|
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: 832.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 1 MSNGFYRHLTEQLEQVKAEGLYKQERIITSAQQAQIAV-GGEQVLNFCANNYLGLANHPDLIAAAHQGLESHGFGMASVR 79
Cdd:PRK06939 1 MSGAFYAQLREELEEIKAEGLYKEERVITSPQGADITVaDGKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 80 FICGTQDQHKALEQKLSAFLGTEDSILYSSCFDANGGLFETLFGAEDAIISDALNHASIIDGVRLCKARRYRYANNDMAE 159
Cdd:PRK06939 81 FICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 160 LEAQLKQADADGARFKLIATDGVFSMDGVIADLKSICDLADKYDALVMVDDSHAVGFIGENGRGTHEYCEVMERVDIITG 239
Cdd:PRK06939 161 LEAQLKEAKEAGARHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDRVDIITG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 240 TLGKALGGASGGYTSGKKEVIDWLRQRSRPYLFSNSLAPSIVSATIKVIDMLAEGHDLRARLKENSAYFRERMSAAGFTL 319
Cdd:PRK06939 241 TLGKALGGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDRLWENARYFREGMTAAGFTL 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2067285890 320 AGADHAIIPVMLGDAKLAAEMASRMLDAGIYVVGFSFPVVPKGQARIRTQMSAAHTREQLDKAIDAFIRIGRELGVI 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: 689.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 5 FYRHLTEQLEQVKAEGLYKQERIITSAQQAQIAVG-GEQVLNFCANNYLGLANHPDLIAAAHQGLESHGFGMASVRFICG 83
Cdd:TIGR01822 1 FYAQLAAELESIREAGLFKSERIITSPQGADIRVAdGREVLNFCANNYLGLSSHPDLIQAAKDALDEHGFGMSSVRFICG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 84 TQDQHKALEQKLSAFLGTEDSILYSSCFDANGGLFETLFGAEDAIISDALNHASIIDGVRLCKARRYRYANNDMAELEAQ 163
Cdd:TIGR01822 81 TQDIHKELEAKIAAFLGTEDTILYASCFDANGGLFETLLGAEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 164 LKQADADGARFKLIATDGVFSMDGVIADLKSICDLADKYDALVMVDDSHAVGFIGENGRGTHEYCEVMERVDIITGTLGK 243
Cdd:TIGR01822 161 LKEARAAGARHRLIATDGVFSMDGVIAPLDEICDLADKYDALVMVDECHATGFLGPTGRGSHELCGVMGRVDIITGTLGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 244 ALGGASGGYTSGKKEVIDWLRQRSRPYLFSNSLAPSIVSATIKVIDMLAEGHDLRARLKENSAYFRERMSAAGFTLAGAD 323
Cdd:TIGR01822 241 ALGGASGGFTTARKEVVELLRQRSRPYLFSNSLPPAVVGASIKVLEMLEASNELRDRLWANTRYFRERMEAAGFDIKPAD 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2067285890 324 HAIIPVMLGDAKLAAEMASRMLDAGIYVVGFSFPVVPKGQARIRTQMSAAHTREQLDKAIDAFIRIGRELGVI 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: 584.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 5 FYRHLTEQLEQVKAEGLYKQERIITSAQQAQIAVGGEQVLNFCANNYLGLANHPDLIAAAHQGLESHGFGMASVRFICGT 84
Cdd:COG0156 1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 85 QDQHKALEQKLSAFLGTEDSILYSSCFDANGGLFETLFGAEDAIISDALNHASIIDGVRLCKARRYRYANNDMAELEAQL 164
Cdd:COG0156 81 TPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 165 KQADAdgARFKLIATDGVFSMDGVIADLKSICDLADKYDALVMVDDSHAVGFIGENGRGTHEYCEVMERVDIITGTLGKA 244
Cdd:COG0156 161 KKARA--ARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDIIMGTLSKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 245 LgGASGGYTSGKKEVIDWLRQRSRPYLFSNSLAPSIVSATIKVIDMLAEGHDLRARLKENSAYFRERMSAAGFTLAGADH 324
Cdd:COG0156 239 L-GSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFDLGPSES 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2067285890 325 AIIPVMLGDAKLAAEMASRMLDAGIYVVGFSFPVVPKGQARIRTQMSAAHTREQLDKAIDAFIRIGRE 392
Cdd:COG0156 318 PIVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
41-390 |
3.36e-168 |
|
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: 474.36 E-value: 3.36e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 41 EQVLNFCANNYLGLANHPDLIAAAHQGLESHGFGMASVRFICGTQDQHKALEQKLSAFLGTEDSILYSSCFDANGGLFET 120
Cdd:cd06454 1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 121 LFGAEDAIISDALNHASIIDGVRLCKARRYRYANNDMAELEAQLKQADAdGARFKLIATDGVFSMDGVIADLKSICDLAD 200
Cdd:cd06454 81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARR-PYGKKLIVTEGVYSMDGDIAPLPELVDLAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 201 KYDALVMVDDSHAVGFIGENGRGTHEYCEVMERVDIITGTLGKALgGASGGYTSGKKEVIDWLRQRSRPYLFSNSLAPSI 280
Cdd:cd06454 160 KYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAF-GAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 281 VSATIKVIDMLAEGHDLRARLKENSAYFRERMSAAGFTLAGA-DHAIIPVMLGDAKLAAEMASRMLDAGIYVVGFSFPVV 359
Cdd:cd06454 239 AAAALAALEVLQGGPERRERLQENVRYLRRGLKELGFPVGGSpSHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTV 318
|
330 340 350
....*....|....*....|....*....|.
gi 2067285890 360 PKGQARIRTQMSAAHTREQLDKAIDAFIRIG 390
Cdd:cd06454 319 PRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
|
|
| PRK05958 |
PRK05958 |
8-amino-7-oxononanoate synthase; Reviewed |
3-390 |
1.92e-133 |
|
8-amino-7-oxononanoate synthase; Reviewed
Pssm-ID: 235655 [Multi-domain] Cd Length: 385 Bit Score: 387.21 E-value: 1.92e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 3 NGFYRHLTEQLEQVKAEGLYKQERIITSAQQAQIAVGGEQVLNFCANNYLGLANHPDLIAAAHQGLESHGFGMASVRFIC 82
Cdd:PRK05958 1 MSWLDRLEAALAQRRAAGLYRSLRPREGGAGRWLVVDGRRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 83 GTQDQHKALEQKLSAFLGTEDSILYSSCFDANGGLFETLFGAEDAIISDALNHASIIDGVRLCKARRYRYANNDMAELEA 162
Cdd:PRK05958 81 GNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 163 QLKQADadgARFKLIATDGVFSMDGVIADLKSICDLADKYDALVMVDDSHAVGFIGENGRG-THEYCEVMERVDIITGTL 241
Cdd:PRK05958 161 LLAKWR---AGRALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGlAAEAGLAGEPDVILVGTL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 242 GKALgGASGGYTSGKKEVIDWLRQRSRPYLFSNSLAPSIVSATIKVIDMLAEGHDLRARLKENSAYFRERMSAAGFTLAG 321
Cdd:PRK05958 238 GKAL-GSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRALGFQLMD 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2067285890 322 ADHAIIPVMLGDAKLAAEMASRMLDAGIYVVGFSFPVVPKGQARIRTQMSAAHTREQLDKAIDAFIRIG 390
Cdd:PRK05958 317 SQSAIQPLIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEALAEAL 385
|
|
| bioF |
TIGR00858 |
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ... |
26-386 |
1.21e-130 |
|
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: 379.30 E-value: 1.21e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 26 RIITSAQQAQIAVGGEQVLNFCANNYLGLANHPDLIAAAHQGLESHGFGMASVRFICGTQDQHKALEQKLSAFLGTEDSI 105
Cdd:TIGR00858 1 RPLDRGPGPEVVRDGRRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 106 LYSSCFDANGGLFETLFGAEDAIISDALNHASIIDGVRLCKARRYRYANNDMAELEAQLKQADadGARFKLIATDGVFSM 185
Cdd:TIGR00858 81 LFSSGYLANVGVISALVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNR--GERRKLIVTDGVFSM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 186 DGVIADLKSICDLADKYDALVMVDDSHAVGFIGENGRGTHEYCEVM-ERVDIITGTLGKALGGAsGGYTSGKKEVIDWLR 264
Cdd:TIGR00858 159 DGDIAPLPQLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKpEPVDIQVGTLSKALGSY-GAYVAGSQALIDYLI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 265 QRSRPYLFSNSLAPSIVSATIKVIDMLAEGHDLRARLKENSAYFRERMSAAGFTLAGADHAIIPVMLGDAKLAAEMASRM 344
Cdd:TIGR00858 238 NRARTLIFSTALPPAVAAAALAALELIQEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEEL 317
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2067285890 345 LDAGIYVVGFSFPVVPKGQARIRTQMSAAHTREQLDKAIDAF 386
Cdd:TIGR00858 318 QQQGIFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEAL 359
|
|
| 5aminolev_synth |
TIGR01821 |
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ... |
5-395 |
4.04e-94 |
|
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: 287.78 E-value: 4.04e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 5 FYRHLTEQLEQVKAEGLYKQ----ERIITSAQQAQ--IAVGGEQVLNFCANNYLGLANHPDLIAAAHQGLESHGFGMASV 78
Cdd:TIGR01821 3 YDQFFNKEIDKLHLEGRYRVfadlERQAGEFPFAQwhRPDGAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAGAGGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 79 RFICGTQDQHKALEQKLSAFLGTEDSILYSSCFDANGGLFETL--FGAEDAIISDALNHASIIDGVRLCKARRYRYANND 156
Cdd:TIGR01821 83 RNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLakIIPGCVIFSDELNHASMIEGIRHSGAEKFIFRHND 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 157 MAELEAQLKQADAdgARFKLIATDGVFSMDGVIADLKSICDLADKYDALVMVDDSHAVGFIGENGRGTHEYCEVMERVDI 236
Cdd:TIGR01821 163 VAHLEKLLQSVDP--NRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 237 ITGTLGKALgGASGGYTSGKKEVIDWLRQRSRPYLFSNSLAPSIVSATIKVIDMLAEGHDLRARLKENSAYFRERMSAAG 316
Cdd:TIGR01821 241 IEGTLAKAF-GVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQDLRRAHQENVKRLKNLLEALG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 317 FTLAGADHAIIPVMLGDAKLAAEmASRML--DAGIYVVGFSFPVVPKGQARIRTQMSAAHTREQLDKAIDAFIRIGRELG 394
Cdd:TIGR01821 320 IPVIPNPSHIVPVIIGDAALCKK-VSDLLlnKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDRLG 398
|
.
gi 2067285890 395 V 395
Cdd:TIGR01821 399 L 399
|
|
| PRK13392 |
PRK13392 |
5-aminolevulinate synthase; Provisional |
5-395 |
3.31e-86 |
|
5-aminolevulinate synthase; Provisional
Pssm-ID: 184023 [Multi-domain] Cd Length: 410 Bit Score: 267.49 E-value: 3.31e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 5 FYRHLTEQLEQVKAEGLYKQ----ERIITSAQQA--QIAVGGEQVLNFCANNYLGLANHPDLIAAAHQGLESHGFGMASV 78
Cdd:PRK13392 4 YDSYFDAALAQLHQEGRYRVfadlEREAGRFPRArdHGPDGPRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAGAGGT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 79 RFICGTQDQHKALEQKLSAFLGTEDSILYSSCFDANGGLFETLFG--AEDAIISDALNHASIIDGVRLCKARRYRYANND 156
Cdd:PRK13392 84 RNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKllPGCVILSDALNHASMIEGIRRSGAEKQVFRHND 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 157 MAELEAQLKQADADgaRFKLIATDGVFSMDGVIADLKSICDLADKYDALVMVDDSHAVGFIGENGRGTHEYCEVMERVDI 236
Cdd:PRK13392 164 LADLEEQLASVDPD--RPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRIDM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 237 ITGTLGKALgGASGGYTSGKKEVIDWLRQRSRPYLFSNSLAPSIVSATIKVIDMLAEGHDLRARLKENSAYFRERMSAAG 316
Cdd:PRK13392 242 IQGTLAKAF-GCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLKTSQTERDAHQDRVAALKAKLNANG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 317 FTLAGADHAIIPVMLGDAKLAAEMASRML-DAGIYVVGFSFPVVPKGQARIRTQMSAAHTREQLDKAIDAFIRIGRELGV 395
Cdd:PRK13392 321 IPVMPSPSHIVPVMVGDPTLCKAISDRLMsEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDRLEL 400
|
|
| PLN02483 |
PLN02483 |
serine palmitoyltransferase |
42-395 |
2.83e-68 |
|
serine palmitoyltransferase
Pssm-ID: 178101 [Multi-domain] Cd Length: 489 Bit Score: 223.49 E-value: 2.83e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 42 QVLNFCANNYLGLANH-----PDLIAAahqgLESHGFGMASVRFICGTQDQHKALEQKLSAFLGTEDSILYSSCFDANGG 116
Cdd:PLN02483 101 RCLNLGSYNYLGFAAAdeyctPRVIES----LKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNST 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 117 LFETLFGAEDAIISDALNHASIIDGVRLCKARRYRYANNDMAELEAQLKQADADGA-----RFK--LIATDGVFSMDGVI 189
Cdd:PLN02483 177 IIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQprthrPWKkiIVIVEGIYSMEGEL 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 190 ADLKSICDLADKYDALVMVDDSHAVGFIGENGRGTHEYCEVMER-VDIITGTLGKALgGASGGYTSGKKEVIDWLRQRSR 268
Cdd:PLN02483 257 CKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPAdVDIMMGTFTKSF-GSCGGYIAGSKELIQYLKRTCP 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 269 PYLFSNSLAPSIVS---ATIKVI---DMLAEGHDLRARLKENSAYFRERMSAAGFTLAGA-DHAIIPVML-GDAKLAAem 340
Cdd:PLN02483 336 AHLYATSMSPPAVQqviSAIKVIlgeDGTNRGAQKLAQIRENSNFFRSELQKMGFEVLGDnDSPVMPIMLyNPAKIPA-- 413
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2067285890 341 ASR-MLDAGIYVVGFSFPVVPKGQARIRTQMSAAHTREQLDKAIDAFIRIGRELGV 395
Cdd:PLN02483 414 FSReCLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGI 469
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
43-386 |
2.77e-67 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 216.79 E-value: 2.77e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 43 VLNFCANNYLGLANhPDLIAAAHQGLESHGfgmasvRFICGTQDQHKALEQKLSAFLGT--------EDSILYSSCFDAN 114
Cdd:pfam00155 3 KINLGSNEYLGDTL-PAVAKAEKDALAGGT------RNLYGPTDGHPELREALAKFLGRspvlkldrEAAVVFGSGAGAN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 115 GGLFETLFG-AEDAIISDALNHASIIDGVRLCKARRYRYA-------NNDMAELEAQLKQADadgarfKLIATDGVFSMD 186
Cdd:pfam00155 76 IEALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKP------KVVLHTSPHNPT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 187 GVIADLKSICDLAD---KYDALVMVDDSHAVGFIGENGRGThEYCEVMERVD-IITGTLGKALG--GASGGYTSGKKEVI 260
Cdd:pfam00155 150 GTVATLEELEKLLDlakEHNILLLVDEAYAGFVFGSPDAVA-TRALLAEGPNlLVVGSFSKAFGlaGWRVGYILGNAAVI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 261 DWLRQRSRPYLFSNSLAPSIVSATIKVIDMLAEGHDLRARLKENSAYFRERMSAAGFTLAGADHAIIPVMLGDAKLAAEM 340
Cdd:pfam00155 229 SQLRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKEL 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2067285890 341 ASRMLD-AGIYVVGFSFPVVPkgqARIRTQMsAAHTREQLDKAIDAF 386
Cdd:pfam00155 309 AQVLLEeVGVYVTPGSSPGVP---GWLRITV-AGGTEEELEELLEAI 351
|
|
| PLN02822 |
PLN02822 |
serine palmitoyltransferase |
27-389 |
5.11e-60 |
|
serine palmitoyltransferase
Pssm-ID: 178417 [Multi-domain] Cd Length: 481 Bit Score: 201.89 E-value: 5.11e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 27 IITSAQQAQIAVGGEQVLNFCANNYLGLANHPDLIAAAHQGLESHGFGMASVRFICGTQDQHKALEQKLSAFLGTEDSIL 106
Cdd:PLN02822 95 VLESAAGPHTIINGKDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSIL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 107 YSSCFDANGGLFETLFGAEDAIISDALNHASIIDGVRLCKARRYRYANNDMAELEAQLKQADADGARFK----LIATDGV 182
Cdd:PLN02822 175 YSYGLSTIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEKLTAENKRKKklrrYIVVEAI 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 183 FSMDGVIADLKSICDLADKYDALVMVDDSHAVGFIGENGRGTHEYCEV-MERVDIITGTLGKALGGAsGGYTSGKKEVID 261
Cdd:PLN02822 255 YQNSGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVpIEKIDIITAAMGHALATE-GGFCTGSARVVD 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 262 WLRQRSRPYLFSNSLAPSIVSATIKVIDMLAEGHDLRARLKENSAYFRERMSA-AGFTLAGadHAIIPVML--------- 331
Cdd:PLN02822 334 HQRLSSSGYVFSASLPPYLASAAITAIDVLEDNPSVLAKLKENIALLHKGLSDiPGLSIGS--NTLSPIVFlhlekstgs 411
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2067285890 332 --GDAKLAAEMASRML-DAGIYVVGFSFPVVPKGQ--ARIRTQMSAAHTREQLDKAIDAFIRI 389
Cdd:PLN02822 412 akEDLSLLEHIADRMLkEDSVLVVVSKRSTLDKCRlpVGIRLFVSAGHTESDILKASESLKRV 474
|
|
| PRK07179 |
PRK07179 |
quorum-sensing autoinducer synthase; |
9-383 |
1.60e-53 |
|
quorum-sensing autoinducer synthase;
Pssm-ID: 180866 [Multi-domain] Cd Length: 407 Bit Score: 182.52 E-value: 1.60e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 9 LTEQLEQvkaeglYKQERIITSAQQAQIAVG---GEQVLNFCANNYLGLANHPDLIAAAHQGLESHGFG--MASVrFICG 83
Cdd:PRK07179 25 IEERLDK------YIEERVNKNWNGKHLVLGktpGPDAIILQSNDYLNLSGHPDIIKAQIAALQEEGDSlvMSAV-FLHD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 84 TQDQHkALEQKLSAFLGTEDSILYSSCFDANGGLFETLFGAEDAIISDALNHASIIDGVRLCKARRYRYANNDMAELEAQ 163
Cdd:PRK07179 98 DSPKP-QFEKKLAAFTGFESCLLCQSGWAANVGLLQTIADPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 164 LKQADADgarfkLIATDGVFSMDGVIADLKSICDLADKYDALVMVDDSHAVGFIGENGRGTHEYCEVMERVDIITGTLGK 243
Cdd:PRK07179 177 IERHGPG-----IIVVDSVYSTTGTIAPLADIVDIAEEFGCVLVVDESHSLGTHGPQGAGLVAELGLTSRVHFITASLAK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 244 ALGGaSGGYTSGKKEVIDWLRQRSRPYLFSNSLAPSIVSATIKVIDMLAEGHDLRARLKENSAYFRERMSAAGFTLAGAD 323
Cdd:PRK07179 252 AFAG-RAGIITCPRELAEYVPFVSYPAIFSSTLLPHEIAGLEATLEVIESADDRRARLHANARFLREGLSELGYNIRSES 330
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 324 HaIIPVMLGDAKLAAEMASRMLDAGIYVVGFSFPVVPKGQARIRTQMSAAHTREQLDKAI 383
Cdd:PRK07179 331 Q-IIALETGSERNTEVLRDALEERNVFGAVFCAPATPKNRNLIRLSLNADLTASDLDRVL 389
|
|
| PLN02955 |
PLN02955 |
8-amino-7-oxononanoate synthase |
41-386 |
1.85e-52 |
|
8-amino-7-oxononanoate synthase
Pssm-ID: 178541 [Multi-domain] Cd Length: 476 Bit Score: 181.80 E-value: 1.85e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 41 EQVLNFCANNYLGLANHPDLIAAAHQGLESHGFGMASVRFICGTQDQHKALEQKLSAFLGTEDSILYSSCFDANGGLF-- 118
Cdd:PLN02955 102 KKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMva 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 119 ----ETLFGAED--------AIISDALNHASIIDGVRLCK----ARRYRYANNDMAELEAQLKQADADGarfKLIATDGV 182
Cdd:PLN02955 182 igsvASLLAASGkplknekvAIFSDALNHASIIDGVRLAErqgnVEVFVYRHCDMYHLNSLLSSCKMKR---KVVVTDSL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 183 FSMDGVIADLKSICDLADKYDALVMVDDSHAVGFIGENGRGTHEYCEVMERVDIITGTLGKAlGGASGGYTSGKKEVIDW 262
Cdd:PLN02955 259 FSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKA-AGCHGGFIACSKKWKQL 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 263 LRQRSRPYLFSNSLAPSIVSATIKVIDMLAEGHDLRARLKENSAYFRErmsaagftLAGAD--HAIIPVMLGDAKLAAEM 340
Cdd:PLN02955 338 IQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEKWRRKAIWERVKEFKA--------LSGVDisSPIISLVVGNQEKALKA 409
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2067285890 341 ASRMLDAGIYVVGFSFPVVPKGQARIRTQMSAAHTREQLDKAIDAF 386
Cdd:PLN02955 410 SRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITAL 455
|
|
| PLN03227 |
PLN03227 |
serine palmitoyltransferase-like protein; Provisional |
44-385 |
3.22e-46 |
|
serine palmitoyltransferase-like protein; Provisional
Pssm-ID: 178766 [Multi-domain] Cd Length: 392 Bit Score: 163.15 E-value: 3.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 44 LNFCANNYLGLANHPDLIAAAHQGLESHGFGMASVRFICGTQDQHKALEQKLSAFLGTEDSILYSSCFDANGGLFETLFG 123
Cdd:PLN03227 1 LNFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 124 AEDAIISDALNHASIIDGVRLCKARRYRYANNDMAELEAQLKQADADGARFKL--------IATDGVFSMDGVIADLKSI 195
Cdd:PLN03227 81 RGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLEQVRAQDVALKRkptdqrrfLVVEGLYKNTGTLAPLKEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 196 CDLADKYDALVMVDDSHAVGFIGENGRGTHEYC--EVMERVDIITGTLGKALGGAsGGYTSGKKEVIDWLRQRSRPYLFS 273
Cdd:PLN03227 161 VALKEEFHYRLILDESFSFGTLGKSGRGSLEHAglKPMVHAEIVTFSLENAFGSV-GGMTVGSEEVVDHQRLSGSGYCFS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 274 NSLAPSIVSATIKVIDMLAEGHDLRARLKENSAYFRERMSAAG-----------FTLAGADHAIIPVMLGDAK------- 335
Cdd:PLN03227 240 ASAPPFLAKADATATAGELAGPQLLNRLHDSIANLYSTLTNSShpyalklrnrlVITSDPISPIIYLRLSDQEatrrtde 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2067285890 336 --LAAEMASRMLDAGIYVVGFSFPVVPKGQAR----IRTQMSAAHTREQLDKAIDA 385
Cdd:PLN03227 320 tlILDQIAHHSLSEGVAVVSTGGHVKKFLQLVpppcLRVVANASHTREDIDKLLTV 375
|
|
| PRK07505 |
PRK07505 |
hypothetical protein; Provisional |
40-394 |
7.55e-44 |
|
hypothetical protein; Provisional
Pssm-ID: 181006 [Multi-domain] Cd Length: 402 Bit Score: 157.06 E-value: 7.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 40 GEQVLNFCANNYLGLANHPDLIAAAHQGLESHGfgmaSVRFICG-TQDQH---KALEQKLSAFLGTEdSILYSSCFDANG 115
Cdd:PRK07505 45 GHTFVNFVSCSYLGLDTHPAIIEGAVDALKRTG----SLHLSSSrTRVRSqilKDLEEALSELFGAS-VLTFTSCSAAHL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 116 GLFETLF------GAEDAIISDALNHASIIDGVRLCK--ARRYRYANNDMAELEAQLKQadadGARFKLIAtDGVFSMDG 187
Cdd:PRK07505 120 GILPLLAsghltgGVPPHMVFDKNAHASLNILKGICAdeTEVETIDHNDLDALEDICKT----NKTVAYVA-DGVYSMGG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 188 ViADLKSICDLADKYDALVMVDDSHAVGFIGENGRGtheYceVMERVD-------IITGTLGKALGGASGGYTSGKKEVI 260
Cdd:PRK07505 195 I-APVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEG---Y--VRSELDyrlnertIIAASLGKAFGASGGVIMLGDAEQI 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 261 DWLRQRSRPYLFSNSL-----APSIVSATIKVIDMLAEghdLRARLKENSAYFRERMSAagfTLAGADHAIIPVMLGDAK 335
Cdd:PRK07505 269 ELILRYAGPLAFSQSLnvaalGAILASAEIHLSEELDQ---LQQKLQNNIALFDSLIPT---EQSGSFLPIRLIYIGDED 342
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2067285890 336 LAAEMASRMLDAGIYVVGFSFPVVPKGQARIRTQMSAAHTREQLDKAIDAFIRIGRELG 394
Cdd:PRK07505 343 TAIKAAKQLLDRGFYTSPVFFPVVAKGRAGLRIMFRASHTNDEIKRLCSLLKEILDEGL 401
|
|
| PRK05937 |
PRK05937 |
8-amino-7-oxononanoate synthase; Provisional |
40-380 |
6.36e-27 |
|
8-amino-7-oxononanoate synthase; Provisional
Pssm-ID: 102071 [Multi-domain] Cd Length: 370 Bit Score: 110.26 E-value: 6.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 40 GEQVLNFCANNYLGLANHPDLIAA------AHQGLESHG-FGMASVRFICGTQDQHKALEQKLSAFLGTEDSILYSSCFD 112
Cdd:PRK05937 3 ESLSIDFVTNDFLGFSRSDTLVHEvekryrLYCRQFPHAqLGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 113 ANGGLFETLFGAEDAIISDALNHASIIDGVRLCKARRYRYANNDMAELEAQLKQADADGARFKLIATDGVFSMDGVIADL 192
Cdd:PRK05937 83 ANLGLCAHLSSVTDYVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLESCRQRSFGRIFIFVCSVYSFKGTLAPL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 193 KSICDLADKYDALVMVDDSHAVGFIGENGRGtheYCEVM--ERVDIITGTLGKALGGASGGYTSgKKEVIDWLRQRSRPY 270
Cdd:PRK05937 163 EQIIALSKKYHAHLIVDEAHAMGIFGDDGKG---FCHSLgyENFYAVLVTYSKALGSMGAALLS-SSEVKQDLMLNSPPL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 271 LFSNSLAP-SIVSATIKVIDMLAEGHDLRARLKENSAYFRERMS--AAGFtlagadhaIIPVMLGDakLAAEMASRMLD- 346
Cdd:PRK05937 239 RYSTGLPPhLLISIQVAYDFLSQEGELARKQLFRLKEYFAQKFSsaAPGC--------VQPIFLPG--ISEQELYSKLVe 308
|
330 340 350
....*....|....*....|....*....|....
gi 2067285890 347 AGIYVVGFSFPVVPKgqarIRTQMSAAHTREQLD 380
Cdd:PRK05937 309 TGIRVGVVCFPTGPF----LRVNLHAFNTEDEVD 338
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
88-256 |
1.45e-26 |
|
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: 104.39 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 88 HKALEQKLSAFLGT--EDSILYSSCFDANGGLFETLFGAEDAIISDALNHAS---IIDGVRLCKARRYRYANNDMAELEA 162
Cdd:cd01494 2 LEELEEKLARLLQPgnDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSrywVAAELAGAKPVPVPVDDAGYGGLDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 163 QLKQADADGARFKLIATDGVFSMDGVIADLKSICDLADKYDALVMVDDSHAVGFIGENgrgthEYCEVMERVDIITGTLG 242
Cdd:cd01494 82 AILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAP-----GVLIPEGGADVVTFSLH 156
|
170
....*....|....
gi 2067285890 243 KALGGASGGYTSGK 256
Cdd:cd01494 157 KNLGGEGGGVVIVK 170
|
|
| OAT_like |
cd00610 |
Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP) ... |
192-389 |
1.01e-13 |
|
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: 72.22 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 192 LKSICDLADKYDALVMVDDShAVGFigenGR----GTHEYCEVmeRVDIITgtLGKALGGAS--GGYTsGKKEVIDWLrq 265
Cdd:cd00610 214 LKALRELCRKHGILLIADEV-QTGF----GRtgkmFAFEHFGV--EPDIVT--LGKGLGGGLplGAVL-GREEIMDAF-- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 266 RSRPYLFS-----NSLAPSIVSATIKVIdmlaEGHDLRARLKENSAYFRERMSAagftLAGADHAIIPV-----MLG--- 332
Cdd:cd00610 282 PAGPGLHGgtfggNPLACAAALAVLEVL----EEEGLLENAAELGEYLRERLRE----LAEKHPLVGDVrgrglMIGiel 353
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2067285890 333 ---------DAKLAAEMASRMLDAGIYvvgfsfpVVPKGQARIRTQMSAAHTREQLDKAIDAFIRI 389
Cdd:cd00610 354 vkdratkppDKELAAKIIKAALERGLL-------LRPSGGNVIRLLPPLIITEEEIDEGLDALDEA 412
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
88-386 |
5.61e-12 |
|
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: 66.21 E-value: 5.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 88 HKALEQKLSAFLG-------TEDSILYSscfdaNGG------LFETLFGAEDAIISDALNHASIIDGVRLCKARRYRYA- 153
Cdd:cd00609 38 LPELREAIAEWLGrrggvdvPPEEIVVT-----NGAqealslLLRALLNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPl 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 154 --NNDMAELEAQLKQADADGARFKLIA-----TDGVFSMDgviaDLKSICDLADKYDALVMVDDSHAvGFIGENGRGTHE 226
Cdd:cd00609 113 deEGGFLLDLELLEAAKTPKTKLLYLNnpnnpTGAVLSEE----ELEELAELAKKHGILIISDEAYA-ELVYDGEPPPAL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 227 YCEVMERVDIITGTLGKALGGAS--GGYTSGKKEVIDWLRQRSRPYLFSNslaPSIVSATIkVIDMLAEGHD----LRAR 300
Cdd:cd00609 188 ALLDAYERVIVLRSFSKTFGLPGlrIGYLIAPPEELLERLKKLLPYTTSG---PSTLSQAA-AAAALDDGEEhleeLRER 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 301 LKENSAYFRERMSAAGFtlagaDHAIIP-----VMLG-DAKLAAEMASRMLD-AGIYVV-GFSFPVVPKGQARIrtqmSA 372
Cdd:cd00609 264 YRRRRDALLEALKELGP-----LVVVKPsggffLWLDlPEGDDEEFLERLLLeAGVVVRpGSAFGEGGEGFVRL----SF 334
|
330
....*....|....
gi 2067285890 373 AHTREQLDKAIDAF 386
Cdd:cd00609 335 ATPEEELEEALERL 348
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
88-265 |
1.11e-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: 40.65 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 88 HKALEQKLSAFLGTEDSILYSSCFDANGGLFETLFGAEDAIIS-DALNHASIidgvRLCK--ARRY----RYAN-NDMAE 159
Cdd:cd00614 42 VDALEKKLAALEGGEAALAFSSGMAAISTVLLALLKAGDHVVAsDDLYGGTY----RLFErlLPKLgievTFVDpDDPEA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 160 LEAQLKqadadgARFKLIATDGVFSMDGVIADLKSICDLADKYDALVMVDDSHAVGFIG---ENGrgtheycevmerVDI 236
Cdd:cd00614 118 LEAAIK------PETKLVYVESPTNPTLKVVDIEAIAELAHEHGALLVVDNTFATPYLQrplELG------------ADI 179
|
170 180 190
....*....|....*....|....*....|...
gi 2067285890 237 ITGTLGKALGGAS---GGYTSGK-KEVIDWLRQ 265
Cdd:cd00614 180 VVHSATKYIGGHSdviAGVVVGSgEALIQRLRF 212
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
122-215 |
1.62e-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: 40.31 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 122 FGAED-AIISDALNHASIIDGVRLCKARRYR--------YANNDMAELEAQLKQadadgaRFKLIATDGVFSMDGVIADL 192
Cdd:pfam00266 85 LKPGDeIVITEMEHHANLVPWQELAKRTGARvrvlpldeDGLLDLDELEKLITP------KTKLVAITHVSNVTGTIQPV 158
|
90 100
....*....|....*....|...
gi 2067285890 193 KSICDLADKYDALVMVDDSHAVG 215
Cdd:pfam00266 159 PEIGKLAHQYGALVLVDAAQAIG 181
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
156-215 |
1.68e-03 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 40.12 E-value: 1.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 156 DMAELEAQLkqadadGARFKLIATDGVFSMDGVIADLKSICDLADKYDALVMVDDSHAVG 215
Cdd:COG0520 143 DLEALEALL------TPRTKLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVP 196
|
|
| PRK00062 |
PRK00062 |
glutamate-1-semialdehyde 2,1-aminomutase; |
186-386 |
3.88e-03 |
|
glutamate-1-semialdehyde 2,1-aminomutase;
Pssm-ID: 234607 [Multi-domain] Cd Length: 426 Bit Score: 39.28 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 186 DGVIADLKSICDladKYDALVMVDdshavgfigengrgtheycEVME--RVDI--------ITG---TLGKALGG----- 247
Cdd:PRK00062 217 PGFLEGLRELCD---EHGALLIFD-------------------EVMTgfRVALggaqgyygVTPdltTLGKIIGGglpvg 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 248 ASGGytsgKKEVIDwlrqrsrpylfsnSLAPS--------------IVSATIKVIDMLAEgHDLRARLKENSAYFRERMS 313
Cdd:PRK00062 275 AFGG----RREIME-------------QLAPLgpvyqagtlsgnplAMAAGLATLKLLKE-PGFYEELEALTKRLAEGLK 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 314 AAgFTLAGADHAI--IPVMLG-----------------DAKLAAEMASRMLDAGIYV------VGFsfpvvpkgqarirt 368
Cdd:PRK00062 337 EA-AKKAGIPLTVnrVGSMFGlfftdepvtnyadakksDTERFARFFHAMLDEGVYLapsqfeAGF-------------- 401
|
250
....*....|....*...
gi 2067285890 369 qMSAAHTREQLDKAIDAF 386
Cdd:PRK00062 402 -VSAAHTDEDIEKTLEAA 418
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
121-313 |
4.09e-03 |
|
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: 38.77 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 121 LFGAEDAIISDALNHASIIDGVRLCKAR-------RYRYANNDMAELEAQLKQADADGARFKL-IATDGVFsmDGVIADL 192
Cdd:cd00615 95 VCGPGDKILIDRNCHKSVINGLVLSGAVpvylkpeRNPYYGIAGGIPPETFKKALIEHPDAKAaVITNPTY--YGICYNL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067285890 193 KSICDLADKYDALVMVDDSHavgfigengrGTHEY-------CEVMERVDIITGTLGKALGGAS-GGYTSGKKEVIDWLR 264
Cdd:cd00615 173 RKIVEEAHHRGLPVLVDEAH----------GAHFRfhpilpsSAAMAGADIVVQSTHKTLPALTqGSMIHVKGDLVNPDR 242
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2067285890 265 QRSRPYLFSnSLAPS---IVSATIKVIDMLAEGHDLRARLKENSAYFRERMS 313
Cdd:cd00615 243 VNEALNLHQ-STSPSyliLASLDVARAMMALEGKELVEELIELALYARQEIN 293
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
156-209 |
7.50e-03 |
|
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to DOPA/tyrosine decarboxylase (DDC), histidine decarboxylase (HDC), and glutamate decarboxylase (GDC). DDC is active as a dimer and catalyzes the decarboxylation of tyrosine. GDC catalyzes the decarboxylation of glutamate and HDC catalyzes the decarboxylation of histidine.
Pssm-ID: 99743 [Multi-domain] Cd Length: 345 Bit Score: 37.95 E-value: 7.50e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2067285890 156 DMAELEAQLKQADADGAR-FKLIATDGVFSmDGVIADLKSICDLADKYDALVMVD 209
Cdd:cd06450 131 DPEALEAAIDEDKAEGLNpIMVVATAGTTD-TGAIDPLEEIADLAEKYDLWLHVD 184
|
|
| |
