|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
1-303 |
3.45e-159 |
|
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: 448.22 E-value: 3.45e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 1 MEYRQLGRSGLKISTITMGTMTIGGGGKFAQ-VGDVGVADASRHVDLCLDAGVNLIDTADIYSTGVCEEIIGEVLGGKRK 79
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGTMTFGGGGGFFGaWGGVDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKGRRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 80 DgVLIATKARFSMGPGPNDGGLSRHHLISACEASLKRLKTDVIDLYQVHEWDGQTPLEETMEALDTLVRQGKVRYIGCSN 159
Cdd:cd19091 81 D-VLIATKVRGRMGEGPNDVGLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVRYIGVSN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 160 YSGWHIMKALGVSALDKRQRFVSQQIHYTLEAREAEYELVPISIDQGLGILVWSPLAGGLLSGKHRRGQS-PEGTRQLAG 238
Cdd:cd19091 160 FSAWQIMKALGISERRGLARFVALQAYYSLLGRDLEHELMPLALDQGVGLLVWSPLAGGLLSGKYRRGQPaPEGSRLRRT 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500691625 239 WNEPPIRDEERLWKIVDILVAIAAERGVSPAQVALAWLIGRQAVTSVIIGGRTEQQFRDNLAAAG 303
Cdd:cd19091 240 GFDFPPVDRERGYDVVDALREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGAAG 304
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-303 |
1.43e-126 |
|
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: 365.27 E-value: 1.43e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 1 MEYRQLGRSGLKIStitmgtmtiggggKFA--------QVGDVGVADASRHVDLCLDAGVNLIDTADIYSTGVCEEIIGE 72
Cdd:COG0667 1 MEYRRLGRSGLKVS-------------RLGlgtmtfggPWGGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 73 VLGGKRKDGVLIATKARFSMGPGPNDGGLSRHHLISACEASLKRLKTDVIDLYQVHEWDGQTPLEETMEALDTLVRQGKV 152
Cdd:COG0667 68 ALKGRPRDDVVIATKVGRRMGPGPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 153 RYIGCSNYSGWHIMKALGVSalDKRQRFVSQQIHYTLEAREAEYELVPISIDQGLGILVWSPLAGGLLSGKHRRGQS-PE 231
Cdd:COG0667 148 RYIGVSNYSAEQLRRALAIA--EGLPPIVAVQNEYSLLDRSAEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGATfPE 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500691625 232 GTRQLAGWNEPpiRDEERLWKIVDILVAIAAERGVSPAQVALAWLIGRQAVTSVIIGGRTEQQFRDNLAAAG 303
Cdd:COG0667 226 GDRAATNFVQG--YLTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAAD 295
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
1-302 |
6.49e-120 |
|
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: 348.41 E-value: 6.49e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 1 MEYRQLGRSGLKISTITMGTMTiggggkFAqvGDVGVADASRHVDLCLDAGVNLIDTADIYSTGVCEEIIGEVLGGKRKD 80
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGTMN------FG--GRTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAGRRDD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 81 gVLIATKARFSMGPGPNDGGLSRHHLISACEASLKRLKTDVIDLYQVHEWDGQTPLEETMEALDTLVRQGKVRYIGCSNY 160
Cdd:cd19087 73 -IVLATKVFGPMGDDPNDRGLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 161 SGWHIMKALGVSALDKRQRFVSQQIHYTLEAREAEYELVPISIDQGLGILVWSPLAGGLLSGKHRRGQSPEGTRQLAGWN 240
Cdd:cd19087 152 AAWQIAKAQGIAARRGLLRFVSEQPMYNLLKRQAELEILPAARAYGLGVIPYSPLAGGLLTGKYGKGKRPESGRLVERAR 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500691625 241 EPPIRDEERLWKIVDILVAIAAERGVSPAQVALAWLIGRQAVTSVIIGGRTEQQFRDNLAAA 302
Cdd:cd19087 232 YQARYGLEEYRDIAERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAAL 293
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
2-301 |
1.09e-106 |
|
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: 314.91 E-value: 1.09e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 2 EYRQLGRSGLKIStitmgtmtiggggKFA----QVGD-------VGVADASRHVDLCLDAGVNLIDTADIYSTGVCEEII 70
Cdd:cd19079 1 EYVRLGNSGLKVS-------------RLClgcmSFGDpkwrpwvLDEEESRPIIKRALDLGINFFDTANVYSGGASEEIL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 71 GEVLGG-KRKDGVLIATKARFSMGPGPNDGGLSRHHLISACEASLKRLKTDVIDLYQVHEWDGQTPLEETMEALDTLVRQ 149
Cdd:cd19079 68 GRALKEfAPRDEVVIATKVYFPMGDGPNGRGLSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 150 GKVRYIGCSNYSGWHIMKALGVSALDKRQRFVSQQIHYTLEAREAEYELVPISIDQGLGILVWSPLAGGLLSGKHRRGQS 229
Cdd:cd19079 148 GKVRYIGASSMYAWQFAKALHLAEKNGWTKFVSMQNHYNLLYREEEREMIPLCEEEGIGVIPWSPLARGRLARPWGDTTE 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500691625 230 -PEGTRQLAGWNEppIRDEERLWKIVDILVAIAAERGVSPAQVALAWLIGRQAVTSVIIGGRTEQQFRDNLAA 301
Cdd:cd19079 228 rRRSTTDTAKLKY--DYFTEADKEIVDRVEEVAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAA 298
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
5-303 |
3.80e-105 |
|
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: 310.69 E-value: 3.80e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 5 QLGRSGLKISTItmgtmtiggggkfaQVG------DVGVADASRHVDLCLDAGVNLIDTADIYST-------GVCEEIIG 71
Cdd:cd19081 1 PLGRTGLSVSPL--------------CLGtmvfgwTADEETSFALLDAFVDAGGNFIDTADVYSAwvpgnagGESETIIG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 72 EVLG--GKRKDgVLIATKARFSMGPgpNDGGLSRHHLISACEASLKRLKTDVIDLYQVHEWDGQTPLEETMEALDTLVRQ 149
Cdd:cd19081 67 RWLKsrGKRDR-VVIATKVGFPMGP--NGPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 150 GKVRYIGCSNYSGWHIMKALGVSALDKRQRFVSQQIHYTLEARE-AEYELVPISIDQGLGILVWSPLAGGLLSGKHRRGQ 228
Cdd:cd19081 144 GKVRYIGASNYSAWRLQEALELSRQHGLPRYVSLQPEYNLVDREsFEGELLPLCREEGIGVIPYSPLAGGFLTGKYRSEA 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500691625 229 SPEGTRQLAGWNEppIRDEERLWKIVDILVAIAAERGVSPAQVALAWLIGRQAVTSVIIGGRTEQQFRDNLAAAG 303
Cdd:cd19081 224 DLPGSTRRGEAAK--RYLNERGLRILDALDEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAG 296
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
39-303 |
3.06e-92 |
|
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: 277.55 E-value: 3.06e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 39 DASRHVDLCLDAGVNLIDTADIYSTGVCEEIIGEVLGGKRKDGVLIATKARFSMGPGPNDGGLSRHHLISACEASLKRLK 118
Cdd:cd19074 23 DAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALKGWPRESYVISTKVFWPTGPGPNDRGLSRKHIFESIHASLKRLQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 119 TDVIDLYQVHEWDGQTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALGVSALDKRQRFVSQQIHYTLEAREAEYEL 198
Cdd:cd19074 103 LDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLARQFGLIPPVVEQPQYNMLWREIEEEV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 199 VPISIDQGLGILVWSPLAGGLLSGKHRRGQS-PEGTRQLAGWNEPPIRD---EERLWKiVDILVAIAAERGVSPAQVALA 274
Cdd:cd19074 183 IPLCEKNGIGLVVWSPLAQGLLTGKYRDGIPpPSRSRATDEDNRDKKRRlltDENLEK-VKKLKPIADELGLTLAQLALA 261
|
250 260
....*....|....*....|....*....
gi 500691625 275 WLIGRQAVTSVIIGGRTEQQFRDNLAAAG 303
Cdd:cd19074 262 WCLRNPAVSSAIIGASRPEQLEENVKASG 290
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
38-301 |
1.16e-90 |
|
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: 273.71 E-value: 1.16e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 38 ADASRHVDLCLDAGVNLIDTADIYSTGVCEEIIGEVLGGKRkDGVLIATKARFSMGPG-PNDGGLSRHHLISACEASLKR 116
Cdd:cd19080 31 EEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAGNR-DRIVLATKYTMNRRPGdPNAGGNHRKNLRRSVEASLRR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 117 LKTDVIDLYQVHEWDGQTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALGVSALDKRQRFVSQQIHYTLEAREAEY 196
Cdd:cd19080 110 LQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDTPAWVVARANTLAELRGWSPFVALQIEYSLLERTPER 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 197 ELVPISIDQGLGILVWSPLAGGLLSGKHRRGQSPEGTRQLAGWNEPPIRDeERLWKIVDILVAIAAERGVSPAQVALAWL 276
Cdd:cd19080 190 ELLPMARALGLGVTPWSPLGGGLLTGKYQRGEEGRAGEAKGVTVGFGKLT-ERNWAIVDVVAAVAEELGRSAAQVALAWV 268
|
250 260
....*....|....*....|....*
gi 500691625 277 IGRQAVTSVIIGGRTEQQFRDNLAA 301
Cdd:cd19080 269 RQKPGVVIPIIGARTLEQLKDNLGA 293
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
33-303 |
3.99e-88 |
|
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: 266.70 E-value: 3.99e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 33 GDVGVADASRHVDLCLDAGVNLIDTADIYSTGVCEEIIGEVLGGKRKDgVLIATKARFSMGPGPNDG-GLSRHHLISACE 111
Cdd:cd19084 20 GEVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKGRRDD-VVIATKCGLRWDGGKGVTkDLSPESIRKEVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 112 ASLKRLKTDVIDLYQVHEWDGQTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALGVSaldkrqRFVSQQIHYTLEA 191
Cdd:cd19084 99 QSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEARKYG------PIVSLQPPYSMLE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 192 REAEYELVPISIDQGLGILVWSPLAGGLLSGKHRRGQSPEGT--RQLAGWNEPPIRdeERLWKIVDILVAIAAERGVSPA 269
Cdd:cd19084 173 REIEEELLPYCRENGIGVLPYGPLAQGLLTGKYKKEPTFPPDdrRSRFPFFRGENF--EKNLEIVDKLKEIAEKYGKSLA 250
|
250 260 270
....*....|....*....|....*....|....
gi 500691625 270 QVALAWLIGRQAVTSVIIGGRTEQQFRDNLAAAG 303
Cdd:cd19084 251 QLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALD 284
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
33-303 |
3.38e-77 |
|
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: 238.64 E-value: 3.38e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 33 GDVGVADASRHVDLCLDAGVNLIDTADIYSTGVCEEIIGEVLGGKRKDgVLIATKArFSMGPGPNDgglsrhhLISACEA 112
Cdd:cd19085 18 GDQDDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKGRRDD-VVIATKV-SPDNLTPED-------VRKSCER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 113 SLKRLKTDVIDLYQVHeW-DGQTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALGVSaldkrqRFVSQQIHYTLEA 191
Cdd:cd19085 89 SLKRLGTDYIDLYQIH-WpSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAG------RIDSNQLPYNLLW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 192 REAEYELVPISIDQGLGILVWSPLAGGLLSGK-HRRGQSPEGTRQ--LAGWNEPPIrdEERLWKIVDILVAIAAERGVSP 268
Cdd:cd19085 162 RAIEYEILPFCREHGIGVLAYSPLAQGLLTGKfSSAEDFPPGDARtrLFRHFEPGA--EEETFEALEKLKEIADELGVTM 239
|
250 260 270
....*....|....*....|....*....|....*
gi 500691625 269 AQVALAWLIGRQAVTSVIIGGRTEQQFRDNLAAAG 303
Cdd:cd19085 240 AQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVD 274
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
38-302 |
1.67e-76 |
|
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: 236.82 E-value: 1.67e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 38 ADASRHVDLCLDAGVNLIDTADIYSTGVCEEIIGEVLGG--KRKDGVLIATKARfsMGPGPNDGGLSRHHLISACEASLK 115
Cdd:pfam00248 18 EEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDypVKRDKVVIATKVP--DGDGPWPSGGSKENIRKSLEESLK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 116 RLKTDVIDLYQVHEWDGQTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALgvsaLDKRQRFVSQQIHYTLEAREAE 195
Cdd:pfam00248 96 RLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKAL----TKGKIPIVAVQVEYNLLRRRQE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 196 YELVPISIDQGLGILVWSPLAGGLLSGKHRRGQSPEGTRQLagWNEPPIRDEERLWkiVDILVAIAAERGVSPAQVALAW 275
Cdd:pfam00248 172 EELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPGERR--RLLKKGTPLNLEA--LEALEEIAKEHGVSPAQVALRW 247
|
250 260
....*....|....*....|....*..
gi 500691625 276 LIGRQAVTSVIIGGRTEQQFRDNLAAA 302
Cdd:pfam00248 248 ALSKPGVTIPIPGASNPEQLEDNLGAL 274
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
33-300 |
4.60e-76 |
|
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: 233.95 E-value: 4.60e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 33 GDVGVADASRHVDLCLDAGVNLIDTADIYSTGVCEEIIGEVLGGKRK-DGVLIATKARFSMGPGPNDGGLSRHHLISACE 111
Cdd:cd06660 12 GDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRGNrDDVVIATKGGHPPGGDPSRSRLSPEHIRRDLE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 112 ASLKRLKTDVIDLYQVHEWDGQTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALGVSALDKRQRFVSQQIHYTL-E 190
Cdd:cd06660 92 ESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKAHGLPGFAAVQPQYSLlD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 191 AREAEYELVPISIDQGLGILVWSPLAGGllsgkhrrgqspegtrqlagwneppirdeerlwkivdilvaiaaergvsPAQ 270
Cdd:cd06660 172 RSPMEEELLDWAEENGLPLLAYSPLARG-------------------------------------------------PAQ 202
|
250 260 270
....*....|....*....|....*....|
gi 500691625 271 VALAWLIGRQAVTSVIIGGRTEQQFRDNLA 300
Cdd:cd06660 203 LALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
1-301 |
4.78e-72 |
|
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: 226.71 E-value: 4.78e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 1 MEYRQLGRSGLKISTITMGtmtiggggkfAQV---GDVGVADASRHVDLCLDAGVNLIDTADIYSTGVCEEIIGEVL--G 75
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFG----------SWVtfgNQVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIkeL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 76 GKRKDGVLIATKARFSM-GPGPNDGGLSRHHLISACEASLKRLKTDVIDLYQVHEWDGQTPLEETMEALDTLVRQGKVRY 154
Cdd:cd19143 71 GWPRSDYVVSTKIFWGGgGPPPNDRGLSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 155 IGCSNYSGWHIMKALGVSALDKRQRFVSQQIHYTLEARE-AEYELVPISIDQGLGILVWSPLAGGLLSGKHRRGqSPEGT 233
Cdd:cd19143 151 WGTSEWSAQQIEEAHEIADRLGLIPPVMEQPQYNLFHRErVEVEYAPLYEKYGLGTTTWSPLASGLLTGKYNNG-IPEGS 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500691625 234 R-QLAGW-NEPPIRDEERLWKI--VDILVAIAAERGVSPAQVALAWLIGRQAVTSVIIGGRTEQQFRDNLAA 301
Cdd:cd19143 230 RlALPGYeWLKDRKEELGQEKIekVRKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEENLKA 301
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
38-302 |
2.14e-70 |
|
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: 222.44 E-value: 2.14e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 38 ADASRHVDLCLDAGVNLIDTADIYST-------GVCEEIIGEVLGGKRK-DGVLIATKA----RFSMGPGPNDGGLSRHH 105
Cdd:cd19094 18 AEAHEQLDYAFDEGVNFIDTAEMYPVppspetqGRTEEIIGSWLKKKGNrDKVVLATKVagpgEGITWPRGGGTRLDREN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 106 LISACEASLKRLKTDVIDLYQVH------------------EWDGQTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMK 167
Cdd:cd19094 98 IREAVEGSLKRLGTDYIDLYQLHwpdrytplfgggyytepsEEEDSVSFEEQLEALGELVKAGKIRHIGLSNETPWGVMK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 168 ALGVSALDKRQRFVSQQIHYTLEAREAEYELVPISIDQGLGILVWSPLAGGLLSGKHRRGQS-PEGTRQLAGWNEPPIRD 246
Cdd:cd19094 178 FLELAEQLGLPRIVSIQNPYSLLNRNFEEGLAEACHRENVGLLAYSPLAGGVLTGKYLDGAArPEGGRLNLFPGYMARYR 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 500691625 247 EERLWKIVDILVAIAAERGVSPAQVALAWLIGRQAVTSVIIGGRTEQQFRDNLAAA 302
Cdd:cd19094 258 SPQALEAVAEYVKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLKENIDAF 313
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
3-302 |
4.84e-63 |
|
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381375 [Multi-domain] Cd Length: 315 Bit Score: 203.27 E-value: 4.84e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 3 YRQLGRSGLKISTITmgtmtiggggkFAQ--------VGDVGVADASRHVDLCLDAGVNLIDTADIYSTGVCEEIIGEVL 74
Cdd:cd19149 1 YRKLGKSGIEASVIG-----------LGTwaigggpwWGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 75 GGKRKDgVLIATKarFSMGPGPNDGG-------------LSRHHLISACEASLKRLKTDVIDLYQVHEWDGQTPLEETME 141
Cdd:cd19149 70 KGRRDK-VVLATK--CGLRWDREGGSfffvrdgvtvyknLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETME 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 142 ALDTLVRQGKVRYIGCSNYSGWHIMKALGVSALDkrqrfvSQQIHYTLEAREAEYELVPISIDQGLGILVWSPLAGGLLS 221
Cdd:cd19149 147 ALEELKRQGKIRAIGASNVSVEQIKEYVKAGQLD------IIQEKYSMLDRGIEKELLPYCKKNNIAFQAYSPLEQGLLT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 222 GKHRRGQSPEGTRQLAG--WNEPpirdeERLWKIVDILVA---IAAERGVSPAQVALAWLIGRQAVTSVIIGGRTEQQFR 296
Cdd:cd19149 221 GKITPDREFDAGDARSGipWFSP-----ENREKVLALLEKwkpLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPEQAE 295
|
....*.
gi 500691625 297 DNLAAA 302
Cdd:cd19149 296 ENAKAG 301
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
48-303 |
5.45e-63 |
|
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: 202.52 E-value: 5.45e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 48 LDAGVNLIDTADIYSTGVCEEIIGEVLGGkRKDGVLIATK-ARFSMGPGPNDGGLSRHHLISACEASLKRLKTDVIDLYQ 126
Cdd:cd19102 36 LDLGINWIDTAAVYGLGHSEEVVGRALKG-LRDRPIVATKcGLLWDEEGRIRRSLKPASIRAECEASLRRLGVDVIDLYQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 127 VHEWDGQTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALGVSALDkrqrfvSQQIHYTLEAREAEYELVPISIDQG 206
Cdd:cd19102 115 IHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQAIHPIA------SLQPPYSLLRRGIEAEILPFCAEHG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 207 LGILVWSPLAGGLLSGKhrrgQSPEGTRQLAgWNEPPIRD----EERL---WKIVDILVAIAAERGVSPAQVALAWLIGR 279
Cdd:cd19102 189 IGVIVYSPMQSGLLTGK----MTPERVASLP-ADDWRRRSpffqEPNLarnLALVDALRPIAERHGRTVAQLAIAWVLRR 263
|
250 260
....*....|....*....|....
gi 500691625 280 QAVTSVIIGGRTEQQFRDNLAAAG 303
Cdd:cd19102 264 PEVTSAIVGARRPDQIDETVGAAD 287
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
3-302 |
9.53e-62 |
|
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: 199.79 E-value: 9.53e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 3 YRQLGRSGLKISTITMGTMTIggggkFaqvGDVGVADASRHVDLC-LDAGVNLIDTADIY--STGVCEEIIGEVL---GG 76
Cdd:cd19089 1 YRRCGRSGLHLPAISLGLWHN-----F---GDYTSPEEARELLRTaFDLGITHFDLANNYgpPPGSAEENFGRILkrdLR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 77 KRKDGVLIATKARFSMGPGPNDGGLSRHHLISACEASLKRLKTDVIDLYQVHEWDGQTPLEETMEALDTLVRQGKVRYIG 156
Cdd:cd19089 73 PYRDELVISTKAGYGMWPGPYGDGGSRKYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 157 CSNYSGWHIMKALGVsaLDKRQ-RFVSQQIHYTLEAREAEYELVPISIDQGLGILVWSPLAGGLLSGKHRRGqSPEGTRQ 235
Cdd:cd19089 153 ISNYPGAKARRAIAL--LRELGvPLIIHQPRYSLLDRWAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKYLNG-IPPDSRR 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500691625 236 LA--GWNEPPIRDEERLWKIvDILVAIAAERGVSPAQVALAWLIGRQAVTSVIIGGRTEQQFRDNLAAA 302
Cdd:cd19089 230 AAesKFLTEEALTPEKLEQL-RKLNKIAAKRGQSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAAL 297
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
4-302 |
4.92e-59 |
|
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: 192.63 E-value: 4.92e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 4 RQLGRSGLKISTITMGTMTIGGGGKFAQVGDvgvADASRHVDLCLDAGVNLIDTADIYSTGVCEEIIGEVLGGKRKDGVL 83
Cdd:cd19083 2 VKLGKSDIDVNPIGLGTNAVGGHNLYPNLDE---EEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLKEYNRNEVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 84 IATKARFSMGPGPNDGGLSRHHLISACEASLKRLKTDVIDLYQVHEWDGQTPLEETMEALDTLVRQGKVRYIGCSNYSGW 163
Cdd:cd19083 79 IATKGAHKFGGDGSVLNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFSLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 164 HIMKALGVSALDKRQRfvsqqiHYTLEAREAEYELVPISIDQGLGILVWSPLAGGLLSGKHRRGQS--PEGTRqlagwNE 241
Cdd:cd19083 159 QLKEANKDGYVDVLQG------EYNLLQREAEEDILPYCVENNISFIPYFPLASGLLAGKYTKDTKfpDNDLR-----ND 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500691625 242 PPIRDEERLWKI---VDILVAIAAERGVSPAQVALAWLIGRQAVTSVIIGGRTEQQFRDNLAAA 302
Cdd:cd19083 228 KPLFKGERFSENldkVDKLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKAL 291
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
33-301 |
3.47e-58 |
|
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: 188.07 E-value: 3.47e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 33 GDVGVADASRHVDLCLDAGVNLIDTADIYSTGVCEEIIGEVLGGKRKDgVLIATKARFSMGPGPNDG-GLSRHHLISACE 111
Cdd:cd19086 19 GDVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKGRRDK-VVIATKFGNRFDGGPERPqDFSPEYIREAVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 112 ASLKRLKTDVIDLYQVHEW-DGQTPLEETMEALDTLVRQGKVRYIGCS---NYSGWHIMKALGVSALdkrqrfvsqQIHY 187
Cdd:cd19086 98 ASLKRLGTDYIDLYQLHNPpDEVLDNDELFEALEKLKQEGKIRAYGVSvgdPEEALAALRRGGIDVV---------QVIY 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 188 TLEAREAEYELVPISIDQGLGILVWSPLAGGLLSGKhrrgqspegtrqlagwneppirdeerlwkivdilvaiaaergvs 267
Cdd:cd19086 169 NLLDQRPEEELFPLAEEHGVGVIARVPLASGLLTGK-------------------------------------------- 204
|
250 260 270
....*....|....*....|....*....|....
gi 500691625 268 PAQVALAWLIGRQAVTSVIIGGRTEQQFRDNLAA 301
Cdd:cd19086 205 LAQAALRFILSHPAVSTVIPGARSPEQVEENAAA 238
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
33-303 |
3.64e-57 |
|
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: 187.44 E-value: 3.64e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 33 GDVGVADASRHVDLCLDAGVNLIDTADIYSTGVCEEIIGEVLGG-KRKDGVLIATKarfsMGPGPNDggLSRHHLISACE 111
Cdd:cd19093 21 GEYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKElGDRDEVVIATK----FAPLPWR--LTRRSVVKALK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 112 ASLKRLKTDVIDLYQVH---EWDGQtpLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKAlgVSALDKRQ-RFVSQQIHY 187
Cdd:cd19093 95 ASLERLGLDSIDLYQLHwpgPWYSQ--IEALMDGLADAVEEGLVRAVGVSNYSADQLRRA--HKALKERGvPLASNQVEY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 188 TLEAREAE-YELVPISIDQGLGILVWSPLAGGLLSGKHRRGQSPEGTRQLagwnEPPIRDEERLWKIVDILVAIAAERGV 266
Cdd:cd19093 171 SLLYRDPEqNGLLPACDELGITLIAYSPLAQGLLTGKYSPENPPPGGRRR----LFGRKNLEKVQPLLDALEEIAEKYGK 246
|
250 260 270
....*....|....*....|....*....|....*..
gi 500691625 267 SPAQVALAWLIGRQAVtsVIIGGRTEQQFRDNLAAAG 303
Cdd:cd19093 247 TPAQVALNWLIAKGVV--PIPGAKNAEQAEENAGALG 281
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
48-302 |
1.32e-55 |
|
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: 183.57 E-value: 1.32e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 48 LDAGVNLIDTADIYSTGVCEEIIGEVLGGKRKDgVLIATKARFSMGPGPNDGGL--SRHHLISACEASLKRLKTDVIDLY 125
Cdd:cd19076 42 LELGVTFLDTADMYGPGTNEELLGKALKDRRDE-VVIATKFGIVRDPGSGFRGVdgRPEYVRAACEASLKRLGTDVIDLY 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 126 QVHEWDGQTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALGV---SALdkrqrfvsqQIHYTLEAREAEYELVPIS 202
Cdd:cd19076 121 YQHRVDPNVPIEETVGAMAELVEEGKVRYIGLSEASADTIRRAHAVhpiTAV---------QSEYSLWTRDIEDEVLPTC 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 203 IDQGLGILVWSPLAGGLLSGKHRR-GQSPEGTRQlaGWNePPIRDE--ERLWKIVDILVAIAAERGVSPAQVALAWLIGR 279
Cdd:cd19076 192 RELGIGFVAYSPLGRGFLTGAIKSpEDLPEDDFR--RNN-PRFQGEnfDKNLKLVEKLEAIAAEKGCTPAQLALAWVLAQ 268
|
250 260
....*....|....*....|...
gi 500691625 280 QAVTSVIIGGRTEQQFRDNLAAA 302
Cdd:cd19076 269 GDDIVPIPGTKRIKYLEENVGAL 291
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
2-301 |
1.97e-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: 183.37 E-value: 1.97e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 2 EYRQLGRSGLKISTITMGTmtiggggkFAQVGDVGVADASRH-VDLCLDAGVNLIDTADIYS--TGVCEEIIGEVLGG-- 76
Cdd:cd19151 1 KYNRCGRSGLKLPAISLGL--------WHNFGDVDRYENSRAmLRRAFDLGITHFDLANNYGppPGSAEENFGRILKEdl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 77 -KRKDGVLIATKARFSMGPGP-NDGGlSRHHLISACEASLKRLKTDVIDLYQVHEWDGQTPLEETMEALDTLVRQGKVRY 154
Cdd:cd19151 73 kPYRDELIISTKAGYTMWPGPyGDWG-SKKYLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 155 IGCSNYS------GWHIMKALGVSALdkrqrfvsqqIH---YTLEAREAEYELVPISIDQGLGILVWSPLAGGLLSGKHR 225
Cdd:cd19151 152 VGISNYPpeeareAAAILKDLGTPCL----------IHqpkYSMFNRWVEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYL 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500691625 226 RGqSPEGTRQLAGW---NEPPIrDEERLWKiVDILVAIAAERGVSPAQVALAWLIGRQAVTSVIIGGRTEQQFRDNLAA 301
Cdd:cd19151 222 NG-IPEDSRAAKGSsflKPEQI-TEEKLAK-VRRLNEIAQARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGA 297
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
29-301 |
1.07e-54 |
|
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: 181.22 E-value: 1.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 29 FAQVGDVGVADASRH-VDLCLDAGVNLIDTADIYSTGVCEEIIGEVLGGKRkdGVLIATKArfsmgPGPNDGGLSRHHLI 107
Cdd:cd19075 10 FGSQGRFTTAEAAAElLDAFLERGHTEIDTARVYPDGTSEELLGELGLGER--GFKIDTKA-----NPGVGGGLSPENVR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 108 SACEASLKRLKTDVIDLYQVHEWDGQTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKalgVSALDKRQRFVSQ---Q 184
Cdd:cd19075 83 KQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAE---IVEICKENGWVLPtvyQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 185 IHYTLEAREAEYELVPISIDQGLGILVWSPLAGGLLSGKHRRGQ-SPEGTR-----QLAGWneppIRDeeRLWK-----I 253
Cdd:cd19075 160 GMYNAITRQVETELFPCLRKLGIRFYAYSPLAGGFLTGKYKYSEdKAGGGRfdpnnALGKL----YRD--RYWKpsyfeA 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 500691625 254 VDILVAIAAERGVSPAQVALAWLIGRQAVTS-----VIIGGRTEQQFRDNLAA 301
Cdd:cd19075 234 LEKVEEAAEKEGISLAEAALRWLYHHSALDGekgdgVILGASSLEQLEENLAA 286
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
48-303 |
1.60e-54 |
|
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: 179.73 E-value: 1.60e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 48 LDAGVNLIDTADIYSTGVCEEIIGEVLGGKRKDGVLIATKarFSmgpgPNdgGLSRHHLISACEASLKRLKTDVIDLYQV 127
Cdd:cd19072 36 IELGINLIDTAEMYGGGHAEELVGKAIKGFDREDLFITTK--VS----PD--HLKYDDVIKAAKESLKRLGTDYIDLYLI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 128 HEWDGQTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALGVSaldKRQRFVSQQIHYTLEAREAEYELVPISIDQGL 207
Cdd:cd19072 108 HWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYL---KKGPIVANQVEYNLFDREEESGLLPYCQKNGI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 208 GILVWSPLAGGLLSGKHRRGqspegtrqlagwneppirdeerlwkivdILVAIAAERGVSPAQVALAWLIgRQAVTSVII 287
Cdd:cd19072 185 AIIAYSPLEKGKLSNAKGSP----------------------------LLDEIAKKYGKTPAQIALNWLI-SKPNVIAIP 235
|
250
....*....|....*.
gi 500691625 288 GGRTEQQFRDNLAAAG 303
Cdd:cd19072 236 KASNIEHLEENAGALG 251
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
48-303 |
2.74e-51 |
|
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: 170.86 E-value: 2.74e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 48 LDAGVNLIDTADIYSTGVCEEIIGEVLGGkRKDGVLIATKA---RfsmgPGPNDGGL--SRHHLISACEASLKRLKTDVI 122
Cdd:cd19088 34 LELGVNFIDTADSYGPDVNERLIAEALHP-YPDDVVIATKGglvR----TGPGWWGPdgSPEYLRQAVEASLRRLGLDRI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 123 DLYQVHEWDGQTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALGVSaldkrqRFVSQQIHYTLEAREAEyELVPIS 202
Cdd:cd19088 109 DLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAIV------RIVSVQNRYNLANRDDE-GVLDYC 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 203 IDQGLGILVWSPLAGGLLSGKHRRGQSpegtrqlagwneppirdeerlwkivdilvaIAAERGVSPAQVALAWLIGRQAV 282
Cdd:cd19088 182 EAAGIAFIPWFPLGGGDLAQPGGLLAE------------------------------VAARLGATPAQVALAWLLARSPV 231
|
250 260
....*....|....*....|.
gi 500691625 283 TSVIIGGRTEQQFRDNLAAAG 303
Cdd:cd19088 232 MLPIPGTSSVEHLEENLAAAG 252
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
45-303 |
1.01e-47 |
|
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: 162.89 E-value: 1.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 45 DLCLDAGVNLIDTADIYST-------GVCEEIIGEVLG--GKRkDGVLIATKARFsMGPGPNDG-----GLSRHHLISAC 110
Cdd:cd19752 24 DRYVAAGGNFLDTANNYAFwteggvgGESERLIGRWLKdrGNR-DDVVIATKVGA-GPRDPDGGpespeGLSAETIEQEI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 111 EASLKRLKTDVIDLYQVHEWDGQTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALGVSALDKRQRFVSQQIHYT-L 189
Cdd:cd19752 102 DKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERARQIARQQGWAEFSAIQQRHSyL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 190 EAREAEYELVPISIDQ----------GLGILVWSPLAGGLLS--GKHRRGQ--SPEGTRQLAgwneppirdeerlwkivd 255
Cdd:cd19752 182 RPRPGADFGVQRIVTDelldyassrpDLTLLAYSPLLSGAYTrpDRPLPEQydGPDSDARLA------------------ 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 500691625 256 ILVAIAAERGVSPAQVALAWLIGRQAVTSVIIGGRTEQQFRDNLAAAG 303
Cdd:cd19752 244 VLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAALD 291
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
48-302 |
3.14e-47 |
|
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: 161.63 E-value: 3.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 48 LDAGVNLIDTADIYSTGVCEEIIGEVLGGKRkDGVLIATKARFSMGPG-PNDGGL--SRHHLISACEASLKRLKTDVIDL 124
Cdd:cd19078 35 VELGITFFDTAEVYGPYTNEELVGEALKPFR-DQVVIATKFGFKIDGGkPGPLGLdsRPEHIRKAVEGSLKRLQTDYIDL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 125 YQVHEWDGQTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKA---LGVSALdkrqrfvsqQIHYTLEAREAEYELVPI 201
Cdd:cd19078 114 YYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETIRRAhavCPVTAV---------QSEYSMMWREPEKEVLPT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 202 SIDQGLGILVWSPLAGGLLSGK-----------HRRGQ---SPEGTRQlagwNEPpirdeerlwkIVDILVAIAAERGVS 267
Cdd:cd19078 185 LEELGIGFVPFSPLGKGFLTGKidentkfdegdDRASLprfTPEALEA----NQA----------LVDLLKEFAEEKGAT 250
|
250 260 270
....*....|....*....|....*....|....*
gi 500691625 268 PAQVALAWLIGRQAVTSVIIGGRTEQQFRDNLAAA 302
Cdd:cd19078 251 PAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAA 285
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
38-299 |
6.50e-47 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 162.33 E-value: 6.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 38 ADASRHVDLCLDAGVNLIDTADIY-------STGVCEEIIGEVL---GGKRKdgVLIATKArfsmgPGP---NDGG---- 100
Cdd:PRK10625 30 ADAHAQLDYAVAQGINLIDVAEMYpvpprpeTQGLTETYIGNWLakrGSREK--LIIASKV-----SGPsrnNDKGirpn 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 101 --LSRHHLISACEASLKRLKTDVIDLYQVH--------------EWDGQTP---LEETMEALDTLVRQGKVRYIGCSNYS 161
Cdd:PRK10625 103 qaLDRKNIREALHDSLKRLQTDYLDLYQVHwpqrptncfgklgySWTDSAPavsLLETLDALAEQQRAGKIRYIGVSNET 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 162 GWHIMKALGVSALDKRQRFVSQQIHYTLEAREAEYELVPISIDQGLGILVWSPLAGGLLSGKHRRGQSPEGTRQLAgWNE 241
Cdd:PRK10625 183 AFGVMRYLHLAEKHDLPRIVTIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLAFGTLTGKYLNGAKPAGARNTL-FSR 261
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 500691625 242 PPIRDEERLWKIVDILVAIAAERGVSPAQVALAWLIGRQAVTSVIIGGRTEQQFRDNL 299
Cdd:PRK10625 262 FTRYSGEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLLGATTMEQLKTNI 319
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
3-301 |
4.75e-46 |
|
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: 159.16 E-value: 4.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 3 YRQLGRSGLKISTITMGTmtiggggkFAQVGDVGVADASRhvDLC---LDAGVNLIDTADIYST--GVCEEIIGEVLG-- 75
Cdd:cd19150 2 YRRCGKSGLKLPALSLGL--------WHNFGDDTPLETQR--AILrtaFDLGITHFDLANNYGPppGSAEENFGRILRed 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 76 -GKRKDGVLIATKARFSMGPGPNDGGLSRHHLISACEASLKRLKTDVIDLYQVHEWDGQTPLEETMEALDTLVRQGKVRY 154
Cdd:cd19150 72 fAGYRDELIISTKAGYDMWPGPYGEWGSRKYLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 155 IGCSNYS------GWHIMKALGVSALdkrqrfvsqqIH---YTLEAREAE-YELVPISIDQGLGILVWSPLAGGLLSGKH 224
Cdd:cd19150 152 VGISSYSpertreAAAILRELGTPLL----------IHqpsYNMLNRWVEeSGLLDTLQELGVGCIAFTPLAQGLLTDKY 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500691625 225 RRGqSPEGTRQLAGWNEPPIRDEERLWKIVDILVAIAAERGVSPAQVALAWLIGRQAVTSVIIGGRTEQQFRDNLAA 301
Cdd:cd19150 222 LNG-IPEGSRASKERSLSPKMLTEANLNSIRALNEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGA 297
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
38-302 |
9.17e-45 |
|
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: 155.02 E-value: 9.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 38 ADASRHVDLCLDAGVNLIDTADIYS----TGVCEEIIGEVLG--GKRKDgVLIATKarfsmG--PGPNDGG---LSRHHL 106
Cdd:cd19082 17 EEAFALLDAFVELGGNFIDTARVYGdwveRGASERVIGEWLKsrGNRDK-VVIATK-----GghPDLEDMSrsrLSPEDI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 107 ISACEASLKRLKTDVIDLYQVHEWDGQTPLEETMEALDTLVRQGKVRYIGCSNysgWHI--MKALGVSALDK-RQRFVSQ 183
Cdd:cd19082 91 RADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASN---WSTerIAEANAYAKAHgLPGFAAS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 184 QIHYTL----EAREAEYELVPISID-------QGLGILVWSPLAGGLLSGKHRRGQSPEGTRQLAGWNEPpirDEERLwk 252
Cdd:cd19082 168 SPQWSLarpnEPPWPGPTLVAMDEEmrawheeNQLPVFAYSSQARGFFSKRAAGGAEDDSELRRVYYSEE---NFERL-- 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 500691625 253 ivDILVAIAAERGVSPAQVALAWLIGRQAVTSVIIGGRTEQQFRDNLAAA 302
Cdd:cd19082 243 --ERAKELAEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAAA 290
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
1-301 |
6.58e-44 |
|
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: 153.66 E-value: 6.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 1 MEYRQLGRSGLKISTITMGTMTIGGggkfaqvGDVGVADASRHVDLCLDAGVNLIDTADIYSTGVCEEIIGEVLGGK--R 78
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTWVTFG-------GQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKgwR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 79 KDGVLIATKARFSmGPGPNDGGLSRHHLISACEASLKRLKTDVIDLYQVHEWDGQTPLEETMEALDTLVRQGKVRYIGCS 158
Cdd:cd19159 74 RSSLVITTKLYWG-GKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 159 NYSGWHIMKALGVSALDKRQRFVSQQIHYTLEARE-AEYELVPISIDQGLGILVWSPLAGGLLSGKHRRGqSPEGTR--- 234
Cdd:cd19159 153 RWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNG-VPESSRasl 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 235 QLAGWNEPPIRDEE---RLWKIVDiLVAIAAERGVSPAQVALAWLIGRQAVTSVIIGGRTEQQFRDNLAA 301
Cdd:cd19159 232 KCYQWLKERIVSEEgrkQQNKLKD-LSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 300
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
48-303 |
1.34e-43 |
|
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: 151.25 E-value: 1.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 48 LDAGVNLIDTADIYSTGVCEEIIGEVLGGKRKDgVLIATKARfsmgpgPNDGglSRHHLISACEASLKRLKTDVIDLYQV 127
Cdd:cd19138 39 IDLGMTLIDTAEMYGDGGSEELVGEAIRGRRDK-VFLVSKVL------PSNA--SRQGTVRACERSLRRLGTDYLDLYLL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 128 HeWDGQTPLEETMEALDTLVRQGKVRYIGCSNYsGWHIMKALgvSALDKRQRFVSQQIHYTLEAREAEYELVPISIDQGL 207
Cdd:cd19138 110 H-WRGGVPLAETVAAMEELKKEGKIRAWGVSNF-DTDDMEEL--WAVPGGGNCAANQVLYNLGSRGIEYDLLPWCREHGV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 208 GILVWSPLA-GGLLsgKHRRGQSPEgtrqlagwneppirdeerlwkivdiLVAIAAERGVSPAQVALAWLIGRQAVTSVI 286
Cdd:cd19138 186 PVMAYSPLAqGGLL--RRGLLENPT-------------------------LKEIAARHGATPAQVALAWVLRDGNVIAIP 238
|
250
....*....|....*..
gi 500691625 287 IGGRtEQQFRDNLAAAG 303
Cdd:cd19138 239 KSGS-PEHARENAAAAD 254
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
37-288 |
2.61e-43 |
|
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: 151.17 E-value: 2.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 37 VADASRHVDLCLDAGVNLIDTADIYSTGVCEEIIGEVL---GGKRkDGVLIATKA--RFSMGPGPNDGG---LSRHHLIS 108
Cdd:cd19092 23 AEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALalnPGLR-EKIEIQTKCgiRLGDDPRPGRIKhydTSKEHILA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 109 ACEASLKRLKTDVIDLYQVHEWDgqtPL---EETMEALDTLVRQGKVRYIGCSNYSGWHImkalgvSALDKR--QRFVSQ 183
Cdd:cd19092 102 SVEGSLKRLGTDYLDLLLLHRPD---PLmdpEEVAEAFDELVKSGKVRYFGVSNFTPSQI------ELLQSYldQPLVTN 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 184 QIHYTLeareaeYELVPIS---IDQ----GLGILVWSPLAGGLLSGKhrrgqspegtrqlagwneppirDEERLWKIVDI 256
Cdd:cd19092 173 QIELSL------LHTEAIDdgtLDYcqllDITPMAWSPLGGGRLFGG----------------------FDERFQRLRAA 224
|
250 260 270
....*....|....*....|....*....|..
gi 500691625 257 LVAIAAERGVSPAQVALAWLIGRQAVTSVIIG 288
Cdd:cd19092 225 LEELAEEYGVTIEAIALAWLLRHPARIQPILG 256
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
29-301 |
2.79e-42 |
|
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: 147.38 E-value: 2.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 29 FAQVGDVGVADASRHVDLCLDAGVNLIDTADIYstGVCEEIIGEVLGGKRKDGVLIATKARFSMGPGPNDGGLSRHHLIS 108
Cdd:cd19095 11 GRVWGVPSEAEAARLLNTALDLGINLIDTAPAY--GRSEERLGRALAGLRRDDLFIATKVGTHGEGGRDRKDFSPAAIRA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 109 ACEASLKRLKTDVIDLYQVHEWDGQTPLEETMEALDTLVRQGKVRYIGCSNYSGwHIMKALGVSALDkrqrFVsqQIHYT 188
Cdd:cd19095 89 SIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVSGDGE-ELEAAIASGVFD----VV--QLPYN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 189 LEAREAEyELVPISIDQGLGILVWSPLAGGLLSGKHRRGQSPEGTRQLAGWneppirdeerlwkivdilvaIAAERGVSP 268
Cdd:cd19095 162 VLDREEE-ELLPLAAEAGLGVIVNRPLANGRLRRRVRRRPLYADYARRPEF--------------------AAEIGGATW 220
|
250 260 270
....*....|....*....|....*....|...
gi 500691625 269 AQVALAWLIGRQAVTSVIIGGRTEQQFRDNLAA 301
Cdd:cd19095 221 AQAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
33-303 |
3.54e-42 |
|
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: 149.50 E-value: 3.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 33 GDVGVADASRHVDLCLDAGVNLIDTADIYSTGVCEEIIGEVLGGKR-KDGVLIATKarFSMGPGP--------NDGGLSR 103
Cdd:cd19146 30 GECDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMASRGnRDEMVLATK--YTTGYRRggpikiksNYQGNHA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 104 HHLISACEASLKRLKTDVIDLYQVHEWDGQTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALGVSALDKRQRFVSQ 183
Cdd:cd19146 108 KSLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSDTPAWVVSKANAYARAHGLTQFVVY 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 184 QIHYTLEAREAEYELVPISIDQGLGILVWSPLAGGllsgkHRRGQSPEGTRQLAGWNEPPIRDEERlwKIVDILVAIAAE 263
Cdd:cd19146 188 QGHWSAAFRDFERDILPMCEAEGMALAPWGVLGQG-----QFRTEEEFKRRGRSGRKGGPQTEKER--KVSEKLEKVAEE 260
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 500691625 264 RGVSPAQVALAWLIGRQAVTSVIIGGRTEQQFRDNLAAAG 303
Cdd:cd19146 261 KGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIEALG 300
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
1-301 |
1.00e-41 |
|
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: 148.00 E-value: 1.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 1 MEYRQLGRSGLKISTITMGTMTIggggkFAQVGDVGVADASrhVDLCLDAGVNLIDTADIYSTGVCEEIIGEVL--GGKR 78
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGTWST-----FSTAISEEQAEEI--VTLAYENGINYFDTSDAFTSGQAETELGRILkkKGWK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 79 KDGVLIATKARFSMGPgpNDGGLSRHHLISACEASLKRLKTDVIDLYQVHEWDGQTPLEETMEALDTLVRQGKVRYIGCS 158
Cdd:cd19142 74 RSSYIVSTKIYWSYGS--EERGLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 159 NYSGWHIMKALGVSaldkRQrF-----VSQQIHYTLEARE-AEYELVPISIDQGLGILVWSPLAGGLLSGKH-------R 225
Cdd:cd19142 152 RWSPVEIMEAFSIA----RQ-FncptpICEQSEYHMFCREkMELYMPELYNKVGVGLITWSPLSLGLDPGISeetrrlvT 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500691625 226 RGQSPEGTRQLAGWNEPPIRDEERLWKIVDILVAIAAERGVSPAQVALAWLIGRQAVTSVIIGGRTEQQFRDNLAA 301
Cdd:cd19142 227 KLSFKSSKYKVGSDGNGIHEETRRASHKLRELSLIAERLGCDLTQLLIAWSLKNENVQCVLIGASSLEQLYSQLNS 302
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
3-301 |
1.49e-41 |
|
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: 147.21 E-value: 1.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 3 YRQLGRSGLKISTITMGTMTIGGggkfAQVGDvgvADASRHVDLCLDAGVNLIDTADIYSTGVCEEIIGEVLGGK--RKD 80
Cdd:cd19141 2 YRNLGKSGLRVSCLGLGTWVTFG----SQISD---EVAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKgwRRS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 81 GVLIATKArFSMGPGPNDGGLSRHHLISACEASLKRLKTDVIDLYQVHEWDGQTPLEETMEALDTLVRQGKVRYIGCSNY 160
Cdd:cd19141 75 SYVITTKI-FWGGKAETERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 161 SGWHIMKALGVSaldkRQrF-----VSQQIHYTLEARE-AEYELVPISIDQGLGILVWSPLAGGLLSGKHRRGQSPEGTR 234
Cdd:cd19141 154 SAMEIMEAYSVA----RQ-FnlippIVEQAEYHLFQREkVEMQLPELFHKIGVGAMTWSPLACGILSGKYDDGVPEYSRA 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500691625 235 QLAG--WNEPPIRDEE--RLWKIVDILVAIAAERGVSPAQVALAWLIGRQAVTSVIIGGRTEQQFRDNLAA 301
Cdd:cd19141 229 SLKGyqWLKEKILSEEgrRQQAKLKELQIIADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQA 299
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
1-301 |
2.01e-41 |
|
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: 147.44 E-value: 2.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 1 MEYRQLGRSGLKISTITMGTMTIGGggkfAQVGDvgvADASRHVDLCLDAGVNLIDTADIYSTGVCEEIIGEVLGGK--R 78
Cdd:cd19160 3 MKYRNLGKSGLRVSCLGLGTWVTFG----SQISD---ETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKgwR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 79 KDGVLIATKArFSMGPGPNDGGLSRHHLISACEASLKRLKTDVIDLYQVHEWDGQTPLEETMEALDTLVRQGKVRYIGCS 158
Cdd:cd19160 76 RSSYVVTTKI-YWGGQAETERGLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 159 NYSGWHIMKALGVSALDKRQRFVSQQIHYTLEARE-AEYELVPISIDQGLGILVWSPLAGGLLSGKHrRGQSPEGTR-QL 236
Cdd:cd19160 155 RWSAMEIMEAYSVARQFNLIPPVCEQAEYHLFQREkVEMQLPELYHKIGVGSVTWSPLACGLITGKY-DGRVPDTCRaAV 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 237 AG--WNEPPIRDEE---RLWKIVDILvAIAAERGVSPAQVALAWLIGRQAVTSVIIGGRTEQQFRDNLAA 301
Cdd:cd19160 234 KGyqWLKEKVQSEEgkkQQAKVKELH-PIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGS 302
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
48-301 |
2.18e-41 |
|
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: 146.81 E-value: 2.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 48 LDAGVNLIDTADIYSTGVCEEIIGEVLGGKRKDGVLIATK--ARFSMGPGPNDGGlSRHHLISACEASLKRLKTDVIDLY 125
Cdd:cd19145 43 FNSGVTFLDTSDIYGPNTNEVLLGKALKDGPREKVQLATKfgIHEIGGSGVEVRG-DPAYVRAACEASLKRLDVDYIDLY 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 126 QVHEWDGQTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALGVSALdkrqrfVSQQIHYTLEAREAEYELVPISIDQ 205
Cdd:cd19145 122 YQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSEASADTIRRAHAVHPI------TAVQLEWSLWTRDIEEEIIPTCREL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 206 GLGILVWSPLAGGLLSGKHRRGQSPEGTRQLAGWnepPIRDEERLWK---IVDILVAIAAERGVSPAQVALAWlIGRQAV 282
Cdd:cd19145 196 GIGIVPYSPLGRGFFAGKAKLEELLENSDVRKSH---PRFQGENLEKnkvLYERVEALAKKKGCTPAQLALAW-VLHQGE 271
|
250 260
....*....|....*....|
gi 500691625 283 TSVIIGGRTE-QQFRDNLAA 301
Cdd:cd19145 272 DVVPIPGTTKiKNLNQNIGA 291
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
1-301 |
2.78e-41 |
|
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: 147.15 E-value: 2.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 1 MEYRQLGRSGLKISTITMGTMTIGGggkfaqvGDVGVADASRHVDLCLDAGVNLIDTADIYSTGVCEEIIGEVLGGK--R 78
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTWVTFG-------GQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKgwR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 79 KDGVLIATKArFSMGPGPNDGGLSRHHLISACEASLKRLKTDVIDLYQVHEWDGQTPLEETMEALDTLVRQGKVRYIGCS 158
Cdd:cd19158 74 RSSLVITTKI-FWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 159 NYSGWHIMKALGVSALDKRQRFVSQQIHYTLEARE-AEYELVPISIDQGLGILVWSPLAGGLLSGKHRRGQSPEGTRQLA 237
Cdd:cd19158 153 RWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLK 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500691625 238 G--WNEPPIRDEE--RLWKIVDILVAIAAERGVSPAQVALAWLIGRQAVTSVIIGGRTEQQFRDNLAA 301
Cdd:cd19158 233 GyqWLKDKILSEEgrRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGA 300
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
48-297 |
3.04e-41 |
|
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: 146.30 E-value: 3.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 48 LDAGVNLIDTADIYSTGVCEEIIGEVL--GGKRkDGVLIATKArfsmGPGPNDGGL-----SRHHLISACEASLKRLKTD 120
Cdd:cd19148 35 LDLGINLIDTAPVYGFGLSEEIVGKALkeYGKR-DRVVIATKV----GLEWDEGGEvvrnsSPARIRKEVEDSLRRLQTD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 121 VIDLYQVHEWDGQTPLEETMEALDTLVRQGKVRYIGCSNYSgwhimkalgVSALDKRQRFV---SQQIHYTLEAREAEYE 197
Cdd:cd19148 110 YIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFS---------PEQMETFRKVAplhTVQPPYNLFEREIEKD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 198 LVPISIDQGLGILVWSPLAGGLLSGKHRRGQSPEG--TRQLAGWNEPPiRDEERLwKIVDILVAIAAER-GVSPAQVALA 274
Cdd:cd19148 181 VLPYARKHNIVTLAYGALCRGLLSGKMTKDTKFEGddLRRTDPKFQEP-RFSQYL-AAVEELDKLAQERyGKSVIHLAVR 258
|
250 260
....*....|....*....|...
gi 500691625 275 WLIGRQAVTSVIIGGRTEQQFRD 297
Cdd:cd19148 259 WLLDQPGVSIALWGARKPEQLDA 281
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
1-302 |
1.06e-40 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 146.50 E-value: 1.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 1 MEYRQLGRSGLKIStitmgtmtiggggKFA------QVGDvgVADASRHVDLCLDAGVNLIDTADIYstGVCEEIIGEVL 74
Cdd:COG1453 1 MQYRRLGKTGLEVS-------------VLGfggmrlPRKD--EEEAEALIRRAIDNGINYIDTARGY--GDSEEFLGKAL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 75 GGKRKDgVLIATKarfsMGPGPNDGGLSRHHLisacEASLKRLKTDVIDLYQVH------EWDGQTPLEETMEALDTLVR 148
Cdd:COG1453 64 KGPRDK-VILATK----LPPWVRDPEDMRKDL----EESLKRLQTDYIDLYLIHglnteeDLEKVLKPGGALEALEKAKA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 149 QGKVRYIGCSNYSGWHIMKAlgvsALDKRQ-RFVsqQIHYTL--EAREAEYELVPISIDQGLGILVWSPLAGGLLSgkhr 225
Cdd:COG1453 135 EGKIRHIGFSTHGSLEVIKE----AIDTGDfDFV--QLQYNYldQDNQAGEEALEAAAEKGIGVIIMKPLKGGRLA---- 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500691625 226 rgqspegtrqlagwNEPPirdeerlwKIVDILvaiaaERGVSPAQVALAWLIGRQAVTSVIIGGRTEQQFRDNLAAA 302
Cdd:COG1453 205 --------------NPPE--------KLVELL-----CPPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENLKTA 254
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
38-301 |
1.21e-40 |
|
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: 145.28 E-value: 1.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 38 ADASRHVDLCLDAGVNLIDTADIYstGVCEEIIGEVL---GGKRKDgVLIATKARFSM----GPGPNDGglSRHHLISAC 110
Cdd:cd19144 34 EERFAVLDAAFELGCTFWDTADIY--GDSEELIGRWFkqnPGKREK-IFLATKFGIEKnvetGEYSVDG--SPEYVKKAC 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 111 EASLKRLKTDVIDLYQVHEWDGQTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALGVSALDkrqrfvSQQIHY--- 187
Cdd:cd19144 109 ETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLSECSAETLRRAHAVHPIA------AVQIEYspf 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 188 TLEAREAEYELVPISIDQGLGILVWSPLAGGLLSGKHRrgqSPE-----GTRQLAgwnepPIRDEERLWKI---VDILVA 259
Cdd:cd19144 183 SLDIERPEIGVLDTCRELGVAIVAYSPLGRGFLTGAIR---SPDdfeegDFRRMA-----PRFQAENFPKNlelVDKIKA 254
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 500691625 260 IAAERGVSPAQVALAWLIGRQAVTSVIIGGRTEQQFRDNLAA 301
Cdd:cd19144 255 IAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLGA 296
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
31-303 |
5.09e-40 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 141.73 E-value: 5.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 31 QVGDVGVADAsrhVDLCLDAGVNLIDTADIYSTgvcEEIIGEVL---GGKRKDgVLIATKARfsmgpgPNDggLSRHHLI 107
Cdd:COG0656 14 QLPGEEAAAA---VRTALEAGYRHIDTAAMYGN---EEGVGEAIaasGVPREE-LFVTTKVW------NDN--HGYDDTL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 108 SACEASLKRLKTDVIDLYQVHeWDGQTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALGVSaldkRQRFVSQQIHY 187
Cdd:COG0656 79 AAFEESLERLGLDYLDLYLIH-WPGPGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAET----GVKPAVNQVEL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 188 TLEAReaEYELVPisIDQGLGILV--WSPLA-GGLLsgkhrrgqspegtrqlagwNEPpirdeerlwkivdILVAIAAER 264
Cdd:COG0656 154 HPYLQ--QRELLA--FCREHGIVVeaYSPLGrGKLL-------------------DDP-------------VLAEIAEKH 197
|
250 260 270
....*....|....*....|....*....|....*....
gi 500691625 265 GVSPAQVALAWLIGRQAVtsVIIGGRTEQQFRDNLAAAG 303
Cdd:COG0656 198 GKTPAQVVLRWHLQRGVV--VIPKSVTPERIRENLDAFD 234
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
1-301 |
3.34e-39 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 142.05 E-value: 3.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 1 MEYRQLGRSGLKISTITMGTmtiggggkFAQVGDVGVADASRHV-DLCLDAGVNLIDTADIYS--TGVCEEIIGEVLG-- 75
Cdd:PRK09912 13 MQYRYCGKSGLRLPALSLGL--------WHNFGHVNALESQRAIlRKAFDLGITHFDLANNYGppPGSAEENFGRLLRed 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 76 -GKRKDGVLIATKARFSMGPGPNDGGLSRHHLISACEASLKRLKTDVIDLYQVHEWDGQTPLEETMEALDTLVRQGKVRY 154
Cdd:PRK09912 85 fAAYRDELIISTKAGYDMWPGPYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 155 IGCSNYSGWHIMKALGVsaldKRQRFVSQQIH---YTLEAREAEYE-LVPISIDQGLGILVWSPLAGGLLSGKHRRGqSP 230
Cdd:PRK09912 165 VGISSYSPERTQKMVEL----LREWKIPLLIHqpsYNLLNRWVDKSgLLDTLQNNGVGCIAFTPLAQGLLTGKYLNG-IP 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500691625 231 EGTRQLAGWNEPPIRDEERLWKI----VDILVAIAAERGVSPAQVALAWLIGRQAVTSVIIGGRTEQQFRDNLAA 301
Cdd:PRK09912 240 QDSRMHREGNKVRGLTPKMLTEAnlnsLRLLNEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQA 314
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-302 |
4.44e-38 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 136.17 E-value: 4.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 1 MEYRQLGRSGLKISTitmgtmtiggggkfaqVGDVGVADASRHVDL---CLDAGVNLIDTADIYSTGVCEEIIGEVLGGK 77
Cdd:cd19105 1 MPYRTLGKTGLKVSR----------------LGFGGGGLPRESPELlrrALDLGINYFDTAEGYGNGNSEEIIGEALKGL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 78 RKDGVLIATKARFSMGPGpndgglSRHHLISACEASLKRLKTDVIDLYQVHEWDGQTPL---EETMEALDTLVRQGKVRY 154
Cdd:cd19105 65 RRDKVFLATKASPRLDKK------DKAELLKSVEESLKRLQTDYIDIYQLHGVDTPEERllnEELLEALEKLKKEGKVRF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 155 IGCSNYSGWH--IMKALGVSALDkrqrFVSQQIHYTLEAREAEyELVPISIDQGLGILVWSPLAGGLLsgkhrrgqspeg 232
Cdd:cd19105 139 IGFSTHDNMAevLQAAIESGWFD----VIMVAYNFLNQPAELE-EALAAAAEKGIGVVAMKTLAGGYL------------ 201
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 233 trqlagwneppirDEERLWKIVdilvaiaaERGVSPAQVALAWLIGRQAVTSVIIGGRTEQQFRDNLAAA 302
Cdd:cd19105 202 -------------QPALLSVLK--------AKGFSLPQAALKWVLSNPRVDTVVPGMRNFAELEENLAAA 250
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
33-302 |
1.36e-36 |
|
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: 133.06 E-value: 1.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 33 GDVGVADASRHVDLCLDAGVNLIDTADIYstGVCEEIIGEVLGGKRKDGVLIATKarfsMGPGPNDGG-LSRHHLISACE 111
Cdd:cd19090 15 GGVDDDEAVATIRAALDLGINYIDTAPAY--GDSEERLGLALAELPREPLVLSTK----VGRLPEDTAdYSADRVRRSVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 112 ASLKRLKTDVIDLYQVHE-----WDGQTPLEETMEALDTLVRQGKVRYIGcsnysgwhimkaLGVSALDKRQRFVSQQI- 185
Cdd:cd19090 89 ESLERLGRDRIDLLMIHDpervpWVDILAPGGALEALLELKEEGLIKHIG------------LGGGPPDLLRRAIETGDf 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 186 -------HYTLEAREAEYELVPISIDQGLGILVWSPLAGGLLSGKhrrgqSPEGTRQLAGWNEPPIRDE-ERLWkivdil 257
Cdd:cd19090 157 dvvltanRYTLLDQSAADELLPAAARHGVGVINASPLGMGLLAGR-----PPERVRYTYRWLSPELLDRaKRLY------ 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 500691625 258 vAIAAERGVSPAQVALAWLIGRQAVTSVIIGGRTEQQFRDNLAAA 302
Cdd:cd19090 226 -ELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAA 269
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
1-302 |
3.89e-35 |
|
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: 129.59 E-value: 3.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 1 MEYRQLGRSGLKISTITMGTMTiggggkFAQV-GDVGVADASRHVDLCLDAGVNLIDTADIYSTGVCEEIIGEVLGGKRK 79
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGASP------LGGVfGPVDEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKALKGIPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 80 DGVLIATKA-RFsmGPGPNDG-GLSRHHLISACEASLKRLKTDVIDLYQVH--EW--DGQTPLEETMEALDTLVRQGKVR 153
Cdd:cd19163 75 DSYYLATKVgRY--GLDPDKMfDFSAERITKSVEESLKRLGLDYIDIIQVHdiEFapSLDQILNETLPALQKLKEEGKVR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 154 YIGCSNYSgwhimkalgvsaLDKRQRFVSQQI----------HYTLEAREAEyELVPISIDQGLGILVWSPLAGGLLSgk 223
Cdd:cd19163 153 FIGITGYP------------LDVLKEVLERSPvkidtvlsycHYTLNDTSLL-ELLPFFKEKGVGVINASPLSMGLLT-- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 224 hrrgqspegTRQLAGWNE--PPIRDEERLwkivdiLVAIAAERGVSPAQVALAWLIGRQAVTSVIIGGRTEQQFRDNLAA 301
Cdd:cd19163 218 ---------ERGPPDWHPasPEIKEACAK------AAAYCKSRGVDISKLALQFALSNPDIATTLVGTASPENLRKNLEA 282
|
.
gi 500691625 302 A 302
Cdd:cd19163 283 A 283
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
38-301 |
4.12e-35 |
|
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: 130.33 E-value: 4.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 38 ADASRHVDLCLDAGVNLIDTADIYSTGVCEEIIGEVLGGKR-KDGVLIATK-----ARFSMGPGP--NDGGLSRHHLISA 109
Cdd:cd19147 34 EQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRKnRDQIVIATKfttdyKAYEVGKGKavNYCGNHKRSLHVS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 110 CEASLKRLKTDVIDLYQVHEWDGQTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALGVSALDKRQRFVSQQIHYTL 189
Cdd:cd19147 114 VRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATAHGKTPFSVYQGRWNV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 190 EAREAEYELVPISIDQGLGILVWSPLAGGLLSGK---HRRGQSPEGTRQLAGWNEPpiRDEERlwKIVDILVAIAAERGV 266
Cdd:cd19147 194 LNRDFERDIIPMARHFGMALAPWDVLGGGKFQSKkavEERKKNGEGLRSFVGGTEQ--TPEEV--KISEALEKVAEEHGT 269
|
250 260 270
....*....|....*....|....*....|....*.
gi 500691625 267 -SPAQVALAWLIGRQAVTSVIIGGRTEQQFRDNLAA 301
Cdd:cd19147 270 eSVTAIALAYVRSKAPNVFPLVGGRKIEHLKDNIEA 305
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
51-303 |
9.07e-35 |
|
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: 128.07 E-value: 9.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 51 GVNLIDTADIYSTGVCEEIIGEVLGGKRKDGVLIATKARFSmgpgpndgGLSRHHLISACEASLKRLKTDVIDLYQVHEW 130
Cdd:cd19137 39 GYTHIDTAEMYGGGHTEELVGKAIKDFPREDLFIVTKVWPT--------NLRYDDLLRSLQNSLRRLDTDYIDLYLIHWP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 131 DGQTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALGVSALDkrqrFVSQQIHYTLEAREAEYE-LVPISIDQGLGI 209
Cdd:cd19137 111 NPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQTP----IVCNQVKYNLEDRDPERDgLLEYCQKNGITV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 210 LVWSPLAGGLLsgkhrrgqspegtrqlagwneppirdeerlwKIVDILVAIAAERGVSPAQVALAWLIGRQAVTSVIIGG 289
Cdd:cd19137 187 VAYSPLRRGLE-------------------------------KTNRTLEEIAKNYGKTIAQIALAWLIQKPNVVAIPKAG 235
|
250
....*....|....
gi 500691625 290 RTEqQFRDNLAAAG 303
Cdd:cd19137 236 RVE-HLKENLKATE 248
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
2-303 |
3.38e-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: 381330 [Multi-domain] Cd Length: 321 Bit Score: 128.15 E-value: 3.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 2 EYRQLGRSGLKISTITmgtmtiggggkF-----AQV-GDVGVADASRHVDLCLDAGVNLIDTADIYSTGVCEEIIGEVLG 75
Cdd:cd19104 1 KYRRFGRTGLKVSELT-----------FggggiGGLmGRTTREEQIAAVRRALDLGINFFDTAPSYGDGKSEENLGRALK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 76 GKRkDGVLIATKARFSMGPGPNDGGlsrhHLISACEASLKRLKTDVIDLYQVHE-------WDGQTPL--------EETM 140
Cdd:cd19104 70 GLP-AGPYITTKVRLDPDDLGDIGG----QIERSVEKSLKRLKRDSVDLLQLHNrigderdKPVGGTLsttdvlglGGVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 141 EALDTLVRQGKVRYIGcsnYSGWHIMKALgvSALDKRQRFVSQQIHYTL------EAREAEY------ELVPISIDQGLG 208
Cdd:cd19104 145 DAFERLRSEGKIRFIG---ITGLGNPPAI--RELLDSGKFDAVQVYYNLlnpsaaEARPRGWsaqdygGIIDAAAEHGVG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 209 ILVWSPLAGGLLSGKHRRGQSPEGTRQlagwnEPPIRDEERlwkiVDILVAIAAERGVSPAQVALAWLIGRQAVTSVIIG 288
Cdd:cd19104 220 VMGIRVLAAGALTTSLDRGREAPPTSD-----SDVAIDFRR----AAAFRALAREWGETLAQLAHRFALSNPGVSTVLVG 290
|
330
....*....|....*
gi 500691625 289 GRTEQQFRDNLAAAG 303
Cdd:cd19104 291 VKNREELEEAVAAEA 305
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
48-302 |
5.51e-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: 5.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 48 LDAGVNLIDTADIYsTGVcEEIIGEVL-----GGKRKDGVLIATKARfsmgPGPNDGGLSRHHLISACEASLKRLKTDVI 122
Cdd:cd19101 33 VDAGLTTFDCADIY-GPA-EELIGEFRkrlrrERDAADDVQIHTKWV----PDPGELTMTRAYVEAAIDRSLKRLGVDRL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 123 DLYQVHEWDGQTP-LEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALgvsalDKRQRFVSQQIHYTLEAREAEYELVPI 201
Cdd:cd19101 107 DLVQFHWWDYSDPgYLDAAKHLAELQEEGKIRHLGLTNFDTERLREIL-----DAGVPIVSNQVQYSLLDRRPENGMAAL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 202 SIDQGLGILVWSPLAGGLLSGKHRrGQsPEGTRqlagwNEPPIRDEERLWKIVD-------------ILVAIAAERGVSP 268
Cdd:cd19101 182 CEDHGIKLLAYGTLAGGLLSEKYL-GV-PEPTG-----PALETRSLQKYKLMIDewggwdlfqellrTLKAIADKHGVSI 254
|
250 260 270
....*....|....*....|....*....|....
gi 500691625 269 AQVALAWLIGRQAVTSVIIGGRTEQQFRDNLAAA 302
Cdd:cd19101 255 ANVAVRWVLDQPGVAGVIVGARNSEHIDDNVRAF 288
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
42-302 |
7.83e-33 |
|
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: 122.67 E-value: 7.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 42 RHVDLCLDAGVNLIDTADIYSTGVCEEIIGEVLGGKRKDGVLIATKARFSMGPGPNDgglSRHHLisacEASLKRLKTDV 121
Cdd:cd19096 25 EMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKEGPREKFYLATKLPPWSVKSAED---FRRIL----EESLKRLGVDY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 122 IDLYQVH-----EWDGQTPLEETMEALDTLVRQGKVRYIGCSnysgWH-----IMKALGVSALDkrqrFVSQQIHYTLEA 191
Cdd:cd19096 98 IDFYLLHglnspEWLEKARKGGLLEFLEKAKKEGLIRHIGFS----FHdspelLKEILDSYDFD----FVQLQYNYLDQE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 192 REAEYELVPISIDQGLGILVWSPLAGGLLSgkhrrgqspegtrqlagwNEPPirdeerlwkivdILVAIAAERGVSPAQV 271
Cdd:cd19096 170 NQAGRPGIEYAAKKGMGVIIMEPLKGGGLA------------------NNPP------------EALAILCGAPLSPAEW 219
|
250 260 270
....*....|....*....|....*....|.
gi 500691625 272 ALAWLIGRQAVTSVIIGGRTEQQFRDNLAAA 302
Cdd:cd19096 220 ALRFLLSHPEVTTVLSGMSTPEQLDENIAAA 250
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
3-300 |
3.03e-32 |
|
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: 120.66 E-value: 3.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 3 YRQLGRSGLKISTITmgtmtiggggkF--AQVGDVGVADASRHVDLCLDAGVNLIDTADIYstGVCEEIIGEVLGGKRKD 80
Cdd:cd19100 1 YRRLGRTGLKVSRLG-----------FggGPLGRLSQEEAAAIIRRALDLGINYFDTAPSY--GDSEEKIGKALKGRRDK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 81 gVLIATKArfsmgpGPNDGGLSRHHLisacEASLKRLKTDVIDLYQVHEWDGQTPLEETM---EALDTLVR---QGKVRY 154
Cdd:cd19100 68 -VFLATKT------GARDYEGAKRDL----ERSLKRLGTDYIDLYQLHAVDTEEDLDQVFgpgGALEALLEakeEGKIRF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 155 IGCSNYSgWHIMKAlgvsALDkrqRFVSQQIHYTL-----EAREAEYELVPISIDQGLGILVWSPLAGGLLsgkhrrgqs 229
Cdd:cd19100 137 IGISGHS-PEVLLR----ALE---TGEFDVVLFPInpagdHIDSFREELLPLAREKGVGVIAMKVLAGGRL--------- 199
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500691625 230 pegtrqlagwneppirdeerlwkivdilvaiAAERGVSPAQvALAWLIGRQAVTSVIIGGRTEQQFRDNLA 300
Cdd:cd19100 200 -------------------------------LSGDPLDPEQ-ALRYALSLPPVDVVIVGMDSPEELDENLA 238
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
35-302 |
2.24e-30 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 117.05 E-value: 2.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 35 VGVADASRHVDLCLDAGVNLIDTADIYSTGVCEEIIGEVLGGKRKDGVLIATKarFSmgpgPNDGGLSRHHLISACEASL 114
Cdd:cd19103 29 LDEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEFLKRYPREDYIISTK--FT----PQIAGQSADPVADMLEGSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 115 KRLKTDVIDLYQVHEwdgQTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKAlgVSALDKRQRFVSQ-QIHYTLEARE 193
Cdd:cd19103 103 ARLGTDYIDIYWIHN---PADVERWTPELIPLLKSGKVKHVGVSNHNLAEIKRA--NEILAKAGVSLSAvQNHYSLLYRS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 194 AEYE-LVPISIDQGLGILVWSPLAGGLLSGKHRRGQS-PEGTRQLAGWNeppiRDEERLWKIVDILVAIAAERGVSPAQV 271
Cdd:cd19103 178 SEEAgILDYCKENGITFFAYMVLEQGALSGKYDTKHPlPEGSGRAETYN----PLLPQLEELTAVMAEIGAKHGASIAQV 253
|
250 260 270
....*....|....*....|....*....|.
gi 500691625 272 ALAWLIGRQavTSVIIGGRTEQQFRDNLAAA 302
Cdd:cd19103 254 AIAWAIAKG--TTPIIGVTKPHHVEDAARAA 282
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
38-303 |
3.25e-30 |
|
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: 115.45 E-value: 3.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 38 ADASRHVDLCLDAGVNLIDTADIYSTgvcEEIIGEVLG--GKRKDGVLIATKArfsmgpgpNDGGLSRHHLISACEASLK 115
Cdd:cd19073 14 DDCANAVKEALELGYRHIDTAEIYNN---EAEVGEAIAesGVPREDLFITTKV--------WRDHLRPEDLKKSVDRSLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 116 RLKTDVIDLYQVHEWDGQTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALGVSALDkrqrFVSQQI--HYTLEARe 193
Cdd:cd19073 83 KLGTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPLP----IAVNQVefHPFLYQA- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 194 aeyELVPISIDQGLGILVWSPLAggllsgkhrRGQSPEgtrqlagwneppirdeerlwkiVDILVAIAAERGVSPAQVAL 273
Cdd:cd19073 158 ---ELLEYCRENDIVITAYSPLA---------RGEVLR----------------------DPVIQEIAEKYDKTPAQVAL 203
|
250 260 270
....*....|....*....|....*....|
gi 500691625 274 AWLIGRQAVtsVIIGGRTEQQFRDNLAAAG 303
Cdd:cd19073 204 RWLVQKGIV--VIPKASSEDHLKENLAIFD 231
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
48-302 |
5.32e-27 |
|
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: 108.10 E-value: 5.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 48 LDAGVNLIDTADIYSTGVCE---EIIGEVLG--GKRKDGVLIATKARFSMGPGPNDGglSRHHLISACEASLKRLK-TDV 121
Cdd:cd19077 35 LDAGSNLWNGGEFYGPPDPHanlKLLARFFRkyPEYADKVVLSVKGGLDPDTLRPDG--SPEAVRKSIENILRALGgTKK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 122 IDLYQVHEWDGQTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALGVSALdkrqrfVSQQIHYTLEAREAEY-ELVP 200
Cdd:cd19077 113 IDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAETIRRAHAVHPI------AAVEVEYSLFSREIEEnGVLE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 201 ISIDQGLGILVWSPLAGGLLSGKHR-RGQSPEG-TRQLagwnePPIRDEERL---WKIVDILVAIAAERGVSPAQVALAW 275
Cdd:cd19077 187 TCAELGIPIIAYSPLGRGLLTGRIKsLADIPEGdFRRH-----LDRFNGENFeknLKLVDALQELAEKKGCTPAQLALAW 261
|
250 260
....*....|....*....|....*...
gi 500691625 276 LIGRQAVTSV-IIGGRTEQQFRDNLAAA 302
Cdd:cd19077 262 ILAQSGPKIIpIPGSTTLERVEENLKAA 289
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
31-302 |
9.18e-27 |
|
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: 106.84 E-value: 9.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 31 QVGDVGVADASRHVDLCLDAGVNLIDTADIYstGVCEEIIGEVLggKRKDGVLIATKarfsMGPGPNDGGLSRHHLISAC 110
Cdd:cd19097 19 KSGKPSEKEAKKILEYALKAGINTLDTAPAY--GDSEKVLGKFL--KRLDKFKIITK----LPPLKEDKKEDEAAIEASV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 111 EASLKRLKTDVIDLYQVHEW-DGQTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALG----------VSALDkrQR 179
Cdd:cd19097 91 EASLKRLKVDSLDGLLLHNPdDLLKHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKALEsfkidiiqlpFNILD--QR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 180 FVSQqihytleareaeyELVPISIDQGLGILVWSPLAGGLLSGKHRRGQSpegtrQLAGWNeppirdeerlwKIVDILVA 259
Cdd:cd19097 169 FLKS-------------GLLAKLKKKGIEIHARSVFLQGLLLMEPDKLPA-----KFAPAK-----------PLLKKLHE 219
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 500691625 260 IAAERGVSPAQVALAWLIGRQAVTSVIIGGRTEQQFRDNLAAA 302
Cdd:cd19097 220 LAKKLGLSPLELALGFVLSLPEIDKIVVGVDSLEQLKEIIAAF 262
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
30-302 |
2.68e-26 |
|
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: 105.90 E-value: 2.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 30 AQVGDVGVADASRHVDLCLDAGVNLIDTADIYSTGVCEEIIGEVLGGKRKDGVLIATKA--RFSMGPGPNDGGLSRHHLI 107
Cdd:cd19162 11 GNLARAGEDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALARHPRAEYVVSTKVgrLLEPGAAGRPAGADRRFDF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 108 SA------CEASLKRLKTDVIDLYQVHEWDGQ--TPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALGVSALDkrqr 179
Cdd:cd19162 91 SAdgirrsIEASLERLGLDRLDLVFLHDPDRHllQALTDAFPALEELRAEGVVGAIGVGVTDWAALLRAARRADVD---- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 180 FVSQQIHYTLEAREAEYELVPISIDQGLGILVWSPLAGGLLSGKHrrgqsPEGTRQLAGWNEPPIRDEerlwkiVDILVA 259
Cdd:cd19162 167 VVMVAGRYTLLDRRAATELLPLCAAKGVAVVAAGVFNSGILATDD-----PAGDRYDYRPATPEVLAR------ARRLAA 235
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 500691625 260 IAAERGVSPAQVALAWLIGRQAVTSVIIGGRTEQQFRDNLAAA 302
Cdd:cd19162 236 VCRRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLALL 278
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
30-302 |
5.41e-26 |
|
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: 104.10 E-value: 5.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 30 AQVGDVGVADAsrhVDLCLDAGVNLIDTADIYSTgvcEEIIGEVL---GGKRKDgVLIATKArfsmgpgpNDGGLSRHHL 106
Cdd:cd19071 9 YKLKPEETAEA---VLAALEAGYRHIDTAAAYGN---EAEVGEAIresGVPREE-LFITTKL--------WPTDHGYERV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 107 ISACEASLKRLKTDVIDLYQVH------EWDGQTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALGVSaldkRQRF 180
Cdd:cd19071 74 REALEESLKDLGLDYLDLYLIHwpvpgkEGGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAA----RIKP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 181 VSQQIhytleareaeyELVPISIDQGL-------GILV--WSPLAGGllsgkhrrgqspegtrqlagwNEPPIRDEerlw 251
Cdd:cd19071 150 AVNQI-----------ELHPYLQQKELvefckehGIVVqaYSPLGRG---------------------RRPLLDDP---- 193
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 500691625 252 kivdILVAIAAERGVSPAQVALAWLIGRQavTSVIIGGRTEQQFRDNLAAA 302
Cdd:cd19071 194 ----VLKEIAKKYGKTPAQVLLRWALQRG--VVVIPKSSNPERIKENLDVF 238
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
34-300 |
3.29e-22 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 95.08 E-value: 3.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 34 DVGVADASRHVDLCLDAGVNLIDTADIYSTGVCEEIIGEVL------GGKRKDGVLIATKARFSmgPGPNDGGLS----- 102
Cdd:cd19099 17 DETDEEYREALKAALDSGINVIDTAINYRGGRSERLIGKALreliekGGIKRDEVVIVTKAGYI--PGDGDEPLRplkyl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 103 ----------------RHHLIS------ACEASLKRLKTDVIDLYQVHE------WDGQTP----LEETMEALDTLVRQG 150
Cdd:cd19099 95 eeklgrglidvadsagLRHCISpayledQIERSLKRLGLDTIDLYLLHNpeeqllELGEEEfydrLEEAFEALEEAVAEG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 151 KVRYIGCSNYSG--------WHIMKALGVSALDKRQ------RFVsqQIHYTLEAREAEYE----------LVPISIDQG 206
Cdd:cd19099 175 KIRYYGISTWDGfrappalpGHLSLEKLVAAAEEVGgdnhhfKVI--QLPLNLLEPEALTEkntvkgealsLLEAAKELG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 207 LGILVWSPLAGGLLSGKHRRGQSPEGTrqlagwneppirdeerlwkivdilvaiaaeRGVSPAQVALAWLIGRQAVTSVI 286
Cdd:cd19099 253 LGVIASRPLNQGQLLGELRLADLLALP------------------------------GGATLAQRALQFARSTPGVDSAL 302
|
330
....*....|....
gi 500691625 287 IGGRTEQQFRDNLA 300
Cdd:cd19099 303 VGMRRPEHVDENLA 316
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
33-301 |
3.56e-21 |
|
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: 90.88 E-value: 3.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 33 GDVGVADasrhVDLCLDAGVNLIDTADIYSTgvcEEIIGEVL--GGKRKDGVLIATKARFSmgpgpndgGLSRHHLISAC 110
Cdd:cd19139 13 DDVVIDS----VRTALELGYRHIDTAQIYDN---EAAVGQAIaeSGVPRDELFITTKIWID--------NLSKDKLLPSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 111 EASLKRLKTDVIDLYQVHeW---DGQTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALGVSALDKrqrFVSQQI-- 185
Cdd:cd19139 78 EESLEKLRTDYVDLTLIH-WpspNDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVGAGA---IATNQIel 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 186 HYTLEAReaeyELVPISIDQGLGILVWSPLAGGLLsgkhrrgqspegtrqlagwneppIRDEerlwkivdILVAIAAERG 265
Cdd:cd19139 154 SPYLQNR----KLVAHCKQHGIHVTSYMTLAYGKV-----------------------LDDP--------VLAAIAERHG 198
|
250 260 270
....*....|....*....|....*....|....*.
gi 500691625 266 VSPAQVALAWLIGRQavTSVIIGGRTEQQFRDNLAA 301
Cdd:cd19139 199 ATPAQIALAWAMARG--YAVIPSSTKREHLRSNLLA 232
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
38-300 |
4.90e-21 |
|
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: 90.78 E-value: 4.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 38 ADASRHVDLCLDAGVNLIDTADIYSTgvcEEIIGEVLG--GKRKDGVLIATKArfsmgpGPNDggLSRHHLISACEASLK 115
Cdd:cd19140 21 EECTRAVEHALELGYRHIDTAQMYGN---EAQVGEAIAasGVPRDELFLTTKV------WPDN--YSPDDFLASVEESLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 116 RLKTDVIDLYQVHeWDG-QTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALGVSALDkrqrFVSQQIHYTlearea 194
Cdd:cd19140 90 KLRTDYVDLLLLH-WPNkDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSEAP----LFTNQVEYH------ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 195 eyelvpISIDQ--------GLGILV--WSPLAggllsgkhrRGQSPegtrqlagwNEPpirdeerlwkivdILVAIAAER 264
Cdd:cd19140 159 ------PYLDQrklldaarEHGIALtaYSPLA---------RGEVL---------KDP-------------VLQEIGRKH 201
|
250 260 270
....*....|....*....|....*....|....*.
gi 500691625 265 GVSPAQVALAWLIgRQAVTSVIIGGRTEQQFRDNLA 300
Cdd:cd19140 202 GKTPAQVALRWLL-QQEGVAAIPKATNPERLEENLD 236
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
44-302 |
3.39e-20 |
|
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: 89.59 E-value: 3.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 44 VDLCLDAGVNLIDTADIYSTGVCEEIIGEVLGGKRKDGVLIATKA-RF---SMGPGPNDGGLSRHHL------------I 107
Cdd:cd19152 26 LVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELGREDYVISTKVgRLlvpLQEVEPTFEPGFWNPLpfdavfdysydgI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 108 SAC-EASLKRLKTDVIDLYQVHEWDGQTPLEETME-----------ALDTLVRQGKVRYIGC-SNysGWH-IMKALGVSA 173
Cdd:cd19152 106 LRSiEDSLQRLGLSRIDLLSIHDPDEDLAGAESDEhfaqaikgafrALEELREEGVIKAIGLgVN--DWEvILRILEEAD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 174 LDkrqrFVSQQIHYTLEAREAEYELVPISIDQGLGILVWSPLAGGLLSGKHRRGQSPEGTRqlagwnEPPIRDEERLWKi 253
Cdd:cd19152 184 LD----WVMLAGRYTLLDHSAARELLPECEKRGVKVVNAGPFNSGFLAGGDNFDYYEYGPA------PPELIARRDRIE- 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 500691625 254 vdilvAIAAERGVSPAQVALAWLIGRQAVTSVIIGGRTEQQFRDNLAAA 302
Cdd:cd19152 253 -----ALCEQHGVSLAAAALQFALAPPAVASVAPGASSPERVEENVALL 296
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
50-303 |
1.22e-19 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 87.72 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 50 AGVNLIDTADIYSTGVCEEIIGEVLGGKRKDgVLIATKARFSMGPgpnDGG----LSRHHLISACEASLKRLKTDVIDLY 125
Cdd:PRK10376 52 LGVNHIDTSDFYGPHVTNQLIREALHPYPDD-LTIVTKVGARRGE---DGSwlpaFSPAELRRAVHDNLRNLGLDVLDVV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 126 QVHEW-DGQTP----LEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALGVSALdkrqrfVSQQIHYTLeAREAEYELVP 200
Cdd:PRK10376 128 NLRLMgDGHGPaegsIEEPLTVLAELQRQGLVRHIGLSNVTPTQVAEARKIAEI------VCVQNHYNL-AHRADDALID 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 201 ISIDQGLGILVWSPLaGGLlsgkhrrgqspegtrqlagwnePPIRDeerlwkivDILVAIAAERGVSPAQVALAWLIGRQ 280
Cdd:PRK10376 201 ALARDGIAYVPFFPL-GGF----------------------TPLQS--------STLSDVAASLGATPMQVALAWLLQRS 249
|
250 260
....*....|....*....|...
gi 500691625 281 AVTSVIIGGRTEQQFRDNLAAAG 303
Cdd:PRK10376 250 PNILLIPGTSSVAHLRENLAAAE 272
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
36-275 |
4.63e-19 |
|
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: 85.38 E-value: 4.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 36 GVADASRHVDLCLDAGVNLIDTADIYSTgvcEEIIGEVL-------GGKRKDgVLIATKArfsmgpGPNDGGLSRhhLIS 108
Cdd:cd19136 13 GEEEVRQAVDAALKAGYRLIDTASVYRN---EADIGKALrdllpkyGLSRED-IFITSKL------APKDQGYEK--ARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 109 ACEASLKRLKTDVIDLYQVHeWDGQTPLE-----------ETMEALDTLVRQGKVRYIGCSNYSGWHIMKALGVSaldKR 177
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIH-WPGVQGLKpsdprnaelrrESWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYC---EV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 178 QRFVSQ-QIHYTLEareaEYELVPISIDQGLGILVWSPLaggllsgkhrrgqspeGTRQLAGWNEPPIRdeerlwkivdi 256
Cdd:cd19136 157 PPAVNQvEFHPHLV----QKELLKFCKDHGIHLQAYSSL----------------GSGDLRLLEDPTVL----------- 205
|
250
....*....|....*....
gi 500691625 257 lvAIAAERGVSPAQVALAW 275
Cdd:cd19136 206 --AIAKKYGRTPAQVLLRW 222
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
29-282 |
1.64e-18 |
|
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: 84.26 E-value: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 29 FAQVGDVGVADASRHVdlcLDAGVNLIDTADIYSTgvcEEIIGEVLGGKRKDGVL------IATKarfsmgpgpndggL- 101
Cdd:cd19116 19 WKLKDDEGVRQAVKHA---IEAGYRHIDTAYLYGN---EAEVGEAIREKIAEGVVkredlfITTK-------------Lw 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 102 ----SRHHLISACEASLKRLKTDVIDLYQVH-----------EWDGQTPLE-----ETMEALDTLVRQGKVRYIGCSNYS 161
Cdd:cd19116 80 nsyhEREQVEPALRESLKRLGLDYVDLYLIHwpvafkenndsESNGDGSLSdidylETWRGMEDLVKLGLTRSIGVSNFN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 162 GWHIMKALGVSALdkrqRFVSQQI--HYTLEareaEYELVPISidQGLGILV--WSPLaggllsGKH-RRGQspegtrql 236
Cdd:cd19116 160 SEQINRLLSNCNI----KPAVNQIevHPTLT----QEKLVAYC--QSNGIVVmaYSPF------GRLvPRGQ-------- 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 500691625 237 agWNEPPIRDEERlwkivdiLVAIAAERGVSPAQVALAWLIGRQAV 282
Cdd:cd19116 216 --TNPPPRLDDPT-------LVAIAKKYGKTTAQIVLRYLIDRGVV 252
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
37-283 |
1.08e-17 |
|
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 81.67 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 37 VADAsrhVDLCLDAGVNLIDTADIYSTgvcEEIIGEVL--GGKRKDGVLIATKARfsmgpgpnDGGLSRHHLISACEASL 114
Cdd:cd19157 26 VVNA---VKTALKNGYRSIDTAAIYGN---EEGVGKGIkeSGIPREELFITSKVW--------NADQGYDSTLKAFEASL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 115 KRLKTDVIDLYQVHeWDGQTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALG-------VSALDKRQRFVSQQIHY 187
Cdd:cd19157 92 ERLGLDYLDLYLIH-WPVKGKYKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLAdaeivpmVNQVEFHPRLTQKELRD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 188 TLEAREAEYElvpisidqglgilVWSPL-AGGLLSgkhrrgqspegtrqlagwneppirdeerlwkiVDILVAIAAERGV 266
Cdd:cd19157 171 YCKKQGIQLE-------------AWSPLmQGQLLD--------------------------------NPVLKEIAEKYNK 205
|
250
....*....|....*..
gi 500691625 267 SPAQVALAWLIGRQAVT 283
Cdd:cd19157 206 SVAQVILRWDLQNGVVT 222
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
33-302 |
1.52e-17 |
|
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: 81.69 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 33 GDVGVAdasrhVDLCLDAGVNLIDTADIYSTgvcEEIIGEVLGG-------KRKDgvLIATKARFSMGPGPNDgglsrhh 105
Cdd:cd19123 25 GEVGQA-----VKQALEAGYRHIDCAAIYGN---EAEIGAALAEvfkegkvKRED--LWITSKLWNNSHAPED------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 106 LISACEASLKRLKTDVIDLYQVHeW-------------------DGQTPLEETMEALDTLVRQGKVRYIGCSNYSgwhIM 166
Cdd:cd19123 88 VLPALEKTLADLQLDYLDLYLMH-WpvalkkgvgfpesgedllsLSPIPLEDTWRAMEELVDKGLCRHIGVSNFS---VK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 167 KALGVSALDKRQRFVSQ-QIHYTLEAREaeyeLVPISIDQGLGILVWSPLAggllsgkhrRGQSPEGTRQLagwNEPPIR 245
Cdd:cd19123 164 KLEDLLATARIKPAVNQvELHPYLQQPE----LLAFCRDNGIHLTAYSPLG---------SGDRPAAMKAE---GEPVLL 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 500691625 246 DEErlwkivdILVAIAAERGVSPAQVALAWLIGRQavTSVIIGGRTEQQFRDNLAAA 302
Cdd:cd19123 228 EDP-------VINKIAEKHGASPAQVLIAWAIQRG--TVVIPKSVNPERIQQNLEAA 275
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
39-275 |
2.49e-17 |
|
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: 80.74 E-value: 2.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 39 DASRHVDLCLDAGVNLIDTADIYSTgvcEEIIGEVL---GGKRKDgVLIATKArfsmGPGPNDgglsrhhLISACEASLK 115
Cdd:cd19120 26 DLVDSVKLALKAGFRHIDTAEMYGN---EKEVGEALkesGVPRED-LFITTKV----SPGIKD-------PREALRKSLA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 116 RLKTDVIDLYQVH----EWDGQTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALgvsALDKRQRFVSQ-QIHYTLE 190
Cdd:cd19120 91 KLGVDYVDLYLIHspffAKEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELL---DTAKIKPAVNQiEFHPYLY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 191 AREAeyELVPISIDQGLGILVWSPLAggllsgkhrrgqspegtrqlagwnePPIRDEERlwKIVDILVAIAAERGVSPAQ 270
Cdd:cd19120 168 PQQP--ALLEYCREHGIVVSAYSPLS-------------------------PLTRDAGG--PLDPVLEKIAEKYGVTPAQ 218
|
....*
gi 500691625 271 VALAW 275
Cdd:cd19120 219 VLLRW 223
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
39-283 |
1.44e-16 |
|
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: 78.25 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 39 DASRHVDLCLDAGVNLIDTADIYSTgvcEEIIGEVL--GGKRKDGVLIATKARfsmgpgpNDGGLSRHHLiSACEASLKR 116
Cdd:cd19126 24 ETERAVQTALENGYRSIDTAAIYKN---EEGVGEAIreSGVPREELFVTTKLW-------NDDQRARRTE-DAFQESLDR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 117 LKTDVIDLYQVHeWDGQTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALGVSaldKRQRFVSQ-QIHYTLEAReae 195
Cdd:cd19126 93 LGLDYVDLYLIH-WPGKDKFIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHA---DVVPAVNQvEFHPYLTQK--- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 196 yELVPISIDQGLGILVWSPLA-GGLLSGKhrrgqspegtrqlagwneppirdeerlwkivdILVAIAAERGVSPAQVALA 274
Cdd:cd19126 166 -ELRGYCKSKGIVVEAWSPLGqGGLLSNP--------------------------------VLAAIGEKYGKSAAQVVLR 212
|
....*....
gi 500691625 275 WLIGRQAVT 283
Cdd:cd19126 213 WDIQHGVVT 221
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
48-301 |
1.91e-16 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 78.14 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 48 LDAGVNLIDTADIYSTgvcEEIIGEVLG--GKRKDGVLIATKARFSmgpgpndgGLSRHHLISACEASLKRLKTDVIDLY 125
Cdd:PRK11172 26 LELGYRAIDTAQIYDN---EAAVGQAIAesGVPRDELFITTKIWID--------NLAKDKLIPSLKESLQKLRTDYVDLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 126 QVHeW---DGQTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALGVSALDKrqrFVSQQI--HYTLEAReaeyELVP 200
Cdd:PRK11172 95 LIH-WpspNDEVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQAIAAVGAEN---IATNQIelSPYLQNR----KVVA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 201 ISIDQGLGILVWSPLAGGLLsgkhrrgqspegtrqlagwneppIRDEerlwkivdILVAIAAERGVSPAQVALAWLIgrQ 280
Cdd:PRK11172 167 FAKEHGIHVTSYMTLAYGKV-----------------------LKDP--------VIARIAAKHNATPAQVILAWAM--Q 213
|
250 260
....*....|....*....|.
gi 500691625 281 AVTSVIIGGRTEQQFRDNLAA 301
Cdd:PRK11172 214 LGYSVIPSSTKRENLASNLLA 234
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
3-302 |
2.61e-16 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 78.28 E-value: 2.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 3 YRQLGRSGLKISTITMGTMTIGGGgkfaqVGDVGVADASRHVDLCLDAGVNLIDTADIYSTGVCEEIIGEVL--GGKRKD 80
Cdd:PLN02587 1 LRELGSTGLKVSSVGFGASPLGSV-----FGPVSEEDAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALkaLGIPRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 81 GVLIATK-ARFSMGpgpndGGLSRHHLISACEASLKRLKTDVIDLYQVHEWD----GQTpLEETMEALDTLVRQGKVRYI 155
Cdd:PLN02587 76 KYVVSTKcGRYGEG-----FDFSAERVTKSVDESLARLQLDYVDILHCHDIEfgslDQI-VNETIPALQKLKESGKVRFI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 156 GCSN---YSGWHIMKALGVSALDkrqrFVSQQIHYTLEAREAEyELVPISIDQGLGILVWSPLAGGLLSGKhrrgQSPEg 232
Cdd:PLN02587 150 GITGlplAIFTYVLDRVPPGTVD----VILSYCHYSLNDSSLE-DLLPYLKSKGVGVISASPLAMGLLTEN----GPPE- 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 233 trqlagWNEPPirdeERLWKIVDILVAIAAERGVSPAQVALAWLIGRQAVTSVIIGGRTEQQFRDNLAAA 302
Cdd:PLN02587 220 ------WHPAP----PELKSACAAAATHCKEKGKNISKLALQYSLSNKDISTTLVGMNSVQQVEENVAAA 279
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
48-299 |
3.10e-16 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381380 [Multi-domain] Cd Length: 303 Bit Score: 78.22 E-value: 3.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 48 LDAGVNLIDTADIYSTgvcEEIIGEVL------GGKRKDGVLIATKARFsmgpgpndGGLSRHHLISACEASLKRLKTDV 121
Cdd:cd19154 35 LKAGYRLIDTAFLYQN---EEAIGEALaelleeGVVKREDLFITTKLWT--------HEHAPEDVEEALRESLKKLQLEY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 122 IDLYQVH-------------------EWDGQTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALGVSaldkRQRFVS 182
Cdd:cd19154 104 VDLYLIHapaafkddegesgtmengmSIHDAVDVEDVWRGMEKVYDEGLTKAIGVSNFNNDQIQRILDNA----RVKPHN 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 183 QQIHytLEAREAEYELVPISIDQGLGILVWSPLAggllsgkhrrgqSPEGT--RQLAGWNEPPIRDEERlwkivdILVAI 260
Cdd:cd19154 180 NQVE--CHLYFPQKELVEFCKKHNISVTSYATLG------------SPGRAnfTKSTGVSPAPNLLQDP------IVKAI 239
|
250 260 270
....*....|....*....|....*....|....*....
gi 500691625 261 AAERGVSPAQVALAWLIGRQAVtsVIIGGRTEQQFRDNL 299
Cdd:cd19154 240 AEKHGKTPAQVLLRYLLQRGIA--VIPKSATPSRIKENF 276
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
49-283 |
5.69e-16 |
|
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: 76.59 E-value: 5.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 49 DAGVNLIDTADIYStgvCEEIIGEVL---GGKRKDgVLIATKArfsmgpGPNDGGLSRhhLISACEASLKRLKTDVIDLY 125
Cdd:cd19135 37 ECGYRHIDTAKRYG---CEELLGKAIkesGVPRED-LFLTTKL------WPSDYGYES--TKQAFEASLKRLGVDYLDLY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 126 QVHEWDGQTP-------LEETMEALDTLVRQGKVRYIGCSNYsgwhimkalGVSALDKRQRFVSQQIHYTlearEAEY-- 196
Cdd:cd19135 105 LLHWPDCPSSgknvketRAETWRALEELYDEGLCRAIGVSNF---------LIEHLEQLLEDCSVVPHVN----QVEFhp 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 197 -----ELVPISIDQGLGILVWSPLAGGLLsgkhrrgqspegtrqlagWNEPPIrdeerlwkivdilVAIAAERGVSPAQV 271
Cdd:cd19135 172 fqnpvELIEYCRDNNIVFEGYCPLAKGKA------------------LEEPTV-------------TELAKKYQKTPAQI 220
|
250
....*....|..
gi 500691625 272 ALAWLIGRQAVT 283
Cdd:cd19135 221 LIRWSIQNGVVT 232
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
44-283 |
6.18e-15 |
|
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: 74.34 E-value: 6.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 44 VDLCLDAGVNLIDTADIYS--TGVCE---EIIGEVLGGKRKDgVLIATKarfsmgpgpndggL--SRHH---LISACEAS 113
Cdd:cd19106 26 VKYALDAGYRHIDCAAVYGneQEVGEalkEKVGPGKAVPRED-LFVTSK-------------LwnTKHHpedVEPALRKT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 114 LKRLKTDVIDLYQVHeW---------------DGQ-----TPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALGVSA 173
Cdd:cd19106 92 LKDLQLDYLDLYLIH-WpyafergdnpfpknpDGTirydsTHYKETWKAMEKLVDKGLVKAIGLSNFNSRQIDDILSVAR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 174 LdkrQRFVSQ-QIHYTLeareAEYELVPISIDQGLGILVWSPLAggllsgkhrrgqSPEgtRQLAGWNEPPIRDEERlwk 252
Cdd:cd19106 171 I---KPAVLQvECHPYL----AQNELIAHCKARGLVVTAYSPLG------------SPD--RPWAKPDEPVLLEEPK--- 226
|
250 260 270
....*....|....*....|....*....|.
gi 500691625 253 ivdiLVAIAAERGVSPAQVALAWLIGRQAVT 283
Cdd:cd19106 227 ----VKALAKKYNKSPAQILLRWQVQRGVVV 253
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
31-301 |
1.46e-14 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; Escherichia coli DkgA/YqhE is a founding member of aldo-keto reductase family 5 member C2 (AKR5C2). DkgA/YqhE (EC 1.1.1.274), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives.
Pssm-ID: 381357 [Multi-domain] Cd Length: 256 Bit Score: 72.40 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 31 QVGDVGVADAsrhVDLCLDAGVNLIDTADIYSTgvcEEIIGEVL--GGKRKDGVLIATKARFSmgpgpnDGGLSRhhLIS 108
Cdd:cd19131 19 QVSNDEAASA---VREALEVGYRSIDTAAIYGN---EEGVGKAIraSGVPREELFITTKLWNS------DQGYDS--TLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 109 ACEASLKRLKTDVIDLYQVHeW--DGQTPLEETMEALDTLVRQGKVRYIGCSNYSGWH---IMKALGVSAldkrqrfVSQ 183
Cdd:cd19131 85 AFDESLRKLGLDYVDLYLIH-WpvPAQDKYVETWKALIELKKEGRVKSIGVSNFTIEHlqrLIDETGVVP-------VVN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 184 QIHytLEAREAEYELVPISIDQGLGILVWSPLA-GGLLSgkhrrgqspegtrqlagwnEPPIRDeerlwkivdilvaIAA 262
Cdd:cd19131 157 QIE--LHPRFQQRELRAFHAKHGIQTESWSPLGqGGLLS-------------------DPVIGE-------------IAE 202
|
250 260 270
....*....|....*....|....*....|....*....
gi 500691625 263 ERGVSPAQVALAWLIgrQAVTSVIIGGRTEQQFRDNLAA 301
Cdd:cd19131 203 KHGKTPAQVVIRWHL--QNGLVVIPKSVTPSRIAENFDV 239
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
38-283 |
2.17e-14 |
|
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from Leishmania major and Trypanosoma brucei are founding members of aldo-keto reductase family 5 member A1 (AKR5A1) and A2 (AKR5A2), respectively. PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity toward the synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde.
Pssm-ID: 381382 [Multi-domain] Cd Length: 266 Bit Score: 72.17 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 38 ADASRHVDLCLDAGVNLIDTADIYSTgvcEEIIGEVL--GGKRKDGVLIATKARFSmgpgpnDGGLSRhhLISACEASLK 115
Cdd:cd19156 23 AEAENAVKWAIEAGYRHIDTAAIYKN---EEGVGQGIreSGVPREEVFVTTKLWNS------DQGYES--TLAAFEESLE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 116 RLKTDVIDLYQVHeWDGQTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALgvsALDKRQRFVSQ-QIHYTLEARea 194
Cdd:cd19156 92 KLGLDYVDLYLIH-WPVKGKFKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELL---KSCKVAPMVNQiELHPLLTQE-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 195 eyELVPISIDQGLGILVWSPLAGGLLSGKHrrgqspegtrqlagwneppirdeerlwkivdILVAIAAERGVSPAQVALA 274
Cdd:cd19156 166 --PLRKFCKEKNIAVEAWSPLGQGKLLSNP-------------------------------VLKAIGKKYGKSAAQVIIR 212
|
....*....
gi 500691625 275 WLIGRQAVT 283
Cdd:cd19156 213 WDIQHGIIT 221
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
38-283 |
8.62e-14 |
|
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: 70.30 E-value: 8.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 38 ADASRHVDLCLDAGVNLIDTADIYSTgvcEEIIGEVL---GGKRKDgVLIATKARFSmgpgpnDGGLSRHhlISACEASL 114
Cdd:cd19133 23 EECERAVLEAIKAGYRLIDTAAAYGN---EEAVGRAIkksGIPREE-LFITTKLWIQ------DAGYEKA--KKAFERSL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 115 KRLKTDVIDLYQVHEWDGQtpLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKalgVSALDKRQRFVSQ-QIHYTLEare 193
Cdd:cd19133 91 KRLGLDYLDLYLIHQPFGD--VYGAWRAMEELYKEGKIRAIGVSNFYPDRLVD---LILHNEVKPAVNQiETHPFNQ--- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 194 aEYELVPISIDQGLGILVWSPLAggllsgkhrrgqspEGTRQLAgwNEPpirdeerlwkivdILVAIAAERGVSPAQVAL 273
Cdd:cd19133 163 -QIEAVEFLKKYGVQIEAWGPFA--------------EGRNNLF--ENP-------------VLTEIAEKYGKSVAQVIL 212
|
250
....*....|
gi 500691625 274 AWLIGRQAVT 283
Cdd:cd19133 213 RWLIQRGIVV 222
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
34-302 |
1.63e-13 |
|
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: 70.05 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 34 DVGVADASRHVDLCLDAGVNLIDTADIYSTGVCEEIIGEVLGGKRKDGVLIATKARFSMGPGPNDGGL------------ 101
Cdd:cd19161 16 AVSNADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKPRDEFVLSTKVGRLLKPAREGSVPdpngfvdplpfe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 102 -----SRHHLISACEASLKRLKTDVIDLYQVHE----WDGQTP----LEETME----ALDTLVRQGKVRYIGCSnYSGWH 164
Cdd:cd19161 96 ivydySYDGIMRSFEDSLQRLGLNRIDILYVHDigvyTHGDRKerhhFAQLMSggfkALEELKKAGVIKAFGLG-VNEVQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 165 IMkalgVSALDKRQR--FVSQQiHYTLEAREAEYELVPISIDQGLGILVWSPLAGGLLSgkhrRGQSPEGTRQlagWNEP 242
Cdd:cd19161 175 IC----LEALDEADLdcFLLAG-RYSLLDQSAEEEFLPRCEQRGTSLVIGGVFNSGILA----TGTKSGAKFN---YGDA 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 243 PirdEERLWKIVDIlVAIAAERGVSPAQVALAWLIGRQAVTSVIIGGRTEQQFRDNLAAA 302
Cdd:cd19161 243 P---AEIISRVMEI-EKICDAYNVPLAAAALQFPLRHPAVASVLTGARNPAQLRQNVEAF 298
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
48-301 |
5.46e-13 |
|
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B (DkgB) from Corynebacterium sp. and 2,5-diketo-D-gluconic acid reductase Zymomonas mobilis are founding members of aldo-keto reductase family 5 member D1 (AKR5D1) and E1 (AKR5E1), respectively. DkgB (EC 1.1.1.274), also called 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381358 [Multi-domain] Cd Length: 255 Bit Score: 68.07 E-value: 5.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 48 LDAGVNLIDTADIYSTgvcEEIIGEVL---GGKRKDgVLIATKArfsmgPGpndgglsRHH----LISACEASLKRLKTD 120
Cdd:cd19132 30 LQAGYRLLDTAFNYEN---EGAVGEAVrrsGVPREE-LFVTTKL-----PG-------RHHgyeeALRTIEESLYRLGLD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 121 VIDLYQVHeWdgqtPLE------ETMEALDTLVRQGKVRYIGCSNYSGWHI---MKALGVSALdkrqrfVSQ-QIHYTLE 190
Cdd:cd19132 94 YVDLYLIH-W----PNPsrdlyvEAWQALIEAREEGLVRSIGVSNFLPEHLdrlIDETGVTPA------VNQiELHPYFP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 191 AREAEyelvpiSIDQGLGILV--WSPLAGG--LLsgkhrrgqspegtrqlagwNEPPIrdeerlwkivdilVAIAAERGV 266
Cdd:cd19132 163 QAEQR------AYHREHGIVTqsWSPLGRGsgLL-------------------DEPVI-------------KAIAEKHGK 204
|
250 260 270
....*....|....*....|....*....|....*
gi 500691625 267 SPAQVALAWLIGRQAVtsVIIGGRTEQQFRDNLAA 301
Cdd:cd19132 205 TPAQVVLRWHVQLGVV--PIPKSANPERQRENLAI 237
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
30-299 |
6.77e-13 |
|
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: 68.21 E-value: 6.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 30 AQVGDVGVAdasrhVDLCLDAGVNLIDTADIYST----GVC-EEIIGEVLGGKRKDgVLIATKARfsmgpgpNdgglSRH 104
Cdd:cd19118 17 AEPGEVGAA-----VKIALKAGYRHLDLAKVYQNqhevGQAlKELLKEEPGVKRED-LFITSKLW-------N----NSH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 105 ---HLISACEASLKRLKTDVIDLYQVHeW-------------------------DGQTPLEETMEALDTLVRQGKVRYIG 156
Cdd:cd19118 80 rpeYVEPALDDTLKELGLDYLDLYLIH-WpvafkptgdlnpltavptnggevdlDLSVSLVDTWKAMVELKKTGKVKSIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 157 CSNYSGWH---IMKALGVsaldkrqRFVSQQIHYtlEAREAEYELVPISIDQGLGILVWSPLaGGLLSGKHRRGQSPEgt 233
Cdd:cd19118 159 VSNFSIDHlqaIIEETGV-------VPAVNQIEA--HPLLLQDELVDYCKSKNIHITAYSPL-GNNLAGLPLLVQHPE-- 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500691625 234 rqlagwneppirdeerlwkivdiLVAIAAERGVSPAQVALAWliGRQAVTSVIIGGRTEQQFRDNL 299
Cdd:cd19118 227 -----------------------VKAIAAKLGKTPAQVLIAW--GIQRGHSVIPKSVTPSRIRSNF 267
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
44-279 |
7.92e-13 |
|
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: 67.91 E-value: 7.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 44 VDLCLDAGVNLIDTADIYSTgvcEEIIGEVL------GGKRKDGVLIATKA-RFSMGPGPNDGGLsrhhlisacEASLKR 116
Cdd:cd19111 23 VDYALFVGYRHIDTALSYQN---EKAIGEALkwwlknGKLKREEVFITTKLpPVYLEFKDTEKSL---------EKSLEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 117 LKTDVIDLYQVH-------EWDGQ------TPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALgvsALDKRQRFVSQ 183
Cdd:cd19111 91 LKLPYVDLYLIHhpcgfvnKKDKGerelasSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINKIL---AYAKVKPSNLQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 184 -QIHYTLEAReaeyELVPISIDQGLGILVWSPLAGGLLSGKHRRGQSPEgtrqlagwnepPIRDEERLwkivdilvAIAA 262
Cdd:cd19111 168 lECHAYLQQR----ELRKFCNKKNIVVTAYAPLGSPGRANQSLWPDQPD-----------LLEDPTVL--------AIAK 224
|
250
....*....|....*..
gi 500691625 263 ERGVSPAQVALAWLIGR 279
Cdd:cd19111 225 ELDKTPAQVLLRFVLQR 241
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
38-300 |
1.09e-12 |
|
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: 67.24 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 38 ADASRHVDLCLDAGVNLIDTADIYSTgvcEEIIGEVLGGK--RKDGVLIATKarfsMGPGPNDGGLSRhhliSACEASLK 115
Cdd:cd19130 23 ADTQRAVATALEVGYRHIDTAAIYGN---EEGVGAAIAASgiPRDELFVTTK----LWNDRHDGDEPA----AAFAESLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 116 RLKTDVIDLYQVHeWdgQTPLE----ETMEALDTLVRQGKVRYIGCSNYSGWHIMKALGVSAldkRQRFVSQ-QIHYTLE 190
Cdd:cd19130 92 KLGLDQVDLYLVH-W--PTPAAgnyvHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVAATG---VVPAVNQiELHPAYQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 191 AREA-EYelvpiSIDQGLGILVWSPLAGGLLSGkhrrgqspegtrqlagwnEPPIrdeerlwkivdilVAIAAERGVSPA 269
Cdd:cd19130 166 QRTIrDW-----AQAHDVKIEAWSPLGQGKLLG------------------DPPV-------------GAIAAAHGKTPA 209
|
250 260 270
....*....|....*....|....*....|.
gi 500691625 270 QVALAWLIgrQAVTSVIIGGRTEQQFRDNLA 300
Cdd:cd19130 210 QIVLRWHL--QKGHVVFPKSVRRERMEDNLD 238
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
30-299 |
1.18e-12 |
|
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase (ALR) from Hordeum vulgare (AKR4C1), Bromus inermis (AKR4C2), Avena fatua (AKR4C3), and Xerophyta viscosa (AKR4C4), two aldose reductases, DpAR1 (AKR4C5) and DpAR2(AKR4C6), from Digitalis purpurea, aldehyde reductase from Zea mays (AKR4C7), four aldo-keto reductases from Arabidopsis thaliana (AKR4C8-11), and another three aldo-keto reductases from Aloe arborescens (AKR4C12) and Oryza sativa (AKR4C14/15). ALR (EC 1.1.1.21), also called AR, aldehyde reductase, or polyol dehydrogenase (NADP(+)), is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. Both DpAR1 and DpAR2 reduce the ketone group of steroid structures. They may be involved in plant steroid metabolism in general and in cardenolide biosynthesis in particular. Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops.
Pssm-ID: 381351 [Multi-domain] Cd Length: 287 Bit Score: 67.37 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 30 AQVGDVGVAdasrhVDLCLDAGVNLIDTADIYstGVCEEI---IGEVLGG---KRKDgVLIATKARFSmgpgpndgGLSR 103
Cdd:cd19125 21 ADPGVVGNA-----VKTAIKEGYRHIDCAAIY--GNEKEIgkaLKKLFEDgvvKRED-LFITSKLWCT--------DHAP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 104 HHLISACEASLKRLKTDVIDLYQVHeW-----DG----------QTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKA 168
Cdd:cd19125 85 EDVPPALEKTLKDLQLDYLDLYLIH-WpvrlkKGahmpepeevlPPDIPSTWKAMEKLVDSGKVRAIGVSNFSVKKLEDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 169 LGVSaldKRQRFVSQ-QIHYTLEareaEYELVPISIDQGLGILVWSPLAggllsgkhrrgqSPEgtrqlAGWNEPPIRDE 247
Cdd:cd19125 164 LAVA---RVPPAVNQvECHPGWQ----QDKLHEFCKSKGIHLSAYSPLG------------SPG-----TTWVKKNVLKD 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 500691625 248 ErlwkivdILVAIAAERGVSPAQVALAWliGRQAVTSVIIGGRTEQQFRDNL 299
Cdd:cd19125 220 P-------IVTKVAEKLGKTPAQVALRW--GLQRGTSVLPKSTNEERIKENI 262
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
44-282 |
1.61e-12 |
|
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: 67.17 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 44 VDLCLDAGVNLIDTADIYSTgvcEEIIGEVL------GGKRKDGVLIATKarfsMGPGPNdgglsRHHLISAC-EASLKR 116
Cdd:cd19155 31 VDTALEAGYRHIDTAYVYRN---EAAIGNVLkkwidsGKVKREELFIVTK----LPPGGN-----RREKVEKFlLKSLEK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 117 LKTDVIDLYQVH---------------------EWDGQTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALGVSALd 175
Cdd:cd19155 99 LQLDYVDLYLIHfpvgslskeddsgkldptgehKQDYTTDLLDIWKAMEAQVDQGLTRSIGLSNFNREQMARILKNARI- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 176 kRQRFVSQQIHYTLEAREaeyeLVPISIDQGLGILVWSPLAggllsgkhrrgqSPEGTRQLAGWNEPPiRDEERLWKIvD 255
Cdd:cd19155 178 -KPANLQVELHVYLQQKD----LVDFCSTHSITVTAYAPLG------------SPGAAHFSPGTGSPS-GSSPDLLQD-P 238
|
250 260
....*....|....*....|....*..
gi 500691625 256 ILVAIAAERGVSPAQVALAWLIGRQAV 282
Cdd:cd19155 239 VVKAIAERHGKSPAQVLLRWLMQRGVV 265
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
33-301 |
4.53e-12 |
|
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: 65.63 E-value: 4.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 33 GDVGVADASRHVDLCLDAGVNLIDTADIYSTGVCEEIIGEVLG--GKRKDGVLIATKarfsMGPGPNDG-GLSRHHLISA 109
Cdd:cd19153 28 DGLEQDEAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAalQVPRSSYTVATK----VGRYRDSEfDYSAERVRAS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 110 CEASLKRLKTDVIDLYQVHE---WDGQTPLEETMEALDTLVRQGKVRYIGCSNYS----GWhIMKALGVSALDKRQRFVs 182
Cdd:cd19153 104 VATSLERLHTTYLDVVYLHDiefVDYDTLVDEALPALRTLKDEGVIKRIGIAGYPldtlTR-ATRRCSPGSLDAVLSYC- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 183 qqiHYTLEAREAEYELVPISIDQGLGILVWSPLAGGLLsgkhrrgqSPEGTRQlagWNepPIRDEERLWKIVDilVAIAA 262
Cdd:cd19153 182 ---HLTLQDARLESDAPGLVRGAGPHVINASPLSMGLL--------TSQGPPP---WH--PASGELRHYAAAA--DAVCA 243
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 500691625 263 ERGVSPAQVALAWLIGRQA-VTSVIIGGRTEQQFRDNLAA 301
Cdd:cd19153 244 SVEASLPDLALQYSLAAHAgVGTVLLGPSSLAQLRSMLAA 283
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
32-299 |
1.52e-11 |
|
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding member of aldo-keto reductase family 5 member H1 (AKR5H1). It is a NADPH-dependent aldo-keto reductase that reduces methylglyoxal and phenylglyoxal.
Pssm-ID: 381360 [Multi-domain] Cd Length: 263 Bit Score: 63.72 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 32 VGDVGVADASRHVDLCLDAGVNLIDTADIYSTgvcEEIIGEVL--GGKRKDGVLIATKARFSmgpgpnDGGLSRHhlISA 109
Cdd:cd19134 18 VGELSDDEAERSVSAALEAGYRLIDTAAAYGN---EAAVGRAIaaSGIPRGELFVTTKLATP------DQGFTAS--QAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 110 CEASLKRLKTDVIDLYQVHeWDG--QTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALGVSALDKrqrfVSQQIHy 187
Cdd:cd19134 87 CRASLERLGLDYVDLYLIH-WPAgrEGKYVDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLTFFTP----AVNQIE- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 188 tLEAREAEYELVPISIDQGLGILVWSPLAGGLLSgkhrrgQSPEGTRqlagwneppirdeerlwkivdilvaIAAERGVS 267
Cdd:cd19134 161 -LHPLLNQAELRKVNAQHGIVTQAYSPLGVGRLL------DNPAVTA-------------------------IAAAHGRT 208
|
250 260 270
....*....|....*....|....*....|..
gi 500691625 268 PAQVALAWLIgrQAVTSVIIGGRTEQQFRDNL 299
Cdd:cd19134 209 PAQVLLRWSL--QLGNVVISRSSNPERIASNL 238
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
48-298 |
1.97e-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: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 48 LDAGVNLIDTADIYSTgvcEEIIGEVL------GGKRKDGVLIATKArfsmgpgpndggLSRHH----LISACEASLKRL 117
Cdd:cd19129 29 LEAGFRHFDCAERYRN---EAEVGEAMqevfkaGKIRREDLFVTTKL------------WNTNHrperVKPAFEASLKRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 118 KTDVIDLYQVHE------WDGQTP--------------LEETMEALDTLVRQGKVRYIGCSNYSgwhimkalgvsaLDKR 177
Cdd:cd19129 94 QLDYLDLYLIHTpfafqpGDEQDPrdangnviyddgvtLLDTWRAMERLVDEGRCKAIGLSDVS------------LEKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 178 QR-FVSQQIHYTLEAREA-----EYELVPISIDQGLGILVWSPLAGGLlsgkhrrgqspegtrqlagwnEP-PIRDEerl 250
Cdd:cd19129 162 REiFEAARIKPAVVQVEShpylpEWELLDFCKNHGIVLQAFAPLGHGM---------------------EPkLLEDP--- 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 500691625 251 wkivdILVAIAAERGVSPAQVALAWLIGRQavTSVIIGGRTEQQFRDN 298
Cdd:cd19129 218 -----VITAIARRVNKTPAQVLLAWAIQRG--TALLTTSKTPSRIREN 258
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
48-299 |
2.23e-11 |
|
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: 64.04 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 48 LDAGVNLIDTADIYSTgvcEEIIGEVLGG-------KRKDgVLIATKARFSmgpgpnDGGlsrhHLISACEASLKRLKTD 120
Cdd:cd19112 34 IKIGYRHFDCAADYKN---EKEVGEALAEafktglvKRED-LFITTKLWNS------DHG----HVIEACKDSLKKLQLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 121 VIDLYQVH-----------------------EWDGQTPLEETMEALDTLVRQGKVRYIGCSNYSgwhIMKALGVSALDKR 177
Cdd:cd19112 100 YLDLYLVHfpvatkhtgvgttgsalgedgvlDIDVTISLETTWHAMEKLVSAGLVRSIGISNYD---IFLTRDCLAYSKI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 178 QRFVSQQIHYTLEAREAeyeLVPISIDQGLGILVWSPLAGGLlSGKHRRGQSPegtrqlagwnepPIRDEerlwkivdIL 257
Cdd:cd19112 177 KPAVNQIETHPYFQRDS---LVKFCQKHGISVTAHTPLGGAA-ANAEWFGSVS------------PLDDP--------VL 232
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 500691625 258 VAIAAERGVSPAQVALAWLIGRQavTSVIIGGRTEQQFRDNL 299
Cdd:cd19112 233 KDLAKKYGKSAAQIVLRWGIQRN--TAVIPKSSKPERLKENI 272
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
48-275 |
3.18e-11 |
|
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: 62.81 E-value: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 48 LDAGVNLIDTADIYSTgvcEEIIGEVL---GGKRKDgVLIATKARFSmgpgpnDGGLSRhhLISACEASLKRLKTDVIDL 124
Cdd:cd19127 32 LADGYRLIDTAAAYGN---EREVGEGIrrsGVDRSD-IFVTTKLWIS------DYGYDK--ALRGFDASLRRLGLDYVDL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 125 YQVHeWDGQTPLEETME---ALDTLVRQGKVRYIGCSNYSGWH---IMKALG-VSALDKRQ--RFVSQQihytlEAREAe 195
Cdd:cd19127 100 YLLH-WPVPNDFDRTIQaykALEKLLAEGRVRAIGVSNFTPEHlerLIDATTvVPAVNQVElhPYFSQK-----DLRAF- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 196 yelvpisiDQGLGILV--WSPLaGGLLSgkhRRGQSPEGTRQlagwnepPIRDEerlwkivdILVAIAAERGVSPAQVAL 273
Cdd:cd19127 173 --------HRRLGIVTqaWSPI-GGVMR---YGASGPTGPGD-------VLQDP--------TITGLAEKYGKTPAQIVL 225
|
..
gi 500691625 274 AW 275
Cdd:cd19127 226 RW 227
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
44-299 |
3.04e-10 |
|
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: 60.23 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 44 VDLCLDAGVNLIDTADIYSTgvcEEIIGEVL-------GGKRKDgVLIATKarfsMGPGPNDGGLSRHHlisaCEASLKR 116
Cdd:cd19128 20 VKNAIKAGYRHIDCAYYYGN---EAFIGIAFseifkdgGVKRED-LFITSK----LWPTMHQPENVKEQ----LLITLQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 117 LKTDVIDLYQVHeW--------------------DGQTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALGVSaldK 176
Cdd:cd19128 88 LQLEYLDLFLIH-WplafdmdtdgdprddnqiqsLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLNYC---K 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 177 RQRFVSQ-QIHYTLEareaEYELVPISIDQGLGILVWSPLAGGLlsgkhrrgqspegtrqlagwneppiRDEERLWKIVD 255
Cdd:cd19128 164 IKPFMNQiECHPYFQ----NDKLIKFCIENNIHVTAYRPLGGSY-------------------------GDGNLTFLNDS 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 500691625 256 ILVAIAAERGVSPAQVALAWLIGRQAVT-SVIIGGRTEQQFRDNL 299
Cdd:cd19128 215 ELKALATKYNTTPPQVIIAWHLQKWPKNySVIPKSANKSRCQQNF 259
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
48-160 |
4.58e-10 |
|
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: 59.98 E-value: 4.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 48 LDAGVNLIDTADIYstGVCEEIIGEVLGGKR----KDGVLIATKA-RFsmgpGPNDGGLSRHHLISACEASLKRLKTDVI 122
Cdd:cd19164 44 LELGIRAFDTSPYY--GPSEIILGRALKALRdefpRDTYFIITKVgRY----GPDDFDYSPEWIRASVERSLRRLHTDYL 117
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 500691625 123 DLYQVH--EWdgqTPLEETMEALDTLVR---QGKVRYIGCSNY 160
Cdd:cd19164 118 DLVYLHdvEF---VADEEVLEALKELFKlkdEGKIRNVGISGY 157
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
39-299 |
4.41e-09 |
|
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: 56.74 E-value: 4.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 39 DASRHVDLCLDAGVNLIDTADIYSTgvcEEIIGEvlgGKRKDGV-----LIATKArfsmgpgpnDGglSRHHLISAC-EA 112
Cdd:cd19117 28 EVAKAVEAALKAGYRHIDTAAIYGN---EEEVGQ---GIKDSGVpreeiFITTKL---------WC--TWHRRVEEAlDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 113 SLKRLKTDVIDLYQVH-------------------------EWDgqtpLEETMEALDTLVRQGKVRYIGCSNYSGWHIMK 167
Cdd:cd19117 91 SLKKLGLDYVDLYLMHwpvpldpdgndflfkkddgtkdhepDWD----FIKTWELMQKLPATGKVKAIGVSNFSIKNLEK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 168 ALGvSALDKRQRFVSQ-QIHYTLeareAEYELVPISIDQGLGILVWSPLaggllsgkhrrGQSpegtrqlagwNEPPIRD 246
Cdd:cd19117 167 LLA-SPSAKIVPAVNQiELHPLL----PQPKLVDFCKSKGIHATAYSPL-----------GST----------NAPLLKE 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 500691625 247 EerlwkivdILVAIAAERGVSPAQVALAWliGRQAVTSVIIGGRTEQQFRDNL 299
Cdd:cd19117 221 P--------VIIKIAKKHGKTPAQVIISW--GLQRGYSVLPKSVTPSRIESNF 263
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
44-299 |
1.80e-08 |
|
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: 54.96 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 44 VDLCLDAGVNLIDTADIYSTgvcEEIIGEVLGGKRKDGVL------IATKARFSmgpgpndggLSRHHLI-SACEASLKR 116
Cdd:cd19110 23 VKVAIDAGYRHFDCAYLYHN---ESEVGAGIREKIKEGVVrredlfIVSKLWCT---------CHKKSLVkTACTRSLKA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 117 LKTDVIDLYQVHeW-------DGQTPLEE-------------TMEALDTLVRQGKVRYIGCSNYSGWHIMKALGVSALdk 176
Cdd:cd19110 91 LKLNYLDLYLIH-WpmgfkpgEPDLPLDRsgmvipsdtdfldTWEAMEDLVIEGLVKNIGVSNFNHEQLERLLNKPGL-- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 177 RQRFVSQQI--HYTLEAReaeyELVPISIDQGLGILVWSPLAGgllsgkhrrgqSPEGTRQLagwNEPPIRdeerlwkiv 254
Cdd:cd19110 168 RVKPVTNQIecHPYLTQK----KLISFCQSRNVSVTAYRPLGG-----------SCEGVDLI---DDPVIQ--------- 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 500691625 255 dilvAIAAERGVSPAQVALAWLIGRQAVtsVIIGGRTEQQFRDNL 299
Cdd:cd19110 221 ----RIAKKHGKSPAQILIRFQIQRNVI--VIPKSVTPSRIKENI 259
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
44-299 |
1.14e-07 |
|
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: 52.81 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 44 VDLCLDAGVNLIDTADIYSTgvcEEIIGEVLGGKRKDGVL------IATKarfsMGPGPNDGGLSRhhliSACEASLKRL 117
Cdd:cd19107 23 VKVAIDAGYRHIDCAYVYQN---ENEVGEAIQEKIKEQVVkredlfIVSK----LWCTFHEKGLVK----GACQKTLSDL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 118 KTDVIDLYQVHeW-------DGQTPLEE-------------TMEALDTLVRQGKVRYIGCSNYSGWHIMKALGVSALdkR 177
Cdd:cd19107 92 KLDYLDLYLIH-WptgfkpgKELFPLDEsgnvipsdttfldTWEAMEELVDEGLVKAIGVSNFNHLQIERILNKPGL--K 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 178 QRFVSQQI--HYTLeareAEYELVPISIDQGLGILVWSPLAggllsgkhrrgqSPEgtRQLAGWNEPPIRDEERlwkivd 255
Cdd:cd19107 169 YKPAVNQIecHPYL----TQEKLIQYCQSKGIVVTAYSPLG------------SPD--RPWAKPEDPSLLEDPK------ 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 500691625 256 iLVAIAAERGVSPAQVALAWLIGRQAVtsVIIGGRTEQQFRDNL 299
Cdd:cd19107 225 -IKEIAAKHNKTTAQVLIRFPIQRNLV--VIPKSVTPERIAENF 265
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
48-275 |
2.33e-07 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 51.61 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 48 LDAGVNLIDTADIYSTgvcEEIIGEVL--GGKRKDGVLIATKARfsmgpgpNDgglSRHHLISACEASLKRLKTDVIDLY 125
Cdd:PRK11565 38 LEVGYRSIDTAAIYKN---EEGVGKALkeASVAREELFITTKLW-------ND---DHKRPREALEESLKKLQLDYVDLY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 126 QVHeWdgQTPLEETM----EALDTLVRQGKVRYIGCSNYSGWHIMKAL---GVSAldkrqrfVSQQI--HYTLEARE--- 193
Cdd:PRK11565 105 LMH-W--PVPAIDHYveawKGMIELQKEGLIKSIGVCNFQIHHLQRLIdetGVTP-------VINQIelHPLMQQRQlha 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 194 --AEYELVPISidqglgilvWSPLAggllsgkhrrgQSPEGTrqlagWNEPPIRDeerlwkivdilvaIAAERGVSPAQV 271
Cdd:PRK11565 175 wnATHKIQTES---------WSPLA-----------QGGKGV-----FDQKVIRD-------------LADKYGKTPAQI 216
|
....
gi 500691625 272 ALAW 275
Cdd:PRK11565 217 VIRW 220
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
55-299 |
2.68e-07 |
|
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: 51.11 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 55 IDTADIYSTgvcEEIIGEVLGGKRKDGvLIATKARFSMGPGPNDGGLSRHHLISACEASLKRLKTDVIDLYQVHeW---- 130
Cdd:cd19124 37 FDTAAAYGT---EEALGEALAEALRLG-LVKSRDELFVTSKLWCSDAHPDLVLPALKKSLRNLQLEYVDLYLIH-Wpvsl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 131 -----------DGQTPL--EETMEALDTLVRQGKVRYIGCSNYSGWHIMKALGVSALDKRqrfVSQ-QIHYTLEARE-AE 195
Cdd:cd19124 112 kpgkfsfpieeEDFLPFdiKGVWEAMEECQRLGLTKAIGVSNFSCKKLQELLSFATIPPA---VNQvEMNPAWQQKKlRE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 196 YelvpisiDQGLGILV--WSPLAGGllsgkhrrgqspeGTRqlagWNEPPIRDEerlwkivDILVAIAAERGVSPAQVAL 273
Cdd:cd19124 189 F-------CKANGIHVtaYSPLGAP-------------GTK----WGSNAVMES-------DVLKEIAAAKGKTVAQVSL 237
|
250 260
....*....|....*....|....*.
gi 500691625 274 AWLIgRQAVtSVIIGGRTEQQFRDNL 299
Cdd:cd19124 238 RWVY-EQGV-SLVVKSFNKERMKQNL 261
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
39-282 |
6.41e-07 |
|
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: 50.22 E-value: 6.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 39 DASRHVDLCLDAGVNLIDTADIYSTgvcEEIIGEVL-----GGKRKDGVLIATKArfsmgpgpndggLSRHH--LISACE 111
Cdd:cd19121 26 EVKAAVAHALKIGYRHIDGALCYQN---EDEVGEGIkeaiaGGVKREDLFVTTKL------------WSTYHrrVELCLD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 112 ASLKRLKTDVIDLYQVHeW-----------------DGQTPLEETMEALDT------LVRQGKVRYIGCSNYS-GW--HI 165
Cdd:cd19121 91 RSLKSLGLDYVDLYLVH-WpvllnpngnhdlfptlpDGSRDLDWDWNHVDTwkqmekVLKTGKTKAIGVSNYSiPYleEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 166 MK-ALGVSAldkrqrfVSQ-QIHYTLeareAEYELVPISIDQGLGILVWSPL--AGGllsgkhrrgqspegtrqlagwne 241
Cdd:cd19121 170 LKhATVVPA-------VNQvENHPYL----PQQELVDFCKEKGILIEAYSPLgsTGS----------------------- 215
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 500691625 242 PPIRDEErlwkivdiLVAIAAERGVSPAQVALAWLIGRQAV 282
Cdd:cd19121 216 PLISDEP--------VVEIAKKHNVGPGTVLISYQVARGAV 248
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
105-303 |
1.43e-06 |
|
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: 49.34 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 105 HLISACEASLKRLKTDVIDLYQVH----------------EWD--------GQTPLEETMEALDTLVRQGKVRYIGCSNY 160
Cdd:cd19115 88 RVEPICRKQLADWGIDYFDLFLIHfpialkyvdpavryppGWFydgkkvefSNAPIQETWTAMEKLVDKGLARSIGVSNF 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 161 SGWHIMKALGVSaldkRQRFVSQQI--HYTLEAReaeyELVPISIDQGLGILVWSPLagGLLSGKHRRGQSPEGTrqlag 238
Cdd:cd19115 168 SAQLLMDLLRYA----RIRPATLQIehHPYLTQP----RLVKYAQKEGIAVTAYSSF--GPQSFLELDLPGAKDT----- 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500691625 239 wnePPIRDEerlwkivDILVAIAAERGVSPAQVALAWLIGRQavTSVIIGGRTEQQFRDNLAAAG 303
Cdd:cd19115 233 ---PPLFEH-------DVIKSIAEKHGKTPAQVLLRWATQRG--IAVIPKSNNPKRLAQNLDVTG 285
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
109-275 |
6.98e-06 |
|
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: 47.06 E-value: 6.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 109 ACEASLKRLKTDVIDLYQVH------------------------EWD-GQTPLEETMEALDTLVRQGKVRYIGCSNYSGW 163
Cdd:cd19113 90 ALNKTLSDLKLDYVDLFLIHfpiafkfvpieekyppgfycgdgdNFVyEDVPILDTWKALEKLVDAGKIKSIGVSNFPGA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 164 HIMKALGVSaldkRQRFVSQQIH---YTLEAREAEYElvpisidQGLGILVwsplaggllsgkhrRGQSPEGTRQLAGWN 240
Cdd:cd19113 170 LILDLLRGA----TIKPAVLQIEhhpYLQQPKLIEYA-------QKAGITI--------------TAYSSFGPQSFVELN 224
|
170 180 190
....*....|....*....|....*....|....*
gi 500691625 241 EPPIRDEERLWKiVDILVAIAAERGVSPAQVALAW 275
Cdd:cd19113 225 QGRALNTPTLFE-HDTIKSIAAKHNKTPAQVLLRW 258
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
122-327 |
2.03e-05 |
|
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: 45.80 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 122 IDLYQVHEWDGQTPLEETMEALDTLVRQGK--VRyIGCSnYSGWH----IMKALGVsALDKRQRFVSQQIHYTL------ 189
Cdd:cd19098 125 LDLYQIHSATLESGVLEDADVLAALAELKAegVK-IGLS-LSGPQqaetLRRALEI-EIDGARLFDSVQATWNLleqsag 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 190 EAREAEYElvpisidQGLGILVWSPLAGGLLSgkhRRGQSPEgtrqlagwneppirdeerLWKIVDILVAIAAERGVSPA 269
Cdd:cd19098 202 EALEEAHE-------AGMGVIVKEALANGRLT---DRNPSPE------------------LAPLMAVLKAVADRLGVTPD 253
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 500691625 270 QVALAWLIGRQAVTSVIIGGRTEQQFRDNLAAAGLRLTEEERELLEAVSRPPViyPYW 327
Cdd:cd19098 254 ALALAAVLAQPFVDVVLSGAATPEQLRSNLRALDVSLDLELLAALADLAEPPE--DYW 309
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
111-282 |
4.21e-05 |
|
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: 44.54 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 111 EASLKRLKTDVIDLYQVHeW----------------DGQTPL--------EETMEALDTLVRQGKVRYIGCSNysgWHIM 166
Cdd:cd19122 93 DNSLKNLKLDYIDLFLVH-WpiaaekndqrspklgpDGKYVIlkdltenpEPTWRAMEEIYESGKAKAIGVSN---WTIP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 167 KALGVSALDKRQRFVSQ-QIHYTLEAReaeyELVPISIDQGLGILVWSPLAGgllsgkhrRGQSPEGTRQLagwNEPPir 245
Cdd:cd19122 169 GLKKLLSFAKVKPHVNQiEIHPFLPNE----ELVDYCFSNDILPEAYSPLGS--------QNQVPSTGERV---SENP-- 231
|
170 180 190
....*....|....*....|....*....|....*..
gi 500691625 246 deerlwkivdILVAIAAERGVSPAQVALAWLIGRQAV 282
Cdd:cd19122 232 ----------TLNEVAEKGGYSLAQVLIAWGLRRGYV 258
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
50-282 |
1.36e-03 |
|
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: 40.23 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 50 AGVNLIDTADIYSTGVceeiigEVLGGKRK---DGvLIATKARFSMGPGPNDGGlSRHHLISACEASLKRLKTDVIDLYQ 126
Cdd:cd19114 29 VGYRLIDGALLYGNEA------EVGRGIRKaiqEG-LVKREDLFIVTKLWNNFH-GKDHVREAFDRQLKDYGLDYIDLYL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 127 VH--------------------------EWDgQTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALGVSALdkRQRF 180
Cdd:cd19114 101 IHfpipaayvdpaenypflwkdkelkkfPLE-QSPMQECWREMEKLVDAGLVRNIGIANFNVQLILDLLTYAKI--KPAV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 181 VSQQIHYTLEAReaeyELVPISIDQGLGILVWSPLaggllsGKHRRGQSPEGTRQLAGWNEPPirdeerlwkivdILVAI 260
Cdd:cd19114 178 LQIEHHPYLQQK----RLIDWAKKQGIQITAYSSF------GNAVYTKVTKHLKHFTNLLEHP------------VVKKL 235
|
250 260
....*....|....*....|..
gi 500691625 261 AAERGVSPAQVALAWLIGRQAV 282
Cdd:cd19114 236 ADKHKRDTGQVLLRWAVQRNIT 257
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
44-298 |
1.95e-03 |
|
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: 39.40 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 44 VDLCLDAGVNLIDTADIYS--TGVCEEIIGEVLGG--KRKD----GVLIATKarfsmgpgpNDGGLSRHHLisacEASLK 115
Cdd:cd19109 27 VKVAIDTGYRHIDGAYIYQneHEVGQAIREKIAEGkvKREDifycGKLWNTC---------HPPELVRPTL----ERTLK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 116 RLKTDVIDLYQVH--------------EWDG-----QTPLEETMEALDTLVRQGKVRYIGCSNYSGWHIMKALGVSALdk 176
Cdd:cd19109 94 VLQLDYVDLYIIEmpmafkpgdeiyprDENGkwlyhKTNLCATWEALEACKDAGLVKSIGVSNFNRRQLELILNKPGL-- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500691625 177 RQRFVSQQIH---YTLEAREAEYelvpisIDQGLGILVwsplaggllsgkhrrGQSPEGTRQLAGW---NEPPIRDEErl 250
Cdd:cd19109 172 KHKPVSNQVEchpYFTQPKLLEF------CQQHDIVIV---------------AYSPLGTCRDPIWvnvSSPPLLEDP-- 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 500691625 251 wkivdILVAIAAERGVSPAQVALAWLIGRQAVtsVIIGGRTEQQFRDN 298
Cdd:cd19109 229 -----LLNSIGKKYNKTAAQVVLRFNIQRGVV--VIPKSFNPERIKEN 269
|
|
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