|
Name |
Accession |
Description |
Interval |
E-value |
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
35-370 |
4.44e-144 |
|
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.
Pssm-ID: 99747 [Multi-domain] Cd Length: 349 Bit Score: 412.34 E-value: 4.44e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 35 QSYINFTSNDYLGIGQLEYQPQNFLDFIKTYSIHLSSSRLVSGNSVVYQQLEQAISEHFNFEDALIFNSGYDANLAVFNI 114
Cdd:cd06454 1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 115 FKNNNVVIFSDQQNHASIIDGIKLSGLSKVIYQHLNYDDLESHLARHTNPDVQKVIVSDSVFSTNGTKADINRLVHLKQR 194
Cdd:cd06454 81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARRPYGKKLIVTEGVYSMDGDIAPLPELVDLAKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 195 YNAILIIDASHSLGLN---------LFEYHADIDIVTSSLSKAWGAHGGVIFSSKDIKDLIINKGRSLIYSSSLPSYHLY 265
Cdd:cd06454 161 YGAILFVDEAHSVGVYgphgrgveeFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 266 FIQVSLQHVIEDTYRREKLNVLSEYFNHQFMELFPDQPLSN-TPIKNIVCDSLASAQAQYDMLFEHGIFVSYLRYPTVSQ 344
Cdd:cd06454 241 AALAALEVLQGGPERRERLQENVRYLRRGLKELGFPVGGSPsHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTVPR 320
|
330 340
....*....|....*....|....*...
gi 488368310 345 PT--LRISLSYFHDTDDIDRLFNVMKQY 370
Cdd:cd06454 321 GTarLRISLSAAHTKEDIDRLLEALKEV 348
|
|
| BioF |
COG0156 |
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ... |
3-369 |
2.43e-118 |
|
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; 7-keto-8-aminopelargonate synthetase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 439926 [Multi-domain] Cd Length: 385 Bit Score: 348.19 E-value: 2.43e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 3 IKAQLKQIQDKVLYRELQPIQSVEKQYIYINDQSYINFTSNDYLGigqLEYQP---QNFLDFIKTYSIHLSSSRLVSGNS 79
Cdd:COG0156 5 LEAELAALKAAGLYRYLRVLESPQGPRVTIDGREVLNFSSNDYLG---LANHPrviEAAAEALDRYGTGSGGSRLVSGTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 80 VVYQQLEQAISEHFNFEDALIFNSGYDANLAVFNIFKNNNVVIFSDQQNHASIIDGIKLSGLSKVIYQHLNYDDLESHLA 159
Cdd:COG0156 82 PLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 160 RHTnPDVQKVIVSDSVFSTNGTKADINRLVHLKQRYNAILIIDASHSLG---------LNLFEYHADIDIVTSSLSKAWG 230
Cdd:COG0156 162 KAR-AARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGvlgetgrglVEHFGLEDRVDIIMGTLSKALG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 231 AHGGVIFSSKDIKDLIINKGRSLIYSSSLPSYHLYFIQVSLQHVIEDTYRREKLNVLSEYFNHQFMEL-FPDQPlSNTPI 309
Cdd:COG0156 241 SSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELgFDLGP-SESPI 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488368310 310 KNIVCDSLASAQAQYDMLFEHGIFVSYLRYPTVSQPT--LRISLSYFHDTDDIDRLFNVMKQ 369
Cdd:COG0156 320 VPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTarLRITLSAAHTEEDIDRLLEALAE 381
|
|
| PRK05958 |
PRK05958 |
8-amino-7-oxononanoate synthase; Reviewed |
2-369 |
1.91e-92 |
|
8-amino-7-oxononanoate synthase; Reviewed
Pssm-ID: 235655 [Multi-domain] Cd Length: 385 Bit Score: 282.05 E-value: 1.91e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 2 DIKAQLKQIQDKVLYRELQPIQSVEKQYIYINDQSYINFTSNDYLGIGQLEYQPQNFLDFIKTYSIHLSSSRLVSGNSVV 81
Cdd:PRK05958 6 RLEAALAQRRAAGLYRSLRPREGGAGRWLVVDGRRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVTGNSPA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 82 YQQLEQAISEHFNFEDALIFNSGYDANLAVFNIFKNNNVVIFSDQQNHASIIDGIKLSGLSKVIYQHLNYDDLESHLARH 161
Cdd:PRK05958 86 HEALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALLAKW 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 162 TNPdvQKVIVSDSVFSTNGTKADINRLVHLKQRYNAILIIDASHSLG---------LNLFEYHADID-IVTSSLSKAWGA 231
Cdd:PRK05958 166 RAG--RALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGvlgpqgrglAAEAGLAGEPDvILVGTLGKALGS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 232 HGGVIFSSKDIKDLIINKGRSLIYSSSLPSYHLYFIQVSLQHVIEDTYRREKLNVLSEYFNHQFMELFPDQPLSNTPIKN 311
Cdd:PRK05958 244 SGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRALGFQLMDSQSAIQP 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 312 IVCDSLASAQAQYDMLFEHGIFVSYLRYPTVSQPT--LRISLSYFHDTDDIDRLFNVMKQ 369
Cdd:PRK05958 324 LIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTsrLRITLTAAHTEADIDRLLEALAE 383
|
|
| bioF |
TIGR00858 |
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ... |
20-368 |
4.55e-84 |
|
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. This model represents 8-amino-7-oxononanoate synthase, the BioF protein of biotin biosynthesis. This model is based on a careful phylogenetic analysis to separate members of this family from 2-amino-3-ketobutyrate and other related pyridoxal phosphate-dependent enzymes. In several species, including Staphylococcus and Coxiella, a candidate 8-amino-7-oxononanoate synthase is confirmed by location in the midst of a biotin biosynthesis operon but scores below the trusted cutoff of this model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]
Pssm-ID: 273303 [Multi-domain] Cd Length: 360 Bit Score: 259.89 E-value: 4.55e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 20 QPIQSVEKQYIYINDQSYINFTSNDYLGIGQLEYQPQNFLDFIKTYSIHLSSSRLVSGNSVVYQQLEQAISEHFNFEDAL 99
Cdd:TIGR00858 1 RPLDRGPGPEVVRDGRRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 100 IFNSGYDANLAVFNIFKNNNVVIFSDQQNHASIIDGIKLSGLSKVIYQHLNYDDLESHLARHTNPDvQKVIVSDSVFSTN 179
Cdd:TIGR00858 81 LFSSGYLANVGVISALVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGER-RKLIVTDGVFSMD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 180 GTKADINRLVHLKQRYNAILIIDASHSLG------LNLFEY----HADIDIVTSSLSKAWGAHGGVIFSSKDIKDLIINK 249
Cdd:TIGR00858 160 GDIAPLPQLVALAERYGAWLMVDDAHGTGvlgedgRGTLEHfglkPEPVDIQVGTLSKALGSYGAYVAGSQALIDYLINR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 250 GRSLIYSSSLPSYHLYFIQVSLQHVIEDTYRREKLNVLSEYFNHQFMELFPDQPLSNTPIKNIVCDSLASAQAQYDMLFE 329
Cdd:TIGR00858 240 ARTLIFSTALPPAVAAAALAALELIQEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEELQQ 319
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 488368310 330 HGIFVSYLRYPTVSQPT--LRISLSYFHDTDDIDRLFNVMK 368
Cdd:TIGR00858 320 QGIFVGAIRPPTVPAGTsrLRLTLSAAHTPGDIDRLAEALK 360
|
|
| PRK06939 |
PRK06939 |
2-amino-3-ketobutyrate coenzyme A ligase; Provisional |
2-362 |
1.96e-59 |
|
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
Pssm-ID: 235893 [Multi-domain] Cd Length: 397 Bit Score: 197.34 E-value: 1.96e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 2 DIKAQLKQIQDKVLYRELQPIQSVEKQYIYIND-QSYINFTSNDYLGIG---QLEYQPQNFLDfikTYSIHLSSSRLVSG 77
Cdd:PRK06939 8 QLREELEEIKAEGLYKEERVITSPQGADITVADgKEVINFCANNYLGLAnhpELIAAAKAALD---SHGFGMASVRFICG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 78 NSVVYQQLEQAISEHFNFEDALIFNSGYDANLAVFNIFKNNNVVIFSDQQNHASIIDGIKLSGLSKVIYQHLNYDDLESH 157
Cdd:PRK06939 85 TQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 158 L-------ARHtnpdvqKVIVSDSVFSTNGTKADINRLVHLKQRYNAILIIDASHSLG---------LNLFEYHADIDIV 221
Cdd:PRK06939 165 LkeakeagARH------KLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGfvgengrgtVEHFGVMDRVDII 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 222 TSSLSKA-WGAHGGVIFSSKDIKDLIINKGRSLIYSSSL-PSYHLYFIQVsLQHVIEDTYRREKLNVLSEYFNHQFMELF 299
Cdd:PRK06939 239 TGTLGKAlGGASGGYTAGRKEVIDWLRQRSRPYLFSNSLaPAIVAASIKV-LELLEESDELRDRLWENARYFREGMTAAG 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488368310 300 PDQPLSNTPIKNIVCDSLASAQAQYDMLFEHGIFVSYLRYPTVSQPTLRI--SLSYFHDTDDIDR 362
Cdd:PRK06939 318 FTLGPGEHPIIPVMLGDAKLAQEFADRLLEEGVYVIGFSFPVVPKGQARIrtQMSAAHTKEQLDR 382
|
|
| 5aminolev_synth |
TIGR01821 |
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ... |
42-367 |
4.32e-49 |
|
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an enzyme for one of two routes to the heme precursor 5-aminolevulinate. The protein is a pyridoxal phosphate-dependent enzyme related to 2-amino-3-ketobutyrate CoA tranferase and 8-amino-7-oxononanoate synthase. This enzyme appears restricted to the alpha Proteobacteria and mitochondrial derivatives. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 273820 [Multi-domain] Cd Length: 402 Bit Score: 170.29 E-value: 4.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 42 SNDYLGIGQLEYQPQNFLDFIKTYSIHLSSSRLVSGNSVVYQQLEQAISEHFNFEDALIFNSGYDANLAVF----NIFKN 117
Cdd:TIGR01821 52 SNDYLGMGQHPEVLQAMHETLDKYGAGAGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLatlaKIIPG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 118 nnVVIFSDQQNHASIIDGIKLSGLSKVIYQHLNYDDLESHLARhTNPDVQKVIVSDSVFSTNGTKADINRLVHLKQRYNA 197
Cdd:TIGR01821 132 --CVIFSDELNHASMIEGIRHSGAEKFIFRHNDVAHLEKLLQS-VDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 198 ILIIDASHSLGL---------NLFEYHADIDIVTSSLSKAWGAHGGVIFSSKDIKDLIINKGRSLIYSSSLPSYHLYFIQ 268
Cdd:TIGR01821 209 LTYLDEVHAVGLygprgggiaERDGLMHRIDIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGAT 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 269 VSLQHVIEDTYRREKLNVLSEYFNHQFMEL-FP--DQPLSNTPIknIVCDSLASAQAQYDMLFEHGIFVSYLRYPTVSQP 345
Cdd:TIGR01821 289 ASIRHLKESQDLRRAHQENVKRLKNLLEALgIPviPNPSHIVPV--IIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRG 366
|
330 340
....*....|....*....|....
gi 488368310 346 T--LRISLSYFHDTDDIDRLFNVM 367
Cdd:TIGR01821 367 TerLRITPTPAHTDKMIDDLVEAL 390
|
|
| PRK13392 |
PRK13392 |
5-aminolevulinate synthase; Provisional |
42-363 |
7.55e-45 |
|
5-aminolevulinate synthase; Provisional
Pssm-ID: 184023 [Multi-domain] Cd Length: 410 Bit Score: 159.25 E-value: 7.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 42 SNDYLGIGQLEYQPQNFLDFIKTYSIHLSSSRLVSGNSVVYQQLEQAISEHFNFEDALIFNSGYDANLAVFNIF--KNNN 119
Cdd:PRK13392 53 SNDYLGMGQHPDVIGAMVDALDRYGAGAGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLgkLLPG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 120 VVIFSDQQNHASIIDGIKLSGLSKVIYQHLNYDDLESHLARhTNPDVQKVIVSDSVFSTNGTKADINRLVHLKQRYNAIL 199
Cdd:PRK13392 133 CVILSDALNHASMIEGIRRSGAEKQVFRHNDLADLEEQLAS-VDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALT 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 200 IIDASHSLGLnlfeYHAD-------------IDIVTSSLSKAWGAHGGVIFSSKDIKDLIINKGRSLIYSSSLPSYHLYF 266
Cdd:PRK13392 212 YVDEVHAVGL----YGARgggiaerdglmdrIDMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 267 IQVSLQHVIEDTYRREKLNVLSEYFNHQFMEL-FPDQPlSNTPIKNIVCDSLASAQAQYDMLF-EHGIFVSYLRYPTVSQ 344
Cdd:PRK13392 288 ATAAIRHLKTSQTERDAHQDRVAALKAKLNANgIPVMP-SPSHIVPVMVGDPTLCKAISDRLMsEHGIYIQPINYPTVPR 366
|
330 340
....*....|....*....|.
gi 488368310 345 PT--LRISLSYFHDTDDIDRL 363
Cdd:PRK13392 367 GTerLRITPTPLHDDEDIDAL 387
|
|
| PLN02955 |
PLN02955 |
8-amino-7-oxononanoate synthase |
40-363 |
1.03e-41 |
|
8-amino-7-oxononanoate synthase
Pssm-ID: 178541 [Multi-domain] Cd Length: 476 Bit Score: 152.52 E-value: 1.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 40 FTSNDYLGIGQLEYQPQNFLDFIKTYSIHLSSSRLVSGNSVVYQQLEQAISEHFNFEDALIFNSGYDANLAVF------- 112
Cdd:PLN02955 107 FSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMvaigsva 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 113 -------NIFKNNNVVIFSDQQNHASIIDGIKLS---GLSKV-IYQHLNYDDLESHLARHTNPdvQKVIVSDSVFSTNGT 181
Cdd:PLN02955 187 sllaasgKPLKNEKVAIFSDALNHASIIDGVRLAerqGNVEVfVYRHCDMYHLNSLLSSCKMK--RKVVVTDSLFSMDGD 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 182 KADINRLVHLKQRYNAILIIDASHSL---GLN------LFEYHADIDIVTSSLSKAWGAHGGVIFSSKDIKDLIINKGRS 252
Cdd:PLN02955 265 FAPMEELSQLRKKYGFLLVIDDAHGTfvcGENgggvaeEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQSRGRS 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 253 LIYSSSLPsyhLYFIQVSLQHVI---EDTYRREKL-NVLSEyfnhqFMELfPDQPLSnTPIKNIVCDSLASAQAQYDMLF 328
Cdd:PLN02955 345 FIFSTAIP---VPMAAAAYAAVVvarKEKWRRKAIwERVKE-----FKAL-SGVDIS-SPIISLVVGNQEKALKASRYLL 414
|
330 340 350
....*....|....*....|....*....|....*..
gi 488368310 329 EHGIFVSYLRYPTVSQPT--LRISLSYFHDTDDIDRL 363
Cdd:PLN02955 415 KSGFHVMAIRPPTVPPNScrLRVTLSAAHTTEDVKKL 451
|
|
| PRK05937 |
PRK05937 |
8-amino-7-oxononanoate synthase; Provisional |
38-372 |
8.35e-35 |
|
8-amino-7-oxononanoate synthase; Provisional
Pssm-ID: 102071 [Multi-domain] Cd Length: 370 Bit Score: 131.44 E-value: 8.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 38 INFTSNDYLGIGQLEYQPQNFLDFIKTYSIHLS-------SSRLVSGNSVVYQQLEQAISEHFNFEDALIFNSGYDANLA 110
Cdd:PRK05937 7 IDFVTNDFLGFSRSDTLVHEVEKRYRLYCRQFPhaqlgygGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 111 V-FNIFKNNNVViFSDQQNHASIIDGIKLSGLSKVIYQHLNYDDLESHLARHTNPDVQKV-IVSDSVFSTNGTKADINRL 188
Cdd:PRK05937 87 LcAHLSSVTDYV-LWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLESCRQRSFGRIfIFVCSVYSFKGTLAPLEQI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 189 VHLKQRYNAILIIDASHSLGL---------------NLFEyhadidiVTSSLSKAWGAHGGVIFSSKDIKDLIINKGRSL 253
Cdd:PRK05937 166 IALSKKYHAHLIVDEAHAMGIfgddgkgfchslgyeNFYA-------VLVTYSKALGSMGAALLSSSEVKQDLMLNSPPL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 254 IYSSSLPSYHLYFIQVSLQH-VIEDTYRREKLNVLSEYFNHQFMELFPD--QPLSNTPIknivcdslaSAQAQYDMLFEH 330
Cdd:PRK05937 239 RYSTGLPPHLLISIQVAYDFlSQEGELARKQLFRLKEYFAQKFSSAAPGcvQPIFLPGI---------SEQELYSKLVET 309
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 488368310 331 GIFVSYLRYPTvsQPTLRISLSYFHDTDDIDRLFNVMKQYDE 372
Cdd:PRK05937 310 GIRVGVVCFPT--GPFLRVNLHAFNTEDEVDILVSVLATYLE 349
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
38-363 |
1.65e-28 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 113.94 E-value: 1.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 38 INFTSNDYLGiGQLEYQPQNFLDfiktysIHLSSSRLVSGNSVVYQQLEQAISEHFNF--------EDALIFNSGYDANL 109
Cdd:pfam00155 4 INLGSNEYLG-DTLPAVAKAEKD------ALAGGTRNLYGPTDGHPELREALAKFLGRspvlkldrEAAVVFGSGAGANI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 110 AVFN-IFKNNNVVIFSDQQNHASIIDGIKLSGLSKVIY-------QHLNYDDLESHLARHTnpdvqKVIVSDSVFSTNG- 180
Cdd:pfam00155 77 EALIfLLANPGDAILVPAPTYASYIRIARLAGGEVVRYplydsndFHLDFDALEAALKEKP-----KVVLHTSPHNPTGt 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 181 --TKADINRLVHLKQRYNAILIIDASHS-LGLNLFEYHADI--------DIVTSSLSKAWGAHG---GVIFSSKDIKDLI 246
Cdd:pfam00155 152 vaTLEELEKLLDLAKEHNILLLVDEAYAgFVFGSPDAVATRallaegpnLLVVGSFSKAFGLAGwrvGYILGNAAVISQL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 247 INKGRSLIYSSSLPSYHLYFIQVSLQHVIEDTYRREKLNVLSEYFNHQFMEL-FPDQPLSNTPIKNIVCDSLASAQAQYD 325
Cdd:pfam00155 232 RKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAgLSVLPSQAGFFLLTGLDPETAKELAQV 311
|
330 340 350
....*....|....*....|....*....|....*...
gi 488368310 326 MLFEHGIFVSYLRYPTVSqPTLRISLSYfHDTDDIDRL 363
Cdd:pfam00155 312 LLEEVGVYVTPGSSPGVP-GWLRITVAG-GTEEELEEL 347
|
|
| PRK07505 |
PRK07505 |
hypothetical protein; Provisional |
22-369 |
2.66e-28 |
|
hypothetical protein; Provisional
Pssm-ID: 181006 [Multi-domain] Cd Length: 402 Bit Score: 114.31 E-value: 2.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 22 IQSVEKQYIYINDQS---YINFTSNDYLGigqLEYQPQ---NFLDFIKTY-SIHLSSSRLVSgNSVVYQQLEQAISEHFN 94
Cdd:PRK07505 30 LTVGEREGILITLADghtFVNFVSCSYLG---LDTHPAiieGAVDALKRTgSLHLSSSRTRV-RSQILKDLEEALSELFG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 95 FEdALIFNSGYDANLAVF-----NIFKNN-NVVIFSDQQNHAS--IIDGIkLSGLSKVIY-QHLNYDDLESHLARHTNPd 165
Cdd:PRK07505 106 AS-VLTFTSCSAAHLGILpllasGHLTGGvPPHMVFDKNAHASlnILKGI-CADETEVETiDHNDLDALEDICKTNKTV- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 166 vqkVIVSDSVFSTNGtKADINRLVHLKQRYNAILIIDASHSL--------GLNLFEYHADID---IVTSSLSKAWGAHGG 234
Cdd:PRK07505 183 ---AYVADGVYSMGG-IAPVKELLRLQEKYGLFLYIDDAHGLsiygkngeGYVRSELDYRLNertIIAASLGKAFGASGG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 235 VIF-SSKDIKDLIINKGRSLIYSSSLPSYHLYFIQVSLQ-HVIED-TYRREKLNVLSEYFNhqfmELFP-DQPLSNTPIK 310
Cdd:PRK07505 259 VIMlGDAEQIELILRYAGPLAFSQSLNVAALGAILASAEiHLSEElDQLQQKLQNNIALFD----SLIPtEQSGSFLPIR 334
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488368310 311 NIVCDSLASAQAQYDMLFEHGIFVSYLRYPTVSQPT--LRISLSYFHDTDDIDRLFNVMKQ 369
Cdd:PRK07505 335 LIYIGDEDTAIKAAKQLLDRGFYTSPVFFPVVAKGRagLRIMFRASHTNDEIKRLCSLLKE 395
|
|
| PRK07179 |
PRK07179 |
quorum-sensing autoinducer synthase; |
38-374 |
1.05e-25 |
|
quorum-sensing autoinducer synthase;
Pssm-ID: 180866 [Multi-domain] Cd Length: 407 Bit Score: 107.02 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 38 INFTSNDYLGIGQleyQPQNFLDFIKTYSIH-----LSSSRLVSGNSVvyQQLEQAISEHFNFEDALIFNSGYDANLAVF 112
Cdd:PRK07179 57 IILQSNDYLNLSG---HPDIIKAQIAALQEEgdslvMSAVFLHDDSPK--PQFEKKLAAFTGFESCLLCQSGWAANVGLL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 113 NIFKNNNVVIFSDQQNHASIIDGIKLSGLSKVIYQHLNYDDLESHLARHTnpdvQKVIVSDSVFSTNGTKADINRLVHLK 192
Cdd:PRK07179 132 QTIADPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIERHG----PGIIVVDSVYSTTGTIAPLADIVDIA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 193 QRYNAILIIDASHSLG---------LNLFEYHADIDIVTSSLSKAWGAHGGVIFSSKDIKDLIINKGRSLIYSSSLPSYH 263
Cdd:PRK07179 208 EEFGCVLVVDESHSLGthgpqgaglVAELGLTSRVHFITASLAKAFAGRAGIITCPRELAEYVPFVSYPAIFSSTLLPHE 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 264 LYFIQVSLQHVIEDTYRREKLNVLSEYFNHQFMEL-FPDQplSNTPIKNIVCDSLASAQAQYDMLFEHGIFVSYLRYPTV 342
Cdd:PRK07179 288 IAGLEATLEVIESADDRRARLHANARFLREGLSELgYNIR--SESQIIALETGSERNTEVLRDALEERNVFGAVFCAPAT 365
|
330 340 350
....*....|....*....|....*....|....*
gi 488368310 343 SQ--PTLRISLSYFHDTDDIDRLFNVMKQ-YDEGD 374
Cdd:PRK07179 366 PKnrNLIRLSLNADLTASDLDRVLEVCREaRDEVD 400
|
|
| PLN02822 |
PLN02822 |
serine palmitoyltransferase |
22-369 |
6.72e-22 |
|
serine palmitoyltransferase
Pssm-ID: 178417 [Multi-domain] Cd Length: 481 Bit Score: 96.73 E-value: 6.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 22 IQSVEKQYIYINDQSYINFTSNDYLGIGQLEYQPQNFLDFIKTYSIHLSSSRLVSGNSVVYQQLEQAISEHFNFEDALIF 101
Cdd:PLN02822 96 LESAAGPHTIINGKDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILY 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 102 NSGYDANLAVFNIFKNNNVVIFSDQQNHASIIDGIKLSgLSKVIY-QHLNYDDLESHLARHTNPD-----VQKVIVSDSV 175
Cdd:PLN02822 176 SYGLSTIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLS-RSTIVYfKHNDMESLRNTLEKLTAENkrkkkLRRYIVVEAI 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 176 FSTNGTKADINRLVHLKQRYNAILIIDASHSLGL------NLFEYHA----DIDIVTSSLSKAWGAHGGVIFSSKDIKDL 245
Cdd:PLN02822 255 YQNSGQIAPLDEIVRLKEKYRFRVLLDESNSFGVlgksgrGLSEHFGvpieKIDIITAAMGHALATEGGFCTGSARVVDH 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 246 IINKGRSLIYSSSLPSYhLYFIQVSLQHVIED-----TYRREKLNVLseyfnHQFMELFPDQPLSNTPIKNIVC----DS 316
Cdd:PLN02822 335 QRLSSSGYVFSASLPPY-LASAAITAIDVLEDnpsvlAKLKENIALL-----HKGLSDIPGLSIGSNTLSPIVFlhleKS 408
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488368310 317 LASAQAQYD--------MLFEHGIFVSYLRYPTVSQ----PTLRISLSYFHDTDDIDRLFNVMKQ 369
Cdd:PLN02822 409 TGSAKEDLSllehiadrMLKEDSVLVVVSKRSTLDKcrlpVGIRLFVSAGHTESDILKASESLKR 473
|
|
| PLN02483 |
PLN02483 |
serine palmitoyltransferase |
38-260 |
8.23e-22 |
|
serine palmitoyltransferase
Pssm-ID: 178101 [Multi-domain] Cd Length: 489 Bit Score: 96.76 E-value: 8.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 38 INFTSNDYLGIGQL-EYQPQNFLDFIKTYSIHLSSSRLVSGNSVVYQQLEQAISEHFNFEDALIFNSGYDANLAVFNIFK 116
Cdd:PLN02483 103 LNLGSYNYLGFAAAdEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTIIPALI 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 117 NNNVVIFSDQQNHASIIDGIKLSGLSKVIYQHLNYDDLESHLARH-------TNPDVQKVIV-SDSVFSTNGTKADINRL 188
Cdd:PLN02483 183 GKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQiaegqprTHRPWKKIIViVEGIYSMEGELCKLPEI 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 189 VHLKQRYNAILIIDASHSLGL------NLFEY----HADIDIVTSSLSKAWGAHGGVIFSSKDIKDLIINKGRSLIYSSS 258
Cdd:PLN02483 263 VAVCKKYKAYVYLDEAHSIGAvgktgrGVCELlgvdPADVDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCPAHLYATS 342
|
..
gi 488368310 259 LP 260
Cdd:PLN02483 343 MS 344
|
|
| PLN03227 |
PLN03227 |
serine palmitoyltransferase-like protein; Provisional |
38-369 |
5.07e-19 |
|
serine palmitoyltransferase-like protein; Provisional
Pssm-ID: 178766 [Multi-domain] Cd Length: 392 Bit Score: 87.65 E-value: 5.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 38 INFTSNDYLGIGQLEYQPQNFLDFIKTYSIHLSSSRLVSGNSVVYQQLEQAISEHFNFEDALIFNSGYDANLAVFNIFKN 117
Cdd:PLN03227 1 LNFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 118 NNVVIFSDQQNHASIIDGIKLSGLSKVIYQHLNYDDL---------ESHLARHTNPDVQKVIVSDSVFSTNGTKADINRL 188
Cdd:PLN03227 81 RGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLrrvleqvraQDVALKRKPTDQRRFLVVEGLYKNTGTLAPLKEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 189 VHLKQRYNAILIIDASHSLGL------NLFEY-----HADIDIVTSSLSKAWGAHGGVIFSSKDIKDLIINKGRSLIYSS 257
Cdd:PLN03227 161 VALKEEFHYRLILDESFSFGTlgksgrGSLEHaglkpMVHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSGYCFSA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 258 SLPSYHLYFIQVSLQHVIED-----------TYRREKLNVLSEYFNHQFMELF-----PDQP-----LSNTPIKNIVCDS 316
Cdd:PLN03227 241 SAPPFLAKADATATAGELAGpqllnrlhdsiANLYSTLTNSSHPYALKLRNRLvitsdPISPiiylrLSDQEATRRTDET 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 488368310 317 LASAQAQYDMLFEHGIFVSYLRYPT-----VSQPTLRISLSYFHDTDDIDRLFNVMKQ 369
Cdd:PLN03227 321 LILDQIAHHSLSEGVAVVSTGGHVKkflqlVPPPCLRVVANASHTREDIDKLLTVLGE 378
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
82-237 |
3.86e-07 |
|
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).
Pssm-ID: 99742 [Multi-domain] Cd Length: 170 Bit Score: 49.69 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 82 YQQLEQAISEHFN--FEDALIFNSGYDANLAVF-NIFKNNNVVIFSDQQNHASIIDGIKLSGLSKVIYQHLNYDDLESHL 158
Cdd:cd01494 2 LEELEEKLARLLQpgNDKAVFVPSGTGANEAALlALLGPGDEVIVDANGHGSRYWVAAELAGAKPVPVPVDDAGYGGLDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 159 ARHTN---PDVQKVIVSDSVFSTNGTKADINRLVHLKQRYNAILIIDASHSLG-------LNLFEYhadIDIVTSSLSKA 228
Cdd:cd01494 82 AILEElkaKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGaspapgvLIPEGG---ADVVTFSLHKN 158
|
170
....*....|
gi 488368310 229 WGAHG-GVIF 237
Cdd:cd01494 159 LGGEGgGVVI 168
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
82-369 |
2.11e-06 |
|
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.
Pssm-ID: 99734 [Multi-domain] Cd Length: 350 Bit Score: 49.26 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 82 YQQLEQAISEHFNF--------EDALIFNSGYDANLAVFNIFKNNN-VVIFSDQqNHASIIDGIKLSGLsKVIYQHLNYD 152
Cdd:cd00609 38 LPELREAIAEWLGRrggvdvppEEIVVTNGAQEALSLLLRALLNPGdEVLVPDP-TYPGYEAAARLAGA-EVVPVPLDEE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 153 ----DLESHLARHTNPDVqKVIV-------SDSVFStngtKADINRLVHLKQRYNAILIIDASHS--------LGLNLFE 213
Cdd:cd00609 116 ggflLDLELLEAAKTPKT-KLLYlnnpnnpTGAVLS----EEELEELAELAKKHGILIISDEAYAelvydgepPPALALL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 214 YHADIDIVTSSLSKAWGAHG---G-VIFSSKDIKDLIINKGRSLIYSSSLPSYHL--YFIQVSLQHVIE--DTY--RREK 283
Cdd:cd00609 191 DAYERVIVLRSFSKTFGLPGlriGyLIAPPEELLERLKKLLPYTTSGPSTLSQAAaaAALDDGEEHLEElrERYrrRRDA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 284 L-NVLSEYFNHQFME------LFPDqplsntpiknivCDSLASAQAQYDMLFEHGIFVSYLR-YPTVSQPTLRISLSYfh 355
Cdd:cd00609 271 LlEALKELGPLVVVKpsggffLWLD------------LPEGDDEEFLERLLLEAGVVVRPGSaFGEGGEGFVRLSFAT-- 336
|
330
....*....|....
gi 488368310 356 DTDDIDRLFNVMKQ 369
Cdd:cd00609 337 PEEELEEALERLAE 350
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
32-231 |
2.01e-05 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 46.29 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 32 INDQSYINFtsnDYLGIGQLeyqPQNFLDFIKTY------SIHLSSSRLVSGNSVVYQQLEQAISEHFN--FEDALIFNS 103
Cdd:COG0520 11 VLGKPLVYL---DNAATGQK---PRPVIDAIRDYyepynaNVHRGAHELSAEATDAYEAAREKVARFIGaaSPDEIIFTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 104 GydA----NLAV--FNIFKNNNVVIFSDQQNHASII--------DGIKLsglsKVIY----QHLNYDDLESHLARHTnpd 165
Cdd:COG0520 85 G--TteaiNLVAygLGRLKPGDEILITEMEHHSNIVpwqelaerTGAEV----RVIPldedGELDLEALEALLTPRT--- 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488368310 166 vqKVIVSDSVFSTNGTKADINRLVHLKQRYNAILIIDASHSLGlnlfeyHADIDIvtsslsKAWGA 231
Cdd:COG0520 156 --KLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVP------HLPVDV------QALGC 207
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
85-253 |
3.78e-03 |
|
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed step of methionine biosynthesis. This pathway is unique to microorganisms and plants, rendering the enzyme an attractive target for the development of antimicrobials and herbicides. This subgroup also includes cystathionine gamma-lyases (CGL), O-acetylhomoserine sulfhydrylases and O-acetylhomoserine thiol lyases. CGL's are very similar to CGS's. Members of this group are widely distributed among all three forms of life.
Pssm-ID: 99738 [Multi-domain] Cd Length: 369 Bit Score: 39.11 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 85 LEQAISEHFNFEDALIFNSGYDANLAVFNIFKN--NNVVIFSD--QQNHASIIDGIKLSGLS-KVIYQhLNYDDLESHLA 159
Cdd:cd00614 45 LEKKLAALEGGEAALAFSSGMAAISTVLLALLKagDHVVASDDlyGGTYRLFERLLPKLGIEvTFVDP-DDPEALEAAIK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 160 RHTnpdvqKVIVSDSVFSTNGTKADINRLVHLKQRYNAILIIDASHSLGLNL--FEYHADIdiVTSSLSKAWGAHGGVIF 237
Cdd:cd00614 124 PET-----KLVYVESPTNPTLKVVDIEAIAELAHEHGALLVVDNTFATPYLQrpLELGADI--VVHSATKYIGGHSDVIA 196
|
170 180
....*....|....*....|.
gi 488368310 238 -----SSKDIKDLIINKGRSL 253
Cdd:cd00614 197 gvvvgSGEALIQRLRFLRLAL 217
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
75-241 |
6.35e-03 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 37.97 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 75 VSGNSVVYQQLEQAISEHFNFEDALIFNSGYDANLAVFNIFKNNNVVIFSDQQNH--------ASIIDGIKLSGlskVIY 146
Cdd:pfam01212 27 VYGGDPTVNRLEDRVAELFGKEAALFVPSGTAANQLALMAHCQRGDEVICGEPAHihfdetggHAELGGVQPRP---LDG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 147 QHLNY---DDLESHLAR---HTNPDVQKVIVSDSVFSTNGT---KADINRLVHLKQRYNAILIID------ASHSLGLNL 211
Cdd:pfam01212 104 DEAGNmdlEDLEAAIREvgaDIFPPTGLISLENTHNSAGGQvvsLENLREIAALAREHGIPVHLDgarfanAAVALGVIV 183
|
170 180 190
....*....|....*....|....*....|.
gi 488368310 212 FEYHADIDIVTSSLSKAWGAH-GGVIFSSKD 241
Cdd:pfam01212 184 KEITSYADSVTMCLSKGLGAPvGSVLAGSDD 214
|
|
|