|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06939 |
PRK06939 |
2-amino-3-ketobutyrate coenzyme A ligase; Provisional |
1-396 |
0e+00 |
|
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
Pssm-ID: 235893 [Multi-domain] Cd Length: 397 Bit Score: 826.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 1 MRGDFYKQLTSNLETARAEGLFKEERIITSAQQADITVGD-SHVINFCANNYLGLANHPELIAAAKSGMDSHGFGMASVR 79
Cdd:PRK06939 1 MSGAFYAQLREELEEIKAEGLYKEERVITSPQGADITVADgKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 80 FICGTQDTHKQLEKKLADFLGMEDAILYSSCFDANGGLFETLLGPEDAIISDALNHASIIDGVRLCKAKRFRYANNDMQE 159
Cdd:PRK06939 81 FICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 160 LEACLKEAREAGARHVLIATDGVFSMDGVIANLKGVCDLADKYDALVMVDDSHAVGFVGENGRGSHEYCDVMGRVDIITG 239
Cdd:PRK06939 161 LEAQLKEAKEAGARHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDRVDIITG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 240 TLGKALGGASGGYTAARKEVVEWLRQRSRPYLFSNSLAPAIVAASIKVLEMVEEGADLRDRLWANARLFREKMTAAGFTL 319
Cdd:PRK06939 241 TLGKALGGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDRLWENARYFREGMTAAGFTL 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496082343 320 AGADHAIIPVMLGEAVVAQNFARELQKEGIYVTGFFYPVVPKGQARIRTQMSAAHTPEQIERAVEAFTRIGKQLGVI 396
Cdd:PRK06939 321 GPGEHPIIPVMLGDAKLAQEFADRLLEEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLDRAIDAFEKVGKELGVI 397
|
|
| 2am3keto_CoA |
TIGR01822 |
glycine C-acetyltransferase; This model represents a narrowly defined clade of animal and ... |
5-396 |
0e+00 |
|
glycine C-acetyltransferase; This model represents a narrowly defined clade of animal and bacterial (almost exclusively Proteobacterial) 2-amino-3-ketobutyrate--CoA ligase, now called glycine C-acetyltransferase. This enzyme can act in threonine catabolism. The closest homolog from Bacillus subtilis, and sequences like it, may be functionally equivalent but were not included in the model because of difficulty in finding reports of function. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130881 [Multi-domain] Cd Length: 393 Bit Score: 725.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 5 FYKQLTSNLETARAEGLFKEERIITSAQQADITVGD-SHVINFCANNYLGLANHPELIAAAKSGMDSHGFGMASVRFICG 83
Cdd:TIGR01822 1 FYAQLAAELESIREAGLFKSERIITSPQGADIRVADgREVLNFCANNYLGLSSHPDLIQAAKDALDEHGFGMSSVRFICG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 84 TQDTHKQLEKKLADFLGMEDAILYSSCFDANGGLFETLLGPEDAIISDALNHASIIDGVRLCKAKRFRYANNDMQELEAC 163
Cdd:TIGR01822 81 TQDIHKELEAKIAAFLGTEDTILYASCFDANGGLFETLLGAEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 164 LKEAREAGARHVLIATDGVFSMDGVIANLKGVCDLADKYDALVMVDDSHAVGFVGENGRGSHEYCDVMGRVDIITGTLGK 243
Cdd:TIGR01822 161 LKEARAAGARHRLIATDGVFSMDGVIAPLDEICDLADKYDALVMVDECHATGFLGPTGRGSHELCGVMGRVDIITGTLGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 244 ALGGASGGYTAARKEVVEWLRQRSRPYLFSNSLAPAIVAASIKVLEMVEEGADLRDRLWANARLFREKMTAAGFTLAGAD 323
Cdd:TIGR01822 241 ALGGASGGFTTARKEVVELLRQRSRPYLFSNSLPPAVVGASIKVLEMLEASNELRDRLWANTRYFRERMEAAGFDIKPAD 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496082343 324 HAIIPVMLGEAVVAQNFARELQKEGIYVTGFFYPVVPKGQARIRTQMSAAHTPEQIERAVEAFTRIGKQLGVI 396
Cdd:TIGR01822 321 HPIIPVMLYDAVLAQRFARRLLEEGIYVTGFFYPVVPKGQARIRVQISAAHTEEQLDRAVEAFTRIGRELGVI 393
|
|
| BioF |
COG0156 |
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ... |
5-392 |
0e+00 |
|
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: 588.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 5 FYKQLTSNLETARAEGLFKEERIITSAQQADITVGDSHVINFCANNYLGLANHPELIAAAKSGMDSHGFGMASVRFICGT 84
Cdd:COG0156 1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 85 QDTHKQLEKKLADFLGMEDAILYSSCFDANGGLFETLLGPEDAIISDALNHASIIDGVRLCKAKRFRYANNDMQELEACL 164
Cdd:COG0156 81 TPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 165 KEAREagARHVLIATDGVFSMDGVIANLKGVCDLADKYDALVMVDDSHAVGFVGENGRGSHEYCDVMGRVDIITGTLGKA 244
Cdd:COG0156 161 KKARA--ARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDIIMGTLSKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 245 LgGASGGYTAARKEVVEWLRQRSRPYLFSNSLAPAIVAASIKVLEMVEEGADLRDRLWANARLFREKMTAAGFTLAGADH 324
Cdd:COG0156 239 L-GSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFDLGPSES 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496082343 325 AIIPVMLGEAVVAQNFARELQKEGIYVTGFFYPVVPKGQARIRTQMSAAHTPEQIERAVEAFTRIGKQ 392
Cdd:COG0156 318 PIVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
41-390 |
9.62e-177 |
|
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: 495.93 E-value: 9.62e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 41 SHVINFCANNYLGLANHPELIAAAKSGMDSHGFGMASVRFICGTQDTHKQLEKKLADFLGMEDAILYSSCFDANGGLFET 120
Cdd:cd06454 1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 121 LLGPEDAIISDALNHASIIDGVRLCKAKRFRYANNDMQELEACLKEAREaGARHVLIATDGVFSMDGVIANLKGVCDLAD 200
Cdd:cd06454 81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARR-PYGKKLIVTEGVYSMDGDIAPLPELVDLAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 201 KYDALVMVDDSHAVGFVGENGRGSHEYCDVMGRVDIITGTLGKALgGASGGYTAARKEVVEWLRQRSRPYLFSNSLAPAI 280
Cdd:cd06454 160 KYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAF-GAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 281 VAASIKVLEMVEEGADLRDRLWANARLFREKMTAAGFTLAGA-DHAIIPVMLGEAVVAQNFARELQKEGIYVTGFFYPVV 359
Cdd:cd06454 239 AAAALAALEVLQGGPERRERLQENVRYLRRGLKELGFPVGGSpSHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTV 318
|
330 340 350
....*....|....*....|....*....|.
gi 496082343 360 PKGQARIRTQMSAAHTPEQIERAVEAFTRIG 390
Cdd:cd06454 319 PRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
|
|
| bioF |
TIGR00858 |
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ... |
26-387 |
3.55e-132 |
|
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: 383.16 E-value: 3.55e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 26 RIITSAQQADITVGDSHVINFCANNYLGLANHPELIAAAKSGMDSHGFGMASVRFICGTQDTHKQLEKKLADFLGMEDAI 105
Cdd:TIGR00858 1 RPLDRGPGPEVVRDGRRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 106 LYSSCFDANGGLFETLLGPEDAIISDALNHASIIDGVRLCKAKRFRYANNDMQELEACLKEAReaGARHVLIATDGVFSM 185
Cdd:TIGR00858 81 LFSSGYLANVGVISALVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNR--GERRKLIVTDGVFSM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 186 DGVIANLKGVCDLADKYDALVMVDDSHAVGFVGENGRGSHEYCDVMG-RVDIITGTLGKALGGAsGGYTAARKEVVEWLR 264
Cdd:TIGR00858 159 DGDIAPLPQLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKPePVDIQVGTLSKALGSY-GAYVAGSQALIDYLI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 265 QRSRPYLFSNSLAPAIVAASIKVLEMVEEGADLRDRLWANARLFREKMTAAGFTLAGADHAIIPVMLGEAVVAQNFAREL 344
Cdd:TIGR00858 238 NRARTLIFSTALPPAVAAAALAALELIQEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEEL 317
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 496082343 345 QKEGIYVTGFFYPVVPKGQARIRTQMSAAHTPEQIERAVEAFT 387
Cdd:TIGR00858 318 QQQGIFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEALK 360
|
|
| PRK05958 |
PRK05958 |
8-amino-7-oxononanoate synthase; Reviewed |
4-390 |
1.04e-131 |
|
8-amino-7-oxononanoate synthase; Reviewed
Pssm-ID: 235655 [Multi-domain] Cd Length: 385 Bit Score: 382.97 E-value: 1.04e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 4 DFYKQLTSNLETARAEGLFKEERIITSAQQADITVGDSHVINFCANNYLGLANHPELIAAAKSGMDSHGFGMASVRFICG 83
Cdd:PRK05958 2 SWLDRLEAALAQRRAAGLYRSLRPREGGAGRWLVVDGRRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 84 TQDTHKQLEKKLADFLGMEDAILYSSCFDANGGLFETLLGPEDAIISDALNHASIIDGVRLCKAKRFRYANNDMQELEAC 163
Cdd:PRK05958 82 NSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 164 LKEAReagARHVLIATDGVFSMDGVIANLKGVCDLADKYDALVMVDDSHAVGFVGENGRGSHEYCDVMGRVDII-TGTLG 242
Cdd:PRK05958 162 LAKWR---AGRALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLAGEPDVIlVGTLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 243 KALgGASGGYTAARKEVVEWLRQRSRPYLFSNSLAPAIVAASIKVLEMVEEGADLRDRLWANARLFREKMTAAGFTLAGA 322
Cdd:PRK05958 239 KAL-GSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRALGFQLMDS 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496082343 323 DHAIIPVMLGEAVVAQNFARELQKEGIYVTGFFYPVVPKGQARIRTQMSAAHTPEQIERAVEAFTRIG 390
Cdd:PRK05958 318 QSAIQPLIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEALAEAL 385
|
|
| 5aminolev_synth |
TIGR01821 |
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ... |
39-395 |
2.11e-91 |
|
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: 280.85 E-value: 2.11e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 39 GDSHVINFCANNYLGLANHPELIAAAKSGMDSHGFGMASVRFICGTQDTHKQLEKKLADFLGMEDAILYSSCFDANGGLF 118
Cdd:TIGR01821 43 GAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAGAGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 119 ETL--LGPEDAIISDALNHASIIDGVRLCKAKRFRYANNDMQELEACLKEAREAGARhvLIATDGVFSMDGVIANLKGVC 196
Cdd:TIGR01821 123 ATLakIIPGCVIFSDELNHASMIEGIRHSGAEKFIFRHNDVAHLEKLLQSVDPNRPK--IIAFESVYSMDGDIAPIEEIC 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 197 DLADKYDALVMVDDSHAVGFVGENGRGSHEYCDVMGRVDIITGTLGKALgGASGGYTAARKEVVEWLRQRSRPYLFSNSL 276
Cdd:TIGR01821 201 DLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRIDIIEGTLAKAF-GVVGGYIAASRKLIDAIRSYAPGFIFTTSL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 277 APAIVAASIKVLEMVEEGADLRDRLWANARLFREKMTAAGFTLAGADHAIIPVMLGEAVVAQNFAREL-QKEGIYVTGFF 355
Cdd:TIGR01821 280 PPAIAAGATASIRHLKESQDLRRAHQENVKRLKNLLEALGIPVIPNPSHIVPVIIGDAALCKKVSDLLlNKHGIYVQPIN 359
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 496082343 356 YPVVPKGQARIRTQMSAAHTPEQIERAVEAFTRIGKQLGV 395
Cdd:TIGR01821 360 YPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDRLGL 399
|
|
| PRK13392 |
PRK13392 |
5-aminolevulinate synthase; Provisional |
39-395 |
3.26e-80 |
|
5-aminolevulinate synthase; Provisional
Pssm-ID: 184023 [Multi-domain] Cd Length: 410 Bit Score: 252.47 E-value: 3.26e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 39 GDSHVINFCANNYLGLANHPELIAAAKSGMDSHGFGMASVRFICGTQDTHKQLEKKLADFLGMEDAILYSSCFDANGGLF 118
Cdd:PRK13392 44 GPRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAGAGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAAL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 119 ETL--LGPEDAIISDALNHASIIDGVRLCKAKRFRYANNDMQELEACLkeAREAGARHVLIATDGVFSMDGVIANLKGVC 196
Cdd:PRK13392 124 STLgkLLPGCVILSDALNHASMIEGIRRSGAEKQVFRHNDLADLEEQL--ASVDPDRPKLIAFESVYSMDGDIAPIEAIC 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 197 DLADKYDALVMVDDSHAVGFVGENGRGSHEYCDVMGRVDIITGTLGKALgGASGGYTAARKEVVEWLRQRSRPYLFSNSL 276
Cdd:PRK13392 202 DLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRIDMIQGTLAKAF-GCLGGYIAASADLIDFVRSFAPGFIFTTAL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 277 APAIVAASIKVLEMVEEGADLRDRLWANARLFREKMTAAGFTLAGADHAIIPVMLGEAVVAQNFARELQKE-GIYVTGFF 355
Cdd:PRK13392 281 PPAVAAGATAAIRHLKTSQTERDAHQDRVAALKAKLNANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEhGIYIQPIN 360
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 496082343 356 YPVVPKGQARIRTQMSAAHTPEQIERAVEAFTRIGKQLGV 395
Cdd:PRK13392 361 YPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDRLEL 400
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
41-386 |
3.92e-75 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 237.20 E-value: 3.92e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 41 SHVINFCANNYLGLAnhpeLIAAAKSGMDshgFGMASVRFICGTQDTHKQLEKKLADFLGM--------EDAILYSSCFD 112
Cdd:pfam00155 1 TDKINLGSNEYLGDT----LPAVAKAEKD---ALAGGTRNLYGPTDGHPELREALAKFLGRspvlkldrEAAVVFGSGAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 113 ANGGLFETLLG-PEDAIISDALNHASIIDGVRLCKAKRFRYA-------NNDMQELEACLKEareagaRHVLIATDGVFS 184
Cdd:pfam00155 74 ANIEALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKE------KPKVVLHTSPHN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 185 MDGVIANLKGVCDLAD---KYDALVMVDDSHAVGFVGENGRGShEYCDVMGRVD-IITGTLGKALG--GASGGYTAARKE 258
Cdd:pfam00155 148 PTGTVATLEELEKLLDlakEHNILLLVDEAYAGFVFGSPDAVA-TRALLAEGPNlLVVGSFSKAFGlaGWRVGYILGNAA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 259 VVEWLRQRSRPYLFSNSLAPAIVAASIKVLEMVEEGADLRDRLWANARLFREKMTAAGFTLAGADHAIIPVMLGEAVVAQ 338
Cdd:pfam00155 227 VISQLRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAK 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 496082343 339 NFARELQKE-GIYVTGFFYPVVPkgqARIRTQMsAAHTPEQIERAVEAF 386
Cdd:pfam00155 307 ELAQVLLEEvGVYVTPGSSPGVP---GWLRITV-AGGTEEELEELLEAI 351
|
|
| PLN02483 |
PLN02483 |
serine palmitoyltransferase |
37-395 |
5.08e-66 |
|
serine palmitoyltransferase
Pssm-ID: 178101 [Multi-domain] Cd Length: 489 Bit Score: 217.71 E-value: 5.08e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 37 TVGDSHVINFCANNYLGLANH-----PELIAAaksgMDSHGFGMASVRFICGTQDTHKQLEKKLADFLGMEDAILYSSCF 111
Cdd:PLN02483 96 TTKTRRCLNLGSYNYLGFAAAdeyctPRVIES----LKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGY 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 112 DANGGLFETLLGPEDAIISDALNHASIIDGVRLCKAKRFRYANNDMQELEACLKEAREAGA-------RHVLIATDGVFS 184
Cdd:PLN02483 172 ATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQprthrpwKKIIVIVEGIYS 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 185 MDGVIANLKGVCDLADKYDALVMVDDSHAVGFVGENGRGSHEYCDVMGR-VDIITGTLGKALgGASGGYTAARKEVVEWL 263
Cdd:PLN02483 252 MEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPAdVDIMMGTFTKSF-GSCGGYIAGSKELIQYL 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 264 RQRSRPYLFSNSLAPAIVA---ASIKVLeMVEEGADL----RDRLWANARLFREKMTAAGFTLAGA-DHAIIPVMLGEAV 335
Cdd:PLN02483 331 KRTCPAHLYATSMSPPAVQqviSAIKVI-LGEDGTNRgaqkLAQIRENSNFFRSELQKMGFEVLGDnDSPVMPIMLYNPA 409
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 336 VAQNFARELQKEGIYVTGFFYPVVPKGQARIRTQMSAAHTPEQIERAVEAFTRIGKQLGV 395
Cdd:PLN02483 410 KIPAFSRECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGI 469
|
|
| PLN02955 |
PLN02955 |
8-amino-7-oxononanoate synthase |
34-387 |
2.88e-57 |
|
8-amino-7-oxononanoate synthase
Pssm-ID: 178541 [Multi-domain] Cd Length: 476 Bit Score: 194.51 E-value: 2.88e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 34 ADITVGDSH-VINFCANNYLGLANHPELIAAAKSGMDSHGFGMASVRFICGTQDTHKQLEKKLADFLGMEDAILYSSCFD 112
Cdd:PLN02955 94 AEERKGRFKkLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 113 ANGGLF------ETLLGPED--------AIISDALNHASIIDGVRLCK----AKRFRYANNDMQELEACLKEAReagARH 174
Cdd:PLN02955 174 ANMAAMvaigsvASLLAASGkplknekvAIFSDALNHASIIDGVRLAErqgnVEVFVYRHCDMYHLNSLLSSCK---MKR 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 175 VLIATDGVFSMDGVIANLKGVCDLADKYDALVMVDDSHAVGFVGENGRGSHEYCDVMGRVDIITGTLGKAlGGASGGYTA 254
Cdd:PLN02955 251 KVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKA-AGCHGGFIA 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 255 ARKEVVEWLRQRSRPYLFSNSLAPAIVAASIKVLEMVEEGADLRDRLWANARLFREkmtaagftLAGAD--HAIIPVMLG 332
Cdd:PLN02955 330 CSKKWKQLIQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEKWRRKAIWERVKEFKA--------LSGVDisSPIISLVVG 401
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 496082343 333 EAVVAQNFARELQKEGIYVTGFFYPVVPKGQARIRTQMSAAHTPEQIERAVEAFT 387
Cdd:PLN02955 402 NQEKALKASRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITALS 456
|
|
| PRK07179 |
PRK07179 |
quorum-sensing autoinducer synthase; |
24-385 |
5.11e-54 |
|
quorum-sensing autoinducer synthase;
Pssm-ID: 180866 [Multi-domain] Cd Length: 407 Bit Score: 184.06 E-value: 5.11e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 24 EERIITSAQQADITVG---DSHVINFCANNYLGLANHPELIAAAKSGMDSHGFG--MASVrFICGTQDTHkQLEKKLADF 98
Cdd:PRK07179 34 EERVNKNWNGKHLVLGktpGPDAIILQSNDYLNLSGHPDIIKAQIAALQEEGDSlvMSAV-FLHDDSPKP-QFEKKLAAF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 99 LGMEDAILYSSCFDANGGLFETLLGPEDAIISDALNHASIIDGVRLCKAKRFRYANNDMQELEaclKEAREAGARhvLIA 178
Cdd:PRK07179 112 TGFESCLLCQSGWAANVGLLQTIADPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLR---RQIERHGPG--IIV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 179 TDGVFSMDGVIANLKGVCDLADKYDALVMVDDSHAVGFVGENGRGSHEYCDVMGRVDIITGTLGKALGGaSGGYTAARKE 258
Cdd:PRK07179 187 VDSVYSTTGTIAPLADIVDIAEEFGCVLVVDESHSLGTHGPQGAGLVAELGLTSRVHFITASLAKAFAG-RAGIITCPRE 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 259 VVEWLRQRSRPYLFSNSLAPAIVAASIKVLEMVEEGADLRDRLWANARLFREKMTAAGFTLAGADHaIIPVMLGEAVVAQ 338
Cdd:PRK07179 266 LAEYVPFVSYPAIFSSTLLPHEIAGLEATLEVIESADDRRARLHANARFLREGLSELGYNIRSESQ-IIALETGSERNTE 344
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 496082343 339 NFARELQKEGIYVTGFFYPVVPKGQARIRTQMSAAHTPEQIERAVEA 385
Cdd:PRK07179 345 VLRDALEERNVFGAVFCAPATPKNRNLIRLSLNADLTASDLDRVLEV 391
|
|
| PLN02822 |
PLN02822 |
serine palmitoyltransferase |
18-393 |
2.38e-50 |
|
serine palmitoyltransferase
Pssm-ID: 178417 [Multi-domain] Cd Length: 481 Bit Score: 176.09 E-value: 2.38e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 18 AEGLFKEERIITSAQQADITVGDSHVINFCANNYLGLANHPELIAAAKSGMDSHGFGMASVRFICGTQDTHKQLEKKLAD 97
Cdd:PLN02822 86 TEEMRPEPPVLESAAGPHTIINGKDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 98 FLGMEDAILYS----------SCFDANGglfetllgpeDAIISDALNHASIIDGVRLCKAKRFRYANNDMQELEACLKEA 167
Cdd:PLN02822 166 FLGTPDSILYSyglstifsviPAFCKKG----------DIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEKL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 168 REAGAR----HVLIATDGVFSMDGVIANLKGVCDLADKYDALVMVDDSHAVGFVGENGRGSHEYCDV-MGRVDIITGTLG 242
Cdd:PLN02822 236 TAENKRkkklRRYIVVEAIYQNSGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVpIEKIDIITAAMG 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 243 KALGGAsGGYTAARKEVVEWLRQRSRPYLFSNSLAPAIVAASIKVLEMVEEGADLRDRLWANARLFREKMTA-AGFTLAG 321
Cdd:PLN02822 316 HALATE-GGFCTGSARVVDHQRLSSSGYVFSASLPPYLASAAITAIDVLEDNPSVLAKLKENIALLHKGLSDiPGLSIGS 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 322 ADHAIIpVMLGEAVVAQNFA-----------RELQKEGIYVTGFFYPVVPKGQ--ARIRTQMSAAHTPEQIERAVEAFTR 388
Cdd:PLN02822 395 NTLSPI-VFLHLEKSTGSAKedlsllehiadRMLKEDSVLVVVSKRSTLDKCRlpVGIRLFVSAGHTESDILKASESLKR 473
|
....*
gi 496082343 389 IGKQL 393
Cdd:PLN02822 474 VAASV 478
|
|
| PRK07505 |
PRK07505 |
hypothetical protein; Provisional |
10-394 |
7.71e-46 |
|
hypothetical protein; Provisional
Pssm-ID: 181006 [Multi-domain] Cd Length: 402 Bit Score: 162.46 E-value: 7.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 10 TSNLETARAEGLFKeeriITSAQQAD--ITVGDSH-VINFCANNYLGLANHPELIAAAKSGMDSHG-FGMASVRFICGTQ 85
Cdd:PRK07505 16 EKFWDAAYDEGLNG----LTVGEREGilITLADGHtFVNFVSCSYLGLDTHPAIIEGAVDALKRTGsLHLSSSRTRVRSQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 86 dTHKQLEKKLADFLGMEdAILYSSCFDANGGLFETL----LGPEDAI--ISDALNHASIIDGVRLCK--AKRFRYANNDM 157
Cdd:PRK07505 92 -ILKDLEEALSELFGAS-VLTFTSCSAAHLGILPLLasghLTGGVPPhmVFDKNAHASLNILKGICAdeTEVETIDHNDL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 158 QELEACLKEAREagarhVLIATDGVFSMDGViANLKGVCDLADKYDALVMVDDSHAVGFVGENGRGsheYcdVMGRVD-- 235
Cdd:PRK07505 170 DALEDICKTNKT-----VAYVADGVYSMGGI-APVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEG---Y--VRSELDyr 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 236 -----IITGTLGKALGGASGGYTAARKEVVEWLRQRSRPYLFSNSLAPAIVAASIKVLEM--VEEGADLRDRLWANARLF 308
Cdd:PRK07505 239 lnertIIAASLGKAFGASGGVIMLGDAEQIELILRYAGPLAFSQSLNVAALGAILASAEIhlSEELDQLQQKLQNNIALF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 309 REKMTAagfTLAGADHAIIPVMLGEAVVAQNFARELQKEGIYVTGFFYPVVPKGQARIRTQMSAAHTPEQIERAVEAFTR 388
Cdd:PRK07505 319 DSLIPT---EQSGSFLPIRLIYIGDEDTAIKAAKQLLDRGFYTSPVFFPVVAKGRAGLRIMFRASHTNDEIKRLCSLLKE 395
|
....*.
gi 496082343 389 IGKQLG 394
Cdd:PRK07505 396 ILDEGL 401
|
|
| PLN03227 |
PLN03227 |
serine palmitoyltransferase-like protein; Provisional |
44-385 |
2.83e-45 |
|
serine palmitoyltransferase-like protein; Provisional
Pssm-ID: 178766 [Multi-domain] Cd Length: 392 Bit Score: 160.46 E-value: 2.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 44 INFCANNYLGLANHPELIAAAKSGMDSHGFGMASVRFICGTQDTHKQLEKKLADFLGMEDAILYSSCFDANGGLFETLLG 123
Cdd:PLN03227 1 LNFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 124 PEDAIISDALNHASIIDGVRLCKAKRFRYANNDMQELEACLKEAREAG--------ARHVLIATDGVFSMDGVIANLKGV 195
Cdd:PLN03227 81 RGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLEQVRAQDvalkrkptDQRRFLVVEGLYKNTGTLAPLKEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 196 CDLADKYDALVMVDDSHAVGFVGENGRGSHEYC--DVMGRVDIITGTLGKALGGAsGGYTAARKEVVEWLRQRSRPYLFS 273
Cdd:PLN03227 161 VALKEEFHYRLILDESFSFGTLGKSGRGSLEHAglKPMVHAEIVTFSLENAFGSV-GGMTVGSEEVVDHQRLSGSGYCFS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 274 NSLAPAIVAASIKVLEMVEEGADLRDRLWANARLFREKMTAAG-----------FTLAGADHAIIPVMLG---------E 333
Cdd:PLN03227 240 ASAPPFLAKADATATAGELAGPQLLNRLHDSIANLYSTLTNSShpyalklrnrlVITSDPISPIIYLRLSdqeatrrtdE 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 496082343 334 AVVAQNFARELQKEG--IYVTGFFYPVVPKGQAR--IRTQMSAAHTPEQIERAVEA 385
Cdd:PLN03227 320 TLILDQIAHHSLSEGvaVVSTGGHVKKFLQLVPPpcLRVVANASHTREDIDKLLTV 375
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
88-256 |
4.60e-31 |
|
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: 116.33 E-value: 4.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 88 HKQLEKKLADFL--GMEDAILYSSCFDANGGLFETLLGPEDAIISDALNHASII-DGVRLCKAK--RFRYANNDMQELEA 162
Cdd:cd01494 2 LEELEEKLARLLqpGNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSRYwVAAELAGAKpvPVPVDDAGYGGLDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 163 CLKEAREAGARHVLIATDGVFSMDGVIANLKGVCDLADKYDALVMVDDSHAVGFVGENgrgshEYCDVMGRVDIITGTLG 242
Cdd:cd01494 82 AILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAP-----GVLIPEGGADVVTFSLH 156
|
170
....*....|....
gi 496082343 243 KALGGASGGYTAAR 256
Cdd:cd01494 157 KNLGGEGGGVVIVK 170
|
|
| PRK05937 |
PRK05937 |
8-amino-7-oxononanoate synthase; Provisional |
41-317 |
6.99e-27 |
|
8-amino-7-oxononanoate synthase; Provisional
Pssm-ID: 102071 [Multi-domain] Cd Length: 370 Bit Score: 110.26 E-value: 6.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 41 SHVINFCANNYLGLANHPELIAAAKSGMDSH-------GFGMASVRFICGTQDTHKQLEKKLADFLGMEDAILYSSCFDA 113
Cdd:PRK05937 4 SLSIDFVTNDFLGFSRSDTLVHEVEKRYRLYcrqfphaQLGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 114 NGGLFETLLGPEDAIISDALNHASIIDGVRLCKAKRFRYANNDMQELEACLKEAREAGARHVLIATDGVFSMDGVIANLK 193
Cdd:PRK05937 84 NLGLCAHLSSVTDYVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLESCRQRSFGRIFIFVCSVYSFKGTLAPLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 194 GVCDLADKYDALVMVDDSHAVGFVGENGRGsheYCDVMGRVDI--ITGTLGKALgGASGGYTAARKEVVEWLRQRSRPYL 271
Cdd:PRK05937 164 QIIALSKKYHAHLIVDEAHAMGIFGDDGKG---FCHSLGYENFyaVLVTYSKAL-GSMGAALLSSSEVKQDLMLNSPPLR 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 496082343 272 FSNSLAP-AIVAASIKVLEMVEEGADLRDRLWANARLFREK--MTAAGF 317
Cdd:PRK05937 240 YSTGLPPhLLISIQVAYDFLSQEGELARKQLFRLKEYFAQKfsSAAPGC 288
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
44-386 |
8.21e-14 |
|
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: 71.99 E-value: 8.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 44 INFCANNYLgLANHPELIAAAKSGMDSHGFgmasvrFICGTQDTHKQLEKKLADFLG--------MEDAILYSSCFDANG 115
Cdd:cd00609 1 IDLSIGEPD-FPPPPEVLEALAAAALRAGL------LGYYPDPGLPELREAIAEWLGrrggvdvpPEEIVVTNGAQEALS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 116 GLFETLLGPEDAIISDALNHASIIDGVRLCKAKRFRYA---NNDMQELEACLKEAREAGARHVLIA-----TDGVFSMDg 187
Cdd:cd00609 74 LLLRALLNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPldeEGGFLLDLELLEAAKTPKTKLLYLNnpnnpTGAVLSEE- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 188 viaNLKGVCDLADKYDALVMVDDSHAvGFVGENGRGSHEYCDVMGRVDIITGTLGKALGGAS--GGYTAARKEVVEWLRQ 265
Cdd:cd00609 153 ---ELEELAELAKKHGILIISDEAYA-ELVYDGEPPPALALLDAYERVIVLRSFSKTFGLPGlrIGYLIAPPEELLERLK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 266 RSRPYLFSNSLAPAIVAAsikvLEMVEEGAD----LRDRLWANARLFREKMTAAGFtlagaDHAIIP-----VMLG--EA 334
Cdd:cd00609 229 KLLPYTTSGPSTLSQAAA----AAALDDGEEhleeLRERYRRRRDALLEALKELGP-----LVVVKPsggffLWLDlpEG 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 496082343 335 VVAQNFARELQKEGIYVT---GFFYPvvpkGQARIRtqMSAAHTPEQIERAVEAF 386
Cdd:cd00609 300 DDEEFLERLLLEAGVVVRpgsAFGEG----GEGFVR--LSFATPEEELEEALERL 348
|
|
| OAT_like |
cd00610 |
Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP) ... |
149-389 |
1.41e-12 |
|
Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to ornithine aminotransferase, acetylornithine aminotransferase, alanine-glyoxylate aminotransferase, dialkylglycine decarboxylase, 4-aminobutyrate aminotransferase, beta-alanine-pyruvate aminotransferase, adenosylmethionine-8-amino-7-oxononanoate aminotransferase, and glutamate-1-semialdehyde 2,1-aminomutase. All the enzymes belonging to this family act on basic amino acids and their derivatives are involved in transamination or decarboxylation.
Pssm-ID: 99735 [Multi-domain] Cd Length: 413 Bit Score: 68.75 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 149 RFRYANNDMQELEAcLKEAREAGARHV--LIA-----TDGVfsmdgVIAN---LKGVCDLADKYDALVMVDDShAVGFvg 218
Cdd:cd00610 167 RYRPPAELADDLEA-LEEALEEHPEEVaaVIVepiqgEGGV-----IVPPpgyLKALRELCRKHGILLIADEV-QTGF-- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 219 enGR----GSHEYCDVmgRVDIITgtLGKALGgasGGY----TAARKEVVEWLrqRSRPYLFSNSLA--PAIVAASIKVL 288
Cdd:cd00610 238 --GRtgkmFAFEHFGV--EPDIVT--LGKGLG---GGLplgaVLGREEIMDAF--PAGPGLHGGTFGgnPLACAAALAVL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 289 EMVEEGaDLRDRLWANARLFREKMTAagftLAGADHAIIPV-----MLG------------EAVVAQNFARELQKEGIYV 351
Cdd:cd00610 307 EVLEEE-GLLENAAELGEYLRERLRE----LAEKHPLVGDVrgrglMIGielvkdratkppDKELAAKIIKAALERGLLL 381
|
250 260 270
....*....|....*....|....*....|....*...
gi 496082343 352 TgffypvvPKGQARIRTQMSAAHTPEQIERAVEAFTRI 389
Cdd:cd00610 382 R-------PSGGNVIRLLPPLIITEEEIDEGLDALDEA 412
|
|
| ArgD |
COG4992 |
Acetylornithine/succinyldiaminopimelate/putrescine aminotransferase [Amino acid transport and ... |
150-389 |
2.41e-05 |
|
Acetylornithine/succinyldiaminopimelate/putrescine aminotransferase [Amino acid transport and metabolism]; Acetylornithine/succinyldiaminopimelate/putrescine aminotransferase is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 444016 [Multi-domain] Cd Length: 396 Bit Score: 46.19 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 150 FRYA-NNDMQELEACLKEAR----------EAGarhVLIATDGvFsmdgvianLKGVCDLADKYDALVMVDDshaV--GF 216
Cdd:COG4992 163 FVFVpFNDLEALEAAIDDDTaavivepiqgEGG---VIPPPPG-Y--------LKGLRELCDEHGALLILDE---VqtGM 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 217 vgenGR-GS---HEYCDVmgRVDIITgtLGKALGgasGGY----TAARKEVVEWLrqrsRPYL----FS-NSLApaiVAA 283
Cdd:COG4992 228 ----GRtGKlfaYEHYGV--EPDILT--LAKGLG---GGFpigaVLAREEVADVF----TPGDhgstFGgNPLA---CAA 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 284 SIKVLEMVEEgadlrDRLWANAR----LFREKMTAagftLAGADHAIIPV-----MLGeaVV----AQNFARELQKEGIY 350
Cdd:COG4992 290 ALAVLDVLEE-----EGLLENVAekgaYLREGLEA----LAAKYPLVKEVrgrglMIG--IElddpAAEVVKALLEEGLL 358
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 496082343 351 VTGF------FYP--VVpkgqarirtqmsaahTPEQIERAVEAFTRI 389
Cdd:COG4992 359 VNAAgpnvirLLPplII---------------TEEEIDEALAALEEA 390
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
88-212 |
8.75e-05 |
|
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to ornithine decarboxylase (ODC), arginine decarboxylase (ADC) and lysine decarboxylase (LDC). ODC is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. ADC catalyzes the decarboxylation of arginine and LDC catalyzes the decarboxylation of lysine. Members of this family are widely found in all three forms of life.
Pssm-ID: 99739 [Multi-domain] Cd Length: 294 Bit Score: 43.78 E-value: 8.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 88 HKQLEKKLADFLGMEDAILY---SSCfdANGGLFETLLGPEDAIISDALNHASIIDGVRLCKAK-------RFRYANN-- 155
Cdd:cd00615 61 IKEAQELAARAFGAKHTFFLvngTSS--SNKAVILAVCGPGDKILIDRNCHKSVINGLVLSGAVpvylkpeRNPYYGIag 138
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 496082343 156 --DMQELEACLKEAREAGArhvLIATDGVFsmDGVIANLKGVCDLADKYDALVMVDDSH 212
Cdd:cd00615 139 giPPETFKKALIEHPDAKA---AVITNPTY--YGICYNLRKIVEEAHHRGLPVLVDEAH 192
|
|
| PRK00062 |
PRK00062 |
glutamate-1-semialdehyde 2,1-aminomutase; |
192-393 |
1.60e-04 |
|
glutamate-1-semialdehyde 2,1-aminomutase;
Pssm-ID: 234607 [Multi-domain] Cd Length: 426 Bit Score: 43.52 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 192 LKGVCDLADKYDALVMVDDshaV--GF-VGENGrgSHEYCDVMGrvDIITgtLGKALGG-----ASGGytaaRKEVVEwl 263
Cdd:PRK00062 220 LEGLRELCDEHGALLIFDE---VmtGFrVALGG--AQGYYGVTP--DLTT--LGKIIGGglpvgAFGG----RREIME-- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 264 rqrsrpYL-----------FS-NSLApaiVAASIKVLEMVEEGaDLRDRLWANARLFREKMTAAgFTLAGADHAI--IPV 329
Cdd:PRK00062 285 ------QLaplgpvyqagtLSgNPLA---MAAGLATLKLLKEP-GFYEELEALTKRLAEGLKEA-AKKAGIPLTVnrVGS 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 330 MLG-----------EAVVAQN------FARELQKEGIYV------TGFfypvvpkgqarirtqMSAAHTPEQIERAVEAF 386
Cdd:PRK00062 354 MFGlfftdepvtnyADAKKSDterfarFFHAMLDEGVYLapsqfeAGF---------------VSAAHTDEDIEKTLEAA 418
|
....*..
gi 496082343 387 TRIGKQL 393
Cdd:PRK00062 419 RKAFAAL 425
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
86-213 |
3.53e-04 |
|
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: 42.19 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 86 DTHKQLEKKLADFLGMEDAILYSSCFDANGGLFETLLGPEDAIIS-DALNHASIidgvRLCK--AKRF----RYAN-NDM 157
Cdd:cd00614 40 PTVDALEKKLAALEGGEAALAFSSGMAAISTVLLALLKAGDHVVAsDDLYGGTY----RLFErlLPKLgievTFVDpDDP 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 496082343 158 QELEACLKEareaGARHVLIATDGvfSMDGVIANLKGVCDLADKYDALVMVDDSHA 213
Cdd:cd00614 116 EALEAAIKP----ETKLVYVESPT--NPTLKVVDIEAIAELAHEHGALLVVDNTFA 165
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
84-215 |
2.27e-03 |
|
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.
Pssm-ID: 425567 [Multi-domain] Cd Length: 368 Bit Score: 39.92 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 84 TQDTHKQLE---KKLADFLGMEDA---ILYSSCFDAN----GGLFETLlGPED-AIISDALNHASIIDGVRLCK---AKR 149
Cdd:pfam00266 38 GKEATQAYEearEKVAEFINAPSNdeiIFTSGTTEAInlvaLSLGRSL-KPGDeIVITEMEHHANLVPWQELAKrtgARV 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496082343 150 FRYANNDMQELEacLKEAREA-GARHVLIATDGVFSMDGVIANLKGVCDLADKYDALVMVDDSHAVG 215
Cdd:pfam00266 117 RVLPLDEDGLLD--LDELEKLiTPKTKLVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQAIG 181
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
164-361 |
2.69e-03 |
|
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), serine-glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT). AGAT is a homodimeric protein, which catalyses the transamination of glyoxylate to glycine, and SGAT converts serine and glyoxylate to hydroxypyruvate and glycine. HKT catalyzes the PLP-dependent transamination of 3-hydroxykynurenine, a potentially toxic metabolite of the kynurenine pathway.
Pssm-ID: 99744 [Multi-domain] Cd Length: 356 Bit Score: 39.58 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 164 LKEAREAGARHVLIATDGVFSMdGVIANLKGVCDLADKYDALVMVDdshAVGFVGengrGSHEYCDVMGrVDI-ITGTlG 242
Cdd:cd06451 116 IAEALEQHDIKAVTLTHNETST-GVLNPLEGIGALAKKHDALLIVD---AVSSLG----GEPFRMDEWG-VDVaYTGS-Q 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082343 243 KALGGASG-GYTAARKEVVEWLRQRSRP---YLFSNSLA------------PAI--VAASIKVLEMV-EEGADLR-DRLW 302
Cdd:cd06451 186 KALGAPPGlGPIAFSERALERIKKKTKPkgfYFDLLLLLkywgegysyphtPPVnlLYALREALDLIlEEGLENRwARHR 265
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496082343 303 ANARLFREKMTAAGFTLAGADHAIIP----VMLGEAVVAQNFARELQKE-GIYVTGFFYPVVPK 361
Cdd:cd06451 266 RLAKALREGLEALGLKLLAKPELRSPtvtaVLVPEGVDGDEVVRRLMKRyNIEIAGGLGPTAGK 329
|
|
| |
