGSALDAGINFIDTADVYS-------EGRSEMLTGQALKNlKVPRENV 85
Cdd:cd19094 1 VSEICLGTMTWGE---------QNTEAEAHEQLDYAFDEGVNFIDTAEMYPvppspetQGRTEEIIGSWLKK-KGNRDKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 86 VVATKVFGETGTAGVNSRGSS---RFHIMESVKESLRRLQLDHIDLYQLH----------GFD--------PATPIEETL 144
Cdd:cd19094 71 VLATKVAGPGEGITWPRGGGTrldRENIREAVEGSLKRLGTDYIDLYQLHwpdrytplfgGGYytepseeeDSVSFEEQL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 145 YALDNLVQQGHVRYIGVSNWAAWQIVKALGISARLGLSRFASLQAYYTIAGRDLERELIPMMQSEGVGLMVWSPLAGGLL 224
Cdd:cd19094 151 EALGELVKAGKIRHIGLSNETPWGVMKFLELAEQLGLPRIVSIQNPYSLLNRNFEEGLAEACHRENVGLLAYSPLAGGVL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 225 SGKYDREGQTAEGGRRQAF--DFPPVNKDRAFDCIDVMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNL 302
Cdd:cd19094 231 TGKYLDGAARPEGGRLNLFpgYMARYRSPQALEAVAEYVKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLKENI 310
|
330
....*....|....*...
gi 1558667949 303 AAVDIQLSEVELAQLDAV 320
Cdd:cd19094 311 DAFDVPLSDELLAEIDAV 328
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
3-319 |
2.23e-85 |
|
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: 260.28 E-value: 2.23e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 3 YQKLGNTGLFVSRLCLGTMTFGGegGMWGkiGQLRQAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNLkvpR 82
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTWAIGG--GPWW--GGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKGR---R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 83 ENVVVATK---VFGETGTAGVNSRGSSRFH-------IMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQ 152
Cdd:cd19149 74 DKVVLATKcglRWDREGGSFFFVRDGVTVYknlspesIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 153 QGHVRYIGVSNWAAWQIVKALgisaRLGlsRFASLQAYYTIAGRDLERELIPMMQSEGVGLMVWSPLAGGLLSGKYDREG 232
Cdd:cd19149 154 QGKIRAIGASNVSVEQIKEYV----KAG--QLDIIQEKYSMLDRGIEKELLPYCKKNNIAFQAYSPLEQGLLTGKITPDR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 233 QTAEGGRRQAFD-FPPVNKDRAFDCIDVMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVDIQLSE 311
Cdd:cd19149 228 EFDAGDARSGIPwFSPENREKVLALLEKWKPLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPEQAEENAKAGDIRLSA 307
|
....*...
gi 1558667949 312 VELAQLDA 319
Cdd:cd19149 308 EDIATMRS 315
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
13-321 |
3.10e-85 |
|
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: 259.44 E-value: 3.10e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 13 VSRLCLGTMTFGGeGGMWGKIgqlRQAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNlkvPRENVVVATKVF 92
Cdd:cd19085 1 VSRLGLGCWQFGG-GYWWGDQ---DDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKG---RRDDVVIATKVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 93 GetgtagvnsRGSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRYIGVSNWAAWQIVKA 172
Cdd:cd19085 74 P---------DNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 173 LGisarlgLSRFASLQAYYTIAGRDLERELIPMMQSEGVGLMVWSPLAGGLLSGKYDREGQTAEG-GRRQAFD-FPPVNK 250
Cdd:cd19085 145 LD------AGRIDSNQLPYNLLWRAIEYEILPFCREHGIGVLAYSPLAQGLLTGKFSSAEDFPPGdARTRLFRhFEPGAE 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1558667949 251 DRAFDCIDVMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVDIQLSEVELAQLDAVS 321
Cdd:cd19085 219 EETFEALEKLKEIADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVDLELSPSVLERLDEIS 289
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
2-317 |
2.07e-80 |
|
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: 247.13 E-value: 2.07e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 2 RYQKLGNTGLFVSRLCLGTMtfggegGMWGKIGQLRQAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNlkvP 81
Cdd:cd19076 1 PTRKLGTQGLEVSALGLGCM------GMSAFYGPADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKD---R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 82 RENVVVATKvFGETGTAGVNSRG--SSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRYI 159
Cdd:cd19076 72 RDEVVIATK-FGIVRDPGSGFRGvdGRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 160 GVSNWAAWQIVKALG---ISArlglsrfasLQAYYTIAGRDLERELIPMMQSEGVGLMVWSPLAGGLLSGKYDREGQTAE 236
Cdd:cd19076 151 GLSEASADTIRRAHAvhpITA---------VQSEYSLWTRDIEDEVLPTCRELGIGFVAYSPLGRGFLTGAIKSPEDLPE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 237 G-GRRQAFDFPPVNKDRAFDCIDVMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVDIQLSEVELA 315
Cdd:cd19076 222 DdFRRNNPRFQGENFDKNLKLVEKLEAIAAEKGCTPAQLALAWVLAQGDDIVPIPGTKRIKYLEENVGALDVVLTPEELA 301
|
..
gi 1558667949 316 QL 317
Cdd:cd19076 302 EI 303
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
5-320 |
1.04e-76 |
|
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: 238.09 E-value: 1.04e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 5 KLGNTGLFVSRLCLGTMTFGGEGGMWGkigqLRQAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNLKvpREN 84
Cdd:cd19083 3 KLGKSDIDVNPIGLGTNAVGGHNLYPN----LDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLKEYN--RNE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 85 VVVATK---VFGETGTAGVNSRGSSRfhimESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRYIGV 161
Cdd:cd19083 77 VVIATKgahKFGGDGSVLNNSPEFLR----SAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 162 SNWAAWQIVKALGISArlglsrFASLQAYYTIAGRDLERELIPMMQSEGVGLMVWSPLAGGLLSGKYDREGQTAEGG-RR 240
Cdd:cd19083 153 SNFSLEQLKEANKDGY------VDVLQGEYNLLQREAEEDILPYCVENNISFIPYFPLASGLLAGKYTKDTKFPDNDlRN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 241 QAFDFPPVNKDRAFDCIDVMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVDIQLSEVELAQLDAV 320
Cdd:cd19083 227 DKPLFKGERFSENLDKVDKLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
13-318 |
1.05e-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: 237.51 E-value: 1.05e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 13 VSRLCLGTMTFGGegGMWGKIGQLRQAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNLKvPRENVVVATKVF 92
Cdd:cd19093 2 VSPLGLGTWQWGD--RLWWGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELG-DRDEVVIATKFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 93 GETGTAGVNSrgssrfhIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLY-ALDNLVQQGHVRYIGVSNWAAWQIVK 171
Cdd:cd19093 79 PLPWRLTRRS-------VVKALKASLERLGLDSIDLYQLHWPGPWYSQIEALMdGLADAVEEGLVRAVGVSNYSADQLRR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 172 ALGISARLGLSrFASLQAYYTIAGRDLER-ELIPMMQSEGVGLMVWSPLAGGLLSGKYDREGQtAEGGRRQAFDFPPVNK 250
Cdd:cd19093 152 AHKALKERGVP-LASNQVEYSLLYRDPEQnGLLPACDELGITLIAYSPLAQGLLTGKYSPENP-PPGGRRRLFGRKNLEK 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1558667949 251 DRAFdcIDVMRVIAEAKGVSVAQIALAWLLHQSAVssVIIGAKRPEQLADNLAAVDIQLSEVELAQLD 318
Cdd:cd19093 230 VQPL--LDALEEIAEKYGKTPAQVALNWLIAKGVV--PIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-319 |
8.81e-76 |
|
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: 235.26 E-value: 8.81e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 13 VSRLCLGTMTFGGeGGMWGKIGQLRQAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNLkvpRENVVVATKVF 92
Cdd:cd19102 1 LTTIGLGTWAIGG-GGWGGGWGPQDDRDSIAAIRAALDLGINWIDTAAVYGLGHSEEVVGRALKGL---RDRPIVATKCG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 93 GETGTAGVNSRGSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRYIGVSNWAAWQIVKA 172
Cdd:cd19102 77 LLWDEEGRIRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 173 LGISArlglsrFASLQAYYTIAGRDLERELIPMMQSEGVGLMVWSPLAGGLLSGKYDRE---GQTAEGGRRQAFDFPPVN 249
Cdd:cd19102 157 QAIHP------IASLQPPYSLLRRGIEAEILPFCAEHGIGVIVYSPMQSGLLTGKMTPErvaSLPADDWRRRSPFFQEPN 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 250 KDRAFDCIDVMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVDIQLSEVELAQLDA 319
Cdd:cd19102 231 LARNLALVDALRPIAERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAADLRLTPEELAEIEA 300
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
13-304 |
4.71e-72 |
|
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase YqkF is a founding member of aldo-keto reductase family 11 member C1 (AKR11C1). It may function as oxidoreductase. This family also includes Bacillus halodurans AKR11C1, an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase.
Pssm-ID: 381312 [Multi-domain] Cd Length: 238 Bit Score: 223.51 E-value: 4.71e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 13 VSRLCLGTMTFGGegGMWGKIGQlrqAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNlkvPRENVVVATKVF 92
Cdd:cd19086 3 VSEIGFGTWGLGG--DWWGDVDD---AEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKG---RRDKVVIATKFG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 93 GETGTAGVNSRGSSRFHIMESVKESLRRLQLDHIDLYQLH-GFDPATPIEETLYALDNLVQQGHVRYIGVS---NWAAWQ 168
Cdd:cd19086 75 NRFDGGPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLHnPPDEVLDNDELFEALEKLKQEGKIRAYGVSvgdPEEALA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 169 IVKALGISarlglsrfaSLQAYYTIAGRDLERELIPMMQSEGVGLMVWSPLAGGLLSGKydregqtaeggrrqafdfppv 248
Cdd:cd19086 155 ALRRGGID---------VVQVIYNLLDQRPEEELFPLAEEHGVGVIARVPLASGLLTGK--------------------- 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1558667949 249 nkdrafdcidvmrviaeakgvsVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAA 304
Cdd:cd19086 205 ----------------------LAQAALRFILSHPAVSTVIPGARSPEQVEENAAA 238
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
3-315 |
2.86e-69 |
|
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: 219.05 E-value: 2.86e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 3 YQKLGNTGLFVSRLCLGtmtfggeggMWGKIG-QLRQAEAEQLVGSALDAGINFIDTADVY--SEGRSEMLTGQALK-NL 78
Cdd:cd19089 1 YRRCGRSGLHLPAISLG---------LWHNFGdYTSPEEARELLRTAFDLGITHFDLANNYgpPPGSAEENFGRILKrDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 79 KVPRENVVVATKVfGETGTAGVNSRGSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRY 158
Cdd:cd19089 72 RPYRDELVISTKA-GYGMWPGPYGDGGSRKYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 159 IGVSNWAAWQIVKALGISARLGlSRFASLQAYYTIAGRDLERELIPMMQSEGVGLMVWSPLAGGLLSGKYDREGQTAEGG 238
Cdd:cd19089 151 VGISNYPGAKARRAIALLRELG-VPLIIHQPRYSLLDRWAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKYLNGIPPDSRR 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1558667949 239 RRQAFDFPPVNKDRA-FDCIDVMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVD-IQLSEVELA 315
Cdd:cd19089 230 AAESKFLTEEALTPEkLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAALKnLDFSEEELA 308
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
15-320 |
1.03e-68 |
|
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: 217.42 E-value: 1.03e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 15 RLCLGTMTFGGEGGMWGKigqlrqAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQalknLKVPRENVVVATKVFGe 94
Cdd:cd19075 2 KIILGTMTFGSQGRFTTA------EAAAELLDAFLERGHTEIDTARVYPDGTSEELLGE----LGLGERGFKIDTKANP- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 95 tGTAGVNSRGSsrfhIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRYIGVSNWAAWQIVKALG 174
Cdd:cd19075 71 -GVGGGLSPEN----VRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 175 ISARLGLSRFASLQAYYTIAGRDLERELIPMMQSEGVGLMVWSPLAGGLLSGKYDREGQTAEGGRrqafdFPPVN----- 249
Cdd:cd19075 146 ICKENGWVLPTVYQGMYNAITRQVETELFPCLRKLGIRFYAYSPLAGGFLTGKYKYSEDKAGGGR-----FDPNNalgkl 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 250 ------KDRAFDCIDVMRVIAEAKGVSVAQIALAWLLHQSAVSS-----VIIGAKRPEQLADNLAAVDI-QLSEVELAQL 317
Cdd:cd19075 221 yrdrywKPSYFEALEKVEEAAEKEGISLAEAALRWLYHHSALDGekgdgVILGASSLEQLEENLAALEKgPLPEEVVKAI 300
|
...
gi 1558667949 318 DAV 320
Cdd:cd19075 301 DEA 303
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
10-318 |
1.09e-66 |
|
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: 210.93 E-value: 1.09e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 10 GLFVSRLCLGTMTFGGegGMWGKIGQlRQAEAEQLVGsALDAGINFIDTADVYSEGRSEMLTGQALKnlKVPRENVVVAT 89
Cdd:cd19072 1 GEEVPVLGLGTWGIGG--GMSKDYSD-DKKAIEALRY-AIELGINLIDTAEMYGGGHAEELVGKAIK--GFDREDLFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 90 KVfgetgtagvNSRGSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRYIGVSNWAAWQI 169
Cdd:cd19072 75 KV---------SPDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 170 VKALGISARLGLsrfASLQAYYTIAGRDLERELIPMMQSEGVGLMVWSPLAGGLLSGKYDREgqtaeggrrqafdfppvn 249
Cdd:cd19072 146 EEAQSYLKKGPI---VANQVEYNLFDREEESGLLPYCQKNGIAIIAYSPLEKGKLSNAKGSP------------------ 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1558667949 250 kdrafdcidVMRVIAEAKGVSVAQIALAWLLHQSAVsSVIIGAKRPEQLADNLAAVDIQLSEVELAQLD 318
Cdd:cd19072 205 ---------LLDEIAKKYGKTPAQIALNWLISKPNV-IAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
10-318 |
3.32e-66 |
|
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: 210.94 E-value: 3.32e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 10 GLFVSRLCLGTMtfggegGMWGKIGQ-LRQAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNlkvPRENVVVA 88
Cdd:cd19078 1 GLEVSAIGLGCM------GMSHGYGPpPDKEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKP---FRDQVVIA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 89 TKvFG---ETGTAGVNSRGSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRYIGVSNWA 165
Cdd:cd19078 72 TK-FGfkiDGGKPGPLGLDSRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 166 AWQIVKALGISArlglsrFASLQAYYTIAGRDLERELIPMMQSEGVGLMVWSPLAGGLLSGKYDrEGQTAEGG--RRQAF 243
Cdd:cd19078 151 VETIRRAHAVCP------VTAVQSEYSMMWREPEKEVLPTLEELGIGFVPFSPLGKGFLTGKID-ENTKFDEGddRASLP 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1558667949 244 DFPPVNKDRAFDCIDVMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVDIQLSEVELAQLD 318
Cdd:cd19078 224 RFTPEALEANQALVDLLKEFAEEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAADIELTPEELREIE 298
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
10-320 |
1.31e-64 |
|
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: 206.77 E-value: 1.31e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 10 GLFVSRLCLGTMTFGGEggMWGKIGQlrqAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNLKvPRENVVVAT 89
Cdd:cd19148 1 DLPVSRIALGTWAIGGW--MWGGTDE---KEAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKEYG-KRDRVVIAT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 90 KVFGETGTAGVNSRGSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRYIGVSNWAAWQI 169
Cdd:cd19148 75 KVGLEWDEGGEVVRNSSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSPEQM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 170 vKALGISARLglsrfASLQAYYTIAGRDLERELIPMMQSEGVGLMVWSPLAGGLLSGKYDREGQTAEGGRRQAF-DFPPV 248
Cdd:cd19148 155 -ETFRKVAPL-----HTVQPPYNLFEREIEKDVLPYARKHNIVTLAYGALCRGLLSGKMTKDTKFEGDDLRRTDpKFQEP 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1558667949 249 NKDRAFDCIDVMRVIAEAK-GVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVDIQLSEVELAQLDAV 320
Cdd:cd19148 229 RFSQYLAAVEELDKLAQERyGKSVIHLAVRWLLDQPGVSIALWGARKPEQLDAVDEVFGWSLNDEDMKEIDAI 301
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
2-307 |
1.33e-63 |
|
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: 204.60 E-value: 1.33e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 2 RYQKLGNTGLFVSRLCLGT-MTFGGeggmwgkigQLRQAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNLKV 80
Cdd:cd19141 1 PYRNLGKSGLRVSCLGLGTwVTFGS---------QISDEVAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKGW 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 81 PRENVVVATKVFgeTGTAGVNSRGSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRYIG 160
Cdd:cd19141 72 RRSSYVITTKIF--WGGKAETERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 161 VSNWAAWQIVKALGISARLGLSRFASLQAYYTIAGRD-LERELIPMMQSEGVGLMVWSPLAGGLLSGKYD---------- 229
Cdd:cd19141 150 TSRWSAMEIMEAYSVARQFNLIPPIVEQAEYHLFQREkVEMQLPELFHKIGVGAMTWSPLACGILSGKYDdgvpeysras 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 230 -------REGQTAEGGRRQAfdfppvNKDRAfdcidvMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNL 302
Cdd:cd19141 230 lkgyqwlKEKILSEEGRRQQ------AKLKE------LQIIADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENL 297
|
....*
gi 1558667949 303 AAVDI 307
Cdd:cd19141 298 QAIQV 302
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
1-310 |
1.55e-63 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 203.84 E-value: 1.55e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 1 MRYQKLGNTGLFVSRLCLGTMTFGGEggmwgkigQLRQAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNLKV 80
Cdd:COG4989 1 MKRIKLGASGLSVSRIVLGCMRLGEW--------DLSPAEAAALIEAALELGITTFDHADIYGGYTCEALFGEALKLSPS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 81 PRENVVVATK---VF-GETGTAGVNSRGSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHV 156
Cdd:COG4989 73 LREKIELQTKcgiRLpSEARDNRVKHYDTSKEHIIASVEGSLRRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELKASGKV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 157 RYIGVSNWAAWQIvkALgISARLGLSRFA-----SLQAYYTIAGRDLErelipMMQSEGVGLMVWSPLAGGLLSGkydre 231
Cdd:COG4989 153 RHFGVSNFTPSQF--EL-LQSALDQPLVTnqielSLLHTDAFDDGTLD-----YCQLNGITPMAWSPLAGGRLFG----- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 232 GQTAeggrrqafDFPPVNKdrafdcidVMRVIAEAKGVSVAQIALAWLL-HQSAVsSVIIGAKRPEQLADNLAAVDIQLS 310
Cdd:COG4989 220 GFDE--------QFPRLRA--------ALDELAEKYGVSPEAIALAWLLrHPAGI-QPVIGTTNPERIKAAAAALDIELT 282
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
10-320 |
1.72e-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: 204.58 E-value: 1.72e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 10 GLFVSRLCLGTMTFGG--EGGMwgkiGQLRQAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNLKVpRENVVV 87
Cdd:cd19146 8 GVRVSPLCLGAMSFGEawKSMM----GECDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMASRGN-RDEMVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 88 ATK-VFGETGTAG----VNSRGSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRYIGVS 162
Cdd:cd19146 83 ATKyTTGYRRGGPikikSNYQGNHAKSLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 163 NWAAWQIVKALGISARLGLSRFASLQAYYTIAGRDLERELIPMMQSEGVGLMVWsplaGGLLSGKYDREGQTAEGGRRQA 242
Cdd:cd19146 163 DTPAWVVSKANAYARAHGLTQFVVYQGHWSAAFRDFERDILPMCEAEGMALAPW----GVLGQGQFRTEEEFKRRGRSGR 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1558667949 243 FDFPPVNKDRAFDciDVMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVDIQLSEVELAQLDAV 320
Cdd:cd19146 239 KGGPQTEKERKVS--EKLEKVAEEKGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIEALGISLSDEEIQEIEDA 314
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
1-315 |
3.17e-60 |
|
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: 195.08 E-value: 3.17e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 1 MRYQKLGNTGLFVSRLCLGTMTFGGEggmwgkIGQLRQAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNlkV 80
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGASPLGGV------FGPVDEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKALKG--I 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 81 PRENVVVATKVfGETGTAGVNSRGSSRFHIMESVKESLRRLQLDHIDLYQLHG--FDPATP--IEETLYALDNLVQQGHV 156
Cdd:cd19163 73 PRDSYYLATKV-GRYGLDPDKMFDFSAERITKSVEESLKRLGLDYIDIIQVHDieFAPSLDqiLNETLPALQKLKEEGKV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 157 RYIGVSNWaawqivkALGISARLgLSRFA----SLQAY--YTIAGRDLErELIPMMQSEGVGLMVWSPLAGGLLSgkydr 230
Cdd:cd19163 152 RFIGITGY-------PLDVLKEV-LERSPvkidTVLSYchYTLNDTSLL-ELLPFFKEKGVGVINASPLSMGLLT----- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 231 egqtaEGGrrqAFDFPPVN---KDRAFDCIDvmrvIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVDI 307
Cdd:cd19163 218 -----ERG---PPDWHPASpeiKEACAKAAA----YCKSRGVDISKLALQFALSNPDIATTLVGTASPENLRKNLEAAEE 285
|
....*...
gi 1558667949 308 QLSEVELA 315
Cdd:cd19163 286 PLDAHLLA 293
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
14-306 |
2.51e-59 |
|
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: 192.77 E-value: 2.51e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 14 SRLCLGTMTFGGeggmwgkigQLRQAEAEQLVGSALDAGINFIDTADVYS----EGRSEMLTGQALKNLKVpRENVVVAT 89
Cdd:cd19082 1 SRIVLGTADFGT---------RIDEEEAFALLDAFVELGGNFIDTARVYGdwveRGASERVIGEWLKSRGN-RDKVVIAT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 90 KvfGetGTAGVNSRGSSRFH---IMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRYIGVSNWAA 166
Cdd:cd19082 71 K--G--GHPDLEDMSRSRLSpedIRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNWST 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 167 WQIVKALGISARLGLSRFASLQAYYTIAGRDLER----ELIPMMQSE-------GVGLMVWSPLAGGLLSGKYDREGQTA 235
Cdd:cd19082 147 ERIAEANAYAKAHGLPGFAASSPQWSLARPNEPPwpgpTLVAMDEEMrawheenQLPVFAYSSQARGFFSKRAAGGAEDD 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1558667949 236 EGGRRqAFDFpPVNKDRAfdciDVMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVD 306
Cdd:cd19082 227 SELRR-VYYS-EENFERL----ERAKELAEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAAAD 291
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
1-320 |
5.41e-59 |
|
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: 193.28 E-value: 5.41e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 1 MRYQKLGNTGLFVSRLCLGT-MTFGGeggmwgkigQLRQAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNLK 79
Cdd:cd19160 3 MKYRNLGKSGLRVSCLGLGTwVTFGS---------QISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 80 VPRENVVVATKVFgeTGTAGVNSRGSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRYI 159
Cdd:cd19160 74 WRRSSYVVTTKIY--WGGQAETERGLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 160 GVSNWAAWQIVKALGISARLGLSRFASLQAYYTIAGRD-LERELIPMMQSEGVGLMVWSPLAGGLLSGKYD--------- 229
Cdd:cd19160 152 GTSRWSAMEIMEAYSVARQFNLIPPVCEQAEYHLFQREkVEMQLPELYHKIGVGSVTWSPLACGLITGKYDgrvpdtcra 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 230 ---------REGQTAEGGRRQAFdfppvnkdrafdcIDVMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLAD 300
Cdd:cd19160 232 avkgyqwlkEKVQSEEGKKQQAK-------------VKELHPIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIE 298
|
330 340
....*....|....*....|..
gi 1558667949 301 NLAAVDI--QLSEVELAQLDAV 320
Cdd:cd19160 299 NLGSIQVlsQLTPQTVMEIDAL 320
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-306 |
1.55e-58 |
|
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: 190.62 E-value: 1.55e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 14 SRLCLGTMTFGGeggmwgkigQLRQAEAEQLVGSALDAGINFIDTADVYSE-------GRSEMLTGQALKNLKVpRENVV 86
Cdd:cd19752 1 SELCLGTMYFGT---------RTDEETSFAILDRYVAAGGNFLDTANNYAFwteggvgGESERLIGRWLKDRGN-RDDVV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 87 VATKV---FGETGTAGVNSRGSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRYIGVSN 163
Cdd:cd19752 71 IATKVgagPRDPDGGPESPEGLSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 164 WAAWQIVKALGISARLGLSRFASLQAYYTI----AGRD------LERELIPMMQSEG-VGLMVWSPlaggLLSGKYDREG 232
Cdd:cd19752 151 FAAWRLERARQIARQQGWAEFSAIQQRHSYlrprPGADfgvqriVTDELLDYASSRPdLTLLAYSP----LLSGAYTRPD 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1558667949 233 QTaeggRRQAFDFPPVNKDRAfdcidVMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVD 306
Cdd:cd19752 227 RP----LPEQYDGPDSDARLA-----VLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAALD 291
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
1-307 |
2.85e-58 |
|
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: 191.02 E-value: 2.85e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 1 MRYQKLGNTGLFVSRLCLGT-MTFGGeggmwgkigQLRQAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNLK 79
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTwVTFGG---------QISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 80 VPRENVVVATKVFgeTGTAGVNSRGSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRYI 159
Cdd:cd19159 72 WRRSSLVITTKLY--WGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYW 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 160 GVSNWAAWQIVKALGISARLGLSRFASLQAYYTIAGRD-LERELIPMMQSEGVGLMVWSPLAGGLLSGKYD--------- 229
Cdd:cd19159 150 GTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKYGngvpessra 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 230 --------REGQTAEGGRRQAfdfppvNKDRafdciDVMRvIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADN 301
Cdd:cd19159 230 slkcyqwlKERIVSEEGRKQQ------NKLK-----DLSP-IAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIEN 297
|
....*.
gi 1558667949 302 LAAVDI 307
Cdd:cd19159 298 LGAIQV 303
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
13-310 |
3.74e-57 |
|
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: 185.88 E-value: 3.74e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 13 VSRLCLGTMTFGGEGGmWGkiGQLRQAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNlkvPRENVVVATKVF 92
Cdd:cd19088 1 VSRLGYGAMRLTGPGI-WG--PPADREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHP---YPDDVVIATKGG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 93 GETGTAGVNSRGSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRYIGVSNWAAWQIVKA 172
Cdd:cd19088 75 LVRTGPGWWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 173 LGISarlglsRFASLQAYYTIAGRDLErELIPMMQSEGVGLMVWSPLAGGLLsgkydregqtAEGGRRqafdfppvnkdr 252
Cdd:cd19088 155 RAIV------RIVSVQNRYNLANRDDE-GVLDYCEAAGIAFIPWFPLGGGDL----------AQPGGL------------ 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1558667949 253 afdcidvMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVDIQLS 310
Cdd:cd19088 206 -------LAEVAARLGATPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
1-320 |
7.05e-57 |
|
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: 187.60 E-value: 7.05e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 1 MRYQKLGNTGLFVSRLCLGT-MTFGGeggmwgkigQLRQAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNLK 79
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTwVTFGG---------QITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 80 VPRENVVVATKVFgeTGTAGVNSRGSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRYI 159
Cdd:cd19158 72 WRRSSLVITTKIF--WGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYW 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 160 GVSNWAAWQIVKALGISARLGLSRFASLQAYYTIAGRD-LERELIPMMQSEGVGLMVWSPLAGGLLSGKYD--------- 229
Cdd:cd19158 150 GTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDsgippysra 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 230 --------REGQTAEGGRRQAFDfppvnkdrafdcIDVMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADN 301
Cdd:cd19158 230 slkgyqwlKDKILSEEGRRQQAK------------LKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMEN 297
|
330 340
....*....|....*....|.
gi 1558667949 302 LAAVDI--QLSEVELAQLDAV 320
Cdd:cd19158 298 IGAIQVlpKLSSSIVHEIDSI 318
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
8-310 |
3.10e-56 |
|
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: 184.68 E-value: 3.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 8 NTGLFVSRLCLGTMTFGGeggMWGKIgqlrqAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNLKVPRENVVV 87
Cdd:cd19092 1 PEGLEVSRLVLGCMRLAD---WGESA-----EELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPGLREKIEI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 88 ATK---VFG-ETGTAGVNSRGSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRYIGVSN 163
Cdd:cd19092 73 QTKcgiRLGdDPRPGRIKHYDTSKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 164 WAAWQIvKALgiSARLGLSRFA-----SLQAYYTIAGRDLErelipMMQSEGVGLMVWSPLAGGLLSGkydregqtaegg 238
Cdd:cd19092 153 FTPSQI-ELL--QSYLDQPLVTnqielSLLHTEAIDDGTLD-----YCQLLDITPMAWSPLGGGRLFG------------ 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1558667949 239 rrqafdfppVNKDRAFDCIDVMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVDIQLS 310
Cdd:cd19092 213 ---------GFDERFQRLRAALEELAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALDIELT 275
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
5-317 |
2.31e-55 |
|
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: 183.41 E-value: 2.31e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 5 KLGNTGLFVSRLCLGTMtfgGEGGMWGkiGQLRQAEAEQLVGSALDAGINFIDTADVYseGRSEMLTGQALKNLKVPREN 84
Cdd:cd19144 5 TLGRNGPSVPALGFGAM---GLSAFYG--PPKPDEERFAVLDAAFELGCTFWDTADIY--GDSEELIGRWFKQNPGKREK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 85 VVVATKVFGE-TGTAGVNSRGSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRYIGVSN 163
Cdd:cd19144 78 IFLATKFGIEkNVETGEYSVDGSPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 164 WAAWQIVKALGISArlglsrFASLQAYYTIAGRDLERELIPMMQS---EGVGLMVWSPLAGGLLSGKYDREGQTAEGG-R 239
Cdd:cd19144 158 CSAETLRRAHAVHP------IAAVQIEYSPFSLDIERPEIGVLDTcreLGVAIVAYSPLGRGFLTGAIRSPDDFEEGDfR 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1558667949 240 RQAFDFPPVNKDRAFDCIDVMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVDIQLSEVELAQL 317
Cdd:cd19144 232 RMAPRFQAENFPKNLELVDKIKAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLGALKVKLTEEEEKEI 309
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
3-315 |
7.80e-55 |
|
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: 181.83 E-value: 7.80e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 3 YQKLGNTGLFVSRLCLGtmtfggeggMWGKIGQLRQAE-AEQLVGSALDAGINFIDTADVYSE--GRSEMLTGQALK-NL 78
Cdd:cd19151 2 YNRCGRSGLKLPAISLG---------LWHNFGDVDRYEnSRAMLRRAFDLGITHFDLANNYGPppGSAEENFGRILKeDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 79 KVPRENVVVATKVfGETGTAGVNSRGSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRY 158
Cdd:cd19151 73 KPYRDELIISTKA-GYTMWPGPYGDWGSKKYLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 159 IGVSNWAAWQIVKALGISARLGLSRFASlQAYYTIAGRDLERELIPMMQSEGVGLMVWSPLAGGLLSGKYDReGQTAEGg 238
Cdd:cd19151 152 VGISNYPPEEAREAAAILKDLGTPCLIH-QPKYSMFNRWVEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYLN-GIPEDS- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 239 rRQAFDFPPVNKDRAF-DCIDVMR---VIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVD-IQLSEVE 313
Cdd:cd19151 229 -RAAKGSSFLKPEQITeEKLAKVRrlnEIAQARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALDnREFSEEE 307
|
..
gi 1558667949 314 LA 315
Cdd:cd19151 308 LA 309
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
1-320 |
7.89e-55 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 182.75 E-value: 7.89e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 1 MRYQKLGNTGLFVSRLCLGTMTFGGeggmwgkigQLRQAEAEQLVGSALDAGINFIDTADVY-------SEGRSEMLTGQ 73
Cdd:PRK10625 1 MQYHRIPHSSLEVSTLGLGTMTFGE---------QNSEADAHAQLDYAVAQGINLIDVAEMYpvpprpeTQGLTETYIGN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 74 ALKNlKVPRENVVVATKVFGETGTAGVNSRGS---SRFHIMESVKESLRRLQLDHIDLYQLH------------GFD--- 135
Cdd:PRK10625 72 WLAK-RGSREKLIIASKVSGPSRNNDKGIRPNqalDRKNIREALHDSLKRLQTDYLDLYQVHwpqrptncfgklGYSwtd 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 136 --PATPIEETLYALDNLVQQGHVRYIGVSNWAAWQIVKALGISARLGLSRFASLQAYYTIAGRDLERELIPMMQSEGVGL 213
Cdd:PRK10625 151 saPAVSLLETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEKHDLPRIVTIQNPYSLLNRSFEVGLAEVSQYEGVEL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 214 MVWSPLAGGLLSGKYdREGQTAEGGRRQAFD-FPPVNKDRAFDCIDVMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGA 292
Cdd:PRK10625 231 LAYSCLAFGTLTGKY-LNGAKPAGARNTLFSrFTRYSGEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLLGA 309
|
330 340
....*....|....*....|....*...
gi 1558667949 293 KRPEQLADNLAAVDIQLSEVELAQLDAV 320
Cdd:PRK10625 310 TTMEQLKTNIESLHLTLSEEVLAEIEAV 337
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
1-320 |
8.46e-55 |
|
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: 182.28 E-value: 8.46e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 1 MRYQKLGNTGLFVSRLCLGTmtfggeggmWGKIGQ-LRQAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNLK 79
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGT---------WSTFSTaISEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILKKKG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 80 VPRENVVVATKVFGETGTAGvnsRGSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRYI 159
Cdd:cd19142 72 WKRSSYIVSTKIYWSYGSEE---RGLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYW 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 160 GVSNWAAWQIVKALGISARLGLSRFASLQAYYTIAGRD-LERELIPMMQSEGVGLMVWSPLAGGLLSGKYDREGQTAEGG 238
Cdd:cd19142 149 GTSRWSPVEIMEAFSIARQFNCPTPICEQSEYHMFCREkMELYMPELYNKVGVGLITWSPLSLGLDPGISEETRRLVTKL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 239 RRQAFDFPPVNKD--------RAFDCIDVMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVDI--Q 308
Cdd:cd19142 229 SFKSSKYKVGSDGngiheetrRASHKLRELSLIAERLGCDLTQLLIAWSLKNENVQCVLIGASSLEQLYSQLNSLQLlpK 308
|
330
....*....|..
gi 1558667949 309 LSEVELAQLDAV 320
Cdd:cd19142 309 LNSAVMEELERI 320
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
5-317 |
9.09e-55 |
|
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: 181.48 E-value: 9.09e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 5 KLGNTGLFVSRLCLGTMtfggegGMWGKIGQLR-QAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNLkvPRE 83
Cdd:cd19145 4 KLGSQGLEVSAQGLGCM------GLSGDYGAPKpEEEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALKDG--PRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 84 NVVVATKvFG--ETGTAGVNSRGSSRFhIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRYIGV 161
Cdd:cd19145 76 KVQLATK-FGihEIGGSGVEVRGDPAY-VRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 162 SNWAAWQIVKALGISArlglsrFASLQAYYTIAGRDLERELIPMMQSEGVGLMVWSPLAGGLLSGKYDREGQTAEGGRRQ 241
Cdd:cd19145 154 SEASADTIRRAHAVHP------ITAVQLEWSLWTRDIEEEIIPTCRELGIGIVPYSPLGRGFFAGKAKLEELLENSDVRK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 242 AFD-FPPVNKDR---AFDCIDVMrviAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVDIQLSEVELAQL 317
Cdd:cd19145 228 SHPrFQGENLEKnkvLYERVEAL---AKKKGCTPAQLALAWVLHQGEDVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
14-304 |
1.93e-54 |
|
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: 178.97 E-value: 1.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 14 SRLCLGTMTFGGeggMWGKIgqlRQAEAEQLVGSALDAGINFIDTADVYseGRSEMLTGQALKNLkvPRENVVVATKVfG 93
Cdd:cd19095 1 SVLGLGTSGIGR---VWGVP---SEAEAARLLNTALDLGINLIDTAPAY--GRSEERLGRALAGL--RRDDLFIATKV-G 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 94 ETGTAGVNSRGSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRYIGVSNwaawqivKAL 173
Cdd:cd19095 70 THGEGGRDRKDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVSG-------DGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 174 GISARLGLSRFASLQAYYTIAGRDlERELIPMMQSEGVGLMVWSPLAGGLLSGKYDREGQTAEGGRRQAFDfppvnkdra 253
Cdd:cd19095 143 ELEAAIASGVFDVVQLPYNVLDRE-EEELLPLAAEAGLGVIVNRPLANGRLRRRVRRRPLYADYARRPEFA--------- 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1558667949 254 fdcidvmrviAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAA 304
Cdd:cd19095 213 ----------AEIGGATWAQAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
10-318 |
5.06e-54 |
|
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: 180.02 E-value: 5.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 10 GLFVSRLCLGTMTFGGEggmW-GKIGQLRQAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNLKVpRENVVVA 88
Cdd:cd19147 7 GIRVSPLILGAMSIGDA---WsGFMGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRKN-RDQIVIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 89 TKV------FGETGTAGVNSRGSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRYIGVS 162
Cdd:cd19147 83 TKFttdykaYEVGKGKAVNYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 163 NWAAWqIVKALGISARL-GLSRFASLQAYYTIAGRDLERELIPMMQSEGVGLMVWSPLAGGLLSGKYDREGQTAEGGRRQ 241
Cdd:cd19147 163 DTPAW-VVSAANYYATAhGKTPFSVYQGRWNVLNRDFERDIIPMARHFGMALAPWDVLGGGKFQSKKAVEERKKNGEGLR 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1558667949 242 AFDFPPVNKDRAFDCIDVMRVIAEAKGV-SVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVDIQLSEVELAQLD 318
Cdd:cd19147 242 SFVGGTEQTPEEVKISEALEKVAEEHGTeSVTAIALAYVRSKAPNVFPLVGGRKIEHLKDNIEALSIKLTPEEIEYLE 319
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
35-319 |
6.52e-52 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 172.55 E-value: 6.52e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 35 QLRQAEAEQLVGSALDAGINFIDTADVYsegRSEMLTGQALKNLKVPRENVVVATKVFGEtgtagvnsrGSSRFHIMESV 114
Cdd:COG0656 14 QLPGEEAAAAVRTALEAGYRHIDTAAMY---GNEEGVGEAIAASGVPREELFVTTKVWND---------NHGYDDTLAAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 115 KESLRRLQLDHIDLYQLHGfdPA-TPIEETLYALDNLVQQGHVRYIGVSNWAAWQIVKALGISARlglsRFASLQAYYTI 193
Cdd:COG0656 82 EESLERLGLDYLDLYLIHW--PGpGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETGV----KPAVNQVELHP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 194 AGRdlERELIPMMQSEGVGLMVWSPLA-GGLLSGkydregqtaeggrrqafdfppvnkdrafdciDVMRVIAEAKGVSVA 272
Cdd:COG0656 156 YLQ--QRELLAFCREHGIVVEAYSPLGrGKLLDD-------------------------------PVLAEIAEKHGKTPA 202
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1558667949 273 QIALAWLLHQSAVssVIIGAKRPEQLADNLAAVDIQLSEVELAQLDA 319
Cdd:COG0656 203 QVVLRWHLQRGVV--VIPKSVTPERIRENLDAFDFELSDEDMAAIDA 247
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
1-320 |
1.38e-51 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 175.01 E-value: 1.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 1 MRYQKLGNTGLFVSRLCLGTMtfggeggmwgKIGQLRQAEAEQLVGSALDAGINFIDTADVYseGRSEMLTGQALKNlkv 80
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGM----------RLPRKDEEEAEALIRRAIDNGINYIDTARGY--GDSEEFLGKALKG--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 81 PRENVVVATKVfgetgTAGVNSRGSSRFHImesvKESLRRLQLDHIDLYQLHGFDPATPIEETLY------ALDNLVQQG 154
Cdd:COG1453 66 PRDKVILATKL-----PPWVRDPEDMRKDL----EESLKRLQTDYIDLYLIHGLNTEEDLEKVLKpggaleALEKAKAEG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 155 HVRYIGVSNWAAWQIVKALgisARLGLSRFASLQAYYTIAGRDLERELIPMMQSEGVGLMVWSPLAGGLLsgkydregqt 234
Cdd:COG1453 137 KIRHIGFSTHGSLEVIKEA---IDTGDFDFVQLQYNYLDQDNQAGEEALEAAAEKGIGVIIMKPLKGGRL---------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 235 aeggrrqaFDFPPVNKDRAfdcidvmrviaeAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVD--IQLSEV 312
Cdd:COG1453 204 --------ANPPEKLVELL------------CPPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENLKTADnlEPLTEE 263
|
....*...
gi 1558667949 313 ELAQLDAV 320
Cdd:COG1453 264 ELAILERL 271
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-305 |
4.50e-50 |
|
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: 167.38 E-value: 4.50e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 1 MRYQKLGNTGLFVSRLCLGTMTFGGEggmwgkigqlrqaeAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKnlKV 80
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFGGGGLPRE--------------SPELLRRALDLGINYFDTAEGYGNGNSEEIIGEALK--GL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 81 PRENVVVATKVfgetgtaGVNSRGSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPI---EETLYALDNLVQQGHVR 157
Cdd:cd19105 65 RRDKVFLATKA-------SPRLDKKDKAELLKSVEESLKRLQTDYIDIYQLHGVDTPEERllnEELLEALEKLKKEGKVR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 158 YIGVS---NWAAWqiVKALgisARLGlsRFASLQAYYTIAGR-DLERELIPMMQSEGVGLMVWSPLAGGLLSGKYDREGQ 233
Cdd:cd19105 138 FIGFSthdNMAEV--LQAA---IESG--WFDVIMVAYNFLNQpAELEEALAAAAEKGIGVVAMKTLAGGYLQPALLSVLK 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1558667949 234 taeggrrqafdfppvnkdrafdcidvmrviaeAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAV 305
Cdd:cd19105 211 --------------------------------AKGFSLPQAALKWVLSNPRVDTVVPGMRNFAELEENLAAA 250
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
9-318 |
5.83e-50 |
|
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: 167.81 E-value: 5.83e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 9 TGLFVSRLCLGTmtfggeggmWGkIGQLRQAEAEQL--VGSALDAGINFIDTADVYSEGRSEMLTGQALKNlkvPRENVV 86
Cdd:cd19138 7 DGTKVPALGQGT---------WY-MGEDPAKRAQEIeaLRAGIDLGMTLIDTAEMYGDGGSEELVGEAIRG---RRDKVF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 87 VATKVFgetgtagvnSRGSSRFHIMESVKESLRRLQLDHIDLYQLHgFDPATPIEETLYALDNLVQQGHVRYIGVSNWAA 166
Cdd:cd19138 74 LVSKVL---------PSNASRQGTVRACERSLRRLGTDYLDLYLLH-WRGGVPLAETVAAMEELKKEGKIRAWGVSNFDT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 167 WQIVKALGIsarLGLSRFASLQAYYTIAGRDLERELIPMMQSEGVGLMVWSPLA-GGLLsgkydregqtaeggRRQAFDF 245
Cdd:cd19138 144 DDMEELWAV---PGGGNCAANQVLYNLGSRGIEYDLLPWCREHGVPVMAYSPLAqGGLL--------------RRGLLEN 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1558667949 246 PPVNKdrafdcidvmrvIAEAKGVSVAQIALAWLLHQSAVSSvIIGAKRPEQLADNLAAVDIQLSEVELAQLD 318
Cdd:cd19138 207 PTLKE------------IAARHGATPAQVALAWVLRDGNVIA-IPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
14-311 |
4.74e-48 |
|
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: 163.11 E-value: 4.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 14 SRLCLGTMTFGGeggMWGKIGQlrqAEAEQLVGSALDAGINFIDTADVYseGRSEMLTGQALKnlKVPRENVVVATKVfg 93
Cdd:cd19090 1 SALGLGTAGLGG---VFGGVDD---DEAVATIRAALDLGINYIDTAPAY--GDSEERLGLALA--ELPREPLVLSTKV-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 94 etgtaGVNSRGS---SRFHIMESVKESLRRLQLDHIDLYQLH-----GFDPATPIEETLYALDNLVQQGHVRYIGVSNW- 164
Cdd:cd19090 69 -----GRLPEDTadySADRVRRSVEESLERLGRDRIDLLMIHdpervPWVDILAPGGALEALLELKEEGLIKHIGLGGGp 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 165 --AAWQIVKALGISARLGLSRfaslqayYTIAGRDLERELIPMMQSEGVGLMVWSPLAGGLLSGKYDREGQTAEGgrrqa 242
Cdd:cd19090 144 pdLLRRAIETGDFDVVLTANR-------YTLLDQSAADELLPAAARHGVGVINASPLGMGLLAGRPPERVRYTYR----- 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1558667949 243 fDFPPVNKDRAFDcidvMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVDIQLSE 311
Cdd:cd19090 212 -WLSPELLDRAKR----LYELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAAEGPLPE 275
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
1-318 |
1.20e-47 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 164.01 E-value: 1.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 1 MRYQKLGNTGLFVSRLCLGtmtfggeggMWGKIGQLRQAEAEQ-LVGSALDAGINFIDTADVYS--EGRSEMLTGQALK- 76
Cdd:PRK09912 13 MQYRYCGKSGLRLPALSLG---------LWHNFGHVNALESQRaILRKAFDLGITHFDLANNYGppPGSAEENFGRLLRe 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 77 NLKVPRENVVVATKVfGETGTAGVNSRGSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHV 156
Cdd:PRK09912 84 DFAAYRDELIISTKA-GYDMWPGPYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 157 RYIGVSNWAAWQIVKALGISARLGLSRFASlQAYYTIAGRDLERE-LIPMMQSEGVGLMVWSPLAGGLLSGKY------- 228
Cdd:PRK09912 163 LYVGISSYSPERTQKMVELLREWKIPLLIH-QPSYNLLNRWVDKSgLLDTLQNNGVGCIAFTPLAQGLLTGKYlngipqd 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 229 ---DREGQTAEGGRRQAFDFPPVNKDRafdcidVMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAV 305
Cdd:PRK09912 242 srmHREGNKVRGLTPKMLTEANLNSLR------LLNEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQAL 315
|
330
....*....|....
gi 1558667949 306 -DIQLSEVELAQLD 318
Cdd:PRK09912 316 nNLTFSTEELAQID 329
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
3-315 |
1.58e-47 |
|
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: 162.62 E-value: 1.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 3 YQKLGNTGLFVSRLCLGtmtfggeggMWGKIGQLRQAEAEQ-LVGSALDAGINFIDTADVYSE--GRSEMLTGQALK-NL 78
Cdd:cd19150 2 YRRCGKSGLKLPALSLG---------LWHNFGDDTPLETQRaILRTAFDLGITHFDLANNYGPppGSAEENFGRILReDF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 79 KVPRENVVVATKVfGETGTAGVNSRGSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRY 158
Cdd:cd19150 73 AGYRDELIISTKA-GYDMWPGPYGEWGSRKYLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 159 IGVSNWAAWQIVKALGISARLGLSRFASlQAYYTIAGRDLER-ELIPMMQSEGVGLMVWSPLAGGLLSGKY-------DR 230
Cdd:cd19150 152 VGISSYSPERTREAAAILRELGTPLLIH-QPSYNMLNRWVEEsGLLDTLQELGVGCIAFTPLAQGLLTDKYlngipegSR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 231 EGQtaEGGRRQAFdfppvNKDRAFDCIDVMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVD-IQL 309
Cdd:cd19150 231 ASK--ERSLSPKM-----LTEANLNSIRALNEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGALDnLTF 303
|
....*.
gi 1558667949 310 SEVELA 315
Cdd:cd19150 304 SADELA 309
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
2-320 |
2.83e-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: 159.74 E-value: 2.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 2 RYQKLGNTGLFVSRLCLGTmtfGGEGGMWGKIgqlRQAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNLkvp 81
Cdd:cd19104 1 KYRRFGRTGLKVSELTFGG---GGIGGLMGRT---TREEQIAAVRRALDLGINFFDTAPSYGDGKSEENLGRALKGL--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 82 RENVVVATKVfgETGTAGVNSRGSsrfHIMESVKESLRRLQLDHIDLYQLH---------GFDPATPIEETLY------A 146
Cdd:cd19104 72 PAGPYITTKV--RLDPDDLGDIGG---QIERSVEKSLKRLKRDSVDLLQLHnrigderdkPVGGTLSTTDVLGlggvadA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 147 LDNLVQQGHVRYIGVSNWAAWQIVKALGISArlglsRFASLQAYYT-----------IAGRDLE-RELIPMMQSEGVGLM 214
Cdd:cd19104 147 FERLRSEGKIRFIGITGLGNPPAIRELLDSG-----KFDAVQVYYNllnpsaaearpRGWSAQDyGGIIDAAAEHGVGVM 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 215 VWSPLAGGLLSGKYDR-EGQTAEGGRRQAFDFppvnkDRAfdciDVMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAK 293
Cdd:cd19104 222 GIRVLAAGALTTSLDRgREAPPTSDSDVAIDF-----RRA----AAFRALAREWGETLAQLAHRFALSNPGVSTVLVGVK 292
|
330 340
....*....|....*....|....*...
gi 1558667949 294 RPEQLADNLAAVDI-QLSEVELAQLDAV 320
Cdd:cd19104 293 NREELEEAVAAEAAgPLPAENLARLEAL 320
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
3-303 |
2.99e-44 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 151.87 E-value: 2.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 3 YQKLGNTGLFVSRLCLGTMTfggeggmwgkIGQLRQAEAEQLVGSALDAGINFIDTADVYseGRSEMLTGQALKNlkvPR 82
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGP----------LGRLSQEEAAAIIRRALDLGINYFDTAPSY--GDSEEKIGKALKG---RR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 83 ENVVVATKvfgetgTAGVNSRGssrfhIMESVKESLRRLQLDHIDLYQLHG----FDPATPIEE--TLYALDNLVQQGHV 156
Cdd:cd19100 66 DKVFLATK------TGARDYEG-----AKRDLERSLKRLGTDYIDLYQLHAvdteEDLDQVFGPggALEALLEAKEEGKI 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 157 RYIGVS--NWAAwqIVKALgisaRLGLsrFASLQAYYTIAGR---DLERELIPMMQSEGVGLMVWSPLAGGLLsgkydre 231
Cdd:cd19100 135 RFIGISghSPEV--LLRAL----ETGE--FDVVLFPINPAGDhidSFREELLPLAREKGVGVIAMKVLAGGRL------- 199
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1558667949 232 gqtaeggrrqafdfppvnkdrafdcidvmrviAEAKGVSVAQiALAWLLHQSAVSSVIIGAKRPEQLADNLA 303
Cdd:cd19100 200 --------------------------------LSGDPLDPEQ-ALRYALSLPPVDVVIVGMDSPEELDENLA 238
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
9-318 |
7.36e-43 |
|
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: 150.47 E-value: 7.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 9 TGLFVSRLCLGTMtfggegGMWGKIGQLRQAEAEQLVGSALDAGINFIDTADVYSegrsemlTGQALKNL--------KV 80
Cdd:cd19077 1 NGKLVGPIGLGLM------GLTWRPNPTPDEEAFETMKAALDAGSNLWNGGEFYG-------PPDPHANLkllarffrKY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 81 P--RENVVVATKVFGETGTAGVnsrGSSRFHIMESVKESLRRL-QLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVR 157
Cdd:cd19077 68 PeyADKVVLSVKGGLDPDTLRP---DGSPEAVRKSIENILRALgGTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 158 YIGVSNWAAWQIVKALGIsarlglSRFASLQAYYTIAGRD-LERELIPMMQSEGVGLMVWSPLAGGLLSGKYDREGQTAE 236
Cdd:cd19077 145 GIGLSEVSAETIRRAHAV------HPIAAVEVEYSLFSREiEENGVLETCAELGIPIIAYSPLGRGLLTGRIKSLADIPE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 237 GGRRQAFD-FPPVNKDRAFDCIDVMRVIAEAKGVSVAQIALAWLLHQSavSSVII---GAKRPEQLADNLAAVDIQLSEV 312
Cdd:cd19077 219 GDFRRHLDrFNGENFEKNLKLVDALQELAEKKGCTPAQLALAWILAQS--GPKIIpipGSTTLERVEENLKAANVELTDE 296
|
....*.
gi 1558667949 313 ELAQLD 318
Cdd:cd19077 297 ELKEIN 302
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
28-318 |
7.53e-43 |
|
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: 149.26 E-value: 7.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 28 GMWGKIGQL-----RQAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNLkvPRENVVVATKVFGETgtagvns 102
Cdd:cd19137 10 GTWGIGGFLtpdysRDEEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKDF--PREDLFIVTKVWPTN------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 103 rgSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRYIGVSNWAAWQIVKALGISArlglS 182
Cdd:cd19137 81 --LRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQ----T 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 183 RFASLQAYYTIAGRDLERE-LIPMMQSEGVGLMVWSPLAGGLLsgkydregqtaeggrrqafdfpPVNkdrafdciDVMR 261
Cdd:cd19137 155 PIVCNQVKYNLEDRDPERDgLLEYCQKNGITVVAYSPLRRGLE----------------------KTN--------RTLE 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1558667949 262 VIAEAKGVSVAQIALAWLLHQSAVSSvIIGAKRPEQLADNLAAVDIQLSEVELAQLD 318
Cdd:cd19137 205 EIAKNYGKTIAQIALAWLIQKPNVVA-IPKAGRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
28-318 |
6.66e-42 |
|
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: 146.26 E-value: 6.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 28 GMWgkigQLRQAEAEQLVGSALDAGINFIDTADVYSegrSEMLTGQALKNLKVPRENVVVATKVFgetgtagvnsrgSSR 107
Cdd:cd19073 7 GTW----QLRGDDCANAVKEALELGYRHIDTAEIYN---NEAEVGEAIAESGVPREDLFITTKVW------------RDH 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 108 FH---IMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRYIGVSNWAAWQIVKALGISARLglsrF 184
Cdd:cd19073 68 LRpedLKKSVDRSLEKLGTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPLP----I 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 185 ASLQAYYTIAGRdlERELIPMMQSEGVGLMVWSPLAggllsgkydregqtaeggRRQAFDFPPVnkdrafdcidvmRVIA 264
Cdd:cd19073 144 AVNQVEFHPFLY--QAELLEYCRENDIVITAYSPLA------------------RGEVLRDPVI------------QEIA 191
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1558667949 265 EAKGVSVAQIALAWLLHQSAVssVIIGAKRPEQLADNLAAVDIQLSEVELAQLD 318
Cdd:cd19073 192 EKYDKTPAQVALRWLVQKGIV--VIPKASSEDHLKENLAIFDWELTSEDVAKID 243
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
28-318 |
4.53e-41 |
|
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. The family includes AKR1A/B/C/D/E/G/I, AKR2A/B/C/D/E, AKR3A/B/C/D/E/G, AKR4A/B/C, AKR5A/B/C/D/E/F/G/H, and similar proteins.
Pssm-ID: 381297 [Multi-domain] Cd Length: 251 Bit Score: 144.16 E-value: 4.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 28 GMWgkigQLRQAEAEQLVGSALDAGINFIDTADVYsegRSEMLTGQALKNLKVPRENVVVATKVfgetgtagvNSRGSSR 107
Cdd:cd19071 7 GTY----KLKPEETAEAVLAALEAGYRHIDTAAAY---GNEAEVGEAIRESGVPREELFITTKL---------WPTDHGY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 108 FHIMESVKESLRRLQLDHIDLYQLH------GFDPATPIEETLYALDNLVQQGHVRYIGVSNWAAWQIVKalgisarlgL 181
Cdd:cd19071 71 ERVREALEESLKDLGLDYLDLYLIHwpvpgkEGGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEE---------L 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 182 SRFAS-----LQAYYTIAGRDleRELIPMMQSEGVGLMVWSPLAggllsgkydregqtaeGGRRQAFDFPPVNKdrafdc 256
Cdd:cd19071 142 LAAARikpavNQIELHPYLQQ--KELVEFCKEHGIVVQAYSPLG----------------RGRRPLLDDPVLKE------ 197
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1558667949 257 idvmrvIAEAKGVSVAQIALAWLLhQSAVsSVIIGAKRPEQLADNLAAVDIQLSEVELAQLD 318
Cdd:cd19071 198 ------IAKKYGKTPAQVLLRWAL-QRGV-VVIPKSSNPERIKENLDVFDFELSEEDMAAID 251
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
18-322 |
2.79e-39 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 140.93 E-value: 2.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 18 LGTMTFG--GEGGMWGKIGQLRQAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNlkVPRENVVVATKvFGET 95
Cdd:cd19103 9 LGTWSWGsgGAGGDQVFGNHLDEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEFLKR--YPREDYIISTK-FTPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 96 GtagvnsRGSSRFHIMESVKESLRRLQLDHIDLYQLHgfDPATPIEETLYALDnLVQQGHVRYIGVSNWAAWQIVKALGI 175
Cdd:cd19103 86 I------AGQSADPVADMLEGSLARLGTDYIDIYWIH--NPADVERWTPELIP-LLKSGKVKHVGVSNHNLAEIKRANEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 176 SARLGLSRFAsLQAYYTIAGRDLERE-LIPMMQSEGVGLMVWSPLAGGLLSGKYDREGQTAEGGRRqAFDFPPVnKDRAF 254
Cdd:cd19103 157 LAKAGVSLSA-VQNHYSLLYRSSEEAgILDYCKENGITFFAYMVLEQGALSGKYDTKHPLPEGSGR-AETYNPL-LPQLE 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1558667949 255 DCIDVMRVIAEAKGVSVAQIALAWLLHQSAVSsvIIGAKRPEQLADNLAAVDIQLSEVELAQLDAVSA 322
Cdd:cd19103 234 ELTAVMAEIGAKHGASIAQVAIAWAIAKGTTP--IIGVTKPHHVEDAARAASITLTDDEIKELEQLAD 299
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
10-319 |
1.94e-37 |
|
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: 134.69 E-value: 1.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 10 GLFVSRLCLGTMtfggeggmwgkigQLRQAEAEQLVGSALDAGINFIDTADVYSegrSEMLTGQALKNLKVPRENVVVAT 89
Cdd:cd19140 5 GVRIPALGLGTY-------------PLTGEECTRAVEHALELGYRHIDTAQMYG---NEAQVGEAIAASGVPRDELFLTT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 90 KVfgetgtaGVNSRGSSRFhiMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLYALDNLVQQGHVRYIGVSNWAAWQI 169
Cdd:cd19140 69 KV-------WPDNYSPDDF--LASVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 170 VKALGISArlglSRFASLQAYY--TIAGRDLE---RELipmmqseGVGLMVWSPLAGGllsgkydregqtaeggrrQAFD 244
Cdd:cd19140 140 REAVELSE----APLFTNQVEYhpYLDQRKLLdaaREH-------GIALTAYSPLARG------------------EVLK 190
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1558667949 245 FPpvnkdrafdcidVMRVIAEAKGVSVAQIALAWLLHQSAVsSVIIGAKRPEQLADNLAAVDIQLSEVELAQLDA 319
Cdd:cd19140 191 DP------------VLQEIGRKHGKTPAQVALRWLLQQEGV-AAIPKATNPERLEENLDIFDFTLSDEEMARIAA 252
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-307 |
9.01e-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: 133.42 E-value: 9.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 14 SRLCLGTMTFGGEGGMWGKIGQLRQAEAEQLVGSALDAGINFIDTADVYseGRSEMLTGQALKNLKvpreNVVVATKVfg 93
Cdd:cd19097 1 SKLALGTAQFGLDYGIANKSGKPSEKEAKKILEYALKAGINTLDTAPAY--GDSEKVLGKFLKRLD----KFKIITKL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 94 etgTAGVNSRGSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLY-ALDNLVQQGHVRYIGVSNWAAWQIVKA 172
Cdd:cd19097 73 ---PPLKEDKKEDEAAIEASVEASLKRLKVDSLDGLLLHNPDDLLKHGGKLVeALLELKKEGLIRKIGVSVYSPEELEKA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 173 LGIsarlglSRFASLQAYYTIAGRDLERE-LIPMMQSEGVGLMVWSPLAGGLLSGKYDRegqtaeggrrqafdfPPVNKD 251
Cdd:cd19097 150 LES------FKIDIIQLPFNILDQRFLKSgLLAKLKKKGIEIHARSVFLQGLLLMEPDK---------------LPAKFA 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1558667949 252 RAFDCIDVMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVDI 307
Cdd:cd19097 209 PAKPLLKKLHELAKKLGLSPLELALGFVLSLPEIDKIVVGVDSLEQLKEIIAAFKK 264
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
14-306 |
7.88e-36 |
|
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: 130.37 E-value: 7.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 14 SRLCLGTMTFGGEGGmwgkiGQLRQAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKnlKVPRENVVVATKVFg 93
Cdd:cd19096 1 SVLGFGTMRLPESDD-----DSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALK--EGPREKFYLATKLP- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 94 etgtagvNSRGSSRFHIMESVKESLRRLQLDHIDLYQLHG-----FDPATPIEETLYALDNLVQQGHVRYIGVSNWAAWQ 168
Cdd:cd19096 73 -------PWSVKSAEDFRRILEESLKRLGVDYIDFYLLHGlnspeWLEKARKGGLLEFLEKAKKEGLIRHIGFSFHDSPE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 169 IVKALgisarLGLSRFASLQAYYTIAGRDLE--RELIPMMQSEGVGLMVWSPLAGGLLsgkydregqtaeggrrqAFDFP 246
Cdd:cd19096 146 LLKEI-----LDSYDFDFVQLQYNYLDQENQagRPGIEYAAKKGMGVIIMEPLKGGGL-----------------ANNPP 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 247 PVNKdrafdcidvmrvIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVD 306
Cdd:cd19096 204 EALA------------ILCGAPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENIAAAD 251
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
14-306 |
2.58e-34 |
|
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: 127.48 E-value: 2.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 14 SRLCLGTMTFGGeggmwgkIGQLRQAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNLkvPRENVVVATKV-- 91
Cdd:cd19162 1 PRLGLGAASLGN-------LARAGEDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALARH--PRAEYVVSTKVgr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 92 ---FGETGTAGVNSR--GSSRFHIMESVKESLRRLQLDHIDLYQLHGFDP--ATPIEETLYALDNLVQQGHVRYIGVS-- 162
Cdd:cd19162 72 llePGAAGRPAGADRrfDFSADGIRRSIEASLERLGLDRLDLVFLHDPDRhlLQALTDAFPALEELRAEGVVGAIGVGvt 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 163 NWAAwqivkALGISARLGLSRFAsLQAYYTIAGRDLERELIPMMQSEGVGLMVWSPLAGGLLSGKyDREGQTAEggRRQA 242
Cdd:cd19162 152 DWAA-----LLRAARRADVDVVM-VAGRYTLLDRRAATELLPLCAAKGVAVVAAGVFNSGILATD-DPAGDRYD--YRPA 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1558667949 243 fdfPPVNKDRAfdciDVMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVD 306
Cdd:cd19162 223 ---TPEVLARA----RRLAAVCRRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLALLR 279
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
3-318 |
3.27e-34 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 127.97 E-value: 3.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 3 YQKLGNTGLFVSrlCLGtmtFGGE--GGMWGKIGQlrqAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNLKV 80
Cdd:PLN02587 1 LRELGSTGLKVS--SVG---FGASplGSVFGPVSE---EDAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKALGI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 81 PRENVVVATKvfgetgtAGVNSRG--SSRFHIMESVKESLRRLQLDHIDLYQLHGFDPAT---PIEETLYALDNLVQQGH 155
Cdd:PLN02587 73 PREKYVVSTK-------CGRYGEGfdFSAERVTKSVDESLARLQLDYVDILHCHDIEFGSldqIVNETIPALQKLKESGK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 156 VRYIGVSNwAAWQIVKALGISARLGLSRFASLQAYYTIAGRDLErELIPMMQSEGVGLMVWSPLAGGLLSGKYDREGQTA 235
Cdd:PLN02587 146 VRFIGITG-LPLAIFTYVLDRVPPGTVDVILSYCHYSLNDSSLE-DLLPYLKSKGVGVISASPLAMGLLTENGPPEWHPA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 236 eggrrqafdfPPVNKDRAFDCIDVMRviaeAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVDiqlsEVELA 315
Cdd:PLN02587 224 ----------PPELKSACAAAATHCK----EKGKNISKLALQYSLSNKDISTTLVGMNSVQQVEENVAAAT----ELETS 285
|
...
gi 1558667949 316 QLD 318
Cdd:PLN02587 286 GID 288
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
28-320 |
4.55e-34 |
|
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: 126.94 E-value: 4.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 28 GMWGKIGQLRQAEaEQLVGSAlDAGINFIDTADVYseGRSEMLTGQALKNLKVPRE---NVVVATKVFGETGTAGVnsrg 104
Cdd:cd19101 14 GGHGGIRDEDAAV-RAMAAYV-DAGLTTFDCADIY--GPAEELIGEFRKRLRRERDaadDVQIHTKWVPDPGELTM---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 105 sSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATP-IEETLYALDNLVQQGHVRYIGVSNWAA---WQIVKAlGIsarlg 180
Cdd:cd19101 86 -TRAYVEAAIDRSLKRLGVDRLDLVQFHWWDYSDPgYLDAAKHLAELQEEGKIRHLGLTNFDTerlREILDA-GV----- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 181 lsRFASLQAYYTIAGRDLERELIPMMQSEGVGLMVWSPLAGGLLSGKYdrEGQtAEGGRRQaFDFPPVNKDRAFdcID-- 258
Cdd:cd19101 159 --PIVSNQVQYSLLDRRPENGMAALCEDHGIKLLAYGTLAGGLLSEKY--LGV-PEPTGPA-LETRSLQKYKLM--IDew 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1558667949 259 -----------VMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVDIQLSEVELAQLDAV 320
Cdd:cd19101 231 ggwdlfqellrTLKAIADKHGVSIANVAVRWVLDQPGVAGVIVGARNSEHIDDNVRAFSFRLDDEDRAAIDAV 303
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
39-319 |
1.04e-33 |
|
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: 124.99 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 39 AEAEQLVGSALDAGINFIDTADVYsegRSEMLTGQALKNLKVPRENVVVATKV----FGETGTagvnsrgssrfhiMESV 114
Cdd:cd19133 23 EECERAVLEAIKAGYRLIDTAAAY---GNEEAVGRAIKKSGIPREELFITTKLwiqdAGYEKA-------------KKAF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 115 KESLRRLQLDHIDLYQLHgfDPATPIEETLYALDNLVQQGHVRYIGVSNWAAWQIVKalgisarlgLSRFAS-------- 186
Cdd:cd19133 87 ERSLKRLGLDYLDLYLIH--QPFGDVYGAWRAMEELYKEGKIRAIGVSNFYPDRLVD---------LILHNEvkpavnqi 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 187 -LQAYYTiagrdlERELIPMMQSEGVGLMVWSPLAggllsgkydregqtaeGGRRQAFDFPpvnkdrafdcidVMRVIAE 265
Cdd:cd19133 156 eTHPFNQ------QIEAVEFLKKYGVQIEAWGPFA----------------EGRNNLFENP------------VLTEIAE 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1558667949 266 AKGVSVAQIALAWLLHQSAVssVIIGAKRPEQLADNLAAVDIQLSEVELAQLDA 319
Cdd:cd19133 202 KYGKSVAQVILRWLIQRGIV--VIPKSVRPERIAENFDIFDFELSDEDMEAIAA 253
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
4-307 |
2.94e-33 |
|
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: 124.96 E-value: 2.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 4 QKLGNTGLFVSRLCLGTMTFGGEGGmwgkiGQLRQAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNLKVPRE 83
Cdd:cd19153 3 ETLEIALGNVSPVGLGTAALGGVYG-----DGLEQDEAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAALQVPRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 84 NVVVATKVfGETGTAGVNsrgSSRFHIMESVKESLRRLQLDHIDLYQLHGF---DPATPIEETLYALDNLVQQGHVRYIG 160
Cdd:cd19153 78 SYTVATKV-GRYRDSEFD---YSAERVRASVATSLERLHTTYLDVVYLHDIefvDYDTLVDEALPALRTLKDEGVIKRIG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 161 VSNWAAWQIVKALgisARLGLSRFASLQAY--YTIAGRDLERELIPMMQSEGVGLMVWSPLAGGLLSGKYDREGQTAEGG 238
Cdd:cd19153 154 IAGYPLDTLTRAT---RRCSPGSLDAVLSYchLTLQDARLESDAPGLVRGAGPHVINASPLSMGLLTSQGPPPWHPASGE 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 239 RRQafdfppvnkdrafdCIDVMRVIAEAKGVSVAQIALAWLL-HQSAVSSVIIGAKRPEQLADNLAAVDI 307
Cdd:cd19153 231 LRH--------------YAAAADAVCASVEASLPDLALQYSLaAHAGVGTVLLGPSSLAQLRSMLAAVDA 286
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
45-319 |
7.16e-32 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 119.77 E-value: 7.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 45 VGSALDAGINFIDTADVYSegrSEMLTGQALKNLKVPRENVVVATKVFGETGTAGvnsrgssrfHIMESVKESLRRLQLD 124
Cdd:cd19139 20 VRTALELGYRHIDTAQIYD---NEAAVGQAIAESGVPRDELFITTKIWIDNLSKD---------KLLPSLEESLEKLRTD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 125 HIDLYQLHGFDP--ATPIEETLYALDNLVQQGHVRYIGVSNWAAWQIVKALGIsarLGLSRFASLQ----AYYTiagrdl 198
Cdd:cd19139 88 YVDLTLIHWPSPndEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAV---VGAGAIATNQielsPYLQ------ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 199 ERELIPMMQSEGVGLMVWSPLAGGllsgkydregqtaeggrrqafdfppvnkdRAFDcIDVMRVIAEAKGVSVAQIALAW 278
Cdd:cd19139 159 NRKLVAHCKQHGIHVTSYMTLAYG-----------------------------KVLD-DPVLAAIAERHGATPAQIALAW 208
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1558667949 279 LLHQSavSSVIIGAKRPEQLADNLAAVDIQLSEVELAQLDA 319
Cdd:cd19139 209 AMARG--YAVIPSSTKREHLRSNLLALDLTLDADDMAAIAA 247
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-303 |
1.18e-31 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 120.89 E-value: 1.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 11 LFVSRLCLGTMTFGGEGGmwgkigqlRQAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNL----KVPRENVV 86
Cdd:cd19099 1 LTLSSLGLGTYRGDSDDE--------TDEEYREALKAALDSGINVIDTAINYRGGRSERLIGKALRELiekgGIKRDEVV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 87 VATKV----------------FGETGTAGVNSR-----GSSRFH---IMESVKESLRRLQLDHIDLYQLH---GFDPATP 139
Cdd:cd19099 73 IVTKAgyipgdgdeplrplkyLEEKLGRGLIDVadsagLRHCISpayLEDQIERSLKRLGLDTIDLYLLHnpeEQLLELG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 140 -------IEETLYALDNLVQQGHVRYIGVSNWAAWQIVKALGISARL------------GLSRFASLQ----------AY 190
Cdd:cd19099 153 eeefydrLEEAFEALEEAVAEGKIRYYGISTWDGFRAPPALPGHLSLeklvaaaeevggDNHHFKVIQlplnllepeaLT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 191 YTIAGRDLERELIPMMQSEGVGLMVWSPLAGGLLSGKydregqtaeggrrqafdfppvnkdrafdcIDVMRVIAEAKGVS 270
Cdd:cd19099 233 EKNTVKGEALSLLEAAKELGLGVIASRPLNQGQLLGE-----------------------------LRLADLLALPGGAT 283
|
330 340 350
....*....|....*....|....*....|...
gi 1558667949 271 VAQIALAWLLHQSAVSSVIIGAKRPEQLADNLA 303
Cdd:cd19099 284 LAQRALQFARSTPGVDSALVGMRRPEHVDENLA 316
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
38-320 |
7.01e-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: 115.02 E-value: 7.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 38 QAEAEQLVGSALDAGINFIDTADVYSegrSEMLTGQALKNLKVPRENVVVATKVFGETGtagvnsrgssrfHIMESVKES 117
Cdd:cd19120 24 QRDLVDSVKLALKAGFRHIDTAEMYG---NEKEVGEALKESGVPREDLFITTKVSPGIK------------DPREALRKS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 118 LRRLQLDHIDLYQLH----GFDPATPIEETLYALDNLVQQGHVRYIGVSNWAAWQIvKALGISARlglsrfaslqayYTI 193
Cdd:cd19120 89 LAKLGVDYVDLYLIHspffAKEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDL-EELLDTAK------------IKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 194 AGRDLE---------RELIPMMQSEGVGLMVWSPLAggllsgkydregqtaeggrrqafdfpPVNKDRAFDCIDVMRVIA 264
Cdd:cd19120 156 AVNQIEfhpylypqqPALLEYCREHGIVVSAYSPLS--------------------------PLTRDAGGPLDPVLEKIA 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1558667949 265 EAKGVSVAQIALAWLLHQSAVssVIIGAKRPEQLADNLAAVDIQLSEVELAQLDAV 320
Cdd:cd19120 210 EKYGVTPAQVLLRWALQKGIV--VVTTSSKEERMKEYLEAFDFELTEEEVEEIDKA 263
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
39-317 |
1.70e-29 |
|
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: 115.12 E-value: 1.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 39 AEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNLkvPRENVVVATKVfgetGTAGVNSRGSSRFH--------- 109
Cdd:cd19161 20 ADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREK--PRDEFVLSTKV----GRLLKPAREGSVPDpngfvdplp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 110 -----------IMESVKESLRRLQLDHIDLYQLHGFDPAT------------PIEETLYALDNLVQQGHVRYIGVS-Nwa 165
Cdd:cd19161 94 feivydysydgIMRSFEDSLQRLGLNRIDILYVHDIGVYThgdrkerhhfaqLMSGGFKALEELKKAGVIKAFGLGvN-- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 166 AWQIVKALGISARLGLsrfASLQAYYTIAGRDLERELIPMMQSEGVGLMVWSPLAGGLLSGKydregqtaeGGRRQAFDF 245
Cdd:cd19161 172 EVQICLEALDEADLDC---FLLAGRYSLLDQSAEEEFLPRCEQRGTSLVIGGVFNSGILATG---------TKSGAKFNY 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1558667949 246 PPVNKDrAFDCIDVMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVDIQLSEVELAQL 317
Cdd:cd19161 240 GDAPAE-IISRVMEIEKICDAYNVPLAAAALQFPLRHPAVASVLTGARNPAQLRQNVEAFQTDIPEELWQAL 310
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
14-305 |
1.11e-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: 1.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 14 SRLCLGTMTFGGeggMWGKIgqlRQAEAEQLVGSALDAGINFIDTADVYSEGRSEMLTGQALKNLkvPRENVVVATKV-- 91
Cdd:cd19152 1 PKLGFGTAPLGN---LYEAV---SDEEAKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALREL--GREDYVISTKVgr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 92 -------FGETGTAGVNSRGSSRFH-------IMESVKESLRRLQLDHIDLYQLHGFDPATPIEETLY-----------A 146
Cdd:cd19152 73 llvplqeVEPTFEPGFWNPLPFDAVfdysydgILRSIEDSLQRLGLSRIDLLSIHDPDEDLAGAESDEhfaqaikgafrA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 147 LDNLVQQGHVRYIGV-SNwaAWQIVKALGISARLGLSRFAslqAYYTIAGRDLERELIPMMQSEGVGLMVWSPLAGGLLS 225
Cdd:cd19152 153 LEELREEGVIKAIGLgVN--DWEVILRILEEADLDWVMLA---GRYTLLDHSAARELLPECEKRGVKVVNAGPFNSGFLA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 226 GkydregqtaeGGRRQAFDFPPVNKDrAFDCIDVMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAV 305
Cdd:cd19152 228 G----------GDNFDYYEYGPAPPE-LIARRDRIEALCEQHGVSLAAAALQFALAPPAVASVAPGASSPERVEENVALL 296
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
1-322 |
2.30e-27 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 108.90 E-value: 2.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 1 MRYQKLGNT----GLFVSRLCLGTMTFGGEGgMWG-------KIGQLRQAEAeqlvgsaldAGINFIDTADVYSEGRSEM 69
Cdd:PRK10376 1 MSTIMSSGTftlgGRSVNRLGYGAMQLAGPG-VFGppkdrdaAIAVLREAVA---------LGVNHIDTSDFYGPHVTNQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 70 LTGQALKnlkvP-RENVVVATKVFGETGTAGVNSRGSSRFHIMESVKESLRRLQLDHIDLYQLH-GFDPATP----IEET 143
Cdd:PRK10376 71 LIREALH----PyPDDLTIVTKVGARRGEDGSWLPAFSPAELRRAVHDNLRNLGLDVLDVVNLRlMGDGHGPaegsIEEP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 144 LYALDNLVQQGHVRYIGVSNWAAWQIVKALGISArlglsrFASLQAYYTIAGRDlERELIPMMQSEGVGLMVWSPLAGgl 223
Cdd:PRK10376 147 LTVLAELQRQGLVRHIGLSNVTPTQVAEARKIAE------IVCVQNHYNLAHRA-DDALIDALARDGIAYVPFFPLGG-- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 224 lsgkydregqtaeggrrqafdFPPVNKdrafdciDVMRVIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLA 303
Cdd:PRK10376 218 ---------------------FTPLQS-------STLSDVAASLGATPMQVALAWLLQRSPNILLIPGTSSVAHLRENLA 269
|
330
....*....|....*....
gi 1558667949 304 AVDIQLSEVELAQLDAVSA 322
Cdd:PRK10376 270 AAELVLSEEVLAELDGIAR 288
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
35-320 |
9.61e-27 |
|
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: 106.56 E-value: 9.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 35 QLR-QAEAEQLVGSALDAGINFIDTADVYsegRSEMLTGQALKNL----KVPRENVVVATKVfgetgtaGVNSRGSSRfh 109
Cdd:cd19136 10 RLRgEEEVRQAVDAALKAGYRLIDTASVY---RNEADIGKALRDLlpkyGLSREDIFITSKL-------APKDQGYEK-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 110 IMESVKESLRRLQLDHIDLYQLH-----GFDPATPIE-----ETLYALDNLVQQGHVRYIGVSNWAawqivkalgisarl 179
Cdd:cd19136 78 ARAACLGSLERLGTDYLDLYLIHwpgvqGLKPSDPRNaelrrESWRALEDLYKEGKLRAIGVSNYT-------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 180 gLSRFASLQAYYTIA---------GRDLERELIPMMQSEGVGLMVWSPLAGGLLSgkydregqtaeggrrqAFDFPPVnk 250
Cdd:cd19136 144 -VRHLEELLKYCEVPpavnqvefhPHLVQKELLKFCKDHGIHLQAYSSLGSGDLR----------------LLEDPTV-- 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 251 drafdcidvmRVIAEAKGVSVAQIALAWLLHQSAvsSVIIGAKRPEQLADNLAAVDIQLSEVELAQLDAV 320
Cdd:cd19136 205 ----------LAIAKKYGRTPAQVLLRWALQQGI--GVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
40-320 |
6.00e-26 |
|
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: 104.06 E-value: 6.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 40 EAEQLVGSALDAGINFIDTADVYsegRSEMLTGQALKNLKVPRENVVVATKVFGETGTAgvnSRGSSRFHimesvkESLR 119
Cdd:cd19126 24 ETERAVQTALENGYRSIDTAAIY---KNEEGVGEAIRESGVPREELFVTTKLWNDDQRA---RRTEDAFQ------ESLD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 120 RLQLDHIDLYQLHgFDPATPIEETLYALDNLVQQGHVRYIGVSNWAAWQIVKALGISARLGLSRFASLQAYYTiagrdlE 199
Cdd:cd19126 92 RLGLDYVDLYLIH-WPGKDKFIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHADVVPAVNQVEFHPYLT------Q 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 200 RELIPMMQSEGVGLMVWSPLA-GGLLSGKydregqtaeggrrqafdfppvnkdrafdcidVMRVIAEAKGVSVAQIALAW 278
Cdd:cd19126 165 KELRGYCKSKGIVVEAWSPLGqGGLLSNP-------------------------------VLAAIGEKYGKSAAQVVLRW 213
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1558667949 279 LLHQSAVssVIIGAKRPEQLADNLAAVDIQLSEVELAQLDAV 320
Cdd:cd19126 214 DIQHGVV--TIPKSVHASRIKENADIFDFELSEDDMTAIDAL 253
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
45-319 |
4.31e-25 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 102.02 E-value: 4.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 45 VGSALDAGINFIDTADVYsegRSEMLTGQALKNLKVPRENVVVATKVFGETGTAGvnsrgssrfHIMESVKESLRRLQLD 124
Cdd:PRK11172 22 VKTALELGYRAIDTAQIY---DNEAAVGQAIAESGVPRDELFITTKIWIDNLAKD---------KLIPSLKESLQKLRTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 125 HIDLYQLHGFDP--ATPIEETLYALDNLVQQGHVRYIGVSNWAAWQIVKALGIsarLGLSRFASLQayytiagrdLE--- 199
Cdd:PRK11172 90 YVDLTLIHWPSPndEVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQAIAA---VGAENIATNQ---------IElsp 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 200 ----RELIPMMQSEGVGLMVWSPLAGGllsgkydregqtaeggrrqafdfpPVNKDrafdciDVMRVIAEAKGVSVAQIA 275
Cdd:PRK11172 158 ylqnRKVVAFAKEHGIHVTSYMTLAYG------------------------KVLKD------PVIARIAAKHNATPAQVI 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1558667949 276 LAWLLHQSavSSVIIGAKRPEQLADNLAAVDIQLSEVELAQLDA 319
Cdd:PRK11172 208 LAWAMQLG--YSVIPSSTKRENLASNLLAQDLQLDAEDMAAIAA 249
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
35-325 |
4.89e-25 |
|
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B (DkgB) from Corynebacterium sp. and 2,5-diketo-D-gluconic acid reductase Zymomonas mobilis are founding members of aldo-keto reductase family 5 member D1 (AKR5D1) and E1 (AKR5E1), respectively. DkgB (EC 1.1.1.274), also called 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381358 [Multi-domain] Cd Length: 255 Bit Score: 101.58 E-value: 4.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 35 QLRQAEAEQLVGSALDAGINFIDTADVYsegRSEMLTGQALKNLKVPRENVVVATKVFGetgtagvnsRGSSRFHIMESV 114
Cdd:cd19132 16 PLKGDEGVEAVVAALQAGYRLLDTAFNY---ENEGAVGEAVRRSGVPREELFVTTKLPG---------RHHGYEEALRTI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 115 KESLRRLQLDHIDLYQLHGFDPATPIE-ETLYALDNLVQQGHVRYIGVSNWAAWQI---VKALGISArlGLSRFaSLQAY 190
Cdd:cd19132 84 EESLYRLGLDYVDLYLIHWPNPSRDLYvEAWQALIEAREEGLVRSIGVSNFLPEHLdrlIDETGVTP--AVNQI-ELHPY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 191 YT-IAGRDLERELipmmqseGVGLMVWSPLaggllsgkydregqtaegGRRQA-FDFPPVNKdrafdcidvmrvIAEAKG 268
Cdd:cd19132 161 FPqAEQRAYHREH-------GIVTQSWSPL------------------GRGSGlLDEPVIKA------------IAEKHG 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1558667949 269 VSVAQIALAWLLHQSAVssVIIGAKRPEQLADNLAAVDIQLSEvelAQLDAVSALPR 325
Cdd:cd19132 204 KTPAQVVLRWHVQLGVV--PIPKSANPERQRENLAIFDFELSD---EDMAAIAALDR 255
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
1-320 |
7.99e-25 |
|
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: 102.10 E-value: 7.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 1 MRYQKLgNTGLFVSRLCLGTmtfggeggmWG-KIGQLRQAeaeqlVGSALDAGINFIDTADVYSegrSEMLTGQALKNL- 78
Cdd:cd19123 1 MKTLPL-SNGDLIPALGLGT---------WKsKPGEVGQA-----VKQALEAGYRHIDCAAIYG---NEAEIGAALAEVf 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 79 ---KVPRENVVVATKVFgetgtagvnsrgsSRFHIMESVKESLRR----LQLDHIDLYQLH------------------- 132
Cdd:cd19123 63 kegKVKREDLWITSKLW-------------NNSHAPEDVLPALEKtladLQLDYLDLYLMHwpvalkkgvgfpesgedll 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 133 GFDPAtPIEETLYALDNLVQQGHVRYIGVSNWAAWQIVKALGiSARLG-------LSRFasLQayytiagrdlERELIPM 205
Cdd:cd19123 130 SLSPI-PLEDTWRAMEELVDKGLCRHIGVSNFSVKKLEDLLA-TARIKpavnqveLHPY--LQ----------QPELLAF 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 206 MQSEGVGLMVWSPLaggllsGKYDREGQTAEGGRRQAFDFPpvnkdrafdcidVMRVIAEAKGVSVAQIALAWLLHQSav 285
Cdd:cd19123 196 CRDNGIHLTAYSPL------GSGDRPAAMKAEGEPVLLEDP------------VINKIAEKHGASPAQVLIAWAIQRG-- 255
|
330 340 350
....*....|....*....|....*....|....*
gi 1558667949 286 SSVIIGAKRPEQLADNLAAVDIQLSEVELAQLDAV 320
Cdd:cd19123 256 TVVIPKSVNPERIQQNLEAAEVELDASDMATIAAL 290
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
35-320 |
1.29e-24 |
|
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: 100.76 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 35 QLRQAEAEQLVGSALDAGINFIDTADVYSegrSEMLTGQALKNLKVPRENVVVATKVFGEtgtagvNSRGSSrfhIMESV 114
Cdd:cd19130 19 KVPPADTQRAVATALEVGYRHIDTAAIYG---NEEGVGAAIAASGIPRDELFVTTKLWND------RHDGDE---PAAAF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 115 KESLRRLQLDHIDLYQLHGFDPATPIE-ETLYALDNLVQQGHVRYIGVSNWAAWQIVKALGISARLGLSRFASLQAYYTi 193
Cdd:cd19130 87 AESLAKLGLDQVDLYLVHWPTPAAGNYvHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVAATGVVPAVNQIELHPAYQ- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 194 agrdlERELIPMMQSEGVGLMVWSPLAGGLLsgkydregqtaeggrrqaFDFPPVNKdrafdcidvmrvIAEAKGVSVAQ 273
Cdd:cd19130 166 -----QRTIRDWAQAHDVKIEAWSPLGQGKL------------------LGDPPVGA------------IAAAHGKTPAQ 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1558667949 274 IALAWLLHQSAVssVIIGAKRPEQLADNLAAVDIQLSEVELAQLDAV 320
Cdd:cd19130 211 IVLRWHLQKGHV--VFPKSVRRERMEDNLDVFDFDLTDTEIAAIDAL 255
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
28-317 |
1.57e-23 |
|
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: 97.44 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 28 GMWgkigQLRQAEAEQLVGSALDAGINFIDTADVYsegRSEMLTGQALKNLKVPRENVVVATKVFgeTGTAGVNSrgssr 107
Cdd:cd19131 16 GVW----QVSNDEAASAVREALEVGYRSIDTAAIY---GNEEGVGKAIRASGVPREELFITTKLW--NSDQGYDS----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 108 fhIMESVKESLRRLQLDHIDLYQLHGFDPAT-PIEETLYALDNLVQQGHVRYIGVSNWAA---WQIVKALGISARLGLsr 183
Cdd:cd19131 82 --TLRAFDESLRKLGLDYVDLYLIHWPVPAQdKYVETWKALIELKKEGRVKSIGVSNFTIehlQRLIDETGVVPVVNQ-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 184 fASLQAYYTiagrdlERELIPMMQSEGVGLMVWSPLA-GGLLSGKydregqtaeggrrqafdfppvnkdrafdcidVMRV 262
Cdd:cd19131 158 -IELHPRFQ------QRELRAFHAKHGIQTESWSPLGqGGLLSDP-------------------------------VIGE 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1558667949 263 IAEAKGVSVAQIALAWLLHQSAVssVIIGAKRPEQLADNLAAVDIQLSEVELAQL 317
Cdd:cd19131 200 IAEKHGKTPAQVVIRWHLQNGLV--VIPKSVTPSRIAENFDVFDFELDADDMQAI 252
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
40-319 |
1.83e-23 |
|
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: 97.46 E-value: 1.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 40 EAEQLVGSALDAGINFIDTADVYsegRSEMLTGQALKNLKVPRENVVVATKVFGETgtAGVNSrgssrfhIMESVKESLR 119
Cdd:cd19157 25 EVVNAVKTALKNGYRSIDTAAIY---GNEEGVGKGIKESGIPREELFITSKVWNAD--QGYDS-------TLKAFEASLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 120 RLQLDHIDLYQLHgfdpaTPIE----ETLYALDNLVQQGHVRYIGVSNWAAWQIVKALGISARLGLSRFASLQAYYTiag 195
Cdd:cd19157 93 RLGLDYLDLYLIH-----WPVKgkykETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAEIVPMVNQVEFHPRLT--- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 196 rdlERELIPMMQSEGVGLMVWSPLAGGllsgkydregqtaeggrrQAFDfppvnkdrafdcIDVMRVIAEAKGVSVAQIA 275
Cdd:cd19157 165 ---QKELRDYCKKQGIQLEAWSPLMQG------------------QLLD------------NPVLKEIAEKYNKSVAQVI 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1558667949 276 LAWLLHQSAVssVIIGAKRPEQLADNLAAVDIQLSEVELAQLDA 319
Cdd:cd19157 212 LRWDLQNGVV--TIPKSIKEHRIIENADVFDFELSQEDMDKIDA 253
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
13-304 |
3.28e-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: 97.73 E-value: 3.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 13 VSRLCLGTMTFGGeggmwGKIGQLRQAEAEQLVGSALDAGINFIDTADVYseGRSEMLTGQALKNL--KVPRENVVVATK 90
Cdd:cd19164 13 LPPLIFGAATFSY-----QYTTDPESIPPVDIVRRALELGIRAFDTSPYY--GPSEIILGRALKALrdEFPRDTYFIITK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 91 VfgetGTAGVNSRGSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATPiEETLYALDNLVQ---QGHVRYIGVSN---- 163
Cdd:cd19164 86 V----GRYGPDDFDYSPEWIRASVERSLRRLHTDYLDLVYLHDVEFVAD-EEVLEALKELFKlkdEGKIRNVGISGyplp 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 164 ---WAAWQIVKALGISARLGLSrfaslQAYYTIAGRDLeRELIPMMQSEGVGLMVW--SPLAGGLLsgkydregqTAEGG 238
Cdd:cd19164 161 vllRLAELARTTAGRPLDAVLS-----YCHYTLQNTTL-LAYIPKFLAAAGVKVVLnaSPLSMGLL---------RSQGP 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 239 RrqafDF---PPVNKDRAFDCIDvmrvIAEAKGVSVAQIALAWLL-HQSAVSSVIIGAKRPEQLADNLAA 304
Cdd:cd19164 226 P----EWhpaSPELRAAAAKAAE----YCQAKGTDLADVALRYALrEWGGEGPTVVGCSNVDELEEAVEA 287
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
35-319 |
4.99e-23 |
|
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: 96.32 E-value: 4.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 35 QLRQAEAEQLVGSALDAGINFIDTADVYsegRSEMLTGQALKNLKVPRENVVVATKVFGETGTAGVNSRGssrfhimesV 114
Cdd:cd19127 18 QTPPEETADAVATALADGYRLIDTAAAY---GNEREVGEGIRRSGVDRSDIFVTTKLWISDYGYDKALRG---------F 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 115 KESLRRLQLDHIDLYQLHgFDPATPIEETL---YALDNLVQQGHVRYIGVSNW---------AAWQIVKALGIsarlgls 182
Cdd:cd19127 86 DASLRRLGLDYVDLYLLH-WPVPNDFDRTIqayKALEKLLAEGRVRAIGVSNFtpehlerliDATTVVPAVNQ------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 183 rfASLQAYYTiagrdlERELIPMMQSEGVGLMVWSPLaGGLLsgkydREGQTAEGGRRQAFDFPPVNKdrafdcidvmrv 262
Cdd:cd19127 158 --VELHPYFS------QKDLRAFHRRLGIVTQAWSPI-GGVM-----RYGASGPTGPGDVLQDPTITG------------ 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1558667949 263 IAEAKGVSVAQIALAWLLHQSAvsSVIIGAKRPEQLADNLAAVDIQLSEVELAQLDA 319
Cdd:cd19127 212 LAEKYGKTPAQIVLRWHLQNGV--SAIPKSVHPERIAENIDIFDFALSAEDMAAIDA 266
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
28-320 |
6.76e-23 |
|
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: 96.83 E-value: 6.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 28 GMWgkigQLRQAEAEQLVGSALDAGINFIDTADVYsegRSEMLTGQALKNL----KVPRENVVVATKVfgetgtagvnSR 103
Cdd:cd19155 18 GTW----QSSPEEIETAVDTALEAGYRHIDTAYVY---RNEAAIGNVLKKWidsgKVKREELFIVTKL----------PP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 104 GSSRFHIMES-VKESLRRLQLDHIDLY---------------------QLHGFDPATPIEETLYALDNLVQQGHVRYIGV 161
Cdd:cd19155 81 GGNRREKVEKfLLKSLEKLQLDYVDLYlihfpvgslskeddsgkldptGEHKQDYTTDLLDIWKAMEAQVDQGLTRSIGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 162 SNWAAWQIVKALGiSARLglsRFASLQ----AYYTiagrdlERELIPMMQSEGVGLMVWSPLAGGLLSGKYdregqTAEG 237
Cdd:cd19155 161 SNFNREQMARILK-NARI---KPANLQvelhVYLQ------QKDLVDFCSTHSITVTAYAPLGSPGAAHFS-----PGTG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 238 GrrqafdfPPVNKDRAFDcIDVMRVIAEAKGVSVAQIALAWLLHQSAVssVIIGAKRPEQLADNLAAVDIQLSEVELAQL 317
Cdd:cd19155 226 S-------PSGSSPDLLQ-DPVVKAIAERHGKSPAQVLLRWLMQRGVV--VIPKSTNAARIKENFQVFDFELTEADMAKL 295
|
...
gi 1558667949 318 DAV 320
Cdd:cd19155 296 SSL 298
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
28-319 |
2.50e-22 |
|
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: 95.04 E-value: 2.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 28 GMWGKIGQLrqaEAEQLVGSALDAGINFIDTADVYsegRSEMLTGQALKNL----KVPRENVVVATKVFGEtgtagvnsr 103
Cdd:cd19116 17 GTWKLKDDE---GVRQAVKHAIEAGYRHIDTAYLY---GNEAEVGEAIREKiaegVVKREDLFITTKLWNS--------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 104 gssrFHIMESV----KESLRRLQLDHIDLYQLH---GF----DPATPIE---------ETLYALDNLVQQGHVRYIGVSN 163
Cdd:cd19116 82 ----YHEREQVepalRESLKRLGLDYVDLYLIHwpvAFkennDSESNGDgslsdidylETWRGMEDLVKLGLTRSIGVSN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 164 WAAWQIVKALgisaRLGLSRFASLQayytiagrdLE-------RELIPMMQSEGVGLMVWSPLaggllsGKYDREGQTae 236
Cdd:cd19116 158 FNSEQINRLL----SNCNIKPAVNQ---------IEvhptltqEKLVAYCQSNGIVVMAYSPF------GRLVPRGQT-- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 237 ggrrqafDFPPVNKDRafdcidVMRVIAEAKGVSVAQIALAWLLHQSAVssVIIGAKRPEQLADNLAAVDIQLSEVELAQ 316
Cdd:cd19116 217 -------NPPPRLDDP------TLVAIAKKYGKTTAQIVLRYLIDRGVV--PIPKSSNKKRIKENIDIFDFQLTPEEVAA 281
|
...
gi 1558667949 317 LDA 319
Cdd:cd19116 282 LNS 284
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
28-321 |
3.56e-22 |
|
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: 94.79 E-value: 3.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 28 GMWgkigQLRQAEAEQLVGSALDAGINFIDTADVYsegRSEMLTGQALKNL----KVPRENVVVATKVFgetgtAGVNSR 103
Cdd:cd19154 18 GTW----QSKGAEGITAVRTALKAGYRLIDTAFLY---QNEEAIGEALAELleegVVKREDLFITTKLW-----THEHAP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 104 GSsrfhIMESVKESLRRLQLDHIDLYQLHG-------------------FDPATPIEETLYALDNLVQQGHVRYIGVSNW 164
Cdd:cd19154 86 ED----VEEALRESLKKLQLEYVDLYLIHApaafkddegesgtmengmsIHDAVDVEDVWRGMEKVYDEGLTKAIGVSNF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 165 AAWQIVKALGISARLGLSRFASLQAYYTiagrdlERELIPMMQSEGVGLMVWSPLAGgllSGKYDREGQTAEGGRRQAFD 244
Cdd:cd19154 162 NNDQIQRILDNARVKPHNNQVECHLYFP------QKELVEFCKKHNISVTSYATLGS---PGRANFTKSTGVSPAPNLLQ 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1558667949 245 FPpvnkdrafdcidVMRVIAEAKGVSVAQIALAWLLhQSAVsSVIIGAKRPEQLADNLAAVDIQLSEVELAQLDAVS 321
Cdd:cd19154 233 DP------------IVKAIAEKHGKTPAQVLLRYLL-QRGI-AVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIE 295
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
33-320 |
1.40e-21 |
|
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: 92.23 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 33 IGQLRQAEAEQLVGSALDAGINFIDTADVYSegrSEMLTGQALKNLKVPRENVVVATKVFgeTGTAGVNSRgssrfhiME 112
Cdd:cd19134 18 VGELSDDEAERSVSAALEAGYRLIDTAAAYG---NEAAVGRAIAASGIPRGELFVTTKLA--TPDQGFTAS-------QA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 113 SVKESLRRLQLDHIDLYQLHGfdPATPIEETLYALDNLVQ---QGHVRYIGVSNWAAWQIVKALGISarlglsrfaslqa 189
Cdd:cd19134 86 ACRASLERLGLDYVDLYLIHW--PAGREGKYVDSWGGLMKlreEGLARSIGVSNFTAEHLENLIDLT------------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 190 YYTIAGRDLerELIPMM-QSE--------GVGLMVWSPLAGGllsgkydregqtaeggrrQAFDFPPVNKdrafdcidvm 260
Cdd:cd19134 151 FFTPAVNQI--ELHPLLnQAElrkvnaqhGIVTQAYSPLGVG------------------RLLDNPAVTA---------- 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 261 rvIAEAKGVSVAQIALAWLLHQSAVssVIIGAKRPEQLADNLAAVDIQLSEVELAQLDAV 320
Cdd:cd19134 201 --IAAAHGRTPAQVLLRWSLQLGNV--VISRSSNPERIASNLDVFDFELTADHMDALDGL 256
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
28-318 |
3.39e-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: 91.79 E-value: 3.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 28 GMWgkigQLRQAEAEQLVGSALDAGINFIDTADVYsegRSEMLTGQALKNL----KVPRENVVVATKV---FGETGTagv 100
Cdd:cd19111 10 GTY----QSPPEEVRAAVDYALFVGYRHIDTALSY---QNEKAIGEALKWWlkngKLKREEVFITTKLppvYLEFKD--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 101 nsrgssrfhIMESVKESLRRLQLDHIDLYQLH---GF----------DPATPIEETLYALDNLVQQGHVRYIGVSNWAAW 167
Cdd:cd19111 80 ---------TEKSLEKSLENLKLPYVDLYLIHhpcGFvnkkdkgereLASSDVTSVWRAMEALVSEGKVKSIGLSNFNPR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 168 QIVKALgisaRLGLSRFASLQ----AYYTiagrdlERELIPMMQSEGVGLMVWSPLaggllsGKYDREGQTAEGGRRQAF 243
Cdd:cd19111 151 QINKIL----AYAKVKPSNLQlechAYLQ------QRELRKFCNKKNIVVTAYAPL------GSPGRANQSLWPDQPDLL 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1558667949 244 DFPPVNKdrafdcidvmrvIAEAKGVSVAQIALAWLLHQSAVssVIIGAKRPEQLADNLAAVDIQLSEVELAQLD 318
Cdd:cd19111 215 EDPTVLA------------IAKELDKTPAQVLLRFVLQRGTG--VLPKSTNKERIEENFEVFDFELTEEHFKKLK 275
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
28-319 |
3.72e-21 |
|
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: 92.06 E-value: 3.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 28 GMW-GKIGQLRQAeaeqlVGSALDAGINFIDTADVYSegrSEMLTGQALKN-----LKVPRENVVVATKVFgetgtagvN 101
Cdd:cd19106 13 GTWkSKPGQVKAA-----VKYALDAGYRHIDCAAVYG---NEQEVGEALKEkvgpgKAVPREDLFVTSKLW--------N 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 102 SRgssrfHIMESVKESLRR----LQLDHIDLYQLH---GFDP----------------ATPIEETLYALDNLVQQGHVRY 158
Cdd:cd19106 77 TK-----HHPEDVEPALRKtlkdLQLDYLDLYLIHwpyAFERgdnpfpknpdgtirydSTHYKETWKAMEKLVDKGLVKA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 159 IGVSNWAAWQIVKALGIsARLglsRFASLQA----YYTiagrdlERELIPMMQSEGVGLMVWSPLaggllsGKYDRegQT 234
Cdd:cd19106 152 IGLSNFNSRQIDDILSV-ARI---KPAVLQVechpYLA------QNELIAHCKARGLVVTAYSPL------GSPDR--PW 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 235 AEGGRRQAFDFPPVNKdrafdcidvmrvIAEAKGVSVAQIALAWLLHQSAVssVIIGAKRPEQLADNLAAVDIQLSEVEL 314
Cdd:cd19106 214 AKPDEPVLLEEPKVKA------------LAKKYNKSPAQILLRWQVQRGVV--VIPKSVTPSRIKQNIQVFDFTLSPEEM 279
|
....*
gi 1558667949 315 AQLDA 319
Cdd:cd19106 280 KQLDA 284
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
8-321 |
1.68e-20 |
|
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: 89.86 E-value: 1.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 8 NTGLFVSRLCLGTmtfggeggmWgkigQLRQAEAEQLVGSALDAGINFIDTADVYsegRSEMLTGQALKNLKVPRENVVV 87
Cdd:cd19117 9 NTGAEIPAVGLGT---------W----QSKPNEVAKAVEAALKAGYRHIDTAAIY---GNEEEVGQGIKDSGVPREEIFI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 88 ATKVFGetgtagvnsrgSSRFHIMESVKESLRRLQLDHIDLYQLHGFDPATP---------------------IEETLYA 146
Cdd:cd19117 73 TTKLWC-----------TWHRRVEEALDQSLKKLGLDYVDLYLMHWPVPLDPdgndflfkkddgtkdhepdwdFIKTWEL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 147 LDNLVQQGHVRYIGVSNWAAWQIVKALgisarlglsrfASLQAYYTIAGRDLE-------RELIPMMQSEGVGLMVWSPL 219
Cdd:cd19117 142 MQKLPATGKVKAIGVSNFSIKNLEKLL-----------ASPSAKIVPAVNQIElhpllpqPKLVDFCKSKGIHATAYSPL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 220 aggllsgkydreGQTAEggrrqafdfpPVNKDRafdcidVMRVIAEAKGVSVAQIALAWLLHQSavSSVIIGAKRPEQLA 299
Cdd:cd19117 211 ------------GSTNA----------PLLKEP------VIIKIAKKHGKTPAQVIISWGLQRG--YSVLPKSVTPSRIE 260
|
330 340
....*....|....*....|..
gi 1558667949 300 DNLAAvdIQLSEVELAQLDAVS 321
Cdd:cd19117 261 SNFKL--FTLSDEEFKEIDELH 280
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
28-327 |
8.75e-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: 88.31 E-value: 8.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 28 GMWgkigQLRQAEAEQLVGSALDAGINFIDTADVYsegRSEMLTGQALKNL----KVPRENVVVATKVFGetgtagvnsr 103
Cdd:cd19112 17 GVW----RMEPGEIKELILNAIKIGYRHFDCAADY---KNEKEVGEALAEAfktgLVKREDLFITTKLWN---------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 104 gSSRFHIMESVKESLRRLQLDHIDLYQLH-----------------------GFDPATPIEETLYALDNLVQQGHVRYIG 160
Cdd:cd19112 80 -SDHGHVIEACKDSLKKLQLDYLDLYLVHfpvatkhtgvgttgsalgedgvlDIDVTISLETTWHAMEKLVSAGLVRSIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 161 VSNWAAWQIVKALGISA-RLGLSRFASlQAYYTiagRDlerELIPMMQSEGVGLMVWSPLAGGLlsgkydregqtaeggr 239
Cdd:cd19112 159 ISNYDIFLTRDCLAYSKiKPAVNQIET-HPYFQ---RD---SLVKFCQKHGISVTAHTPLGGAA---------------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 240 rqafdfppVNKDR--AFDCID--VMRVIAEAKGVSVAQIALAWLLHQSAVssVIIGAKRPEQLADNLAAVDIQLSEVEla 315
Cdd:cd19112 216 --------ANAEWfgSVSPLDdpVLKDLAKKYGKSAAQIVLRWGIQRNTA--VIPKSSKPERLKENIDVFDFQLSKED-- 283
|
330
....*....|..
gi 1558667949 316 qLDAVSALPREY 327
Cdd:cd19112 284 -MKLIKSLDRKY 294
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
28-318 |
2.41e-19 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 86.28 E-value: 2.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 28 GMWgkigQLRQAEAEQLVGSALDAGINFIDTADVYsegRSEMLTGQALKNLKVPRENVVVATKVFgetgtagvNSRgssR 107
Cdd:PRK11565 21 GVW----QASNEEVITAIHKALEVGYRSIDTAAIY---KNEEGVGKALKEASVAREELFITTKLW--------NDD---H 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 108 FHIMESVKESLRRLQLDHIDLYQLHGfdPATPIEETLYA---LDNLVQQGHVRYIGVSNWAAWQIVKAL---GISARLGl 181
Cdd:PRK11565 83 KRPREALEESLKKLQLDYVDLYLMHW--PVPAIDHYVEAwkgMIELQKEGLIKSIGVCNFQIHHLQRLIdetGVTPVIN- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 182 srfaslqayytiagrdlERELIPMMQ---------SEGVGLMVWSPLAggllsgkydregQTAEGgrrqAFDFPPVNKdr 252
Cdd:PRK11565 160 -----------------QIELHPLMQqrqlhawnaTHKIQTESWSPLA------------QGGKG----VFDQKVIRD-- 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1558667949 253 afdcidvmrvIAEAKGVSVAQIALAWLLHQSAVssVIIGAKRPEQLADNLAAVDIQLSEVEL---AQLD 318
Cdd:PRK11565 205 ----------LADKYGKTPAQIVIRWHLDSGLV--VIPKSVTPSRIAENFDVFDFRLDKDELgeiAKLD 261
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
38-327 |
2.62e-19 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 87.01 E-value: 2.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 38 QAEAEQLVGSALDAGINFIDTADVYseGRSEMLTGQALKNLKVPRENVVVATKvFGETGTAGVNSRGS-------SRFHI 110
Cdd:cd19098 34 RAHTHAVLDAAWAAGVRYFDAARSY--GRAEEFLGSWLRSRNIAPDAVFVGSK-WGYTYTADWQVDAAvhevkdhSLARL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 111 MESVKESLRRLQlDHIDLYQLHGFDPATPI---EETLYALDNLVQQGhvRYIGVSNWAAWQ---IVKALGIsARLGLSRF 184
Cdd:cd19098 111 LKQWEETRSLLG-KHLDLYQIHSATLESGVledADVLAALAELKAEG--VKIGLSLSGPQQaetLRRALEI-EIDGARLF 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 185 ASLQAYYTIagrdLERELIP---MMQSEGVGLMVWSPLAGGLLSGKYDREGQTAEGGrrqafdfppvnkdrafdcidVMR 261
Cdd:cd19098 187 DSVQATWNL----LEQSAGEaleEAHEAGMGVIVKEALANGRLTDRNPSPELAPLMA--------------------VLK 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1558667949 262 VIAEAKGVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAAVDIQLSEVELAQLDAVSALPREY 327
Cdd:cd19098 243 AVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRALDVSLDLELLAALADLAEPPEDY 308
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
50-321 |
1.73e-18 |
|
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381361 [Multi-domain] Cd Length: 265 Bit Score: 83.91 E-value: 1.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 50 DAGINFIDTADVYsegRSEMLTGQALKNLKVPRENVVVATKVF-GETGTAGVnsrgssrfhiMESVKESLRRLQLDHIDL 128
Cdd:cd19135 37 ECGYRHIDTAKRY---GCEELLGKAIKESGVPREDLFLTTKLWpSDYGYEST----------KQAFEASLKRLGVDYLDL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 129 YQLHGFDPATP-------IEETLYALDNLVQQGHVRYIGVSNWaawqivkalGISARLGLSRFASL-----QAYYTIAGR 196
Cdd:cd19135 104 YLLHWPDCPSSgknvketRAETWRALEELYDEGLCRAIGVSNF---------LIEHLEQLLEDCSVvphvnQVEFHPFQN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 197 DleRELIPMMQSEGVGLMVWSPLAGGllsgkydregqtaeggrrQAFDFPPVNKdrafdcidvmrvIAEAKGVSVAQIAL 276
Cdd:cd19135 175 P--VELIEYCRDNNIVFEGYCPLAKG------------------KALEEPTVTE------------LAKKYQKTPAQILI 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1558667949 277 AWLLHQSAVssVIIGAKRPEQLADNLAAVDIQLSEVELAQLDAVS 321
Cdd:cd19135 223 RWSIQNGVV--TIPKSTKEERIKENCQVFDFSLSEEDMATLDSLH 265
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
28-323 |
3.79e-18 |
|
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), also called aldehyde reductase, is the prototype of this family. It catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
Pssm-ID: 381354 [Multi-domain] Cd Length: 277 Bit Score: 82.96 E-value: 3.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 28 GMWgkigQLRQAEAEQLVGSALDAGINFIDTADVYseGRSEML---TGQALKNLKVPRENVVVATKVFgetgtagvnsrg 104
Cdd:cd19128 7 GTY----KITESESKEAVKNAIKAGYRHIDCAYYY--GNEAFIgiaFSEIFKDGGVKREDLFITSKLW------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 105 sSRFHIMESVKE----SLRRLQLDHIDLYQLH---GFDP----------------ATPIEETLYALDNLVQQGHVRYIGV 161
Cdd:cd19128 69 -PTMHQPENVKEqlliTLQDLQLEYLDLFLIHwplAFDMdtdgdprddnqiqslsKKPLEDTWRAMEQCVDEKLTKNIGV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 162 SNWAAWQIVKALGISARLGLSRFASLQAYYTiagrdlERELIPMMQSEGVGLMVWSPLAGgllsgkydregqtaeggrRQ 241
Cdd:cd19128 148 SNYSTKLLTDLLNYCKIKPFMNQIECHPYFQ------NDKLIKFCIENNIHVTAYRPLGG------------------SY 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 242 AFDfppvnkDRAFDCIDVMRVIAEAKGVSVAQIALAWLLHQ-SAVSSVIIGAKRPEQLADNLAAVDIQLSEvelAQLDAV 320
Cdd:cd19128 204 GDG------NLTFLNDSELKALATKYNTTPPQVIIAWHLQKwPKNYSVIPKSANKSRCQQNFDINDLALTK---EDMDAI 274
|
...
gi 1558667949 321 SAL 323
Cdd:cd19128 275 NTL 277
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
39-328 |
1.01e-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: 81.80 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 39 AEAEQLVGSALDAGINFIDTADVYSEGRSemlTGQALKNLKVPRENVVVATKVFGETgtAGVNSrgssrfhIMESVKESL 118
Cdd:cd19156 23 AEAENAVKWAIEAGYRHIDTAAIYKNEEG---VGQGIRESGVPREEVFVTTKLWNSD--QGYES-------TLAAFEESL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 119 RRLQLDHIDLYQLHgFDPATPIEETLYALDNLVQQGHVRYIGVSNWAAWQIVKALGISARLGLSRFASLQAYYTiagrdl 198
Cdd:cd19156 91 EKLGLDYVDLYLIH-WPVKGKFKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCKVAPMVNQIELHPLLT------ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 199 ERELIPMMQSEGVGLMVWSPLAGG-LLSGKydregqtaeggrrqafdfppvnkdrafdcidVMRVIAEAKGVSVAQIALA 277
Cdd:cd19156 164 QEPLRKFCKEKNIAVEAWSPLGQGkLLSNP-------------------------------VLKAIGKKYGKSAAQVIIR 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1558667949 278 WLLHQSAVssVIIGAKRPEQLADNLAAVDIQLSEVELAQLDAVSALPREYP 328
Cdd:cd19156 213 WDIQHGII--TIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTDHRYGP 261
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
45-325 |
2.74e-16 |
|
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: 78.23 E-value: 2.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 45 VGSALDAGINFIDTADVYSegrSEMLTGQ----ALKNLKVPRENVVVATKVFgetgtagvNSrgssrFHIMESVKESLRR 120
Cdd:cd19115 32 VYNAIKAGYRLFDGACDYG---NEVEAGQgvarAIKEGIVKREDLFIVSKLW--------NT-----FHDGERVEPICRK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 121 ----LQLDHIDLYQLHgF-------DPA------------------TPIEETLYALDNLVQQGHVRYIGVSNWAAwQIVK 171
Cdd:cd19115 96 qladWGIDYFDLFLIH-FpialkyvDPAvryppgwfydgkkvefsnAPIQETWTAMEKLVDKGLARSIGVSNFSA-QLLM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 172 ALGISARLglsRFASLQ----AYYTiagrdlERELIPMMQSEGVGLMVWSPLagGLLSGKydregqtaEGGRRQAFDFPP 247
Cdd:cd19115 174 DLLRYARI---RPATLQiehhPYLT------QPRLVKYAQKEGIAVTAYSSF--GPQSFL--------ELDLPGAKDTPP 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1558667949 248 VnkdraFDCiDVMRVIAEAKGVSVAQIALAWLLHQSAvsSVIIGAKRPEQLADNLAAVDIQLSEVElaqLDAVSALPR 325
Cdd:cd19115 235 L-----FEH-DVIKSIAEKHGKTPAQVLLRWATQRGI--AVIPKSNNPKRLAQNLDVTGFDLEAEE---IKAISALDI 301
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
48-320 |
5.57e-15 |
|
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: 74.23 E-value: 5.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 48 ALDAGINFIDTADVYsegRSEMLTGQALK-----NLKVPRENVVVATKVFGETGTAGvnsrgssrfHIMESVKESLRRLQ 122
Cdd:cd19124 29 AIEVGYRHFDTAAAY---GTEEALGEALAealrlGLVKSRDELFVTSKLWCSDAHPD---------LVLPALKKSLRNLQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 123 LDHIDLYQLH-------GFDPATPIEETLYALDnlvqqghvrYIGVsnWAAWQIVKALGISARLGLSRFAS-----LQAY 190
Cdd:cd19124 97 LEYVDLYLIHwpvslkpGKFSFPIEEEDFLPFD---------IKGV--WEAMEECQRLGLTKAIGVSNFSCkklqeLLSF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 191 YTI--AGRDLE-------RELIPMMQSEGVGLMVWSPLaggllsgkydregqtaeGGRRQAFDFPPVNKDrafdciDVMR 261
Cdd:cd19124 166 ATIppAVNQVEmnpawqqKKLREFCKANGIHVTAYSPL-----------------GAPGTKWGSNAVMES------DVLK 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1558667949 262 VIAEAKGVSVAQIALAWLLHQSAvsSVIIGAKRPEQLADNLAAVDIQLSEVELAQLDAV 320
Cdd:cd19124 223 EIAAAKGKTVAQVSLRWVYEQGV--SLVVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
2-318 |
2.18e-14 |
|
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: 72.38 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 2 RYQKLgNTGLFVSRLCLGTmtfggeggmWgkigQLRQAEAEQLVGSALDAGINFIDTADVYSegrSEMLTGQALKNL--- 78
Cdd:cd19125 1 RFFKL-NTGAKIPAVGLGT---------W----QADPGVVGNAVKTAIKEGYRHIDCAAIYG---NEKEIGKALKKLfed 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 79 -KVPRENVVVATKVFgetgtagVNSRGSSRfhIMESVKESLRRLQLDHIDLYQLH----------GFDPA----TPIEET 143
Cdd:cd19125 64 gVVKREDLFITSKLW-------CTDHAPED--VPPALEKTLKDLQLDYLDLYLIHwpvrlkkgahMPEPEevlpPDIPST 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 144 LYALDNLVQQGHVRYIGVSNWAawqiVKALGisarlGLSRFASLQAyytiAGRDLE-------RELIPMMQSEGVGLMVW 216
Cdd:cd19125 135 WKAMEKLVDSGKVRAIGVSNFS----VKKLE-----DLLAVARVPP----AVNQVEchpgwqqDKLHEFCKSKGIHLSAY 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 217 SPLaggllsgkydregqtaeGGRRQAFDFPPVNKDrafdciDVMRVIAEAKGVSVAQIALAWLLHQSavSSVIIGAKRPE 296
Cdd:cd19125 202 SPL-----------------GSPGTTWVKKNVLKD------PIVTKVAEKLGKTPAQVALRWGLQRG--TSVLPKSTNEE 256
|
330 340
....*....|....*....|..
gi 1558667949 297 QLADNLAAVDIQLSEVELAQLD 318
Cdd:cd19125 257 RIKENIDVFDWSIPEEDFAKFS 278
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
28-317 |
2.71e-13 |
|
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: 69.60 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 28 GMWgkigQLRQAEAEQLVGSALDAGINFIDTADVY-SEGRSEMLTGQALKNLKVPRENVVVATKVFGETGTAGVnsrgss 106
Cdd:cd19110 10 GTW----KASPGEVTEAVKVAIDAGYRHFDCAYLYhNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKSL------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 107 rfhIMESVKESLRRLQLDHIDLYQLH---GFDPA---TPIEE-------------TLYALDNLVQQGHVRYIGVSNWAAW 167
Cdd:cd19110 80 ---VKTACTRSLKALKLNYLDLYLIHwpmGFKPGepdLPLDRsgmvipsdtdfldTWEAMEDLVIEGLVKNIGVSNFNHE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 168 QIVKALGisaRLGLsRFASLQAYYTIAGRDLERELIPMMQSEGVGLMVWSPLAGgllsgkydregqTAEGgrrqafdfpp 247
Cdd:cd19110 157 QLERLLN---KPGL-RVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGG------------SCEG---------- 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1558667949 248 vnkdraFDCID--VMRVIAEAKGVSVAQIALAWLLHQSAVssVIIGAKRPEQLADNLAAVDIQLSEVELAQL 317
Cdd:cd19110 211 ------VDLIDdpVIQRIAKKHGKSPAQILIRFQIQRNVI--VIPKSVTPSRIKENIQVFDFELTEHDMDNL 274
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
28-320 |
8.75e-13 |
|
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent D-xylose reductase (XR) from Pichia stipites, Kluyveromyces lactis, Pachysolen tannophilus, Candida tropicalis, and Candida tenuis, Gre3p from Saccharomyces cerevisiae, XR from Candida tropicalis, Pichia guilliermondii, Debaryomyces hansenli, and Debaryomyces nepalensis, which correspond to aldo-keto reductase family 2 member B1-B10 (AKR2B1-10), respectively. XR (EC1.1.1.307) catalyzes the NAD(P)H dependent reduction of xylose to xylitol.
Pssm-ID: 381339 [Multi-domain] Cd Length: 310 Bit Score: 67.86 E-value: 8.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 28 GMWgkigQLRQAEAEQLVGSALDAGINFIDTADVYSegrSEMLTGQ----ALKNLKVPRENVVVATKVFgetgtagvNSr 103
Cdd:cd19113 17 GCW----KLDNATAADQIYQAIKAGYRLFDGAEDYG---NEKEVGEgvnrAIDEGLVKREELFLTSKLW--------NN- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 104 gssrFHIMESVKESLRR----LQLDHIDLYQLH----------------GF---------DPATPIEETLYALDNLVQQG 154
Cdd:cd19113 81 ----FHDPKNVETALNKtlsdLKLDYVDLFLIHfpiafkfvpieekyppGFycgdgdnfvYEDVPILDTWKALEKLVDAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 155 HVRYIGVSNWAAwQIVKALGISARLglsRFASLQ----AYYTiagrdlERELIPMMQSEGVGLMVWSPLagGLLSgkydr 230
Cdd:cd19113 157 KIKSIGVSNFPG-ALILDLLRGATI---KPAVLQiehhPYLQ------QPKLIEYAQKAGITITAYSSF--GPQS----- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 231 egqTAEGGRRQAFDFPPVNKDrafdciDVMRVIAEAKGVSVAQIALAWLLHQSAvsSVIIGAKRPEQLADNLAAVDIQLS 310
Cdd:cd19113 220 ---FVELNQGRALNTPTLFEH------DTIKSIAAKHNKTPAQVLLRWATQRGI--AVIPKSNLPERLLQNLSVNDFDLT 288
|
330
....*....|
gi 1558667949 311 EVELAQLDAV 320
Cdd:cd19113 289 KEDFEEIAKL 298
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
28-317 |
9.57e-13 |
|
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: 67.83 E-value: 9.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 28 GMW-GKIGQLRQAeaeqlVGSALDAGINFIDTADVYS------EGRSEMLTGQALKnlkvpRENVVVATKVFgetgtagv 100
Cdd:cd19107 10 GTWkSPPGQVTEA-----VKVAIDAGYRHIDCAYVYQnenevgEAIQEKIKEQVVK-----REDLFIVSKLW-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 101 nsrgsSRFHIMESVKE----SLRRLQLDHIDLYQLH---GFDPA----------------TPIEETLYALDNLVQQGHVR 157
Cdd:cd19107 72 -----CTFHEKGLVKGacqkTLSDLKLDYLDLYLIHwptGFKPGkelfpldesgnvipsdTTFLDTWEAMEELVDEGLVK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 158 YIGVSNWAAWQIVKAL---GISARLGLSRFASlQAYYTiagrdlERELIPMMQSEGVGLMVWSPLaggllsGKYDREGQT 234
Cdd:cd19107 147 AIGVSNFNHLQIERILnkpGLKYKPAVNQIEC-HPYLT------QEKLIQYCQSKGIVVTAYSPL------GSPDRPWAK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 235 AEGgrrqafdfPPVNKDRAfdcidvMRVIAEAKGVSVAQIALAWLLHQSAVssVIIGAKRPEQLADNLAAVDIQLSEVEL 314
Cdd:cd19107 214 PED--------PSLLEDPK------IKEIAAKHNKTTAQVLIRFPIQRNLV--VIPKSVTPERIAENFKVFDFELSSEDM 277
|
...
gi 1558667949 315 AQL 317
Cdd:cd19107 278 ATI 280
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
1-314 |
2.62e-12 |
|
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, EC 1.1.1.365), also called D-galacturonic acid reductase, or GalUR, is a founding member of aldo-keto reductase family 3 member D1 (AKR3D1). It mediates the reduction of D-galacturonate to L-galactonate, the first step in D-galacturonate catabolic process. It also has activity with D-glucuronate and DL-glyceraldehyde. Its activity is seen only with NADPH and not with NADH.
Pssm-ID: 381347 [Multi-domain] Cd Length: 279 Bit Score: 66.40 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 1 MRYQKLgNTGLFVSRLCLGTmtfggeggmWgkigQLRQAEAEQLVGSALDAGINFIDTADVYsegRSEMLTGQALK---N 77
Cdd:cd19121 1 MTSFKL-NTGASIPAVGLGT---------W----QAKAGEVKAAVAHALKIGYRHIDGALCY---QNEDEVGEGIKeaiA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 78 LKVPRENVVVATKVFgetgtagvnsrgsSRFH--IMESVKESLRRLQLDHIDLYQLH--------GFDPATPIEE----- 142
Cdd:cd19121 64 GGVKREDLFVTTKLW-------------STYHrrVELCLDRSLKSLGLDYVDLYLVHwpvllnpnGNHDLFPTLPdgsrd 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 143 ---------TLYALDNLVQQGHVRYIGVSNWAAWQIVKALGISARLGLSRFASLQAYYTiagrdlERELIPMMQSEGVGL 213
Cdd:cd19121 131 ldwdwnhvdTWKQMEKVLKTGKTKAIGVSNYSIPYLEELLKHATVVPAVNQVENHPYLP------QQELVDFCKEKGILI 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 214 MVWSPL--AGGLLsgkydregqtaeggrrqaFDFPPVNKdrafdcidvmrvIAEAKGVSVAQIALAWLLHQSAVssVIIG 291
Cdd:cd19121 205 EAYSPLgsTGSPL------------------ISDEPVVE------------IAKKHNVGPGTVLISYQVARGAV--VLPK 252
|
330 340
....*....|....*....|...
gi 1558667949 292 AKRPEQLADNLAAVDIQLSEVEL 314
Cdd:cd19121 253 SVTPDRIKSNLEIIDLDDEDMNK 275
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
8-320 |
7.99e-12 |
|
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: 64.74 E-value: 7.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 8 NTGLFVSRLCLGTmtfggeggmW-GKIGQLRQAeaeqlVGSALDAGINFIDTADVYsEGRSEMltGQALKNLK-----VP 81
Cdd:cd19118 2 NTGNKIPAIGLGT---------WqAEPGEVGAA-----VKIALKAGYRHLDLAKVY-QNQHEV--GQALKELLkeepgVK 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 82 RENVVVATKVFgetgtagvNSRgssrfHIMESVK----ESLRRLQLDHIDLYQLH---GFDPATPIE------------- 141
Cdd:cd19118 65 REDLFITSKLW--------NNS-----HRPEYVEpaldDTLKELGLDYLDLYLIHwpvAFKPTGDLNpltavptnggevd 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 142 --------ETLYALDNLVQQGHVRYIGVSNWAAwQIVKALgISArlGLSRFASLQAYYtiAGRDLERELIPMMQSEGVGL 213
Cdd:cd19118 132 ldlsvslvDTWKAMVELKKTGKVKSIGVSNFSI-DHLQAI-IEE--TGVVPAVNQIEA--HPLLLQDELVDYCKSKNIHI 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 214 MVWSPLaGGLLSGKydregqtaeggrrqafdfPPVNKDrafdciDVMRVIAEAKGVSVAQIALAWLLHQSavSSVIIGAK 293
Cdd:cd19118 206 TAYSPL-GNNLAGL------------------PLLVQH------PEVKAIAAKLGKTPAQVLIAWGIQRG--HSVIPKSV 258
|
330 340
....*....|....*....|....*..
gi 1558667949 294 RPEQLADNLAAVDiqLSEVELAQLDAV 320
Cdd:cd19118 259 TPSRIRSNFEQVE--LSDDEFNAVTAL 283
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
42-163 |
1.74e-11 |
|
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family.
Pssm-ID: 381355 [Multi-domain] Cd Length: 295 Bit Score: 64.02 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 42 EQLVGSALDAGINFIDTADVYsegRSEMLTGQALKNL----KVPRENVVVATKVFgetgtagvNSRgssrfHIMESVK-- 115
Cdd:cd19129 22 RNAVKAALEAGFRHFDCAERY---RNEAEVGEAMQEVfkagKIRREDLFVTTKLW--------NTN-----HRPERVKpa 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 116 --ESLRRLQLDHIDLYQLHG--------------------FDPATPIEETLYALDNLVQQGHVRYIGVSN 163
Cdd:cd19129 86 feASLKRLQLDYLDLYLIHTpfafqpgdeqdprdangnviYDDGVTLLDTWRAMERLVDEGRCKAIGLSD 155
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
40-325 |
1.22e-10 |
|
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.
Pssm-ID: 381340 [Multi-domain] Cd Length: 302 Bit Score: 61.42 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 40 EAEQLVGSALDAGINFIDTADVYSEgRSEMLTG--QALKNLKVPRENVVVATKVFgetgtagvnsrgsSRFHIMESVKE- 116
Cdd:cd19114 18 ETEEVIYNAIKVGYRLIDGALLYGN-EAEVGRGirKAIQEGLVKREDLFIVTKLW-------------NNFHGKDHVREa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 117 ---SLRRLQLDHIDLYQLHG------FDPAT-------------------PIEETLYALDNLVQQGHVRYIGVSNWAAWQ 168
Cdd:cd19114 84 fdrQLKDYGLDYIDLYLIHFpipaayVDPAEnypflwkdkelkkfpleqsPMQECWREMEKLVDAGLVRNIGIANFNVQL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 169 IVKALgisarlglsrfaslqAYYTIAGRDLERELIPMMQSEgvGLMVWSPlAGGLLSGKYDREGQTAeggrrqAFDFPPV 248
Cdd:cd19114 164 ILDLL---------------TYAKIKPAVLQIEHHPYLQQK--RLIDWAK-KQGIQITAYSSFGNAV------YTKVTKH 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1558667949 249 NKDRA-FDCIDVMRVIAEAKGVSVAQIALAWLLHQSAVssVIIGAKRPEQLADNLAAVDIQLSEVELAQLDAVSALPR 325
Cdd:cd19114 220 LKHFTnLLEHPVVKKLADKHKRDTGQVLLRWAVQRNIT--VIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANAR 295
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
18-321 |
3.40e-10 |
|
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: 60.33 E-value: 3.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 18 LGTMTFGGEGGmwgkigqlrQAEAEQLVGSALDAGINFIDTADVYsegRSEMLTGQALK-----NLKVPRENVVVATKVF 92
Cdd:cd19122 12 VGFGTFANEGA---------KGETYAAVTKALDVGYRHLDCAWFY---LNEDEVGDAVRdflkeNPSVKREDLFICTKVW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 93 getgtagvnsrgsSRFHIME----SVKESLRRLQLDHIDLYQLH---------------GFDPATPI--------EETLY 145
Cdd:cd19122 80 -------------NHLHEPEdvkwSIDNSLKNLKLDYIDLFLVHwpiaaekndqrspklGPDGKYVIlkdltenpEPTWR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 146 ALDNLVQQGHVRYIGVSNWAAWQIVKalgisarlgLSRFASLQAYYT---IAGRDLERELIPMMQSEGVGLMVWSPLAGg 222
Cdd:cd19122 147 AMEEIYESGKAKAIGVSNWTIPGLKK---------LLSFAKVKPHVNqieIHPFLPNEELVDYCFSNDILPEAYSPLGS- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 223 llsgkydrEGQTAEGGRRqafdfppVNKDRafdcidVMRVIAEAKGVSVAQIALAWLLHQSAVssVIIGAKRPEQLADNL 302
Cdd:cd19122 217 --------QNQVPSTGER-------VSENP------TLNEVAEKGGYSLAQVLIAWGLRRGYV--VLPKSSTPSRIESNF 273
|
330
....*....|....*....
gi 1558667949 303 AAvdIQLSEVELAQLDAVS 321
Cdd:cd19122 274 KS--IELSDEDFEAINQVA 290
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
8-328 |
8.37e-10 |
|
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar proteins; Saccharomyces cerevisiae Ara1p (EC 1.1.1.117), also called D-arabinose 1-dehydrogenase (NAD(P)(+)), is a founding members of aldo-keto reductase family 3 member C1 (AKR3C1). It catalyzes the oxidation of D-arabinose, L-xylose, L-fucose, and L-galactose in the presence of NADP(+).
Pssm-ID: 381345 [Multi-domain] Cd Length: 294 Bit Score: 59.05 E-value: 8.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 8 NTGLFVSRLCLGTmtfggeggmWGKIGQLrqAEAEQLVGSALDAGINFIDTADVYSegrSEMLTGQALKNL----KVPRE 83
Cdd:cd19119 7 NTGASIPALGLGT---------ASPHEDR--AEVKEAVEAAIKEGYRHIDTAYAYE---TEDFVGEAIKRAiddgSIKRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 84 NVVVATKVFgetgtagvnsrgsSRFH--IMESVKESLRRLQLDHIDLYQLH--------------GFDPATPIEETLYA- 146
Cdd:cd19119 73 ELFITTKVW-------------PTFYdeVERSLDESLKALGLDYVDLLLVHwpvcfekdsddsgkPFTPVNDDGKTRYAa 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 147 ----------LDNLVQQGHVRYIGVSNWAawqIVKalgISARLGLSRFASLQAYYTIAGRDLERELIPMMQSEGVGLMVW 216
Cdd:cd19119 140 sgdhittykqLEKIYLDGRAKAIGVSNYS---IVY---LERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAY 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 217 SPLaggllsgkydregqtaeGGRRQAFDFPPVNKDrafdcidvmrvIAEAKGVSVAQIALAWllHQSAVSSVIIGAKRPE 296
Cdd:cd19119 214 SPL-----------------GSHGAPNLKNPLVKK-----------IAEKYNVSTGDILISY--HVRQGVIVLPKSLKPV 263
|
330 340 350
....*....|....*....|....*....|..
gi 1558667949 297 QLADNLAAVdiQLSEVELAQLDAVSalpREYP 328
Cdd:cd19119 264 RIVSNGKIV--SLTKEDLQKLDDIG---EKYP 290
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
45-338 |
2.19e-09 |
|
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: 57.89 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 45 VGSALDAGINFIDTADVYSegrSEMLTGQALKNL----KVPRENVVVATKVFgetgtagvnsrgsSRFHIMESVKESLRR 120
Cdd:cd19109 27 VKVAIDTGYRHIDGAYIYQ---NEHEVGQAIREKiaegKVKREDIFYCGKLW-------------NTCHPPELVRPTLER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 121 ----LQLDHIDLYQLH---GFDPAtpieETLYALDnlvQQGHVRYIG---VSNWAAWQIVKALGISARLGLSRFASLQ-- 188
Cdd:cd19109 91 tlkvLQLDYVDLYIIEmpmAFKPG----DEIYPRD---ENGKWLYHKtnlCATWEALEACKDAGLVKSIGVSNFNRRQle 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 189 --------------------AYYTiagrdlERELIPMMQSEGVGLMVWSPLAggllsgkydregqTAEGGRRQAFDFPPV 248
Cdd:cd19109 164 lilnkpglkhkpvsnqvechPYFT------QPKLLEFCQQHDIVIVAYSPLG-------------TCRDPIWVNVSSPPL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 249 NKDrafdciDVMRVIAEAKGVSVAQIALAWLLHQSAVssVIIGAKRPEQLADNLAAVDIQLSEVELAQLDAVSALPREYP 328
Cdd:cd19109 225 LED------PLLNSIGKKYNKTAAQVVLRFNIQRGVV--VIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYVE 296
|
330
....*....|
gi 1558667949 329 GWMLERQGEY 338
Cdd:cd19109 297 LLMWRDHPEY 306
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
40-163 |
4.76e-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: 50.69 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 40 EAEQLVGSALDAGINFIDTADVYsegRSEMLTGQAL----KNLKVPRENVVVATKVFgetgtagvnsrgsSRFHIMESVK 115
Cdd:cd19108 28 KALEATKLAIDAGFRHIDSAYLY---QNEEEVGQAIrskiADGTVKREDIFYTSKLW-------------CTFHRPELVR 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1558667949 116 ----ESLRRLQLDHIDLYQLHGFDPATPIEE-------------------TLYALDNLVQQGHVRYIGVSN 163
Cdd:cd19108 92 paleKSLKKLQLDYVDLYLIHFPVALKPGEElfpkdengklifdtvdlcaTWEAMEKCKDAGLAKSIGVSN 162
|
|
| PRK14863 |
PRK14863 |
bifunctional regulator KidO; Provisional |
13-304 |
3.04e-06 |
|
bifunctional regulator KidO; Provisional
Pssm-ID: 184865 [Multi-domain] Cd Length: 292 Bit Score: 47.99 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 13 VSRLCLGTMTFGGEGGMWGKI-GQLRQAEAEQLVGSALDAGINFIDTADVYseGRSEMLTGQALknlkvPRENVvvatkv 91
Cdd:PRK14863 5 VSKLGLAAAQFGLDPGSSSAPrGRTPEAEARDILNIAARAGLSVLDASGLF--GRAETVLGQLI-----PRPVP------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 92 FGETGTAGVNSRGSSRfhIMESVKESLRRLQLDHIDLYQLHG----FDPATP-IEETLYALDNlvqQGHVRYIGVSNWAA 166
Cdd:PRK14863 72 FRVTLSTVRADRGPDF--VEAEARASLRRMGVERADAILVHSptelFGPHGAaLWERLQALKD---QGLFAKIGVSAHAS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1558667949 167 WQIVkalGISARLG---LSRFASLQAYYTIAGRDLERelipmMQSEGVGLMVWSPLAGGLLSGKYDRegqtaeggrrqaf 243
Cdd:PRK14863 147 DDPV---GVARRFKpdiLQAPASLLDQRLLADGSLQR-----IAGMGVEVHLRSIFLNGLLFLPPDR------------- 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1558667949 244 dFPPVNKDRAFDCIDVMRVIAEAKgVSVAQIALAWLLHQSAVSSVIIGAKRPEQLADNLAA 304
Cdd:PRK14863 206 -VPAQLKGASGRLSRVRRMIAEGR-SDPLQAALGFALSRPEGSAVLVGVNSAAELSAVVAA 264
|
|
| |
